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@Article{arendt97,
  Title                    = {Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active site formation},
  Author                   = {Arendt, C. S. and Hochstrasser, M.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {1997},
  Number                   = {14},
  Pages                    = {7156-7161},
  Volume                   = {94},

  Doi                      = {DOI 10.1073/pnas.94.14.7156},
  ISSN                     = {0027-8424},
  Keywords                 = {multicatalytic proteinase complex saccharomyces-cerevisiae shuttle vectors in-vivo proteolysis degradation acidophilum activation binding genes},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1997XJ87600008}
}

@Article{armon90,
  Title                    = {Assembly of the 26S complex that degrades proteins ligated to ubiquitin is accompanied by the formation of ATPase activity},
  Author                   = {Armon, T. and Ganoth, D. and Hershko, A.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {1990},
  Number                   = {34},
  Pages                    = {20723-20726},
  Volume                   = {265},

  ISSN                     = {0021-9258},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1990EL02000003}
}

@Article{arrigo88,
  Title                    = {Identity of the 19S prosome particle with the large multi-functional protease complex of mammalian cells (the proteasome)},
  Author                   = {Arrigo, A. P. and Tanaka, K. and Goldberg, A. L. and Welch, W. J.},
  Journal                  = {Nature},
  Year                     = {1988},
  Number                   = {6152},
  Pages                    = {192-194},
  Volume                   = {331},

  Doi                      = {Doi 10.1038/331192a0},
  ISSN                     = {0028-0836},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1988L668800078}
}

@Article{barthelme12,
  Title                    = {Identification of the Cdc48-20S proteasome as an ancient AAA proteolytic machine},
  Author                   = {Barthelme, D. and Sauer, R. T.},
  Journal                  = {Science},
  Year                     = {2012},
  Number                   = {6096},
  Pages                    = {843-846},
  Volume                   = {337},

  Doi                      = {DOI 10.1126/science.1224352},
  ISSN                     = {0036-8075},
  Keywords                 = {regulatory particle n-domain atpase degradation p97/vcp p97},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000307535600043}
}

@Article{baumeister88,
  Title                    = {Electron microscopy and image analysis of the multi-catalytic proteinase},
  Author                   = {Baumeister, W. and Dahlmann, B. and Hegerl, R. and Kopp, F. and Kühn, L. and Pfeifer, G.},
  Journal                  = {FEBS Lett.},
  Year                     = {1988},
  Number                   = {1-2},
  Pages                    = {239-245},
  Volume                   = {241},

  Doi                      = {Doi 10.1016/0014-5793(88)81069-X},
  ISSN                     = {0014-5793},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1988R372700052}
}

@Article{beck12,
  Title                    = {Near-atomic resolution structural model of the yeast 26S proteasome},
  Author                   = {Beck, F. and Unverdorben, P. and Bohn, S. and Schweitzer, A. and Pfeifer, G. and Sakata, E. and Nickell, S. and Plitzko, J. M. and Villa, E. and Baumeister, W. and Förster, F.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {2012},
  Number                   = {37},
  Pages                    = {14870-14875},
  Volume                   = {109},

  Doi                      = {DOI 10.1073/pnas.1213333109},
  ISSN                     = {0027-8424},
  Keywords                 = {protein degradation electron microscopy deubiquitylating enzyme regulatory particle electron-microscopy molecular architecture polyubiquitin chains crystal-structure 20s proteasome degradation domain rpn11 core},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000309208000039}
}

@Article{berndsen14,
  Title                    = {New insights into ubiquitin E3 ligase mechanisms},
  Author                   = {Berndsen, C. E. and Wolberger, C.},
  Journal                  = {Nature Structural \& Molecular Biology},
  Year                     = {2014},
  Number                   = {4},
  Pages                    = {301-307},
  Volume                   = {21},

  Doi                      = {Doi 10.1038/Nsmb.2780},
  ISSN                     = {1545-9993},
  Keywords                 = {conjugating enzyme e2 linear polyubiquitin chains ring-ring complex structural basis allosteric activation crystal-structure domain proteins reveals parkin},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000334349000005}
}

@Article{besche14,
  Title                    = {Auto-ubiquitination of the 26S proteasome on Rpn13 regulates breakdown of ubiquitin conjugates},
  Author                   = {Besche, H. C. and Sha, Z. and Kukushkin, N. V. and Peth, A. and Hock, E. M. and Kim, W. and Gygi, S. P. and Gutierrez, J. A. and Liao, H. and Dick, L. R. and Goldberg, A. L.},
  Journal                  = {EMBO J.},
  Year                     = {2014},
  Number                   = {10},
  Pages                    = {1159-1176},
  Volume                   = {33},

  Doi                      = {DOI 10.1002/embj.201386906},
  ISSN                     = {0261-4189},
  Keywords                 = {26s proteasomes proteasome inhibitors proteasome regulation ube3c/hul5 ubiquitination interacting proteins s proteasome affinity purification mass-spectrometry research tools degradation complexes substrate polyubiquitin atpases},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000336495900008}
}

@Article{bhattacharyya14,
  Title                    = {Regulated protein turnover: snapshots of the proteasome in action},
  Author                   = {Bhattacharyya, S. and Yu, H. and Mim, C. and Matouschek, A.},
  Journal                  = {Nat. Rev. Mol. Cell Biol.},
  Year                     = {2014},
  Number                   = {2},
  Pages                    = {122-133},
  Volume                   = {15},

  Doi                      = {Doi 10.1038/Nrm3741},
  ISSN                     = {1471-0072},
  Keywords                 = {26 s proteasome nf-kappa-b atp-dependent proteolysis DNA packaging motor 20s proteasome structural basis ubiquitin receptors core particle methanocaldococcus-jannaschii saccharomyces-cerevisiae},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000330190100011}
}

@Article{book10,
  Title                    = {Affinity purification of the Arabidopsis 26S proteasome reveals a diverse array of plant proteolytic complexes},
  Author                   = {Book, A. J. and Gladman, N. P. and Lee, S. S. and Scalf, M. and Smith, L. M. and Vierstra, R. D.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {2010},
  Number                   = {33},
  Pages                    = {25554-25569},
  Volume                   = {285},

  Doi                      = {DOI 10.1074/jbc.M110.136622},
  ISSN                     = {0021-9258},
  Keywords                 = {regulatory particle subunits mass-spectrometric analysis 20s proteasome ubiquitylated proteins cop9 signalosome yeast proteasome core particle identification proteomics binding},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000280682400050}
}

@Article{ciechanover80,
  Title                    = {Characterization of the heat-stable polypeptide of the ATP-dependent proteolytic system from reticulocytes},
  Author                   = {Ciechanover, A. and Elias, S. and Heller, H. and Ferber, S. and Hershko, A.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {1980},
  Number                   = {16},
  Pages                    = {7525-8},
  Volume                   = {255},

  ISSN                     = {0021-9258 (Print) 0021-9258 (Linking)},
  Keywords                 = {Amino Acids/analysis Animals *Chromosomal Proteins, Non-Histone Drug Stability Hot Temperature Proteins/*metabolism Rabbits Reticulocytes/*metabolism Ubiquitins},
  Type                     = {Journal Article},
  Url                      = {http://www.ncbi.nlm.nih.gov/pubmed/6249802}
}

@Article{ciechanover84,
  Title                    = {Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85},
  Author                   = {Ciechanover, A. and Finley, D. and Varshavsky, A.},
  Journal                  = {Cell},
  Year                     = {1984},
  Number                   = {1},
  Pages                    = {57-66},
  Volume                   = {37},

  Doi                      = {Doi 10.1016/0092-8674(84)90300-3},
  ISSN                     = {0092-8674},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1984SR71400011}
}

@Article{ciechanover80-frAQB,
  Title                    = {ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation},
  Author                   = {Ciechanover, A. and Heller, H. and Elias, S. and Haas, A. L. and Hershko, A.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {1980},
  Number                   = {3},
  Pages                    = {1365-1368},
  Volume                   = {77},

  Doi                      = {DOI 10.1073/pnas.77.3.1365},
  ISSN                     = {0027-8424},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1980JL81400024}
}

@Article{dange11,
  Title                    = {The Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism},
  Author                   = {Dange, T. and Smith, D. M. and Noy, T. and Rommel, P. C. and Jurzitza, L. and Cordero, R. J. and Legendre, A. and Finley, D. and Goldberg, A. L. and Schmidt, M.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {2011},
  Number                   = {50},
  Pages                    = {42830-42839},
  Volume                   = {286},

  Doi                      = {DOI 10.1074/jbc.M111.300178},
  ISSN                     = {0021-9258},
  Keywords                 = {20 s-proteasomes saccharomyces-cerevisiae proteolytic machine regulatory particle gene disruption 26s proteasome core particle c-termini atpases complex},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000298351300004}
}

@Article{elsasser02,
  Title                    = {Proteasome subunit Rpn1 binds ubiquitin-like protein domains},
  Author                   = {Elsasser, S. and Gali, R. R. and Schwickart, M. and Larsen, C. N. and Leggett, D. S. and Müller, B. and Feng, M. T. and Tübing, F. and Dittmar, G. A. and Finley, D.},
  Journal                  = {Nat. Cell Biol.},
  Year                     = {2002},
  Number                   = {9},
  Pages                    = {725-730},
  Volume                   = {4},

  Doi                      = {Doi 10.1038/Ncb845},
  ISSN                     = {1465-7392},
  Keywords                 = {saccharomyces-cerevisiae regulatory particle 26s proteasome uba domain DNA-repair degradation yeast recognition motif rad23},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000177783900019}
}

@Article{etlinger77,
  Title                    = {A soluble, ATP-dependent proteolytic system responsible for degradation of abnormal proteins in reticulocytes},
  Author                   = {Etlinger, J. D. and Goldberg, A. L.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {1977},
  Number                   = {1},
  Pages                    = {54-58},
  Volume                   = {74},

