text:
@article{wernegreen2012,
	title = {Mutualism meltdown in insects: bacteria constrain thermal adaptation},
	volume = {15},
	issn = {1369-5274},
	shorttitle = {Ecology and industrial {microbiology/Special} section: Microbial proteomics},
	url = {http://www.sciencedirect.com/science/article/pii/S1369527412000173},
	doi = {10.1016/j.mib.2012.02.001},
	abstract = {Predicting whether and how organisms will successfully cope with climate change presents critical questions for biologists and environmental scientists. Models require knowing how organisms interact with their abiotic environment, as well understanding biotic interactions that include a network of symbioses in which all species are embedded. Bacterial symbionts of insects offer valuable models to examine how microbes can facilitate and constrain adaptation to a changing environment. While some symbionts confer plasticity that accelerates adaptation, long-term bacterial mutualists of insects are characterized by tight lifestyle constraints, genome deterioration, and vulnerability to thermal stress. These essential bacterial partners are eliminated at high temperatures, analogous to the loss of zooanthellae during coral bleaching. Recent field-based studies suggest that thermal sensitivity of bacterial mutualists constrains insect responses. In this sense, highly dependent mutualisms may be the Achilles' heel of thermal responses in insects.},
	number = {3},
	urldate = {2013-08-15},
	journal = {Current Opinion in Microbiology},
	author = {Wernegreen, Jennifer J},
	month = jun,
	year = {2012},
	pages = {255--262},
	file = {ScienceDirect Snapshot:/home/ego/.mozilla/firefox/2olrcvl3.François/zotero/storage/XMRSAG44/S1369527412000173.html:text/html;Wernegreen et al, 2012.pdf:/home/ego/.mozilla/firefox/2olrcvl3.François/zotero/storage/JVAPS2PZ/Wernegreen et al, 2012.pdf:application/pdf}
}
@article{rosenberg2007,
	title = {The role of microorganisms in coral health, disease and evolution},
	volume = {5},
	copyright = {© 2007 Nature Publishing Group},
	issn = {1740-1526},
	url = {http://www.nature.com/nrmicro/journal/v5/n5/abs/nrmicro1635.html#top},
	doi = {10.1038/nrmicro1635},
	abstract = {Coral microbiology is an emerging field, driven largely by a desire to understand, and ultimately prevent, the worldwide destruction of coral reefs. The mucus layer, skeleton and tissues of healthy corals all contain large populations of eukaryotic algae, bacteria and archaea. These microorganisms confer benefits to their host by various mechanisms, including photosynthesis, nitrogen fixation, the provision of nutrients and infection prevention. Conversely, in conditions of environmental stress, certain microorganisms cause coral bleaching and other diseases. Recent research indicates that corals can develop resistance to specific pathogens and adapt to higher environmental temperatures. To explain these findings the coral probiotic hypothesis proposes the occurrence of a dynamic relationship between symbiotic microorganisms and corals that selects for the coral holobiont that is best suited for the prevailing environmental conditions. Generalization of the coral probiotic hypothesis has led us to propose the hologenome theory of evolution.},
	language = {en},
	number = {5},
	urldate = {2013-10-01},
	journal = {Nature Reviews Microbiology},
	author = {Rosenberg, Eugene and Koren, Omry and Reshef, Leah and Efrony, Rotem and Zilber-Rosenberg, Ilana},
	month = may,
	year = {2007},
	pages = {355--362},
	file = {Rosenberg et al. - 2007 - The role of microorganisms in coral health, diseas.html:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/X2U3BIHG/Rosenberg et al. - 2007 - The role of microorganisms in coral health, diseas.html:text/html;Rosenberg et al. - 2007 - The role of microorganisms in coral health, diseas.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/9JPU2EHD/Rosenberg et al. - 2007 - The role of microorganisms in coral health, diseas.pdf:application/pdf}
}
@article{douglas1998,
	title = {Nutritional interactions in insect-microbial symbioses: Aphids and their symbiotic bacteria {\textit{Buchnera}}},
	volume = {43},
	shorttitle = {Nutritional Interactions in Insect-Microbial Symbioses},
	url = {http://www.annualreviews.org/doi/abs/10.1146/annurev.ento.43.1.17},
	doi = {10.1146/annurev.ento.43.1.17},
	abstract = {Most aphids possess intracellular bacteria of the genus Buchnera. The bacteria are transmitted vertically via the aphid ovary, and the association is obligate for both partners: Bacteria-free aphids grow poorly and produce few or no offspring, and Buchnera are both unknown apart from aphids and apparently unculturable. The symbiosis has a nutritional basis. Specifically, bacterial provisioning of essential amino acids has been demonstrated. Nitrogen recycling, however, is not quantitatively important to the nutrition of aphid species studied, and there is strong evidence against bacterial involvement in the lipid and sterol nutrition of aphids. Buchnera have been implicated in various non-nutritional functions. Of these, just one has strong experimental support: promotion of aphid transmission of circulative viruses. It is argued that strong parallels may exist between the nutritional interactions (including the underlying mechanisms) in the aphid-Buchnera association and other insect symbioses with intracellular microorganisms.},
	number = {1},
	urldate = {2013-10-01},
	journal = {Annual Review of Entomology},
	author = {Douglas, A. E.},
	year = {1998},
	note = {{PMID:} 15012383},
	keywords = {amino acids, arthropod, Endosymbiosis, mycetocyte, nutrition},
	pages = {17--37},
	file = {Douglas - 1998 - Nutritional Interactions in Insect-Microbial Symbi.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/JTPDS3DB/Douglas - 1998 - Nutritional Interactions in Insect-Microbial Symbi.pdf:application/pdf}
}
@article{schaffner2013,
	title = {Public health significance of invasive mosquitoes in Europe},
	volume = {19},
	issn = {{1198743X}},
	url = {https://cisr-ssl-vpn2.univ-lyon1.fr/+CSCO+0h756767633A2F2F62617976617279766F656E656C2E6A7679726C2E70627A++/doi/10.1111/1469-0691.12189/abstract},
	doi = {10.1111/1469-0691.12189},
	number = {8},
	urldate = {2013-08-24},
	journal = {Clinical Microbiology and Infection},
	author = {Schaffner, F. and Medlock, J. M. and Van Bortel, W.},
	month = aug,
	year = {2013},
	pages = {685--692},
	file = {Public health significance of invasive mosquitoes in Europe - Schaffner - 2013 - Clinical Microbiology and Infection - Wiley Online Library:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/UAMSERVQ/abstract.html:text/html;Schaffner et al. - 2013 - Public health significance of invasive mosquitoes .pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/24ZBC8IN/Schaffner et al. - 2013 - Public health significance of invasive mosquitoes .pdf:application/pdf}
}
@article{feldhaar2011,
	title = {Bacterial symbionts as mediators of ecologically important traits of insect hosts},
	volume = {36},
	copyright = {© 2011 The Author. Ecological Entomology © 2011 The Royal Entomological Society},
	issn = {1365-2311},
	url = {http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2311.2011.01318.x/abstract},
	doi = {10.1111/j.1365-2311.2011.01318.x},
	abstract = {1. Bacterial symbionts play a prominent role in insect nutritional ecology by aiding in digestion of food or providing nutrients that are limited or lacking in the diet. Thereby, endosymbionts open niches to their insect host that would otherwise be unavailable.2. Currently, several other ecologically relevant traits mediated by endosymbionts are being investigated, including enhanced parasite resistance, enhanced heat tolerance, and influences on insect–plant interactions such as manipulation of plant physiology to the benefit of the insect.3. Traits mediated by endosymbionts are often identified by correlative studies where traits are found to be altered in the presence of a particular symbiont. Recent developments in genomic tools offer the opportunity for studying the impact of bacteria–insect symbioses under natural conditions in a population and community ecology context. In vivo experiments specifically testing putative functions of endosymbionts in parallel to population-level studies on the prevalence of endosymbionts allow disentangling host versus symbiont contribution to phenotypic variability observed in individuals. Effects of symbionts on host phenotype are often large and relevant to host fitness, e.g. by significantly enhancing survival or fecundity in a context-dependent manner.4. Predominantly vertically transmitted endosymbionts contribute to the heritable genetic variation present in a host species. Phenotypic variation on which selection can act may be due to differences either among host genomes, symbiont genomes, or genotype × genotype interactions. Therefore the holobiont, i.e. the host including all symbionts, should be regarded as the unit of selection as the association between host and symbionts may affect the fitness of the holobiont depending on the environment.},
	language = {en},
	number = {5},
	urldate = {2013-10-01},
	journal = {Ecological Entomology},
	author = {Feldhaar, Heike},
	year = {2011},
	keywords = {endosymbiont, holobiont, hologenome, multilevel selection, mutualism},
	pages = {533–543},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/RPSC6INC/Feldhaar - 2011 - Bacterial symbionts as mediators of ecologically i.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/XZAMV2T7/full.html:text/html}
}
@article{brumin2011,
	title = {\textit{Rickettsia} influences thermotolerance in the whitefly {\textit{Bemisia tabaci}} B biotype},
	volume = {18},
	copyright = {© 2011 The Authors Journal compilation © Institute of Zoology, Chinese Academy of Sciences},
	issn = {1744-7917},
	url = {http://onlinelibrary.wiley.com/doi/10.1111/j.1744-7917.2010.01396.x/abstract},
	doi = {10.1111/j.1744-7917.2010.01396.x},
	abstract = {Abstract The whitefly Bemisia tabaci harbors Portiera aleyrodidarum, an obligatory symbiotic bacterium, as well as several secondary symbionts, including Rickettsia, Hamiltonella, Wolbachia, Arsenophonus, Cardinium and Fritschea, the function of which is unknown. In Israel, Rickettsia is found in both the B and Q of B. tabaci biotypes, and while all other secondary symbionts are located in the bacteriomes, Rickettsia can occupy most of the body cavity of the insect. We tested whether Rickettsia influences the biology of B. tabaci and found that exposing a Rickettsia-containing population to increasing temperatures significantly increases its tolerance to heat shock that reached {40°C}, compared to a Rickettsia-free population. This increase in tolerance to heat shock was not associated with specific induction of heat-shock protein gene expression; however, it was associated with reduction in Rickettsia numbers as was assessed by quantitative real-time polymerase chain reaction and fluorescence in situ hybridization analyses. To assess the causes for thermotolerance when Rickettsia is reduced, we tested whether its presence is associated with the induction of genes required for thermotolerance. We found that under normal {25°C} rearing temperature, genes associated with response to stress such as cytoskeleton genes are induced in the Rickettsia-containing population. Thus, the presence of Rickettsia in B. tabaci under normal conditions induces the expression of genes required for thermotolerance that under high temperatures indirectly lead to this tolerance.},
	language = {en},
	number = {1},
	urldate = {2013-10-01},
	journal = {Insect Science},
	author = {Brumin, Marina and Kontsedalov, Svetlana and Ghanim, Murad},
	year = {2011},
	keywords = {cytoskeleton, gene expression, heat shock, Symbiont},
	pages = {57–66},
	file = {Brumin et al. - 2011 - Rickettsia influences thermotolerance in the white.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/FQ46GZM3/Brumin et al. - 2011 - Rickettsia influences thermotolerance in the white.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/9847A3AB/abstract.html:text/html}
}
@article{dunbar2007,
	title = {Aphid thermal tolerance is governed by a point mutation in bacterial symbionts},
	volume = {5},
	url = {http://dx.doi.org/10.1371/journal.pbio.0050096},
	doi = {10.1371/journal.pbio.0050096},
	abstract = {A recurring single-nucleotide deletion in a heat-shock transcriptional promoter in the {bacterialBuchnera} symbiont of the pea aphid(Acyrthosiphon pisum) dramatically affects host fitness in a thermal-dependent manner.},
	number = {5},
	urldate = {2013-10-01},
	journal = {{PLoS} Biol},
	author = {Dunbar, Helen E and Wilson, Alex C. C and Ferguson, Nicole R and Moran, Nancy A},
	month = apr,
	year = {2007},
	pages = {e96},
	file = {PLoS Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/7N7KGCBG/Dunbar et al. - 2007 - Aphid Thermal Tolerance Is Governed by a Point Mut.pdf:application/pdf;PLoS Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/4425CQZU/journal.pbio.html:text/html}
}
@article{stoll2009,
	title = {Transcriptional profiling of the endosymbiont {\textit{Blochmannia floridanus}} during different developmental stages of its holometabolous ant host},
	volume = {11},
	copyright = {Journal compilation © 2008 Society for Applied Microbiology and Blackwell Publishing Ltd. No claim to original German government works},
	issn = {1462-2920},
	url = {http://onlinelibrary.wiley.com/doi/10.1111/j.1462-2920.2008.01808.x/abstract},
	doi = {10.1111/j.1462-2920.2008.01808.x},
	abstract = {The transcriptome of Blochmannia floridanus, the endosymbiont of the carpenter ant Camponotus floridanus, is presented during various developmental stages of its holometabolous host by use of a whole-genome {DNA} macroarray. The detected transcription patterns indicate the presence of local transcription units as well as global regulatory mechanisms. Yet, the overall regulation scale is very modest, rarely exceeding a factor of three. A large number of genes show differential expression in different life stages and a distinct expression pattern of genes possibly involved in symbiotic function as compared with housekeeping genes is apparent. However, these transcriptional changes are small as compared with the changes in the number of bacteria during host development, which is the highest in pupae and in young imagines. Control of replication of the bacteria in certain life stages may therefore be the decisive parameter influencing the overall level of gene expression of Blochmannia in the animal. The few highly expressed genes like those encoding molecular chaperones exhibit a significantly higher {G+C} content than moderately expressed genes.},
	language = {en},
	number = {4},
	urldate = {2013-10-01},
	journal = {Environmental Microbiology},
	author = {Stoll, Sascha and Feldhaar, Heike and Gross, Roy},
	year = {2009},
	pages = {877–888},
	annote = {Alors ça ça parle apparement de {groEL} qui serait surexprimé par les ß et qui pourraient partir dans l'hémolymphe.},
	file = {Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/QE8HCFUZ/abstract.html:text/html;Stoll et al. - 2009 - Transcriptional profiling of the endosymbiont Bloc.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/HZIJMM5V/Stoll et al. - 2009 - Transcriptional profiling of the endosymbiont Bloc.pdf:application/pdf}
}
@article{arakaki2001,
	title = {{\textit{Wolbachia}}-mediated parthenogenesis in the predatory thrips {\textit{Franklinothrips vespiformis}} ({\textit{Thysanoptera}: \textit{Insecta}})},
	volume = {268},
	issn = {0962-8452, 1471-2954},
	shorttitle = {Wolbachia–mediated parthenogenesis in the predatory thrips Franklinothrips vespiformis (Thysanoptera},
	url = {http://rspb.royalsocietypublishing.org/content/268/1471/1011},
	doi = {10.1098/rspb.2001.1628},
	abstract = {Wolbachia are bacterial endosymbionts in arthropods and filarial nematodes. They cause thelytoky, which is a form of parthenogenesis in which females produce females without males, in hymenopteran insects. Infection of this parthenogenesis‐inducing Wolbachia has been restricted to the order Hymenoptera, but was found in another insect order, Thysanoptera. A parthenogenetic colony of a predatory thrips Franklinothrips vespiformis (Aeolothripidae) possessed B-group Wolbachia. Male progeny were produced from this thrips by heat and tetracycline treatments. Males produced motile sperm, which were transferred to the female spermatheca by mating. However, the mating did not affect the sex ratios of the next generation, suggesting that the sperm do not fertilize the eggs.},
	language = {en},
	number = {1471},
	urldate = {2013-10-02},
	journal = {Proceedings of the Royal Society of London. Series B: Biological Sciences},
	author = {Arakaki, N. and Miyoshi, T. and Noda, H.},
	month = may,
	year = {2001},
	note = {{PMID:} 11375084},
	keywords = {Franklinothrips vespiformis, parthenogenesis, Symbiont, thelytoky, thrips, Wolbachia},
	pages = {1011--1016},
	annote = {Là, l'aspect heat-choc est accessoire, ils ont traité thermiquement des bestoioles, et ont observé un effet sur {l'IC.}},
	file = {Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/U7CAFSNE/1011.html:text/html}
}
@article{federhoffmann1999,
	title = {Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology.},
	volume = {61},
	shorttitle = {Heat-shock proteins, molecular chaperones, and the stress response},
	url = {http://www.annualreviews.org/doi/abs/10.1146/annurev.physiol.61.1.243},
	doi = {10.1146/annurev.physiol.61.1.243},
	abstract = {Molecular chaperones, including the heat-shock proteins (Hsps), are a ubiquitous feature of cells in which these proteins cope with stress-induced denaturation of other proteins. Hsps have received the most attention in model organisms undergoing experimental stress in the laboratory, and the function of Hsps at the molecular and cellular level is becoming well understood in this context. A complementary focus is now emerging on the Hsps of both model and nonmodel organisms undergoing stress in nature, on the roles of Hsps in the stress physiology of whole multicellular eukaryotes and the tissues and organs they comprise, and on the ecological and evolutionary correlates of variation in Hsps and the genes that encode them. This focus discloses that (a) expression of Hsps can occur in nature, (b) all species have hsp genes but they vary in the patterns of their expression, (c) Hsp expression can be correlated with resistance to stress, and (d) species' thresholds for Hsp expression are correlated with levels of stress that they naturally undergo. These conclusions are now well established and may require little additional confirmation; many significant questions remain unanswered concerning both the mechanisms of Hsp-mediated stress tolerance at the organismal level and the evolutionary mechanisms that have diversified the hsp genes.},
	number = {1},
	urldate = {2013-10-02},
	journal = {Annual Review of Physiology},
	author = {Feder, Martin E. and Hofmann, Gretchen E.},
	year = {1999},
	note = {{PMID:} 10099689},
	keywords = {environmental gradients, hsp, inducible tolerance, protein denaturation and folding, Temperature},
	pages = {243--282},
	annote = {Vieille review.
Citée dans Brumin et al 2011 pour {"HSP} régulées par la chaleur"
avec Hoffmann et al 2003},
	file = {Feder et Hofmann - 1999 - HEAT-SHOCK PROTEINS, MOLECULAR CHAPERONES, AND THE.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/SUSJNJPP/Feder et Hofmann - 1999 - HEAT-SHOCK PROTEINS, MOLECULAR CHAPERONES, AND THE.pdf:application/pdf}
}
@article{zhang2011,
	title = {Chaperone proteins and winter survival by a freeze tolerant insect},
	volume = {57},
	issn = {0022-1910},
	url = {http://www.sciencedirect.com/science/article/pii/S002219101100059X},
	doi = {10.1016/j.jinsphys.2011.02.016},
	abstract = {The role of chaperone proteins in the winter survival of insects was evaluated in freeze tolerant gall fly larvae, Eurosta solidaginis. Levels of four heat shock proteins (Hsp110, Hsp70, Hsp60, Hsp40), two glucose-regulated proteins (Grp75, Grp78) and three others (tailless complex polypeptide 1 [{TCP-1]}, {αA-crystallin}, {αB-crystallin)} were tracked in outdoor larvae from September to April and, in addition, laboratory experiments assessed chilling, freezing, and anoxia effects on these proteins. Gall fly larvae showed consistent elevation of Hsp110, Hsp70, Hsp40, Grp78 and {αB-crystallin} over the late autumn and winter months, generally 1.5–2.0-fold higher than September values. This suggests that these proteins contribute to cell preservation over the winter months via protection and stabilization of macromolecules. By contrast, levels of the mitochondrial Hsp60 fell to just 40\% of September values by midwinter, paralleling the responses by numerous mitochondrial enzymes and consistent with a reduction in total mitochondria numbers over the winter. None of the proteins were altered when 15 {°C} acclimated larvae were chilled to 3 {°C} for 24 h but Hsp70, Hsp40 and Grp75 increased during freezing at −16 {°C} for 24 h whereas others (Hsp110, {TCP-1} and both crystallins) increased significantly after larvae thawed at 3 {°C.} Anoxia exposure (24 h under N2 gas at 15 {°C)} elevated levels of Hsp70, Grp78 and the two crystallins. Levels of active hyperphosphorylated heat shock transcription factor ({HSF1)} were also analyzed, giving an indication of the state of hsp gene transcription in the larvae. {HSF1} was high in September and October but fell to less than 40\% of September values in midwinter consistent with suppression of gene transcription in diapause larvae. {HSF1} levels responded positively to freezing and increased robustly by 4.9-fold under anoxia. Overall, the data provide strong evidence for the importance of protein chaperones as a mechanism of cell preservation in freeze tolerant insects.},
	number = {8},
	urldate = {2013-10-03},
	journal = {Journal of Insect Physiology},
	author = {Zhang, Guijun and Storey, Janet M. and Storey, Kenneth B.},
	month = aug,
	year = {2011},
	keywords = {Anoxia, Cold hardiness, Cytoprotection, Eurosta solidaginis, Glucose-regulated proteins, heat shock proteins},
	pages = {1115--1122},
	file = {ScienceDirect Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/G5RRRGE4/S002219101100059X.html:text/html;Zhang et al. - 2011 - Chaperone proteins and winter survival by a freeze.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/IA8XAE7C/Zhang et al. - 2011 - Chaperone proteins and winter survival by a freeze.pdf:application/pdf}
}
@article{sorensen2003,
	title = {The evolutionary and ecological role of heat shock proteins},
	volume = {6},
	issn = {1461-0248},
	url = {http://onlinelibrary.wiley.com/doi/10.1046/j.1461-0248.2003.00528.x/abstract},
	doi = {10.1046/j.1461-0248.2003.00528.x},
	abstract = {Most heat shock proteins (Hsp) function as molecular chaperones that help organisms to cope with stress of both an internal and external nature. Here, we review the recent evidence of the relationship between stress resistance and inducible Hsp expression, including a characterization of factors that induce the heat shock response and a discussion of the associated costs. We report on studies of stress resistance including mild stress, effects of high larval densities, inbreeding and age on Hsp expression, as well as on natural variation in the expression of Hsps. The relationship between Hsps and life history traits is discussed with special emphasis on the ecological and evolutionary relevance of Hsps. It is known that up-regulation of the Hsps is a common cellular response to increased levels of non-native proteins that facilitates correct protein folding/refolding or degradation of non-functional proteins. However, we also suggest that the expression level of Hsp in each species and population is a balance between benefits and costs, i.e. a negative impact on growth, development rate and fertility as a result of overexpression of Hsps. To date, investigations have focused primarily on the Hsp70 family. There is evidence that representatives of this Hsp family and other molecular chaperones play significant roles in relation to stress resistance. Future studies including genomic and proteonomic analyses will increase our understanding of molecular chaperones in stress research.},
	language = {en},
	number = {11},
	urldate = {2013-10-02},
	journal = {Ecology Letters},
	author = {Sørensen, Jesper Givskov and Kristensen, Torsten Nygaard and Loeschcke, Volker},
	year = {2003},
	keywords = {Adaptation, environmental stress resistance, genetic stress, hsp, protein quality control},
	pages = {1025–1037},
	annote = {Cité par Bramine et tant que "hsp = réponse à plein de stress factors".},
	file = {Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/DK47GX73/full.html:text/html;Sørensen et al. - 2003 - The evolutionary and ecological role of heat shock.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/FI5KWAEW/Sørensen et al. - 2003 - The evolutionary and ecological role of heat shock.pdf:application/pdf}
}
@article{duman2001,
	title = {Antifreeze and Ice Nucleator Proteins in Terrestrial Arthropods},
	volume = {63},
	url = {http://www.annualreviews.org/doi/abs/10.1146/annurev.physiol.63.1.327},
	doi = {10.1146/annurev.physiol.63.1.327},
	abstract = {Terrestrial arthropods survive subzero temperatures by becoming either freeze tolerant (survive body fluid freezing) or freeze avoiding (prevent body fluid freezing). Protein ice nucleators ({PINs)}, which limit supercooling and induce freezing, and antifreeze proteins ({AFPs)}, which function to prevent freezing, can have roles in both freeze tolerance and avoidance. Many freeze-tolerant insects produce hemolymph {PINs}, which induce freezing at high subzero temperatures thereby inhibiting lethal intracellular freezing. Some freeze-tolerant species have {AFPs} that function as cryoprotectants to prevent freeze damage. Although the mechanism of this cryoprotection is not known, it may involve recrystallization inhibition and perhaps stabilization of the cell membrane. Freeze-avoiding species must prevent inoculative freezing initiated by external ice across the cuticle and extend supercooling abilities. Some insects remove {PINs} in the winter to promote supercooling, whereas others have selected against surfaces with ice-nucleating abilities on an evolutionary time scale. However, many freeze-avoiding species do have proteins with ice-nucleating activity, and these proteins must be masked in winter. In the beetle Dendroides canadensis, {AFPs} in the hemolymph and gut inhibit ice nucleators. Also, hemolymph {AFPs} and those associated with the layer of epidermal cells under the cuticle inhibit inoculative freezing. Two different insect {AFPs} have been characterized. One type from the beetles D. canadensis and Tenebrio molitor consists of 12- and 13-mer repeating units with disulfide bridges occurring at least every six residues. The spruce budworm {AFP} lacks regular repeat units. Both have much higher activities than any known {AFPs.}},
	number = {1},
	urldate = {2013-10-08},
	journal = {Annual Review of Physiology},
	author = {Duman, John G},
	year = {2001},
	note = {{PMID:} 11181959},
	keywords = {antifreeze proteins, freeze tolerance, insect cold tolerance, supercooling},
	pages = {327--357}
},

@article{xu1998,
	title = {Isolation and characterization of an antifreeze protein with ice nucleation activity from the plant growth promoting rhizobacterium Pseudomonas putida {GR12-2}},
	volume = {44},
	issn = {0008-4166},
	url = {http://www.nrcresearchpress.com/doi/abs/10.1139/w97-126},
	doi = {10.1139/w97-126},
	abstract = {An antifreeze protein secreted to the growth medium by the plant growth promoting rhizobacterium Pseudomonas putida {GR12-2} was purified to apparent homogeneity. The purified protein has a molecular mass of 164 ± 15 {kDa} and an isoelectric point of 5.3, contains both carbohydrate and lipid moieties, and is relatively rich in glycine and alanine. The properties of the purified antifreeze protein are similar to the properties previously reported for bacterial ice-nucleation proteins. In fact, the purified antifreeze protein also displays a low level of ice-nucleation activity. Removal of approximately 92 {kDa} of carbohydrate from the 164-{kDa} antifreeze glycoprotein did not noticeably alter the antifreeze activity of the molecule, although it did diminish the ice-nucleation activity. This is the first report of an antifreeze protein that also is active as an ice-nucleation {protein.Key} words: antifreeze protein, plant growth promoting rhizobacteria, freezing tolerance, ice-nucleation protein., Une protéine antigel sécrétée dans le milieu de culture d'une rhizobactérie qui favorise la croissance des plantes, le Pseudomonas putida {GR12-2}, a été purifiée jusqu'à homogénéité apparente. Cette protéine purifiée, de masse moléculaire de 164 ± 15 {kDa} et de point isoélectrique de 5,3, contient des parties égales de lipide et d'hydrate de carbone et elle est relativement riche en glycine et alanine. Les propriétés de cette protéine purifiée ressemblent à celles qui furent antérieurement rapportées pour les protéines bactériennes qui causent la nucléation de cristaux de glace. De fait, la protéine antigel purifiée présente également une activité de nucléation de cristaux de glace à un faile niveau. 'enlèvement d'environ 92 {kDa} d'hydrates de carbone de la glycoprotéine de 164 {kDa} n'a pas altéré notablement l'activité antigel de la molécule, mais l'activité de nucléation de cristaux de glace a été diminuée. Ce rapport est le premier d'une protéine qui est active comme antigel, mais aussi comme agent de nucl...},
	number = {1},
	urldate = {2013-10-08},
	journal = {Canadian Journal of Microbiology},
	author = {Xu, Hao and Griffith, Marilyn and Patten, Cheryl L and Glick, Bernard R},
	month = jan,
	year = {1998},
	pages = {64--73},
	file = {NRC Research Press PDF fulltext:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/ESFRZJF9/Xu et al. - 1998 - Isolation and characterization of an antifreeze pr.pdf:application/pdf;NRC Research Press Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/GP66UHWU/w97-126.html:text/html}
}
@article{lee1996,
	title = {Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in {\textit{Saccharomyces cerevisiae}}.},
	volume = {16},
	issn = {0270-7306, 1098-5549},
	url = {http://mcb.asm.org/content/16/9/4773},
	abstract = {In Escherichia coli and mitochondria, the molecular chaperone {DnaJ} is required not only for protein folding but also for selective degradation of certain abnormal polypeptides. Here we demonstrate that in the yeast cytosol, the homologous chaperone Ydj1 is also required for ubiquitin-dependent degradation of certain abnormal proteins. The temperature-sensitive ydj1-151 mutant showed a large defect in the overall breakdown of short-lived cell proteins and abnormal polypeptides containing amino acid analogs, especially at 38 degrees C. By contrast, the degradation of long-lived cell proteins, which is independent of ubiquitin, was not altered nor was cell growth affected. The inactivation of Ydj1 markedly reduced the rapid, ubiquitin-dependent breakdown of certain beta-galactosidase (beta-gal) fusion polypeptides. Although degradation of N-end rule substrates (arginine-beta-gal and leucine-beta-gal) and the B-type cyclin Clb5-beta-gal occurred normally, degradation of the abnormal polypeptide ubiquitin-proline-beta-gal (Ub-P-beta-gal) and that of the short-lived normal protein Gcn4 were inhibited. As a consequence of reduced degradation of Ub-P-beta-gal, the beta-gal activity was four to five times higher in temperature-sensitive ydj1-151 mutant cells than in wild-type cells; thus, the folding and assembly of this enzyme do not require Ydj1 function. In wild-type cells, but not in ydj1-151 mutant cells, this chaperone is associated with the short-lived substrate Ub-P-beta-gal and not with stable beta-gal constructs. Furthermore, in the ydj1-151 mutant, the ubiquitination of Ub-P-beta-gal was blocked and the total level of ubiquitinated protein in the cell was reduced. Thus, Ydj1 is essential for the ubiquitin-dependent degradation of certain proteins. This chaperone may facilitate the recognition of unfolded proteins or serve as a cofactor for certain ubiquitin-ligating enzymes.},
	language = {en},
	number = {9},
	urldate = {2013-10-09},
	journal = {Molecular and Cellular Biology},
	author = {Lee, D. H. and Sherman, M. Y. and Goldberg, A. L.},
	month = jan,
	year = {1996},
	note = {{PMID:} 8756635},
	pages = {4773--4781},
	annote = {Homologue de {DnaJ} impliqué dans process ubiquitine.},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/8P8H6IGD/Lee et al. - 1996 - Involvement of the molecular chaperone Ydj1 in the.pdf:application/pdf;Lee et al. - 1996 - Involvement of the molecular chaperone Ydj1 in the.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/4A6AJZRH/Lee et al. - 1996 - Involvement of the molecular chaperone Ydj1 in the.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/DVMPCARJ/4773.html:text/html}
}
@article{montllor2002,
	title = {Facultative bacterial endosymbionts benefit pea aphids \textit{Acyrthosiphon pisum} under heat stress},
	volume = {27},
	issn = {1365-2311},
	url = {http://onlinelibrary.wiley.com/doi/10.1046/j.1365-2311.2002.00393.x/abstract},
	doi = {10.1046/j.1365-2311.2002.00393.x},
	abstract = {Abstract 1. Natural populations of pea aphids in California contain at least two facultative bacterial secondary symbionts (pea aphid secondary symbiont, {PASS}, or pea aphid rickettsia, {PAR)} in a range of frequencies throughout the state.2. Two pea aphid clones without either of these facultative associates failed to reproduce in the first 8 days after the final moult if they had been heat-stressed for a period of about 4 h at 39 {°C} as 1-day-old larvae in the laboratory.3. Aphids infected artificially with {PASS}, however, were able to produce up to 48\% of the normal complement of offspring produced by {PASS-positive} aphids that had not been heat-stressed. Clones infected artificially with {PAR} did not have the same advantage as those with {PASS} after heat stress.4. In aphids without {PASS} or {PAR}, heat stress reduced the number of bacteriocytes (in which the obligate primary symbiont, Buchnera, resides) to 7\% of non-heat-stressed aphids, while aphids with only {PASS} retained 70\% of their bacteriocytes. Bacteriocytes in aphids with {PAR} but not {PASS} were reduced to 42\% of controls.5. When larvae were heat-stressed as older instars (5 days old), a similar pattern emerged, though the effect of heat stress was less extreme. Clones containing {PASS} produced the most offspring, three to 14 times as many as aphids without {PASS} or {PAR.} Aphids with {PAR} only, or {PASS} and {PAR} together, had reduced or no advantage over aphids without facultative symbionts.6. Aphids of all clones that had been heat-stressed as later instars gave birth to a variable number of stillborn offspring. Aphids without facultative symbionts produced the most stillborn larvae.7. Field studies showed a higher incidence of {PASS} in aphids collected in California in summer compared with aphids from the same sites collected 2–4 months earlier. The difference was significant in two of three widely dispersed locations.},
	language = {en},
	number = {2},
	urldate = {2013-10-11},
	journal = {Ecological Entomology},
	author = {Montllor, Clytia B. and Maxmen, Amy and Purcell, Alexander H.},
	year = {2002},
	keywords = {Aphididae, Buchnera, endosymbiont, fecundity, Rickettsia, secondary symbiont},
	pages = {189–195},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/U27HMMSI/Montllor et al. - 2002 - Facultative bacterial endosymbionts benefit pea ap.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/E292RFRM/abstract.html:text/html}
}
@article{harmon2009,
	title = {Species Response to Environmental Change: Impacts of Food Web Interactions and Evolution},
	volume = {323},
	issn = {0036-8075, 1095-9203},
	shorttitle = {Species Response to Environmental Change},
	url = {http://www.sciencemag.org/content/323/5919/1347},
	doi = {10.1126/science.1167396},
	abstract = {How environmental change affects species abundances depends on both the food web within which species interact and their potential to evolve. Using field experiments, we investigated both ecological and evolutionary responses of pea aphids (Acyrthosiphon pisum), a common agricultural pest, to increased frequency of episodic heat shocks. One predator species ameliorated the decrease in aphid population growth with increasing heat shocks, whereas a second predator did not, with this contrast caused by behavioral differences between predators. We also compared aphid strains with stably inherited differences in heat tolerance caused by bacterial endosymbionts and showed the potential for rapid evolution for heat-shock tolerance. Our results illustrate how ecological and evolutionary complexities should be incorporated into predictions of the consequences of environmental change for species' populations.},
	language = {en},
	number = {5919},
	urldate = {2013-10-01},
	journal = {Science},
	author = {Harmon, Jason P. and Moran, Nancy A. and Ives, Anthony R.},
	month = jun,
	year = {2009},
	note = {{PMID:} 19265021},
	pages = {1347--1350},
	annote = {The secondary endosymbionts Serratia symbiotica and Hamiltonella defensa can ameliorate aphid fitness under heat stress presum-ably by enhancing retention of bacteriocytes and survival of Buchnera under heat stress.
Fedhar 2011},
	file = {Harmon et al. - 2009 - Species Response to Environmental Change Impacts .pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/882BDNTW/Harmon et al. - 2009 - Species Response to Environmental Change Impacts .pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/SMWEU9XK/1347.html:text/html}
}
@article{fink1999,
	title = {Chaperone-Mediated Protein Folding},
	volume = {79},
	issn = {0031-9333, 1522-1210},
	url = {http://physrev.physiology.org/content/79/2/425},
	abstract = {The folding of most newly synthesized proteins in the cell requires the interaction of a variety of protein cofactors known as molecular chaperones. These molecules recognize and bind to nascent polypeptide chains and partially folded intermediates of proteins, preventing their aggregation and misfolding. There are several families of chaperones; those most involved in protein folding are the 40-{kDa} heat shock protein ({HSP40;} {DnaJ)}, 60-{kDa} heat shock protein ({HSP60;} {GroEL)}, and 70-{kDa} heat shock protein ({HSP70;} {DnaK)} families. The availability of high-resolution structures has facilitated a more detailed understanding of the complex chaperone machinery and mechanisms, including the {ATP-dependent} reaction cycles of the {GroEL} and {HSP70} chaperones. For both of these chaperones, the binding of {ATP} triggers a critical conformational change leading to release of the bound substrate protein. Whereas the main role of the {HSP70/HSP40} chaperone system is to minimize aggregation of newly synthesized proteins, the {HSP60} chaperones also facilitate the actual folding process by providing a secluded environment for individual folding molecules and may also promote the unfolding and refolding of misfolded intermediates.},
	language = {en},
	number = {2},
	urldate = {2013-10-03},
	journal = {Physiological Reviews},
	author = {Fink, Anthony L.},
	month = jan,
	year = {1999},
	note = {{PMID:} 10221986},
	pages = {425--449},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/U7NCW7Q3/Fink - 1999 - Chaperone-Mediated Protein Folding.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/K47ZX94B/425.html:text/html}
}
@article{chiosis2013,
	title = {A global view of Hsp90 functions},
	volume = {20},
	copyright = {© 2013 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.},
	issn = {1545-9993},
	url = {http://www.nature.com/nsmb/journal/v20/n1/full/nsmb.2481.html},
	doi = {10.1038/nsmb.2481},
	abstract = {The Sixth International Conference on Hsp90 in 2012 revealed new functions of this key molecular chaperone. Attendees of the meeting at Les Diablerets, Switzerland, addressed new discoveries about Hsp90 and its cochaperones.},
	language = {en},
	number = {1},
	urldate = {2013-10-14},
	journal = {Nature Structural \& Molecular Biology},
	author = {Chiosis, Gabriela and Dickey, Chad A. and Johnson, Jill L.},
	month = jan,
	year = {2013},
	pages = {1--4},
	file = {Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/TFHNDMCV/nsmb.2481.html:text/html}
}
@article{liu2013,
	title = {Overexpression of small heat shock protein 21 protects the Chinese oak silkworm Antheraea pernyi against thermal stress},
	volume = {59},
	issn = {0022-1910},
	url = {http://www.sciencedirect.com/science/article/pii/S0022191013001339},
	doi = {10.1016/j.jinsphys.2013.06.001},
	abstract = {Abstract