  Doi                      = {Doi 10.1073/Pnas.74.1.54},
  ISSN                     = {0027-8424},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1977CT87000012}
}

@Article{farmer10,
  Title                    = {The RAD23 family provides an essential connection between the 26S proteasome and ubiquitylated proteins in Arabidopsis},
  Author                   = {Farmer, L. M. and Book, A. J. and Lee, K. H. and Lin, Y. L. and Fu, H. and Vierstra, R. D.},
  Journal                  = {Plant Cell},
  Year                     = {2010},
  Number                   = {1},
  Pages                    = {124-142},
  Volume                   = {22},

  Doi                      = {DOI 10.1105/tpc.109.072660},
  ISSN                     = {1040-4651},
  Keywords                 = {multiubiquitin-chain-binding ubiquitin-like protein saccharomyces-cerevisiae functional-analysis s proteasome yeast dsk2p cell-cycle degradation domains recognition},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000275926100012}
}

@Article{fatimababy10,
  Title                    = {Cross-species divergence of the major recognition pathways of ubiquitylated substrates for ubiquitin/26S proteasome-mediated proteolysis},
  Author                   = {Fatimababy, A. S. and Lin, Y. L. and Usharani, R. and Radjacommare, R. and Wang, H. T. and Tsai, H. L. and Lee, Y. and Fu, H.},
  Journal                  = {FEBS J.},
  Year                     = {2010},
  Number                   = {3},
  Pages                    = {796-816},
  Volume                   = {277},

  Doi                      = {DOI 10.1111/j.1742-4658.2009.07531.x},
  ISSN                     = {1742-464X},
  Keywords                 = {rpn10 rpn13 ubiquitin receptor ubiquitin recognition ubl-uba factors multiubiquitin-chain-binding uba protein ddi1 26s proteasome polyubiquitin chains degradation signal subunit mcb1 aaa-atpase domains system receptors},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000273723200025}
}

@Article{finley09,
  Title                    = {Recognition and processing of ubiquitin-protein conjugates by the proteasome},
  Author                   = {Finley, D.},
  Journal                  = {Annu. Rev. Biochem.},
  Year                     = {2009},
  Pages                    = {477-513},
  Volume                   = {78},

  Doi                      = {DOI 10.1146/annurev.biochem.78.081507.101607},
  ISSN                     = {0066-4154},
  Keywords                 = {deubiquitination protease proteasome protein degradation ubiquitin 26 s-proteasome atp-dependent proteases multiubiquitin-chain-binding uch37 deubiquitinating enzyme 19s regulatory particle reg-gamma proteasome DNA-repair 20s proteasome cell-cycle saccharomyces-cerevisiae},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000268069200018}
}

@Article{finley84,
  Title                    = {Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85},
  Author                   = {Finley, D. and Ciechanover, A. and Varshavsky, A.},
  Journal                  = {Cell},
  Year                     = {1984},
  Number                   = {1},
  Pages                    = {43-55},
  Volume                   = {37},

  Doi                      = {Doi 10.1016/0092-8674(84)90299-X},
  ISSN                     = {0092-8674},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1984SR71400010}
}

@Article{finley87,
  Title                    = {The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses},
  Author                   = {Finley, D. and Ozkaynak, E. and Varshavsky, A.},
  Journal                  = {Cell},
  Year                     = {1987},
  Number                   = {6},
  Pages                    = {1035-1046},
  Volume                   = {48},

  Doi                      = {Doi 10.1016/0092-8674(87)90711-2},
  ISSN                     = {0092-8674},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1987G694600013}
}

@Article{fu99,
  Title                    = {Structural and functional analyses of the 26S proteasome subunits from plants},
  Author                   = {Fu, H. and Girod, P. A. and Doelling, J. H. and Van Nocker, S. and Hochstrasser, M. and Finley, D. and Vierstra, R. D.},
  Journal                  = {Mol. Biol. Rep.},
  Year                     = {1999},
  Number                   = {1-2},
  Pages                    = {137-146},
  Volume                   = {26},

  Doi                      = {Doi 10.1023/A:1006926322501},
  ISSN                     = {0301-4851},
  Keywords                 = {arabidopsis physcomitrella patens proteasome proteolysis ubiquitin yeast saccharomyces-cerevisiae proteasome moss physcomitrella-patens 20s proteasome regulatory particle protein-degradation phytochrome degradation ubiquitin system yeast resolution family},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000080186800023}
}

@Article{fu98,
  Title                    = {Multi-ubiquitin chain binding and protein degradation are mediated by distinct domains within the 26S proteasome subunit MCB1},
  Author                   = {Fu, H. and Sadis, S. and Rubin, D. M. and Glickman, M. H. and Van Nocker, S. and Finley, D. and Vierstra, R. D.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {1998},
  Number                   = {4},
  Pages                    = {1970-1981},
  Volume                   = {273},

  Doi                      = {DOI 10.1074/jbc.273.4.1970},
  ISSN                     = {0021-9258},
  Keywords                 = {saccharomyces-cerevisiae proteolytic pathway molecular-cloning shuttle vectors ubiquitin expression component complex system gene},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000071595200022}
}

@Article{fujinami94,
  Title                    = {Purification and characterization of the 26S proteasome from spinach leaves},
  Author                   = {Fujinami, K. and Tanahashi, N. and Tanaka, K. and Ichihara, A. and Cejka, Z. and Baumeister, W. and Miyawaki, M. and Sato, T. and Nakagawa, H.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {1994},
  Number                   = {41},
  Pages                    = {25905-25910},
  Volume                   = {269},

  ISSN                     = {0021-9258},
  Keywords                 = {multicatalytic proteinase complex rabbit reticulocyte lysate molecular-weight proteases ubiquitin-ligated proteins proteolytic complex dependent proteolysis electron-microscopy multiple forms higher-plant atp},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1994PQ49100097}
}

@Article{funakoshi09,
  Title                    = {Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base},
  Author                   = {Funakoshi, M. and Tomko, R. J. and Kobayashi, H. and Hochstrasser, M.},
  Journal                  = {Cell},
  Year                     = {2009},
  Number                   = {5},
  Pages                    = {887-899},
  Volume                   = {137},

  Doi                      = {DOI 10.1016/j.cell.2009.04.061},
  ISSN                     = {0092-8674},
  Keywords                 = {26 s-proteasome 20s proteasome protein-degradation atpase subunits yeast complex identification recognition destruction activation},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000266454800019}
}

@Article{ganoth88,
  Title                    = {A multi-component system that degrades proteins conjugated to ubiquitin: resolution of factors and evidence for ATP-dependent complex formation},
  Author                   = {Ganoth, D. and Leshinsky, E. and Eytan, E. and Hershko, A.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {1988},
  Number                   = {25},
  Pages                    = {12412-12419},
  Volume                   = {263},

  ISSN                     = {0021-9258},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1988P861100042}
}

@Article{glickman98,
  Title                    = {A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3},
  Author                   = {Glickman, M. H. and Rubin, D. M. and Coux, O. and Wefes, I. and Pfeifer, G. and Cjeka, Z. and Baumeister, W. and Fried, V. A. and Finley, D.},
  Journal                  = {Cell},
  Year                     = {1998},
  Number                   = {5},
  Pages                    = {615-623},
  Volume                   = {94},

  Doi                      = {Doi 10.1016/S0092-8674(00)81603-7},
  ISSN                     = {0092-8674},
  Keywords                 = {initiation-factor eif3 20s proteasome multicatalytic protease dependent proteases 20-s proteasome 11-s regulator subunits complex yeast purification},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000075851900009}
}

@Article{glickman98-c8Wsa,
  Title                    = {The regulatory particle of the Saccharomyces cerevisiae proteasome},
  Author                   = {Glickman, M. H. and Rubin, D. M. and Fried, V. A. and Finley, D.},
  Journal                  = {Mol. Cell. Biol.},
  Year                     = {1998},
  Number                   = {6},
  Pages                    = {3149-3162},
  Volume                   = {18},

  ISSN                     = {0270-7306},
  Keywords                 = {tat-mediated transactivation atp-dependent activator human 26s proteasome cdna cloning intersegmental muscles developmental-changes proteolytic pathway functional-analysis degradation signal molecular-cloning},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000073628800006}
}

@Article{glotzer91,
  Title                    = {Cyclin is degraded by the ubiquitin pathway},
  Author                   = {Glotzer, M. and Murray, A. W. and Kirschner, M. W.},
  Journal                  = {Nature},
  Year                     = {1991},
  Number                   = {6305},
  Pages                    = {132-138},
  Volume                   = {349},

  Doi                      = {Doi 10.1038/349132a0},
  ISSN                     = {0028-0836},
  Keywords                 = {recognition particle srp embryonic-cell cycle short-lived protein sea-urchin eggs messenger-rna phytochrome degradation biochemical-mutants proteolytic system conjugating enzyme activating enzyme},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1991ER41800049}
}

@Article{groll00,
  Title                    = {A gated channel into the proteasome core particle},
  Author                   = {Groll, M. and Bajorek, M. and Köhler, A. and Moroder, L. and Rubin, D. M. and Huber, R. and Glickman, M. H. and Finley, D.},
  Journal                  = {Nat. Struct. Biol.},
  Year                     = {2000},
  Number                   = {11},
  Pages                    = {1062-1067},
  Volume                   = {7},

  Doi                      = {Doi 10.1038/80992},
  ISSN                     = {1072-8368},
  Keywords                 = {active-site formation 20s proteasome regulatory particle beta-subunits yeast mechanisms resolution maturation cleavage protein},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000165110500018}
}

@Article{groll99,
  Title                    = {The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study},
  Author                   = {Groll, M. and Heinemeyer, W. and Jäger, S. and Ullrich, T. and Bochtler, M. and Wolf, D. H. and Huber, R.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {1999},
  Number                   = {20},
  Pages                    = {10976-10983},
  Volume                   = {96},