Small heat shock proteins ({sHSPs)} usually act as molecular chaperones to prevent proteins from being denatured in extreme conditions. We first report the {sHSP21} gene, named as Ap-{sHSP21}, in the Chinese oak silkworm Antheraea pernyi (Lepidoptera: Saturniidae). The full-length {cDNA} of Ap-{sHSP21} is 976 bp, including a 5′-untranslated region ({UTR)} of 99 bp, a 3′-{UTR} of 316 bp and an open reading frame ({ORF)} of 561 bp encoding a polypeptide of 186 amino acids. The deduced A. pernyi {sHSP21} protein sequence reveals the percent identity is 82–93\% in comparison to other {sHSPs} from insects. Real-time quantitative reverse transcription-{PCR} ({qRT-PCR)} analysis shows that Ap-{sHSP21} expression is higher in testis than that in other examined tissues and significantly up-regulated after heat shock. In addition, prokaryotic expression and purification of the Ap-{sHSP21} protein were performed. {SDS–PAGE} and Western blot analysis demonstrated that a 25 {kDa} recombinant protein was successfully expressed in Escherichia coli cells and the purified recombinant protein was also confirmed to protect restriction enzymes from thermal inactivation. The expression of Ap-{sHSP21} was significantly down-regulated after {RNA} interference, which was confirmed by {qRT-PCR} and Western blot analysis. All together, these results suggest that Ap-{sHSP21} play a key role in thermal tolerance.},
	number = {8},
	urldate = {2013-10-14},
	journal = {Journal of Insect Physiology},
	author = {Liu, Qiu-Ning and Zhu, Bao-Jian and Dai, Li-Shang and Fu, Wei-Wei and Lin, Kun-Zhang and Liu, Chao-Liang},
	month = aug,
	year = {2013},
	keywords = {Antheraea pernyi, Expression, Heat shock protein, Temperature},
	pages = {848--854},
	file = {Liu et al. - 2013 - Overexpression of small heat shock protein 21 prot.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/9HGJRK3E/Liu et al. - 2013 - Overexpression of small heat shock protein 21 prot.pdf:application/pdf;ScienceDirect Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/586PESUC/S0022191013001339.html:text/html}
}
@article{andersen2006,
	title = {Dopamine levels in the mosquito Aedes aegypti during adult development, following blood feeding and in response to heat stress},
	volume = {52},
	issn = {0022-1910},
	url = {http://www.sciencedirect.com/science/article/pii/S0022191006001545},
	doi = {10.1016/j.jinsphys.2006.08.004},
	abstract = {Dopamine, a catecholamine neurotransmitter, is important for insect development and is known to be involved in insect stress responses. In the current study, dopamine was analysed in Aedes aegypti heads by {HPLC.} We found that immediately after adult emergence, males have significantly higher concentrations of dopamine than females, and that dopamine concentrations decrease with age in both sexes. Dopamine levels increase in females following a blood meal suggesting that dopamine might be involved in ovarian- and/or egg-development. We also found that female mosquitoes have a higher tolerance to a short term thermal stress in a water bath than males up to 44 {°C}, however, both sexes die if exposed to short term temperatures between 44 and 45 {°C.} Finally, we did not find any indication that dopamine levels were associated with short time thermal stress response in female mosquitoes.},
	number = {11–12},
	urldate = {2013-08-15},
	journal = {Journal of Insect Physiology},
	author = {Andersen, Janne Pleidrup and Schwartz, Alex and Gramsbergen, Jan Bert and Loeschcke, Volker},
	month = nov,
	year = {2006},
	keywords = {Ecdysone, {HPLC}, Juvenile hormone, Stress response, Thermal limits},
	pages = {1163--1170},
	file = {Andersen et al, 2006.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/362XPBK5/Andersen et al, 2006.pdf:application/pdf;ScienceDirect Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/44UU7UH7/S0022191006001545.html:text/html}
}
@article{armstrong2012,
	title = {Cold hardening modulates K+ homeostasis in the brain of \textit{Drosophila melanogaster} during chill coma},
	volume = {58},
	issn = {0022-1910},
	url = {http://www.sciencedirect.com/science/article/pii/S0022191012002338},
	doi = {10.1016/j.jinsphys.2012.09.006},
	abstract = {Environmental temperature is one of the most important abiotic factors affecting insect behaviour; virtually all physiological processes, including those which regulate nervous system function, are affected. At both low and high temperature extremes insects enter a coma during which individuals do not display behaviour and are unresponsive to stimulation. We investigated neurophysiological correlates of chill and hyperthermic coma in Drosophila melanogaster. Coma resulting from anoxia causes a profound loss of K+ homeostasis characterized by a surge in extracellular K+ concentration ([K+]o) in the brain. We recorded [K+]o in the brain during exposure to both low and high temperatures and observed a similar surge in [K+]o which recovered to baseline concentrations following return to room temperature. We also found that rapid cold hardening ({RCH)} using a cold pretreatment (4 {°C} for 2 h; 2 h recovery at room temperature) increased the peak brain [K+]o reached during a subsequent chill coma and increased the rates of accumulation and clearance of [K+]o. We conclude that {RCH} preserves K+ homeostasis in the fly brain during exposure to cold by reducing the temperature sensitivity of the rates of homeostatic processes.},
	number = {11},
	urldate = {2013-10-14},
	journal = {Journal of Insect Physiology},
	author = {Armstrong, Gary {A.B.} and Rodríguez, Esteban C. and Meldrum Robertson, R.},
	month = nov,
	year = {2012},
	keywords = {Anoxic coma, Chill coma, Drosophila, Environmental stress, Hypothermic coma, K+ homeostasis, Spreading depression},
	pages = {1511--1516},
	file = {ScienceDirect Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/VAJVVJCP/Armstrong et al. - 2012 - Cold hardening modulates K+ homeostasis in the bra.pdf:application/pdf;ScienceDirect Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/7DUEUUC3/S0022191012002338.html:text/html}
}
@article{ananthan1986,
	title = {Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes},
	volume = {232},
	issn = {0036-8075, 1095-9203},
	url = {http://www.sciencemag.org/content/232/4749/522},
	doi = {10.1126/science.3083508},
	language = {en},
	issue = {4749},
	pages = {522-524},
	journaltitle = {Science},
	shortjournal = {Science},
	author = {Ananthan, J. and Goldberg, A. L. and Voellmy, R.},
	urldate = {2013-11-04},
	date = {1986-04-25},
	note = {{PMID:} 3083508},
	file = {Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/6IAETT6Z/522.html:text/html}
}
@article{voellmy2004,
	title = {On mechanisms that control heat shock transcription factor activity in metazoan cells},
	volume = {9},
	issn = {1355-8145, 1466-1268},
	url = {http://www.ncbi.nlm.nih.gov.gate1.inist.fr/pmc/articles/PMC1065292/},
	doi = {10.1379/CSC-14R.1},
	issue = {2},
	pages = {122},
	journaltitle = {Cell Stress \& Chaperones},
	author = {Voellmy, Richard},
	urldate = {2013-11-04},
	date = {2004},
	file = {On mechanisms that control heat shock transcription factor activity in metazoan cells:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/P8G4Q3RU/PMC1065292.html:text/html}
}
@article{meadows2013,
	title = {Hardship Strengthens Mutual Bonds},
	volume = {11},
	url = {http://dx.doi.org/10.1371/journal.pbio.1001706},
	doi = {10.1371/journal.pbio.1001706},
	issue = {11},
	pages = {e1001706},
	journaltitle = {{PLoS} Biol},
	shortjournal = {{PLoS} Biol},
	author = {Meadows, Robin},
	urldate = {2013-11-06},
	date = {2013-11-05},
	file = {PLoS Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/JFEJTJ9U/Meadows - 2013 - Hardship Strengthens Mutual Bonds.pdf:application/pdf;PLoS Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/5D6RKHRD/journal.pbio.html:text/html}
}
@article{russell2006,
	title = {Costs and benefits of symbiont infection in aphids: variation among symbionts and across temperatures},
	volume = {273},
	issn = {0962-8452},
	doi = {10.1098/rspb.2005.3348},
	shorttitle = {Costs and benefits of symbiont infection in aphids},
	language = {eng},
	issue = {1586},
	pages = {603-610},
	journaltitle = {Proceedings. Biological sciences / The Royal Society},
	shortjournal = {Proc. Biol. Sci.},
	author = {Russell, Jacob A and Moran, Nancy A},
	date = {2006-03-07},
	note = {{PMID:} 16537132},
	keywords = {Animals, Aphids, Enterobacteriaceae, Female, Fertility, Logistic Models, Serratia, symbiosis, Temperature},
	file = {Russell et Moran - 2006 - Costs and benefits of symbiont infection in aphids.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/7I6J6E92/Russell et Moran - 2006 - Costs and benefits of symbiont infection in aphids.pdf:application/pdf}
}
@article{bordenstein2011,
	title = {Temperature Affects the Tripartite Interactions between Bacteriophage {WO}, \textit{Wolbachia}, and Cytoplasmic Incompatibility},
	volume = {6},
	url = {http://dx.doi.org/10.1371/journal.pone.0029106},
	doi = {10.1371/journal.pone.0029106},
	issue = {12},
	pages = {e29106},
	journaltitle = {{PLoS} {ONE}},
	shortjournal = {{PLoS} {ONE}},
	author = {Bordenstein, Sarah R. and Bordenstein, Seth R.},
	urldate = {2013-11-12},
	date = {2011-12-15},
	file = {Bordenstein et Bordenstein - 2011 - Temperature Affects the Tripartite Interactions be.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/82MPUD2U/Bordenstein et Bordenstein - 2011 - Temperature Affects the Tripartite Interactions be.pdf:application/pdf;PLoS Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/7C7Q87KC/journal.pone.html:text/html}
}
@article{tissieres1974,
	title = {Protein synthesis in salivary glands of \textit{Drosophila melanogaster}: Relation to chromosome puffs},
	volume = {84},
	issn = {0022-2836},
	url = {http://www.sciencedirect.com/science/article/pii/0022283674904471},
	doi = {10.1016/0022-2836(74)90447-1},
	shorttitle = {Protein synthesis in salivary glands of Drosophila melanogaster},
	issue = {3},
	pages = {389-398},
	journaltitle = {Journal of Molecular Biology},
	shortjournal = {Journal of Molecular Biology},
	author = {Tissiéres, Alfred and Mitchell, Herschel K. and Tracy, Ursula M.},
	urldate = {2013-11-17},
	date = {1974-04-15},
	file = {ScienceDirect Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/GT4XG2P8/0022283674904471.html:text/html}
}
@article{kampinga2009,
	title = {Guidelines for the nomenclature of the human heat shock proteins},
	volume = {14},
	issn = {1355-8145, 1466-1268},
	url = {http://link.springer.com/article/10.1007/s12192-008-0068-7},
	doi = {10.1007/s12192-008-0068-7},
	language = {en},
	issue = {1},
	pages = {105-111},
	journaltitle = {Cell Stress and Chaperones},
	shortjournal = {Cell Stress and Chaperones},
	author = {Kampinga, Harm H. and Hageman, Jurre and Vos, Michel J. and Kubota, Hiroshi and Tanguay, Robert M. and Bruford, Elspeth A. and Cheetham, Michael E. and Chen, Bin and Hightower, Lawrence E.},
	urldate = {2013-11-17},
	date = {2009},
	keywords = {Biochemistry, general, Biomedicine general, Cancer Research, Cell Biology, Human heat shock proteins, Immunology, Nomenclature},
	file = {Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/9NX8X8X3/s12192-008-0068-7.html:text/html}
}
@article{gupta1995,
	title = {Evolution of the chaperonin families ({HSP60}, {HSP} 10 and {TCP-1)} of proteins and the origin of eukaryotic cells},
	volume = {15},
	issn = {1365-2958},
	url = {http://onlinelibrary.wiley.com.gate1.inist.fr/doi/10.1111/j.1365-2958.1995.tb02216.x/abstract},
	doi = {10.1111/j.1365-2958.1995.tb02216.x},
	language = {en},
	issue = {1},
	pages = {1–11},
	journaltitle = {Molecular Microbiology},
	author = {Gupta, Radhey S.},
	urldate = {2013-11-18},
	date = {1995},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/TBX7CR92/Gupta - 1995 - Evolution of the chaperonin families (HSP60, HSP 1.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/9DVUA46H/abstract.html:text/html}
}
@article{dillondillon,
	title = {The gut bacteria of insects: Nonpathogenic Interactions},
	volume = {49},
	url = {http://www.annualreviews.org/doi/abs/10.1146/annurev.ento.49.061802.123416},
	doi = {10.1146/annurev.ento.49.061802.123416},
	shorttitle = {{THE} {GUT} {BACTERIA} {OF} {INSECTS}},
	issue = {1},
	pages = {71-92},
	journaltitle = {Annual Review of Entomology},
	author = {Dillon, {R.J.} and Dillon, {V.M.}},
	urldate = {2013-06-13},
	date = {2004},
	note = {{PMID:} 14651457},
	keywords = {intestine, microbiota, multitrophic, mutualism, symbiosis},
	file = {Dillon et Dillon - 2004 - The gut bacteria of insects Nonpathogenic Interac.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/PTWJ37C9/Dillon et Dillon - 2004 - The gut bacteria of insects Nonpathogenic Interac.pdf:application/pdf}
}
@article{sharon2010,
	title = {Commensal bacteria play a role in mating preference of \textit{Drosophila melanogaster}},
	volume = {107},
	issn = {0027-8424, 1091-6490},
	url = {http://www.pnas.org/content/107/46/20051},
	doi = {10.1073/pnas.1009906107},
	language = {en},
	issue = {46},
	pages = {20051-20056},
	journaltitle = {Proceedings of the National Academy of Sciences},
	shortjournal = {{PNAS}},
	author = {Sharon, Gil and Segal, Daniel and Ringo, John M. and Hefetz, Abraham and Zilber-Rosenberg, Ilana and Rosenberg, Eugene},
	urldate = {2013-11-21},
	date = {2010-11-16},
	note = {{PMID:} 21041648},
	keywords = {holobiont, hologenome, Lactobacillus, microbiota, symbiosis},
	file = {Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/5BCPB3S9/20051.html:text/html}
}
@article{tsuchida2010,
  title={Symbiotic bacterium modifies aphid body color},
  author={Tsuchida, Tsutomu and Koga, Ryuichi and Horikawa, Mitsuyo and Tsunoda, Tetsuto and Maoka, Takashi and Matsumoto, Shogo and Simon, Jean-Christophe and Fukatsu, Takema},
  journal={Science},
  volume={330},
  number={6007},
  pages={1102--1104},
  year={2010},
  publisher={American Association for the Advancement of Science}
}

@inbook{ryan1996,
	title = {Stress proteins as molecular biomarkers for environmental toxicology},
	rights = {©1996 Birkhäuser Basel},
	isbn = {978-3-0348-9901-7, 978-3-0348-9088-5},
	url = {http://link.springer.com/chapter/10.1007/978-3-0348-9088-5_28},
	language = {en},
	pages = {411-424},
	number = {77},
	booktitle = {Stress-Inducible Cellular Responses},
	series = {{EXS}},
	publisher = {Birkhäuser Basel},
	author = {Ryan, J. A. and Hightower, L. E.},
	editor = {Feige, Dr U. and Yahara, Dr I. and Morimoto, Dr R. I. and Polla, Dr B. S.},
	urldate = {2013-11-21},
	date = {1996},
	keywords = {Biomedicine general, Life Sciences, general},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/CA8AK4FK/Ryan et Hightower - 1996 - Stress proteins as molecular biomarkers for enviro.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/7GXQAX56/978-3-0348-9088-5_28.html:text/html}
}
@article{feder1997,
	title = {Natural thermal stress and heat-shock protein expression in \textit{Drosophila} larvae and pupae},
	volume = {11},
	rights = {1997 British Ecological Society},
	issn = {1365-2435},
	url = {http://onlinelibrary.wiley.com.gate1.inist.fr/doi/10.1046/j.1365-2435.1997.00060.x/abstract},
	doi = {10.1046/j.1365-2435.1997.00060.x},
	language = {en},
	issue = {1},
	pages = {90–100},
	journaltitle = {Functional Ecology},
	author = {Feder, M. E. and Blair, N. and Figueras, H.},
	urldate = {2013-11-21},
	date = {1997},
	keywords = {Heat-shock response, hsp 70, lethal temperature, molecular chaperone, thermotolerance},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/X6B9CXZ5/Feder et al. - 1997 - Natural thermal stress and heat-shock protein expr.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/5UPH2KDI/full.html:text/html}
}