  Doi                      = {DOI 10.1073/pnas.96.20.10976},
  ISSN                     = {0027-8424},
  Keywords                 = {beta-subunits protein acidophilum resolution cleavage yeast},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000082868500010}
}

@Article{hanna06,
  Title                    = {The deubiquitinating enzyme Ubp6 functions non-catalytically to delay proteasomal degradation},
  Author                   = {Hanna, J. and Hathaway, N. A. and Tone, Y. and Crosas, B. and Elsasser, S. and Kirkpatrick, D. S. and Leggett, D. S. and Gygi, S. P. and King, R. W. and Finley, D.},
  Journal                  = {Cell},
  Year                     = {2006},
  Number                   = {1},
  Pages                    = {99-111},
  Volume                   = {127},

  Doi                      = {DOI 10.1016/j.cell.2006.07.038},
  ISSN                     = {0092-8674},
  Keywords                 = {ubiquitin-specific protease yeast inhibitors proteins depletion fidelity rpn11 usp14},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000241445800017}
}

@Article{hatfield89,
  Title                    = {Ubiquitin-dependent proteolytic pathway in wheat germ: isolation of multiple forms of the E1 ubiquitin-activating enzyme},
  Author                   = {Hatfield, P. M. and Vierstra, R. D.},
  Journal                  = {Biochemistry (Mosc.)},
  Year                     = {1989},
  Number                   = {2},
  Pages                    = {735-742},
  Volume                   = {28},

  Doi                      = {Doi 10.1021/Bi00428a048},
  ISSN                     = {0006-2960},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1989T049000048}
}

@Article{heinemeyer97,
  Title                    = {The active sites of the eukaryotic 20S proteasome and their involvement in subunit precursor processing},
  Author                   = {Heinemeyer, W. and Fischer, M. and Krimmer, T. and Stachon, U. and Wolf, D. H.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {1997},
  Number                   = {40},
  Pages                    = {25200-25209},
  Volume                   = {272},

  Doi                      = {DOI 10.1074/jbc.272.40.25200},
  ISSN                     = {0021-9258},
  Keywords                 = {multicatalytic proteinase complex peptide-hydrolyzing activity yeast proteasome thermoplasma-acidophilum saccharomyces-cerevisiae interferon-gamma multifunctional proteinase proteolytic activities antigenic peptides encoded subunits},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1997XY97000073}
}

@Article{hershko80,
  Title                    = {Proposed role of ATP in protein breakdown: conjugation of proteins with multiple chains of the polypeptide of ATP-dependent proteolysis},
  Author                   = {Hershko, A. and Ciechanover, A. and Heller, H. and Haas, A. L. and Rose, I. A.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {1980},
  Number                   = {4},
  Pages                    = {1783-1786},
  Volume                   = {77},

  Doi                      = {DOI 10.1073/pnas.77.4.1783},
  ISSN                     = {0027-8424},
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@Article{hochstrasser91,
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  Doi                      = {DOI 10.1073/pnas.88.11.4606},
  ISSN                     = {0027-8424},
  Keywords                 = {ubiquitin protein degradation saccharomyces-cerevisiae alpha-2 repressor epitope tagging saccharomyces-cerevisiae protein-degradation conjugating enzymes shuttle vectors c-myc yeast system genes},
  Type                     = {Journal Article},
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@Article{hough86,
  Title                    = {Ubiquitin-lysozyme conjugates: identification and characterization of an ATP-dependent protease from rabbit reticulocyte lysates},
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@Article{hough86-1xVPf,
  Title                    = {Ubiquitin-lysozyme conjugates: purification and susceptibility to proteolysis},
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  ISSN                     = {0021-9258},
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@Article{hua13,
  Title                    = {Epigenomic programming contributes to the genomic drift evolution of the F-Box protein superfamily in Arabidopsis},
  Author                   = {Hua, Z. and Pool, J. E. and Schmitz, R. J. and Schultz, M. D. and Shiu, S. H. and Ecker, J. R. and Vierstra, R. D.},
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  Doi                      = {DOI 10.1073/pnas.1316009110},
  ISSN                     = {0027-8424},
  Keywords                 = {ubiquitylation population genomics gene birth-and-death DNA methylation thaliana genes diversity plants rna selection patterns complex},
  Type                     = {Journal Article},
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@Article{hua11,
  Title                    = {The cullin-RING ubiquitin-protein ligases},
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  Doi                      = {DOI 10.1146/annurev-arplant-042809-112256},
  ISSN                     = {1543-5008},
  Keywords                 = {f-box protein systemic acquired-resistance recognizes sugar chains DNA-binding activity c-terminal domain skp1 gene family arabidopsis-thaliana self-incompatibility s-rnase cop9 signalosome},
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@Article{husnjak12,
  Title                    = {Ubiquitin-binding proteins: decoders of ubiquitin-mediated cellular functions},
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  Doi                      = {DOI 10.1146/annurev-biochem-051810-094654},
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  Keywords                 = {ubiquitination autophagy nf-kappa b 26s proteasome endocytosis ubiquitin receptor nf-kappa-b 63-linked polyubiquitin chains transcription factor met4 receptor down-regulation zinc-finger domain cross-link repair structural basis uba domains interacting motif proteasomal degradation},
  Type                     = {Journal Article},
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@Article{husnjak08,
  Title                    = {Proteasome subunit Rpn13 is a novel ubiquitin receptor},
  Author                   = {Husnjak, K. and Elsasser, S. and Zhang, N. and Chen, X. and Randles, L. and Shi, Y. and Hofmann, K. and Walters, K. J. and Finley, D. and Dikic, I.},
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  Doi                      = {Doi 10.1038/Nature06926},
  ISSN                     = {0028-0836},
  Keywords                 = {deubiquitinating enzyme 26s proteasome polyubiquitin chains protein interactome uba domains degradation proteolysis rad23 binds uch37},
  Type                     = {Journal Article},
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@Article{kim13,
  Title                    = {Advanced proteomic analyses yield a deep catalog of ubiquitylation targets in Arabidopsis},
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  Doi                      = {DOI 10.1105/tpc.112.108613},
  ISSN                     = {1040-4651},
  Keywords                 = {ubiquitin-proteasome system 26s proteasome phytochrome degradation sporophyte development affinity purification subcellular location nitrate reductase autophagy pathway diverse array proteins},
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@Article{kisselev05,
  Title                    = {Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates},
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  Doi                      = {Doi 10.1016/S0076-6879(05)98030-0},
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  Keywords                 = {20s proteasome hybrid proteasomes site formation core particle degradation specificity proteolysis complexes proteins channel},
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@Article{köhler01,
  Title                    = {The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release},
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  Keywords                 = {20s proteasome antigen presentation regulatory particle dependent proteases protein breakdown chaperone clpa degradation peptides mechanism yeast},
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@Article{kremp86,
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@Article{kusmierczyk08,
  Title                    = {A multimeric assembly factor controls the formation of alternative 20S proteasomes},
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  Keywords                 = {yeast saccharomyces-cerevisiae active-site formation protein-degradation 26s proteasome core particle identification completion biogenesis chaperones complexes},
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@Article{lander12,
  Title                    = {Complete subunit architecture of the proteasome regulatory particle},
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  Keywords                 = {electron-microscopy 26s proteasome saccharomyces-cerevisiae ubiquitin chains new-generation core particle degradation translocation proteins atpases},
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@Article{lasker12,
  Title                    = {Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach},
  Author                   = {Lasker, K. and Förster, F. and Bohn, S. and Walzthoeni, T. and Villa, E. and Unverdorben, P. and Beck, F. and Aebersold, R. and Sali, A. and Baumeister, W.},
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  Doi                      = {DOI 10.1073/pnas.1120559109},
  ISSN                     = {0027-8424},
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@Article{le07,
  Title                    = {20S proteasome assembly is orchestrated by two distinct pairs of chaperones in yeast and mammals},
  Author                   = {Le Tallec, B. and Barrault, M. B. and Courbeyrette, R. and Guérois, R. and Marsolier-Kergoat, M. C. and Peyroche, A.},
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  Doi                      = {DOI 10.1016/j.molcel.2007.06.025},
  ISSN                     = {1097-2765},
  Keywords                 = {active-site formation DNA-damage response saccharomyces-cerevisiae precursor complexes 26s proteasome beta-subunits s proteasome maturation biogenesis checkpoint},
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@Article{leggett05,
  Title                    = {Purification of proteasomes, proteasome sub-complexes, and proteasome-associated proteins from budding yeast},
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  Doi                      = {10.1385/1-59259-895-1:057},
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  Keywords                 = {Chromatography, Affinity/methods Proteasome Endopeptidase Complex/*chemistry/*isolation \& purification Saccharomyces cerevisiae/*enzymology},
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@Article{leggett02,
  Title                    = {Multiple associated proteins regulate proteasome structure and function},
  Author                   = {Leggett, D. S. and Hanna, J. and Borodovsky, A. and Crosas, B. and Schmidt, M. and Baker, R. T. and Walz, T. and Ploegh, H. L. and Finley, D.},
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  ISSN                     = {1097-2765},
  Keywords                 = {doa4 deubiquitinating enzyme 26s proteasome saccharomyces-cerevisiae core particle ubiquitin yeast identification pathway complex domain},
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@Article{lehmann10,
  Title                    = {Ecm29 fulfils quality control functions in proteasome assembly},
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  Doi                      = {DOI 10.1016/j.molcel.2010.06.016},
  ISSN                     = {1097-2765},
  Keywords                 = {20s proteasome 26s proteasome core particle protein-degradation yeast maturation subunit completion biogenesis chaperones},
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@Article{lin11,
  Title                    = {The defective proteasome, not substrate recognition function, is responsible for the null phenotypes of the Arabidopsis proteasome subunit RPN10},
  Author                   = {Lin, Y. L. and Sung, S. C. and Tsai, H. L. and Yu, T. T. and Radjacommare, R. and Usharani, R. and Fatimababy, A. S. and Lin, H. Y. and Wang, Y. Y. and Fu, H.},
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  Year                     = {2011},
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  Doi                      = {DOI 10.1105/tpc.111.086702},
  ISSN                     = {1040-4651},
  Keywords                 = {lys48-linked polyubiquitin chain ubiquitin-binding proteins 26s proteasome regulatory particle gametophyte development degradation signal transgenic plants uba domain aaa-atpase pathway},
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@Article{malik04,
  Title                    = {The 26S proteasome in garlic (Allium sativum): purification and partial characterization},
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  Doi                      = {DOI 10.1021/jf035309r},
  ISSN                     = {0021-8561},
  Keywords                 = {allium sativum multicatalytic protease prosome purification molecular cloning mass fingerprint analysis polymerase chain reaction calf brain rat-liver proteins complex degradation ubiquitin proteolysis apoptosis pituitary pathway},
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@Article{murray97,
  Title                    = {Purification and characterization of the 20S proteasome from wheat leaves},
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  Volume                   = {125},