@article{colinet2007,
	title = {Proteomic profiling of a parasitic wasp exposed to constant and fluctuating cold exposure},
	volume = {37},
	issn = {0965-1748},
	url = {http://www.sciencedirect.com/science/article/pii/S0965174807001713},
	doi = {10.1016/j.ibmb.2007.07.004},
	issue = {11},
	pages = {1177-1188},
	journaltitle = {Insect Biochemistry and Molecular Biology},
	shortjournal = {Insect Biochemistry and Molecular Biology},
	author = {Colinet, Hervé and Nguyen, Thi Thuy An and Cloutier, Conrad and Michaud, Dominique and Hance, Thierry},
	urldate = {2013-11-21},
	date = {2007-11},
	keywords = {Chill injuries, cold stress, parasitoid, Proteomics, recovery},
	file = {Colinet et al. - 2007 - Proteomic profiling of a parasitic wasp exposed to.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/KABH69IM/Colinet et al. - 2007 - Proteomic profiling of a parasitic wasp exposed to.pdf:application/pdf;ScienceDirect Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/VS9CTNZF/S0965174807001713.html:text/html}
}
@article{hirashima2000,
	title = {Biogenic Amines in \textit{Drosophila virilis} under Stress Conditions},
	volume = {64},
	issue = {12},
	pages = {2625-2630},
	journaltitle = {Bioscience, Biotechnology, and Biochemistry},
	author = {Hirashima, Akinori and Sukhanova, Madina Jh and Rauschenbach, Inga Yu},
	date = {2000},
	keywords = {biogenic amine, Drosophila virilis, heat stress, line 101, line 147},
	file = {Jstage - Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/R2ACFDHQ/Hirashima et al. - 2000 - Biogenic Amines in iDrosophila virilisi under.pdf:application/pdf}
}
@article{malmendal2006,
	title = {Metabolomic profiling of heat stress: hardening and recovery of homeostasis in \textit{Drosophila}},
	volume = {291},
	rights = {Copyright © 2006 the American Physiological Society},
	url = {http://ajpregu.physiology.org/content/291/1/R205},
	doi = {10.1152/ajpregu.00867.2005},
	shorttitle = {Metabolomic profiling of heat stress},
	language = {en},
	issue = {1},
	pages = {R205-R212},
	journaltitle = {American Journal of Physiology - Regulatory, Integrative and Comparative Physiology},
	author = {Malmendal, Anders and Overgaard, Johannes and Bundy, Jacob G. and Sørensen, Jesper G. and Nielsen, Niels Chr and Loeschcke, Volker and Holmstrup, Martin},
	urldate = {2013-11-21},
	date = {2006},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/CSAG3DDR/Malmendal et al. - 2006 - Metabolomic profiling of heat stress hardening an.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/ZM88PSCT/R205.html:text/html}
}
@article{deitch1995,
	title = {Induction of heat shock gene expression in colonic epithelial cells after incubation with Escherichia coli or endotoxin},
	volume = {23},
	issn = {0090-3493},
	language = {eng},
	issue = {8},
	pages = {1371-1376},
	journaltitle = {Critical care medicine},
	shortjournal = {Crit. Care Med.},
	author = {Deitch, E A and Beck, S C and Cruz, N C and De Maio, A},
	date = {1995-08},
	note = {{PMID:} 7634807},
	keywords = {Adenocarcinoma, Colon, Colonic Neoplasms, Endotoxins, Epithelial Cells, Escherichia coli, Gene Expression Regulation, Heat-Shock Proteins, {HSP72} Heat-Shock Proteins, Humans, Phagocytosis, Time Factors, Tumor Cells, Cultured}
}
@article{feder1999,
	title = {Interaction of \textit{Drosophila} and Its Endosymbiont \textit{Wolbachia}: Natural Heat Shock and the Overcoming of Sexual Incompatibility},
	volume = {39},
	issn = {1540-7063, 1557-7023},
	url = {http://icb.oxfordjournals.org/content/39/2/363},
	doi = {10.1093/icb/39.2.363},
	shorttitle = {Interaction of Drosophila and Its Endosymbiont Wolbachia},
	language = {en},
	issue = {2},
	pages = {363-373},
	journaltitle = {American Zoologist},
	shortjournal = {Amer. Zool.},
	author = {Feder, Martin E. and Karr, Timothy L. and Yang, William and Hoekstra, Jonathan M. and James, Avis C.},
	urldate = {2013-11-22},
	date = {1999},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/M2R3SIFT/Feder et al. - 1999 - Interaction of Drosophila and Its Endosymbiont Wol.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/E94VW58U/363.html:text/html}
}
@article{lindquist1988,
	title = {The Heat-Shock Proteins},
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	url = {http://www.annualreviews.org/doi/abs/10.1146/annurev.ge.22.120188.003215},
	doi = {10.1146/annurev.ge.22.120188.003215},
	issue = {1},
	pages = {631-677},
	journaltitle = {Annual Review of Genetics},
	author = {Lindquist, S and Craig, E A},
	urldate = {2013-10-02},
	date = {1988},
	note = {{PMID:} 2853609},
	file = {LindquistCraig1988ARG.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/J8FAWZIH/LindquistCraig1988ARG.pdf:application/pdf}
}
@article{lindquist1986,
        title = {The Heat-Shock Response},
        volume = {55},
        url = {http://www.annualreviews.org/doi/abs/10.1146/annurev.bi.55.070186.005443},
        doi = {10.1146/annurev.bi.55.070186.005443},
        issue = {1},
        pages = {1151-1191},
        journaltitle = {Annual Review of Biochemistry},
        author = {Lindquist, S},
        urldate = {2013-10-02},
        date = {1986},
        note = {{PMID:} 2427013},
        file = {Lindquist - 1986 - The Heat-Shock Response.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/SGIPZ7ND/Lindquist - 1986 - The Heat-Shock Response.pdf:application/pdf}
}
@article{zhao2009,
	title = {Identification of Genes Differentially Expressed During Heat Shock Treatment in \textit{Aedes aegypti}},
	volume = {46},
	issn = {0022-2585},
	url = {http://www.bioone.org/doi/abs/10.1603/033.046.0312},
	doi = {10.1603/033.046.0312},
	issue = {3},
	pages = {490-495},
	journaltitle = {Journal of Medical Entomology},
	shortjournal = {Journal of Medical Entomology},
	author = {Zhao, Liming and Pridgeon, Julia W. and Becnel, James J. and Clark, Gary G. and Linthicum, Kenneth J.},
	urldate = {2013-08-15},
	date = {2009-05-01},
	file = {BioOne Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/6A4EGZ6R/033.046.html:text/html;Zhao et al. - 2009 - Identification of Genes Differentially Expressed D.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/AHK92VZP/Zhao et al. - 2009 - Identification of Genes Differentially Expressed D.pdf:application/pdf}
}
@article{somero2010,
	title = {The physiology of climate change: how potentials for acclimatization and genetic adaptation will determine "winners" and "losers"},
	volume = {213},
	issn = {0022-0949, 1477-9145},
	url = {http://jeb.biologists.org/content/213/6/912},
	doi = {10.1242/jeb.037473},
	shorttitle = {The physiology of climate change},
	language = {en},
	issue = {6},
	pages = {912-920},
	journaltitle = {The Journal of Experimental Biology},
	shortjournal = {J Exp Biol},
	author = {Somero, G. N.},
	urldate = {2013-11-25},
	date = {2010-03-15},
	note = {{PMID:} 20190116},
	keywords = {Acclimation, acclimatization, Adaptation, biogeography, climate change, extinction, Genome, global warming, intertidal zone, thermal adaptation},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/6797G87H/Somero - 2010 - The physiology of climate change how potentials f.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/8WCAWS6C/912.html:text/html}
}
@article{ritossa1962,
	title = {A new puffing pattern induced by temperature shock and {DNP} in drosophila},
	volume = {18},
	issn = {0014-4754, 1420-9071},
	url = {http://link.springer.com/article/10.1007/BF02172188},
	doi = {10.1007/BF02172188},
	language = {en},
	issue = {12},
	pages = {571-573},
	journaltitle = {Experientia},
	shortjournal = {Experientia},
	author = {Ritossa, F.},
	urldate = {2013-11-25},
	date = {1962-12-01},
	keywords = {Biochemistry, general, Biomedicine general, Cell Biology, Life Sciences, general},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/VMA5SURD/Ritossa - 1962 - A new puffing pattern induced by temperature shock.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/WQWXSW9V/BF02172188.html:text/html}
}

@article{ritossa1996,
	title = {Discovery of the heat shock response},
	volume = {1},
	url = {/pmc/articles/PMC248460/?report=abstract},
	language = {en},
	issue = {2},
	pages = {97},
	journaltitle = {Cell Stress \& Chaperones},
	author = {Ritossa, Ferruccio},
	urldate = {2013-11-25},
	date = {1996-06},
	note = {{PMID:} 9222594},
	file = {Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/42HGPWVB/PMC248460.html:text/html}
}
@article{clark2008,
	title = {How insects survive the cold: molecular mechanisms—a review},
	volume = {178},
	issn = {0174-1578, 1432-{136X}},
	url = {http://link.springer.com/10.1007/s00360-008-0286-4},
	doi = {10.1007/s00360-008-0286-4},
	shorttitle = {How insects survive the cold},
	issue = {8},
	pages = {917-933},
	journaltitle = {Journal of Comparative Physiology B},
	author = {Clark, Melody S. and Worland, M. Roger},
	urldate = {2013-11-10},
	date = {2008-06-27},
	file = {Clark et Worland - 2008 - How insects survive the cold molecular mechanisms.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/TV4PTP7J/Clark et Worland - 2008 - How insects survive the cold molecular mechanisms.pdf:application/pdf}
}
@article{neven2000,
	title = {Physiological responses of insects to heat},
	volume = {21},
	issn = {0925-5214},
	url = {http://www.sciencedirect.com/science/article/pii/S0925521400001691},
	doi = {10.1016/S0925-5214(00)00169-1},
	issue = {1},
	pages = {103-111},
	journaltitle = {Postharvest Biology and Technology},
	shortjournal = {Postharvest Biology and Technology},
	author = {Neven, Lisa G},
	urldate = {2013-11-26},
	date = {2000-12},
	keywords = {heat, heat shock, Insects, Metabolism, Respiration},
	file = {ScienceDirect Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/7DN9FJAQ/Neven - 2000 - Physiological responses of insects to heat.pdf:application/pdf;ScienceDirect Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/PVVVPQFE/S0925521400001691.html:text/html}
}
@article{hendrix1998,
	title = {Polyol metabolism in homopterans at high temperatures: accumulation of mannitol in aphids (Aphididae: Homoptera) and sorbitol in whiteflies (Aleyrodidae: Homoptera)},
	volume = {120},
	issn = {1095-6433},
	url = {http://www.sciencedirect.com/science/article/pii/S1095643398100582},
	doi = {10.1016/S1095-6433(98)10058-2},
	shorttitle = {Polyol metabolism in homopterans at high temperatures},
	issue = {3},
	pages = {487-494},
	journaltitle = {Comparative Biochemistry and Physiology Part A: Molecular \& Integrative Physiology},
	shortjournal = {Comparative Biochemistry and Physiology Part A: Molecular \& Integrative Physiology},
	author = {Hendrix, Donald L and Salvucci, Michael E},
	urldate = {2013-11-26},
	date = {1998-07-01},
	keywords = {Aphids, Honeydew, Ketose reductase, Mannitol dehydrogenase, Sorbitol dehydrogenase, Thermoprotection, Whiteflies},
	file = {ScienceDirect Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/BNF8S6XG/Hendrix et Salvucci - 1998 - Polyol metabolism in homopterans at high temperatu.pdf:application/pdf;ScienceDirect Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/EBCV8REJ/S1095643398100582.html:text/html}
}
@inproceedings{rosenberg2008,
  title={From bacterial bleaching to the hologenome theory of evolution},
  author={Rosenberg, E and Zilber-Rosenberg, I},
  booktitle={11th International Coral Reef Symposium},
  year={2008}
}
@article{burke2011,
	title = {Responses of the pea aphid transcriptome to infection by facultative symbionts},
	volume = {20},
	rights = {© 2011 The Authors. Insect Molecular Biology © 2011 The Royal Entomological Society},
	issn = {1365-2583},
	url = {http://onlinelibrary.wiley.com.gate1.inist.fr/doi/10.1111/j.1365-2583.2011.01070.x/abstract},
	doi = {10.1111/j.1365-2583.2011.01070.x},
	language = {en},
	issue = {3},
	pages = {357–365},
	journaltitle = {Insect Molecular Biology},
	author = {Burke, G. R. and Moran, N. A.},
	urldate = {2013-11-21},
	date = {2011},
	keywords = {Acyrthosiphon pisum, immunity, pea aphid, Serratia symbiotica, Symbiont, transcriptome},
	file = {Burke et Moran - 2011 - Responses of the pea aphid transcriptome to infect.pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/RS9RGKP7/Burke et Moran - 2011 - Responses of the pea aphid transcriptome to infect.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/4Q8JWRIR/abstract.html:text/html}
}
@article{burke2009,
	title = {Effects of facultative symbionts and heat stress on the metabolome of pea aphids},
	volume = {4},
	rights = {© 2009 Nature Publishing Group},
	issn = {1751-7362},
	url = {http://www.nature.com.gate1.inist.fr/ismej/journal/v4/n2/abs/ismej2009114a.html},
	doi = {10.1038/ismej.2009.114},
	language = {en},
	issue = {2},
	pages = {242-252},
	journaltitle = {The {ISME} Journal},
	shortjournal = {{ISME} J},
	author = {Burke, Gaelen and Fiehn, Oliver and Moran, Nancy},
	urldate = {2013-11-26},
	date = {2009-11-12},
	keywords = {facultative symbiont, heat-shock, metabolomics, Serratia symbiotica},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/W7DFCUXV/Burke et al. - 2009 - Effects of facultative symbionts and heat stress o.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/8FV4SHDZ/ismej2009114a.html:text/html}
}
@article{zhao2012,
  title={Expression of heat shock protein genes in insect stress responses},
  author={Zhao, Liming and Jones, WA},
  journal={Invertebrate Survival Journal},
  volume={9},
  pages={93--101},
  year={2012}
}
@book{ecoloboek,
	title={Écologie},
	author={Ricklefs, Robert E. and Miller, Garry L.},
	publisher={De Boeck},
	year={2005}
}
@article{salvucci2000,
	title = {Heat shock proteins in whiteflies, an insect that accumulates sorbitol in response to heat stress},
	volume = {25},
	issn = {0306-4565},
	url = {http://www.sciencedirect.com/science/article/pii/S0306456599001084},
	doi = {10.1016/S0306-4565(99)00108-4},
	issue = {5},
	pages = {363-371},
	journaltitle = {Journal of Thermal Biology},
	shortjournal = {Journal of Thermal Biology},
	author = {Salvucci, Michael E. and Stecher, Dawn S. and Henneberry, Thomas J.},
	urldate = {2013-11-25},
	date = {2000-10-01},
	keywords = {Bemisia, heat shock proteins, heat stress, hsp, Polyols, Sorbitol, thermotolerance},
	file = {Salvucci et al. - 2000 - Heat shock proteins in whiteflies, an insect that .pdf:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/RDEA723C/Salvucci et al. - 2000 - Heat shock proteins in whiteflies, an insect that .pdf:application/pdf;ScienceDirect Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/3RZFTIMM/S0306456599001084.html:text/html}
}
@article{nakaminami2006,
	title = {Functional conservation of cold shock domains in bacteria and higher plants},
	volume = {103},
	issn = {0027-8424, 1091-6490},
	url = {http://www.pnas.org/content/103/26/10122},
	doi = {10.1073/pnas.0603168103},
	language = {en},
	issue = {26},
	pages = {10122-10127},
	journaltitle = {Proceedings of the National Academy of Sciences},
	shortjournal = {{PNAS}},
	author = {Nakaminami, Kentaro and Karlson, Dale T. and Imai, Ryozo},
	urldate = {2013-11-30},
	date = {2006-06-27},
	note = {{PMID:} 16788067},
	keywords = {cold acclimation, cold shock protein, {RNA} binding, {RNA} chaperone, wheat},
	file = {Full Text PDF:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/TUQ8NUHD/Nakaminami et al. - 2006 - Functional conservation of cold shock domains in b.pdf:application/pdf;Snapshot:/home/ego/.mozilla/firefox/e94dk8of.default/zotero/storage/9ZHBEH4N/10122.html:text/html}
}