  ISSN                     = {0168-9452},
  Keywords                 = {multicatalytic proteinase 20 s proteasome proteolysis wheat leaves protein-degradation proteolytic pathway ubiquitin subunit acidophilum resolution expression yeast cell},
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@Article{nelson14,
  Title                    = {Quantitative analysis of protein turnover in plants},
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  Doi                      = {DOI 10.1002/pmic.201300240},
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@Article{ozaki92,
  Title                    = {Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea},
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  Keywords                 = {multicatalytic proteinase complex molecular-weight proteases sodium dodecyl-sulfate mammalian-cells rat-liver eukaryotic cells ubiquitin subunits degradation involvement},
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@Article{paraskevopoulos14,
  Title                    = {Dss1 is a 26S proteasome ubiquitin receptor},
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  Doi                      = {DOI 10.1016/j.molcel.2014.09.008},
  ISSN                     = {1097-2765},
  Keywords                 = {regulatory particle binding proteins fission yeast degradation subunit complex domain sem1 localization recognition},
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@Article{pathare12,
  Title                    = {The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory sub-complexes together},
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  ISSN                     = {0027-8424},
  Keywords                 = {26s proteasome cryoelectron microscopy psmd11 s9 pci domain 26s proteasome saccharomyces-cerevisiae 20s proteasome angstrom resolution functional-analysis crystal-structure complex particle proteins eif3},
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@Article{peters91,
  Title                    = {Ultrastructure of the approximately 26S complex containing the approximately 20S cylinder particle (multi-catalytic proteinase/proteasome)},
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  Keywords                 = {approximately 20s cylinder particle multicatalytic proteinase proteasome approximately 26s ubiquitin-dependent protease molecular-weight proteases mammalian-cells xenopus-laevis shaped miniparticles cultured-cells ubiquitin prosome purification drosophila yeast},
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@Article{rabl08,
  Title                    = {Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases},
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  Keywords                 = {activator reg-alpha substrate entry core particle identification resolution pan purification acidophilum regulator channel},
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@Article{ramos98,
  Title                    = {Ump1p is required for proper maturation of the 20S proteasome and becomes its substrate upon completion of the assembly},
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  Doi                      = {Doi 10.1016/S0092-8674(00)80942-3},
  ISSN                     = {0092-8674},
  Keywords                 = {n-end rule yeast saccharomyces-cerevisiae protein-degradation shuttle vectors ubiquitin pathway subunit enzyme gene construction},
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@Article{roelofs09,
  Title                    = {Chaperone-mediated pathway of proteasome regulatory particle assembly},
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  Doi                      = {DOI 10.1038/nature08063},
  ISSN                     = {0028-0836},
  Keywords                 = {yeast 26s proteasome 20s proteasomes s proteasome complex proteins subunits atpase transcription oncoprotein substrate},
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@Article{ruschak10,
  Title                    = {The proteasome antechamber maintains substrates in an unfolded state},
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  Journal                  = {Nature},
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  ISSN                     = {0028-0836},
  Keywords                 = {side-chain dynamics 20s proteasome nmr-spectroscopy folding pathway methyl-groups beta-sheet ww domain relaxation protein mechanism},
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@Article{russell13,
  Title                    = {Characterization and quantification of intact 26S proteasome proteins by real-time measurement of intrinsic fluorescence prior to top-down mass spectrometry},
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  ISSN                     = {1932-6203 (Electronic) 1932-6203 (Linking)},
  Keywords                 = {Amino Acid Sequence Arabidopsis/chemistry Arabidopsis Proteins/analysis/chemistry Carrier Proteins/analysis/chemistry Fluorescence *Mass Spectrometry/methods Proteasome Endopeptidase Complex/analysis/*chemistry Proteins/analysis/*chemistry Reproducibility of Results Tandem Mass Spectrometry},
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@Article{sadre-bazzaz10,
  Title                    = {Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening},
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  ISSN                     = {1097-2765},
  Keywords                 = {20s proteasome angstrom resolution activator pa200 s-proteasome yeast conformation acidophilum atpases subunit termini},
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@Article{saeki09,
  Title                    = {Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle},
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  Journal                  = {Cell},
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  Volume                   = {137},

  Doi                      = {DOI 10.1016/j.cell.2009.05.005},
  ISSN                     = {0092-8674},
  Keywords                 = {26 s-proteasome saccharomyces-cerevisiae ubiquitin system 20s proteasomes cdna cloning hsm3 gene gankyrin degradation subunits atpases},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000266454800020}
}

@Article{sakata12,
  Title                    = {Localization of the proteasomal ubiquitin receptors Rpn10 and Rpn13 by electron cryo-microscopy},
  Author                   = {Sakata, E. and Bohn, S. and Mihalache, O. and Kiss, P. and Beck, F. and Nagy, I. and Nickell, S. and Tanaka, K. and Saeki, Y. and Förster, F. and Baumeister, W.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {2012},
  Number                   = {5},
  Pages                    = {1479-1484},
  Volume                   = {109},

  Doi                      = {DOI 10.1073/pnas.1119394109},
  ISSN                     = {0027-8424},
  Keywords                 = {em single-particle analysis protein degradation ubiquitin-proteasome pathway subunit localization quantitative mass spectrometry 26s proteasome regulatory particle methanocaldococcus-jannaschii deubiquitinating enzyme polyubiquitin chains binding protein uba domains subunit complex identification},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000299731400034}
}

@Article{sakata11,
  Title                    = {The catalytic activity of Ubp6 enhances maturation of the proteasomal regulatory particle},
  Author                   = {Sakata, E. and Stengel, F. and Fukunaga, K. and Zhou, M. and Saeki, Y. and Förster, F. and Baumeister, W. and Tanaka, K. and Robinson, C. V.},
  Journal                  = {Mol. Cell},
  Year                     = {2011},
  Number                   = {5},
  Pages                    = {637-649},
  Volume                   = {42},

  Doi                      = {DOI 10.1016/j.molcel.2011.04.021},
  ISSN                     = {1097-2765},
  Keywords                 = {human 26s proteasome mass-spectrometry protein complexes macromolecular assemblies subunit architecture 20s proteasome pathway identification binding destruction},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000291670600012}
}

@Article{schliephacke91,
  Title                    = {Prosomes (proteasomes) of higher plants},
  Author                   = {Schliephacke, M. and Kremp, A. and Schmid, H. P. and Köhler, K. and Kull, U.},
  Journal                  = {Eur. J. Cell Biol.},
  Year                     = {1991},
  Number                   = {1},
  Pages                    = {114-121},
  Volume                   = {55},

  ISSN                     = {0171-9335},
  Keywords                 = {prosomes proteasomes multicatalytic protease serological relationship glycoproteins multicatalytic proteinase cylinder particles mammalian-cells skeletal-muscle xenopus-laevis drosophila complex rna glycosylation purification},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1991FU93800011}
}

@Article{schmid84,
  Title                    = {The prosome: a ubiquitous morphologically distinct RNP particle associated with repressed mRNPs and containing specific scRNA and a characteristic set of proteins},
  Author                   = {Schmid, H. P. and Akhayat, O. and Martins, C. and Puvion, F. and Köhler, K. and Scherrer, K.},
  Journal                  = {EMBO J.},
  Year                     = {1984},
  Number                   = {1},
  Pages                    = {29-34},
  Volume                   = {3},

  ISSN                     = {0261-4189},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1984RZ48900005}
}

@Article{schmidt05,
  Title                    = {The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle},
  Author                   = {Schmidt, M. and Haas, W. and Crosas, B. and Santamaria, P. G. and Gygi, S. P. and Walz, T. and Finley, D.},
  Journal                  = {Nature Structural \& Molecular Biology},
  Year                     = {2005},
  Number                   = {4},
  Pages                    = {294-303},
  Volume                   = {12},

  Doi                      = {DOI 10.1038/nsmb914},
  ISSN                     = {1545-9985},
  Keywords                 = {saccharomyces-cerevisiae 26s proteasome hybrid proteasomes gene disruption 20s proteasomes activator pa28 degradation ubiquitin complex expression},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000228126200009}
}

@Article{schreiner08,
  Title                    = {Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction},
  Author                   = {Schreiner, P. and Chen, X. and Husnjak, K. and Randles, L. and Zhang, N. and Elsasser, S. and Finley, D. and Dikic, I. and Walters, K. J. and Groll, M.},
  Journal                  = {Nature},
  Year                     = {2008},
  Number                   = {7194},
  Pages                    = {548-552},
  Volume                   = {453},

  Doi                      = {Doi 10.1038/Nature06924},
  ISSN                     = {0028-0836},
  Keywords                 = {deubiquitinating enzyme structural basis multiubiquitin chain protein interactome eap45-glue domain recognition degradation complex binding subunit},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000256023700048}
}

@Article{shanklin87,
  Title                    = {Red light-induced formation of ubiquitin-phytochrome conjugates: identification of possible intermediates of phytochrome degradation},
  Author                   = {Shanklin, J. and Jabben, M. and Vierstra, R. D.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {1987},
  Number                   = {2},
  Pages                    = {359-363},
  Volume                   = {84},

  Doi                      = {DOI 10.1073/pnas.84.2.359},
  ISSN                     = {0027-8424},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1987F689000009}
}

@Article{skoda92,
  Title                    = {Dry pea seed proteasome: purification and enzymatic activities},
  Author                   = {Skoda, B. and Malek, L.},
  Journal                  = {Plant Physiol.},
  Year                     = {1992},
  Number                   = {4},
  Pages                    = {1515-1519},
  Volume                   = {99},

  Doi                      = {Doi 10.1104/Pp.99.4.1515},
  ISSN                     = {0032-0889},
  Keywords                 = {heat-shock multicatalytic proteinase ubiquitin complex yeast chlamydomonas degradation temperature drosophila particles},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1992JK72300039}
}

@Article{smalle04,
  Title                    = {The ubiquitin-26S proteasome proteolytic pathway},
  Author                   = {Smalle, J. A. and Vierstra, R. D.},
  Journal                  = {Annu. Rev. Plant Biol.},
  Year                     = {2004},
  Pages                    = {555-590},
  Volume                   = {55},

  Doi                      = {DOI 10.1146/annurev.arplant.55.031903.141801},
  ISSN                     = {1040-2519},
  Keywords                 = {proteolysis arabidopsis cell regulation polypeptide tags f-box protein n-end rule multiubiquitin chain binding anaphase-promoting complex plant-cell cycle arabidopsis-thaliana cop9 signalosome regulatory particle 20s proteasome disease resistance},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000222766000022}
}

@Article{smith05,
  Title                    = {ATP binding to PAN or the 26S ATPases causes association with the 20S proteasome, gate opening, and translocation of unfolded proteins},
  Author                   = {Smith, D. M. and Kafri, G. and Cheng, Y. and Ng, D. and Walz, T. and Goldberg, A. L.},
  Journal                  = {Mol. Cell},
  Year                     = {2005},
  Number                   = {5},
  Pages                    = {687-698},
  Volume                   = {20},

  Doi                      = {DOI 10.1016/j.molcel.2005.10.019},
  ISSN                     = {1097-2765},
  Keywords                 = {regulatory particle escherichia-coli core particle proteolytic activity degradation complex hydrolysis ubiquitin ratchet site},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000234033400007}
}

@Article{tomko13,
  Title                    = {Molecular architecture and assembly of the eukaryotic proteasome},
  Author                   = {Tomko, R. J. and Hochstrasser, M.},
  Journal                  = {Annu. Rev. Biochem.},
  Year                     = {2013},
  Pages                    = {415-445},
  Volume                   = {82},

  Doi                      = {DOI 10.1146/annurev-biochem-060410-150257},
  ISSN                     = {0066-4154},
  Keywords                 = {proteasome ubiquitin assembly atpase deubiquitylation proteolysis yeast 26s proteasome 19s regulatory particle mammalian 20s proteasomes 2.75 angstrom resolution s-proteasome saccharomyces-cerevisiae core particle structural basis methanocaldococcus-jannaschii precursor complexes},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000321698100015}
}

@Article{unverdorben14,
  Title                    = {Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome},
  Author                   = {Unverdorben, P. and Beck, F. and Śledź, P. and Schweitzer, A. and Pfeifer, G. and Plitzko, J. M. and Baumeister, W. and Förster, F.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {2014},
  Number                   = {15},
  Pages                    = {5544-5549},
  Volume                   = {111},

  Doi                      = {DOI 10.1073/pnas.1403409111},
  ISSN                     = {0027-8424},
  Keywords                 = {conformational switching proteolysis proteostasis quality control atp-fueled machines regulatory particle molecular architecture crystal-structure 20s proteasome s proteasome resolution translocation degradation insights},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000334288600036}
}

@Article{van96,
  Title                    = {The Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome},
  Author                   = {Van Nocker, S. and Deveraux, Q. and Rechsteiner, M. and Vierstra, R. D.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {1996},
  Number                   = {2},
  Pages                    = {856-860},
  Volume                   = {93},

  Doi                      = {DOI 10.1073/pnas.93.2.856},
  ISSN                     = {0027-8424},
  Keywords                 = {protein degradation proteolysis inhibitor protein interaction human multiubiquitin chain carrier protein invivo degradation lysine-48 pathway},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1996TR32600062}
}

@Article{verma02,
  Title                    = {Role of the Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome},
  Author                   = {Verma, R. and Aravind, L. and Oania, R. and McDonald, W. H. and Yates, J. R. and Koonin, E. V. and Deshaies, R. J.},
  Journal                  = {Science},
  Year                     = {2002},
  Number                   = {5593},
  Pages                    = {611-615},
  Volume                   = {298},

  Doi                      = {DOI 10.1126/science.1075898},
  ISSN                     = {0036-8075},
  Keywords                 = {s-phase ubiquitin yeast gene signal transcription proteolysis recognition activation particle},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000178634800044}
}

@Article{vierstra09,
  Title                    = {The ubiquitin-26S proteasome system at the nexus of plant biology},
  Author                   = {Vierstra, R. D.},
  Journal                  = {Nat. Rev. Mol. Cell Biol.},
  Year                     = {2009},
  Number                   = {6},
  Pages                    = {385-397},
  Volume                   = {10},

  Doi                      = {Doi 10.1038/Nrm2688},
  ISSN                     = {1471-0072},
  Keywords                 = {f-box proteins 26s proteasome arabidopsis-thaliana gene family self-incompatibility auxin receptor ethylene biosynthesis gibberellin receptor rapid degradation cop9 signalosome},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000266270900013}
}

@Article{vierstra93,
  Title                    = {Protein degradation in plants},
  Author                   = {Vierstra, R. D.},
  Journal                  = {Annual Review of Plant Physiology and Plant Molecular Biology},
  Year                     = {1993},
  Pages                    = {385-410},
  Volume                   = {44},

  Doi                      = {DOI 10.1146/annurev.arplant.44.1.385},
  ISSN                     = {0066-4294},
  Keywords                 = {proteolysis ubiquitin arabidopsis cell regulation biotechnology ubiquitin-activating enzyme n-end rule cycle mutant ts85 saccharomyces-cerevisiae abnormal proteins escherichia-coli arabidopsis-thaliana polyubiquitin gene conjugating enzyme pea-chloroplasts},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1993LE09000017}
}

@Article{vierstra88,
  Title                    = {Hemin inhibits ubiquitin-dependent proteolysis in both a higher plant and yeast},
  Author                   = {Vierstra, R. D. and Sullivan, M. L.},
  Journal                  = {Biochemistry (Mosc.)},
  Year                     = {1988},
  Number                   = {9},
  Pages                    = {3290-3295},
  Volume                   = {27},

  Doi                      = {Doi 10.1021/Bi00409a025},
  ISSN                     = {0006-2960},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1988N345400025}
}

@Article{waxman87,
  Title                    = {Demonstration of two distinct high molecular weight proteases in rabbit reticulocytes, one of which degrades ubiquitin conjugates},
  Author                   = {Waxman, L. and Fagan, J. M. and Goldberg, A. L.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {1987},
  Number                   = {6},
  Pages                    = {2451-2457},
  Volume                   = {262},

  ISSN                     = {0021-9258},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1987G187400005}
}

@Article{weberruss13,
  Title                    = {Blm10 facilitates nuclear import of proteasome core particles},
  Author                   = {Weberruss, M. H. and Savulescu, A. F. and Jando, J. and Bissinger, T. and Harel, A. and Glickman, M. H. and Enenkel, C.},
  Journal                  = {EMBO J.},
  Year                     = {2013},
  Number                   = {20},
  Pages                    = {2697-2707},
  Volume                   = {32},

  Doi                      = {DOI 10.1038/emboj.2013.192},
  ISSN                     = {0261-4189},
  Keywords                 = {blm10 nuclear import proteasome activator protein aggregation quiescence thermoplasma 20s proteasomes heat-repeat protein nucleocytoplasmic transport saccharomyces-cerevisiae angstrom resolution 26s proteasome pore complex yeast beta activator},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000325714100006}
}

@Article{wilkinson80,
  Title                    = {Ubiquitin is the ATP-dependent proteolysis factor I of rabbit reticulocytes},
  Author                   = {Wilkinson, K. D. and Urban, M. K. and Haas, A. L.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {1980},
  Number                   = {16},
  Pages                    = {7529-7532},
  Volume                   = {255},

  ISSN                     = {0021-9258},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1980KF60600008}
}

@Article{woffenden98,
  Title                    = {Proteasome inhibitors prevent tracheary element differentiation in Zinnia mesophyll cell cultures},
  Author                   = {Woffenden, B. J. and Freeman, T. B. and Beers, E. P.},
  Journal                  = {Plant Physiol.},
  Year                     = {1998},
  Number                   = {2},
  Pages                    = {419-429},
  Volume                   = {118},

  Doi                      = {Doi 10.1104/Pp.118.2.419},
  ISSN                     = {0032-0889},
  Keywords                 = {suspension-cultures ubiquitin pathway elegans l in-vitro death protein degradation activation plant induction},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000076403300009}
}

@Article{worden14,
  Title                    = {Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation},
  Author                   = {Worden, E. J. and Padovani, C. and Martin, A.},
  Journal                  = {Nature Structural \& Molecular Biology},
  Year                     = {2014},
  Number                   = {3},
  Pages                    = {220-227},
  Volume                   = {21},

  Doi                      = {DOI 10.1038/nsmb.2771},
  ISSN                     = {1545-9993},
  Keywords                 = {26s proteasome regulatory particle functional asymmetries polyubiquitin recognition domain resolution complexes proteins subunit},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000332594900003}
}