text:
// © 2016-2017 Helix OpCo LLC. All rights reserved.
// Initial Author: Chris Williams

/*
This package assists with chaining together providers by providing default implementations for
LogProvider interface methods that don't panic if we're the last in the chain.
*/
package chaining

import (
	"github.com/myhelix/contextlogger/providers"

	"context"
)

type provider struct {
	nextProvider providers.LogProvider
}

func LogProvider(nextProvider providers.LogProvider) providers.LogProvider {
	return provider{nextProvider}
}

func (p provider) Error(ctx context.Context, report bool, args ...interface{}) {
	if p.nextProvider != nil {
		p.nextProvider.Error(ctx, report, args...)
	}
}

func (p provider) Warn(ctx context.Context, report bool, args ...interface{}) {
	if p.nextProvider != nil {
		p.nextProvider.Warn(ctx, report, args...)
	}
}

func (p provider) Info(ctx context.Context, report bool, args ...interface{}) {
	if p.nextProvider != nil {
		p.nextProvider.Info(ctx, report, args...)
	}
}

func (p provider) Debug(ctx context.Context, report bool, args ...interface{}) {
	if p.nextProvider != nil {
		p.nextProvider.Debug(ctx, report, args...)
	}
}

func (p provider) Record(ctx context.Context, metrics map[string]interface{}) {
	if p.nextProvider != nil {
		p.nextProvider.Record(ctx, metrics)
	}
}

func (p provider) RecordEvent(ctx context.Context, eventName string, metrics map[string]interface{}) {
	if p.nextProvider != nil {
		p.nextProvider.RecordEvent(ctx, eventName, metrics)
	}
}

func (p provider) Wait() {
	if p.nextProvider != nil {
		p.nextProvider.Wait()
	}
}

license: MIT

repository: myhelix/contextlogger

license_type: permissive

repo_name: myhelix/contextlogger

branch_name: refs/heads/master

gha_license_id: MIT

gha_language: Go

extension: go


text:
DESCRIPTION = "g-tracer is a gsignal run-time inspection and debugging utility"
HOMEPAGE = "http://sf.net/project/gtracer"
SECTION = "x11/devel"
LICENSE = "BSD"
DEPENDS = "glib-2.0 gtk+ intltool-native"