@Article{xie00,
  Title                    = {Physical association of ubiqutin ligases and the 26S proteasome},
  Author                   = {Xie, Y. and Varshavsky, A.},
  Journal                  = {Proc. Natl. Acad. Sci. U. S. A.},
  Year                     = {2000},
  Number                   = {6},
  Pages                    = {2497-2502},
  Volume                   = {97},

  Doi                      = {DOI 10.1073/pnas.060025497},
  ISSN                     = {0027-8424},
  Keywords                 = {e3 n-end rule ubiquitin fusion degradation pathway ubr1p ufd4p n-end rule saccharomyces-cerevisiae proteasome regulatory particle multiubiquitin-chain degradation signal ubiquitin pathway protein component},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000085941400019}
}

@Article{yanagawa99,
  Title                    = {Purification and characterization of the 26S proteasome from cultured rice (Oryza sativa) cells},
  Author                   = {Yanagawa, Y. and Ohhashi, A. and Murakami, Y. and Saeki, Y. and Yokosawa, H. and Tanaka, K. and Hashimoto, J. and Sato, T. and Nakagawa, H.},
  Journal                  = {Plant Science},
  Year                     = {1999},
  Number                   = {1},
  Pages                    = {33-41},
  Volume                   = {149},

  Doi                      = {Doi 10.1016/S0168-9452(99)00140-5},
  ISSN                     = {0168-9452},
  Keywords                 = {26s proteasome 20s proteasome rice (oryza sativa l.) tat-binding protein ornithine decarboxylase arabidopsis-thaliana molecular characterization regulatory particle spinacia-oleracea ubiquitin system 26-s proteasome gene family alpha-type},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000083652500004}
}

@Article{yang04,
  Title                    = {Purification of the Arabidopsis 26S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms},
  Author                   = {Yang, P. and Fu, H. and Walker, J. M. and Papa, C. M. and Smalle, J. and Ju, Y. M. and Vierstra, R. D.},
  Journal                  = {J. Biol. Chem.},
  Year                     = {2004},
  Number                   = {8},
  Pages                    = {6401-6413},
  Volume                   = {279},

  Doi                      = {DOI 10.1074/jbc.M311977200},
  ISSN                     = {0021-9258},
  Keywords                 = {regulatory particle subunits multiubiquitin-chain-binding rabbit reticulocyte lysate yeast 26s proteasome saccharomyces-cerevisiae 20s proteasome cell-cycle functional-characterization deubiquitinating enzyme dependent proteolysis},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:000188969200026}
}

@Article{yoshimura93,
  Title                    = {Molecular characterization of the 26S proteasome complex from rat liver},
  Author                   = {Yoshimura, T. and Kameyama, K. and Takagi, T. and Ikai, A. and Tokunaga, F. and Koide, T. and Tanahashi, N. and Tamura, T. and Cejka, Z. and Baumeister, W. and Tanaka, K. and Ichihara, A.},
  Journal                  = {J. Struct. Biol.},
  Year                     = {1993},
  Number                   = {3},
  Pages                    = {200-211},
  Volume                   = {111},

  Doi                      = {DOI 10.1006/jsbi.1993.1050},
  ISSN                     = {1047-8477},
  Keywords                 = {rabbit reticulocyte lysate n-end rule multicatalytic proteinase cdna cloning hepatoma-cells multifunctional proteinase thermoplasma-acidophilum proteolytic complex dependent proteases weight proteases},
  Type                     = {Journal Article},
  Url                      = {<Go to ISI>://WOS:A1993NG94800004}
}

repository: dcgemperline/withesis

repo_name: dcgemperline/withesis


text:
PV = "0.0+cvs${SRCDATE}"
PR = "r1"
SECTION = "libs"
DEPENDS = "renderext virtual/libx11"
DESCRIPTION = "X Render extension library."
LICENSE = "BSD"

SRC_URI = "${FREEDESKTOP_CVS}/xlibs;module=Xrender"
S = "${WORKDIR}/Xrender"

inherit autotools pkgconfig

do_stage() {
	autotools_stage_all
}

license: MIT

license_type: permissive

branch_name: refs/heads/master

extension: bb


text:
---
---

@INPROCEEDINGS{8591018,
  author={K. {Fertakis} and S. {Gerangelos} and G. {Goumas} and N. {Koziris}},
  booktitle={2018 IEEE International Conference on Cloud Computing Technology and Science (CloudCom)},
  title={RACCEX: Towards Remote Accelerated Computing Environments},
  year={2018},
  volume={},
  number={},
  pages={212-217},}

repository: kfertakis/personalWebpage

repo_name: kfertakis/personalWebpage

extension: bib


text:
PR = "r0"

inherit debian-package allarch

SUMMARY = "Debian configuration management system"
DESCRIPTION = "\
 Debconf is a configuration management system for debian packages. Packages\
 use Debconf to ask questions when they are installed.\
"
LICENSE = "BSD-2-Clause"
SECTION = "admin"
LIC_FILES_CHKSUM = "file://debian/copyright;md5=1aa3b78d3182195ba56c01cb7227ead3"

DEBIAN_PATCH_TYPE = "nopatch"

do_configure() {
	:
}

do_compile() {
	:
}

do_install() {
	prefix="${D}" oe_runmake install-utils
	prefix="${D}" oe_runmake install-rest
}

PACKAGES =+ "${PN}-utils"
FILES_${PN}-utils = " \
${bindir}/debconf-get-selections \
${bindir}/debconf-getlang \
${bindir}/debconf-loadtemplate \
${bindir}/debconf-mergetemplate \
"
FILES_${PN} += "${datadir} ${libdir}"

repository: nghiaht-tsdv/meta-debian

repo_name: nghiaht-tsdv/meta-debian

branch_name: refs/heads/jethro

gha_language: BitBake


text:
@article{Ladino2017:TR-C,
  author    = {Ladino, Andres and Kibangou, A. Y. and {Canudas de Wit}, C. and Fourati, H.},
  doi       = {10.1016/j.trc.2017.05.002},
  issn      = {0968090X},
  journal   = {Transportation Research Part C: Emerging Technologies},
  keywords  = {Clustering,Kalman filter,Sensor fusion,Traffic forecasting,Travel time forecasting},
  pages     = {216--238},
  publisher = {Elsevier Ltd},
  title     = {{A real time forecasting tool for dynamic travel time from clustered time series}},
  url       = {http://dx.doi.org/10.1016/j.trc.2017.05.002},
  volume    = {80},
  year      = {2017}
}

repository: aladinoster/al-website

repo_name: aladinoster/al-website

gha_license_id: MIT

gha_language: Jupyter Notebook


text:
DESCRIPTION = "Panel plugin displaying instant disk/partition performance"
HOMEPAGE = "http://goodies.xfce.org/projects/panel-plugins/xfce4-diskperf-plugin"
LICENSE = "RogerSeguin"
LIC_FILES_CHKSUM = "file://COPYING;md5=d3e627798d6a60bece47aa8b3532e1f1"

inherit xfce-panel-plugin

SRC_URI[md5sum] = "2db453fc3ea2e4fe073ec313a25b0961"
SRC_URI[sha256sum] = "aab6b9c4e2f78620920efac6874c4edf426f05b63b94cfda0da8c99a91110a0b"

repository: ExorEmbedded/exor-workspace

repo_name: ExorEmbedded/exor-workspace

gha_language: Python


text:
require ${BPN}.inc

inherit cmake-lib

DEPENDS += "${BPN}-native karchive ki18n kcoreaddons kconfig kdoctools"

# cross libs / headers
CMAKE_ALIGN_SYSROOT[1] = "KF5Package, -S${libdir}/lib, -S${STAGING_LIBDIR}/lib"
CMAKE_ALIGN_SYSROOT[2] = "KF5Package, -S${includedir}, -S${STAGING_INCDIR}"
CMAKE_ALIGN_SYSROOT[3] = "KF5Package, -S${bindir}, -S${STAGING_BINDIR_NATIVE}"

FILES_${PN} += "${datadir}/k*5"


text:
@article{barron2010deteccion,
 author = {Barrón-Cedeño, Alberto and Vila, Marta and Rosso, Paolo},
 journal = {Panorama actual de la lingüística forense en el ámbito legal y policial: Teoría y práctica. Jornadas (in) formativas de lingüística forense},
 pages = {76--96},
 publisher = {Euphonia Ediciones SL Madrid},
 title = {Detección automática de plagio: de la copia exacta a la paráfrasis},
 year = {2010}
}

repository: albarron/academic-kickstart

repo_name: albarron/academic-kickstart


text:
/* Global */

html {
	height: 100%;
	min-height: 500px;
}
body {
  height: 100%;
  width: auto;
  background-color: #727272;
  overflow-x: hidden;
}
body, html {
    margin: 0;
    padding: 0;
    height: 100%;
    width: 100%;
}
h2,
h3
 {
   font-family: "Helvetica Neue", Helvetica , arial, sans-serif;
     font-weight: 900;
  font-style: normal;
  letter-spacing: 3px;
  margin-top: 0;
  margin-bottom: 0;

}
h4 {
    font-family: "Helvetica Neue", Helvetica , arial, sans-serif;
    font-weight: 100;
    font-size: 4.3rem;
  letter-spacing: 3.4px;
  font-weight: 100;
   font-size: 1.7rem;
   margin-top: 0;
   margin-bottom: 0;
}

h1 {
    font-family: "Helvetica Neue", Helvetica , arial, sans-serif;
font-weight: 100;
    font-size: 4.3rem;
  letter-spacing: 3.4px;
  font-weight: 100;
  line-height: 43px;
  margin-top: 0;
  margin-bottom: 0;
}
h2 {
  padding-top: 20px;
  font-size: 23px;
}
h3 {
    font-family: "Helvetica Neue", Helvetica , arial, sans-serif;

    font-weight: 900;
  	font-size: 23px;
  	padding-top: 20px;
}
a {
	color: #ffffff;
	cursor: pointer;
}
ul{
	list-style: none;
	padding-left: 0;
}
#main {
	display: block;
}
section {
	/*position: static;
	width: 100%;
	max-height: 100%;
	overflow-x: hidden;*/
}
button {
	padding: 10px 27px 10px;
	border-radius: 2.02px;
	height: auto;
	width: auto;
	font-size: 16px;
    letter-spacing: 2.5px;
    font-family: "Helvetica Neue", Helvetica , arial, sans-serif;
    font-weight: 900;
    color: #ffffff;
}
/* Modal Close Override */
.close {
    opacity: 1.0;
}

.btn-call2 {
    font-size: 9px;
    font-weight: 400;
    margin-top: 41px;
    background-color: #4caf50;
    border-radius: 3px;
    border: none;
    padding-top: 7px;
    padding-bottom: 7px;
    min-width: 187px;
}
.btn-call2:nth-child(2){
    border:solid 1px #4caf50;
    background-color: transparent;
    color: #4caf50;
}
.out {
	font-family: 'Open Sans', sans-serif;
	border: solid 1px #ffcd29;
	background: transparent;
	color: #fff;
}
.out:hover {
	color: #414042;
	background: #ffcd29;
}
@media (max-width: 650px){
	h1{
		font-size: 24px;
		line-height: 22px;
	}
	h2 {
		font-size: 16px;
	}
	h3 {
		font-size: 23px;
	}
}

/* Main Globals */
.greenMe {
	    width: 100%;
		background : -moz-linear-gradient(50% 100% 90deg,rgba(76, 175, 80, 1) 0%,rgba(112, 191, 115, 1) 51.58%,rgba(76, 175, 80, 1) 100%);
	    background : -webkit-linear-gradient(90deg, rgba(76, 175, 80, 1) 0%, rgba(112, 191, 115, 1) 51.58%, rgba(76, 175, 80, 1) 100%);
	    background : -webkit-gradient(linear,50% 100% ,50% 0% ,color-stop(0,rgba(76, 175, 80, 1) ),color-stop(0.5158,rgba(112, 191, 115, 1) ),color-stop(1,rgba(76, 175, 80, 1) ));
	    background : -o-linear-gradient(90deg, rgba(76, 175, 80, 1) 0%, rgba(112, 191, 115, 1) 51.58%, rgba(76, 175, 80, 1) 100%);
	    background : -ms-linear-gradient(90deg, rgba(76, 175, 80, 1) 0%, rgba(112, 191, 115, 1) 51.58%, rgba(76, 175, 80, 1) 100%);
	    -ms-filter: "progid:DXImageTransform.Microsoft.gradient(startColorstr='#4CAF50', endColorstr='#4CAF50' ,GradientType=0)";
	    background : linear-gradient(0deg, rgba(76, 175, 80, 1) 0%, rgba(112, 191, 115, 1) 51.58%, rgba(76, 175, 80, 1) 100%);
	    border-style : Solid;
	    border-color : #727272;
	    border-color : rgba(114, 114, 114, 1);
	    border-width : 1px;
		-webkit-box-shadow: 0px 1px 7.3px rgba(70, 70, 70, 0.86);
	  	-moz-box-shadow: 0px 1px 7.3px rgba(70, 70, 70, 0.86);
		box-shadow: 0px 1px 7.3px rgba(70, 70, 70, 0.86);
		z-index: 1000;
	    filter: progid:DXImageTransform.Microsoft.dropshadow(OffX=0, OffY=-2, Color='#333333') progid:DXImageTransform.Microsoft.gradient(startColorstr='#4CAF50',endColorstr='#4CAF50' , GradientType=0);
		color: #ffffff;

}
 .white{
	display: block;
	color: #414042;
	background-color: #f2f2f2;
}
.white h1 {
}
.white p {
	color: #58595b;
}
button.gold {
	padding: 6px 11px 5px;
	color: #ffffff;
	border: none;
	background-color: #eead4c;
    -webkit-box-shadow : 0px 1px 1px rgba(70, 70, 70, 0.65);
    -moz-box-shadow : 0px 1px 1px rgba(70, 70, 70, 0.65);
    box-shadow : 0px 1px 1px rgba(70, 70, 70, 0.65);
    filter: progid:DXImageTransform.Microsoft.dropshadow(OffX=0, OffY=1, Color='#464646');
}
.innerCont {
}
.btn-exp {
    font-weight: 400;
    min-width: 254px;
    background-color: #4caf50;
    border-radius: 3px;
    border: none;
    font-size: 16px;
    color: #ffffff;
}
.btn-exp:hover {
    -webkit-transition: all 1s ease;
    -moz-transition: all 1s ease;
    -o-transition: all 1s ease;
    transition: all 1s ease;

    background-color: #4caf50;
    color: #ffffff;
    border: none;
    -webkit-box-shadow: 0px 1px 40.3px rgba(70, 70, 70, 0.86);
  	-moz-box-shadow: 0px 1px 40.3px rgba(70, 70, 70, 0.86);
	box-shadow: 0px 1px 40.3px rgba(70, 70, 70, 0.86);
}
#exp .btn-exp {
    margin-top: 41px;
}
.squeeze {
	position: relative;
}
.squeeze h1 {
	width: 167px;
	position: absolute;
	margin-left: auto;
	margin-right: auto;
	left: 0;
	right: 0;
	top: 100px;
}
/* End of Main Globals */
/* Main Nav */
form input {
	border: none;
}
form textarea {
	border: solid 1px #5c5c5c;
	background: transparent;
}

#logo {
	position: absolute;
	top: 100px;
	width: 80%;
	height: auto;
}
#logo img {
	width: 500px;
	height: auto;
}
#logo h2 {
	position: relative;
	font-size: 14px;
	margin-top: 0;
	margin-left: 4px;
}

#content-wrapper {

  height: 100%;
  min-height: 500px;
  width: 100%;
  overflow-x: hidden;
  padding-left: 0;
  -webkit-transition: all 0.5s ease;
  -moz-transition: all 0.5s ease;
  -o-transition: all 0.5s ease;
  transition: all 0.5s ease;
}

#content-wrapper.toggled {
}

#content-wrapper.toggled #sidebar-wrapper {
    width: 250px;
}

#sidebar-wrapper {
	border-left: solid 1px #cccccc;
	z-index: 1004;
    position: fixed;
    right: -250px;
    width: 0;
    height: 100%;
    margin-right: -250px;
    overflow-y: auto;
	background-color:#f2f2f2;
    -webkit-transition: all 0.5s ease;
    -moz-transition: all 0.5s ease;
    -o-transition: all 0.5s ease;
    transition: all 0.5s ease;
	-webkit-box-shadow :  -1.5px 0px 1.5px rgba(70, 70, 70, 0.8);
  	-moz-box-shadow :  -1.5px 0px 1.5px rgba(70, 70, 70, 0.8);
	box-shadow : -1.5px 0px 1.5px rgba(70, 70, 70, 0.8);
}
#sidebar-wrapper a{
    color: #020202;
}
#menu-toggle {
    display: none;
}

#menu-toggle {
	position: fixed;
	right: 33px;
	top: 33px;
	cursor: pointer;
	z-index: 333;
}
#cont-form {
	font-family: 'Open Sans', sans-serif;
	font-weight: 300;
	font-size: 13px;
	color: #ffffff;
	border-bottom: solid 1px #828282;
	padding-right: 15px;
	text-align: center;
	margin-bottom: 5px;
}
#sidebar-wrapper form {
	font-family: 'Open Sans', sans-serif;
	padding-left: 15px;
	color: #bfbfbf;
	position: absolute;
	bottom: 1px;
	width: 233px;
}
#sidebar-wrapper input {
	border-bottom: solid 1px #5c5c5c;
	background: transparent;
}
#sidebar-wrapper form textarea {
	width: 220px;
	height: 75px;
}
ul#navWords {
    display: inline-block;
    position: fixed;
    top: 0;
    right: 15px;
}
form button {
	margin-bottom: 15px;
	margin-top: 10px;
	border: solid 1px #5c5c5c;
	background: transparent;
	font-size: 12px;
}
form button:hover {
	background-color: #000;
	color: #ffffff;
}
#logo-cent, #logo-left {
	margin-top: 10px;
	height: 59px;
	width: auto;
	display: inline;
	padding-left: 33px;

}

/*#logo-left {
	display: none;
} */
@media(min-width: 1200px) {
	#logo-cent, #logo-left {
		height: 59px;
		width: auto;
		display: inline;

	}
	/* #logo-left {
		display: none;
	} */
}
.sidebar-nav {
    position: absolute;
    top: 0;
    width: 250px;
    margin: 0;
    padding: 0;
    list-style: none;
}

.sidebar-nav li {
	padding-left: 15px;
	padding-right: 15px;

    line-height: 24px;
}

.
.sidebar-nav li a {
	font-family: 'Open Sans', sans-serif;
	font-weight: 100;
    display: block;
    text-decoration: none;
    color: #727272;
	outline: none;
	letter-spacing: .6px;
}

.sidebar-nav li a:hover {
    text-decoration: none;
    color: #ffffff;
}

.sidebar-nav li a:active,
.sidebar-nav li a:focus {
    text-decoration: none;
}

.sidebar-nav > .sidebar-brand {
    height: 65px;
    font-size: 18px;
    line-height: 60px;
}

.sidebar-nav > .sidebar-brand a {
    color: #999999;
}

.sidebar-nav > .sidebar-brand a:hover {
    color: #fff;
    background: none;
}

@media(min-width:768px) {
    #content-wrapper {
        padding-left: -250px;
    }