SRC_URI = "${SOURCEFORGE_MIRROR}/gtracer/gtracer-${PV}.tar.bz2"

inherit autotools

SRC_URI[md5sum] = "8f21636a60ed57265feb34806ffe4b00"
SRC_URI[sha256sum] = "ce2a88a784c73d49b3600b5927f65624f665460684dc4b479989ad1c53e565c5"

repository: overo/overo-oe-natty

repo_name: overo/overo-oe-natty

branch_name: HEAD

extension: bb


text:
@misc{miller2014anonymous,
  title={Anonymous byzantine consensus from moderately-hard puzzles: A model for bitcoin},
  author={Miller, Andrew and LaViola Jr, Joseph J},
  url={https://nakamotoinstitute.org/static/docs/anonymous-byzantine-consensus.pdf},
  year={2014}
}

@misc{monerocrusher2019,
  title={Analysis: More than 85\% of the current Monero Hashrate is ASICs and each machine is doing 128 kh/s},
  author={MoneroCrusher},
  url={https://medium.com/@MoneroCrusher/analysis-more-than-85-of-the-current-monero-hashrate-is-asics-and-each-machine-is-doing-128-kh-s-f39e3dca7d78},
  year={2019}
}

@misc{aliaga2018,
  title={Deep Diving into Ethereum Mining Pools},
  author={Aliaga, Matthias De},
  url={https://medium.com/tokenanalyst/deep-diving-into-ethereum-mining-pools-1d51848223b7},
  year={2018}
}

@misc{sinnige2018,
  title={Blockchain: how a 51\% attack works (double spend attack)},
  author={Sinnige, Jimi},
  url={https://medium.com/coinmonks/what-is-a-51-attack-or-double-spend-attack-aa108db63474},
  year={2018}
}

@misc{ethereum1,
  title={What are the benefits of proof of stake as opposed to proof of work?},
  author={Ethereum},
  url={https://github.com/ethereum/wiki/wiki/Proof-of-Stake-FAQ\#what-are-the-benefits-of-proof-of-stake-as-opposed-to-proof-of-work}
}

@misc{ethereum2,
  title={What is the "nothing at stake" problem and how can it be fixed?},
  author={Ethereum},
  url={https://github.com/ethereum/wiki/wiki/Proof-of-Stake-FAQ#what-is-the-nothing-at-stake-problem-and-how-can-it-be-fixed}
}

@article{popov2016probabilistic,
  title={A probabilistic analysis of the nxt forging algorithm},
  author={Popov, Serguei},
  journal={Ledger},
  volume={1},
  pages={69--83},
  year={2016}
}

@misc{begichava2018,
  title={Fair Proof of Stake},
  author={Begichava, A and Kofman, A},
  url={https://forum.wavesplatform.com/uploads/default/original/1X/b9f220c13f73c3a41dff7f4523c6c4a1fc03ebf6.pdf},
  year={2018},
}

@article{brown2018formal,
  title={Formal barriers to longest-chain proof-of-stake protocols},
  author={Brown-Cohen, Jonah and Narayanan, Arvind and Psomas, Christos-Alexandros and Weinberg, S Matthew},
  journal={arXiv preprint arXiv:1809.06528},
  year={2018}
}

@misc{bitcointalk2011pos,
  title={Proof of stake instead of proof of work},
  author={QuantumMechanic},
  url={https://bitcointalk.org/index.php?topic=27787.0},
  year={2011}
}

@misc{king2012,
  title={PPCoin: Peer-to-Peer Crypto-Currency with Proof-of-Stake},
  author={King, Sunny and Nadal, Scott},
  url={https://decred.org/research/king2012.pdf},
  year={2012}
}

@misc{jepson2015,
  title={DTB001: Decred Technical Brief},
  author={Jepson, Christina},
  url={https://cryptorating.eu/whitepapers/Decred/decred.pdf},
  year={2015}
}

@misc{nakamoto2008,
  title={Bitcoin: A Peer-to-Peer Electronic Cash System},
  author={Nakamoto, Satoshi},
  url={https://bitcoin.org/bitcoin.pdf},
  year={2008}
}

@article{eyal2018majority,
  title={Majority is not enough: Bitcoin mining is vulnerable},
  author={Eyal, Ittay and Sirer, Emin G{\"u}n},
  journal={Communications of the ACM},
  volume={61},
  number={7},
  pages={95--102},
  year={2018},
  publisher={ACM}
}

@misc{bitfury2015,
  title={Proof of Stake versus Proof of Work},
  author={BitFury Group},
  url={https://bitfury.com/content/downloads/pos-vs-pow-1.0.2.pdf},
  year={2015}
}

@misc{pishro2016introduction,
  title={Introduction to probability, statistics, and random processes},
  author={Pishro-Nik, Hossein},
  year={2016},
  url={https://www.probabilitycourse.com/chapter11/11_1_3_merging_and_splitting_poisson_processes.php}
}

@misc{buterin_randomness,
  title={Validator Ordering and Randomness in PoS},
  author={Buterin, Vitalik}, url={https://vitalik.ca/files/randomness.html},
  journal={Vitalik Buterin's website}
}

@misc{ouroboros,
    author = {Aggelos Kiayias and Alexander Russell and Bernardo David and Roman Oliynykov},
    title = {Ouroboros: A Provably Secure Proof-of-Stake Blockchain Protocol},
    howpublished = {Cryptology ePrint Archive, Report 2016/889},
    year = {2016},
    note = {\url{https://eprint.iacr.org/2016/889}},
}

@article{BentovGM14,
  author    = {Iddo Bentov and
               Ariel Gabizon and
               Alex Mizrahi},
  title     = {Cryptocurrencies without Proof of Work},
  journal   = {CoRR},
  volume    = {abs/1406.5694},
  year      = {2014},
  url       = {http://arxiv.org/abs/1406.5694},
  archivePrefix = {arXiv},
  eprint    = {1406.5694},
  timestamp = {Mon, 13 Aug 2018 16:47:59 +0200},
  biburl    = {https://dblp.org/rec/bib/journals/corr/BentovGM14},
  bibsource = {dblp computer science bibliography, https://dblp.org}
}

@misc{buterin_plutocracy, title={Governance, Part 2: Plutocracy Is Still Bad}, url={https://vitalik.ca/general/2018/03/28/plutocracy.html}, journal={Governance, Part 2: Plutocracy Is Still Bad}, author={Buterin, Vitalik}, year={2018}, month={Mar}}

@misc{nxt_wiki, title={Forging}, url={https://nxtwiki.org/wiki/Forging}, journal={Forging - Nxt Wiki}}

repository: aionnetwork/unity

repo_name: aionnetwork/unity

gha_language: Jupyter Notebook

extension: bib


text:
package main

import (
	"encoding/json"
	"io"
	"io/ioutil"
	"log"
	"net/http"

	"github.com/julienschmidt/httprouter"
	"github.com/nickbirnberg/churner/common"
	"gopkg.in/mgo.v2/bson"
)

// GetAction gets an action
func GetAction(w http.ResponseWriter, r *http.Request, ps httprouter.Params) {
	w.Header().Set("Content-Type", "application/json; charset=UTF-8")

	id := ps.ByName("action")
	if !bson.IsObjectIdHex(id) {
		w.WriteHeader(http.StatusBadRequest)
		return
	}

	objectID := bson.ObjectIdHex(id)

	userAction := common.Action{}
	err := db.C("actions").FindId(objectID).One(&userAction)
	if err != nil {
		w.WriteHeader(http.StatusBadRequest)
		return
	}

	w.WriteHeader(http.StatusOK)
	json.NewEncoder(w).Encode(userAction)
}

// PostAction stores an action to the database
func PostAction(w http.ResponseWriter, r *http.Request, ps httprouter.Params) {
	w.Header().Set("Content-Type", "application/json; charset=UTF-8")

	body, err := ioutil.ReadAll(io.LimitReader(r.Body, 10e6))
	if err != nil {
		w.WriteHeader(http.StatusRequestEntityTooLarge)
		return
	}

	userAction := common.Action{}

	err = json.Unmarshal(body, &userAction)
	if err != nil {
		w.WriteHeader(422)
		return
	}

	userAction.ID = bson.NewObjectId()
	err = db.C("actions").Insert(userAction)
	if err != nil {
		log.Printf("could not store action: %v\n", err)
		w.WriteHeader(http.StatusInternalServerError)
		return
	}
	w.WriteHeader(http.StatusCreated)
}

repository: nickbirnberg/churner

repo_name: nickbirnberg/churner


text:
package encoding_test

import (
	"reflect"
	"testing"

	"github.com/ibllex/go-encoding"
)

type MockStruct struct {
	X int
}

func (s MockStruct) MockMethod() {}

type MockInterface interface {
	MockMethod()
}

var (
	structType                   = MockStruct{1}
	ptrStruct                    = &MockStruct{2}
	emptyIface     interface{}   = MockStruct{3}
	iface1         MockInterface = MockStruct{4}
	sliceStruct                  = []MockStruct{{5}, {6}, {7}}
	ptrSliceStruct               = []*MockStruct{{8}, {9}, {10}}

	valueMap = map[string]interface{}{
		"bytes":          []byte{0x61, 0x62, 0x63, 0x64},
		"string":         "string",
		"bool":           true,
		"int":            5,
		"int8":           int8(5),
		"int16":          int16(5),
		"int32":          int32(5),
		"int64":          int64(5),
		"uint":           uint(5),
		"uint8":          uint8(5),
		"uint16":         uint16(5),
		"uint32":         uint32(5),
		"uint64":         uint64(5),
		"float32":        float32(5),
		"float64":        float64(5),
		"array":          [5]int{1, 2, 3, 4, 5},
		"slice":          []int{1, 2, 3, 4, 5},
		"emptyIf":        emptyIface,
		"Iface1":         iface1,
		"map":            map[string]string{"foo": "bar"},
		"ptrStruct":      ptrStruct,
		"structType":     structType,
		"sliceStruct":    sliceStruct,
		"ptrSliceStruct": ptrSliceStruct,
	}
)

func TestRoundTrip(t *testing.T) {
	compressor := encoding.NewGzipCompressor()

	codecs := map[string]encoding.Codec{
		"gob":     encoding.NewGobCodec(compressor),
		"msgpack": encoding.NewMsgPackCodec(compressor),
		"json":    encoding.NewJsonCodec(compressor),
	}

	for name, codec := range codecs {
		for _, expected := range valueMap {
			bytes, err := codec.Marshal(expected)
			if err != nil {
				t.Error(err)
				continue
			}

			ptrActual := reflect.New(reflect.TypeOf(expected)).Interface()
			err = codec.Unmarshal(bytes, ptrActual)
			if err != nil {
				t.Error(err)
				continue
			}

			actual := reflect.ValueOf(ptrActual).Elem().Interface()
			if !reflect.DeepEqual(expected, actual) {
				t.Errorf("[%s] (expected) %T %v != %T %v (actual)", name, expected, expected, actual, actual)
			}
		}

	}
}

repository: ibllex/go-encoding

repo_name: ibllex/go-encoding

branch_name: refs/heads/main