    ##content-wrapper.toggled {
        padding-left: 0;
    }

    #sidebar-wrapper {
        width: 250px;
    }

    #content-wrapper.toggled #sidebar-wrapper {
        width: 0;
    }

    #page-content-wrapper {
        padding: 20px;
        position: relative;
    }

    #content-wrapper.toggled #page-content-wrapper {
        position: relative;
        margin-right: 0;
    }
}
/* ++++++ NEW NAVBAR Styles +++++*/

/* ++++++ /NEW NAVBAR Styles +++++*/
.navbar {
	top: 0px;
	position: fixed;
    -webkit-transition: top 0.5s ease;
    -moz-transition: top 0.5s ease;
    -o-transition: top 0.5s ease;
    transition: top 0.5s ease;
    background-color: rgba(250, 250, 250, .5);

	-webkit-box-shadow: 0px 1px 10.3px rgba(70, 70, 70, 0.86);
  	-moz-box-shadow: 0px 1px 10.3px rgba(70, 70, 70, 0.86);
	box-shadow: 0px 1px 10.3px rgba(70, 70, 70, 0.86);
	height: 79px;
	width: 100%;
	z-index: 888;
    margin-bottom: 0;
}
.navbar.entNav {
    -webkit-transition: top 0.5s ease;
    -moz-transition: top 0.5s ease;
    -o-transition: top 0.5s ease;
    transition: top 0.5s ease;
	  top: 0;
}
.navbar.entNav.srnkNav {
    -webkit-transition: height 0.5s ease;
    -moz-transition: height 0.5s ease;
    -o-transition: height 0.5s ease;
    transition: height 0.5s ease;
	  height: 1px;
}
.navbar .col-xs-2 {
	padding-right: 33px;
	padding-left: 0;
}
.navbar .col-xs-10{
	margin-top: 47px;
	padding-right: 0;
    text-align: left;
}
.navbar ul {
    position: relative;
    right: 28px;
}
.navbar ul li {
	text-align: center;
	padding-right: 5px;
	display: inline;
	height: 105px;
	border-top:solid 4px #f2f2f2;
	position: relative;
	top: -1px;
	left: 0;
	padding-top: 44px;
}
#navWords .dropdown {
    background-color: transparent;
    border: none;
}
.navbar ul.dropdown-menu {
        position: absolute;

    right: 0px !important;
    float: right;
    top: 64px;
    /* text-align: right; */
    width: 294px;
}
.navbar .dropdown-menu {
    left: auto;
    right: 0 !important;
}
@-moz-document url-prefix() {
  .navbar ul li {
     padding-top: 43px;
  }
}
.navbar ul li a {
    font-weight: 400;
    font-size: 12px;
	padding-left: 3px;
}
li#contactB {
    margin-left: 0;
}
@media (max-width: 1024px){
	.navbar ul li {
		padding-top: 43px;
	}
}
.navbar ul li:hover {
	border-top:solid 4px #4caf50;
}
.navbar ul li a:hover {
	text-decoration: none;
}
@media (min-width: 1000px){
	.navbar ul li {
		margin-left: 5px;
	}
}
.navbar ul {
	width: 100%;
	margin-left: 0;
}
.navbar ul li a {
    font-family: "Helvetica Neue", Helvetica , arial, sans-serif;
    color: #9e9e9e;
	font-size: 13px;
    letter-spacing: 2px;
    font-weight: bold;
}

@media(max-width: 650px){

	#logo-cent {
		display: none;
	}
	#logo-left {
		display: block;
		height: 36px;
		width: auto;
		margin-top: 13;
		padding-left: 0;
	}
	.navbar {
		-webkit-box-shadow : 0px 1px 1.3px rgba(70, 70, 70, 0.8);
		-moz-box-shadow : 0px 1px 1.3px rgba(70, 70, 70, 0.8);
		box-shadow : 0px 1px 1.3px rgba(70, 70, 70, 0.8);
		min-height: 0;
		height: 70px;
		width: 100%;
	}
}
#t-top {
	border-bottom:solid 2px #4caf50;
    width: 100%;
	height: 29px;
}
.navbar .row {
	margin-left: 0px;
    margin-top: -13px;
	margin-right: 0px;
}
button#call {
	color: #ffffff;
	background-color: #4caf50;
	font-size: 15px;
	padding: 3px 13px 4px;
	position: absolute;
	top: 0;
	right: 33px;
	border: none;
	border-radius: 0;
}
button#lastVid{
    color: #ffffff;
    background-color: #4caf50;
    font-size: 15px;
    padding: 3px 13px 4px;
    position: absolute;
    top: 0;
    left: 33px;
    border: none;
    border-radius: 0;
}
.glyphicon .glyphicon-earphone {
	top: 2px;
}

#pressRel {
	padding-top: 59px;
	padding-bottom: 79px;
}
#pressRel h1 {
	color: #ffffff;
	font-weight: 300;

}
#pressRel img {
	display: block;
	position: relative;
	left: 0;
	right: 0;
	margin-left: auto;
	margin-right: auto;

}
#pressRel #pressLogo0, #pressRel #pressLogo2 {
	margin-top: 26px;
	width: auto;
	height: 43px;
}
#pressRel #pressLogo1 {
	width: auto;
	height: 73px;
    padding-right: 13px;
}
#pressRel ul {
	position: relative;
	padding-top: 27px;
	display: inline-flex;

}
#pressRel ul li {
	display: inline;
}
#freeConsult .modal-dialog,
#emailCatcher .modal-dialog {
    width: 100%;
    max-width: 900px;

}
#freeConsult .modal-body,
#emailCatcher .modal-body {
    padding: 0;
}
#freeConsult .contact-main,
#emailCatcher .contact-main {
    border: none;
    background: #f2f2f2;
    padding-top: 24px;
    padding-bottom: 7px;

}
#freeConsult .modal-header,
#emailCatcher .modal-header {
    background-color: #4caf50;
    height: 51px;

}
#freeConsult img,
#emailCatcher img {
    display: block;
    position: relative;
    top: 13px;
    left: 0;
    right: 0;
    margin-left: auto;
    margin-right: auto;
}
#freeConsult .contact-main button,
#emailCatcher .contact-main button {
    margin-top: 29px;
}
#freeConsult .modal-content,
#emailCatcher .modal-content {
    border-radius: 7px;
}
#freeConsult .modal-header,
#emailCatcher .modal-header {
    border-top-left-radius: 7px;
    border-top-right-radius: 7px;
}
#freeConsult .btn-call2,
#emailCatcher .btn-call2 {
    background-color: transparent;
    color: #4caf50;
    border:solid 1px #4caf50;
}
#freeConsult .btn-call2:hover,
#emailCatcher .btn-call2:hover {
    background-color: #4caf50;
    color: #ffffff;

}
@media(max-width: 650px){
	#t-top {
		border-bottom: none;
	}
	button#call {
		position: absolute;
		left: 0;
		right: 0;
		margin-left: auto;
		margin-right: auto;
		font-size: 9px;
	}
}
@media (max-width: 1423px){
	#navWords {
		display: none;
    }
		#menu-toggle {
			position: fixed;
			right: 34px;
			cursor: pointer;
			display: block;
			z-index: 900;
		}
}
@media (max-width: 768px){
    #menu-toggle {
        top: 25px;
    }
       #logo-left {
        margin-top: 25px;
        padding-left: 9px;
    }
}
@media (max-width: 480px){

    #menu-toggle{
        top:  22px;
        right: 34px;
    }
    #logo-left {
        margin-top: 18px;
    }

}
@media (max-width: 320px){

    #menu-toggle{
        top:  25px;
        right: 27px;
    }

}
footer {
	width: 100%;
	height: auto;
    padding: 27px;
	background : -moz-linear-gradient(50% 100% 90deg,rgba(76, 175, 80, 1) 0%,rgba(112, 191, 115, 1) 51.58%,rgba(76, 175, 80, 1) 100%);
	    background : -webkit-linear-gradient(90deg, rgba(76, 175, 80, 1) 0%, rgba(112, 191, 115, 1) 51.58%, rgba(76, 175, 80, 1) 100%);
	    background : -webkit-gradient(linear,50% 100% ,50% 0% ,color-stop(0,rgba(76, 175, 80, 1) ),color-stop(0.5158,rgba(112, 191, 115, 1) ),color-stop(1,rgba(76, 175, 80, 1) ));
	    background : -o-linear-gradient(90deg, rgba(76, 175, 80, 1) 0%, rgba(112, 191, 115, 1) 51.58%, rgba(76, 175, 80, 1) 100%);
	    background : -ms-linear-gradient(90deg, rgba(76, 175, 80, 1) 0%, rgba(112, 191, 115, 1) 51.58%, rgba(76, 175, 80, 1) 100%);
	    -ms-filter: "progid:DXImageTransform.Microsoft.gradient(startColorstr='#4CAF50', endColorstr='#4CAF50' ,GradientType=0)";
	    background : linear-gradient(0deg, rgba(76, 175, 80, 1) 0%, rgba(112, 191, 115, 1) 51.58%, rgba(76, 175, 80, 1) 100%);
	    border-style : Solid;
	    border-color : #727272;
	    border-color : rgba(114, 114, 114, 1);
	    border-width : 1px;
		z-index: 1000;
	    filter: progid:DXImageTransform.Microsoft.dropshadow(OffX=0, OffY=-2, Color='#333333') progid:DXImageTransform.Microsoft.gradient(startColorstr='#4CAF50',endColorstr='#4CAF50' , GradientType=0);
}
footer h3 {
    font-size: 17px;
    color: #ffffff;
}
#solid {
    font-weight: 100;
    font-size: 12px;
}
footer li {
    padding-top: 0;
    list-style: none;
    margin-left: 0;

}
footer ul li a {
    padding-left: 12px;
    font-weight: 100;
}
#copyRight {
    color: #f2f2f2;
}
footer a:hover {
    color: #ffffff;
}

/* End--Scene SEVEN */
/* End--Navigation */

gha_language: HTML

extension: css