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Linked References

1. K. Yamanaka, L. Fang, and M. Inouye, “The CspA family in Escherichia coli: multiple gene duplication for stress adaptation,” Molecular Microbiology, vol. 27, no. 2, pp. 247–255, 1998. View at Publisher · View at Google Scholar
2. F. Narberhaus, T. Waldminghaus, and S. Chowdhury, “RNA thermometers,” FEMS Microbiology Reviews, vol. 30, no. 1, pp. 3–16, 2006. View at Publisher · View at Google Scholar · View at PubMed
3. R. Hurme and M. Rhen, “Temperature sensing in bacterial gene regulation—what it all boils down to,” Molecular Microbiology, vol. 30, no. 1, pp. 1–6, 1998. View at Publisher · View at Google Scholar
4. L. Ramos, “Scaling with temperature and concentration of the nonlinear rheology of a soft hexagonal phase,” Physical Review E, vol. 64, no. 6, Article ID 061502, 7 pages, 2001. View at Publisher · View at Google Scholar
5. P. G. Lemaux, S. L. Herendeen, P. L. Bloch, and F. C. Neidhardt, “Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts,” Cell, vol. 13, no. 3, pp. 427–434, 1978. View at Publisher · View at Google Scholar
6. J. R. Hazel, “Thermal adaptation in biological membranes: is homeoviscous adaptation the explanation?,” Annual Review of Physiology, vol. 57, pp. 19–42, 1995. View at Publisher · View at Google Scholar · View at PubMed
7. M. B. Al-Fageeh and C. M. Smales, “Control and regulation of the cellular responses to cold shock: the responses in yeast and mammalian systems,” Biochemical Journal, vol. 397, no. 2, pp. 247–259, 2006. View at Publisher · View at Google Scholar · View at PubMed
8. A. T. Maurelli and P. J. Sansonetti, “Identification of a chromosomal gene controlling temperature-regulated expression of Shigella virulence,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 8, pp. 2820–2824, 1988. View at Publisher · View at Google Scholar
9. S. C. Straley and R. D. Perry, “Environmental modulation of gene expression and pathogenesis in Yersinia,” Trends in Microbiology, vol. 3, no. 8, pp. 310–317, 1995. View at Publisher · View at Google Scholar
10. A. C. Collins, A. Smolen, A. L. Wayman, and M. J. Marks, “Ethanol and temperature effects on five membrane bound enzymes,” Alcohol, vol. 1, no. 3, pp. 237–246, 1984. View at Publisher · View at Google Scholar
11. A. Ferrer-Montiel, C. García-Martínez, C. Morenilla-Palao, et al., “Molecular architecture of the vanilloid receptor: insights for drug design,” European Journal of Biochemistry, vol. 271, no. 10, pp. 1820–1826, 2004. View at Publisher · View at Google Scholar · View at PubMed
12. L. Ginsberg, D. L. Gilbert, and N. L. Gershfeld, “Membrane bilayer assembly in neural tissue of rat and squid as a critical phenomenon: influence of temperature and membrane proteins,” Journal of Membrane Biology, vol. 119, no. 1, pp. 65–73, 1991. View at Publisher · View at Google Scholar
13. M. Mandal and R. R. Breaker, “Gene regulation by riboswitches,” Nature Reviews Molecular Cell Biology, vol. 5, no. 6, pp. 451–463, 2004. View at Publisher · View at Google Scholar · View at PubMed
14. L. Vigh, B. Maresca, and J. L. Harwood, “Does the membrane's physical state control the expression of heat shock and other genes?,” Trends in Biochemical Sciences, vol. 23, no. 10, pp. 369–374, 1998. View at Publisher · View at Google Scholar
15. P. S. Aguilar, J. E. Cronan, Jr., and D. de Mendoza, “A Bacillus subtilis gene induced by cold shock encodes a membrane phospholipid desaturase,” Journal of Bacteriology, vol. 180, no. 8, pp. 2194–2200, 1998.
16. P. S. Aguilar, A. M. Hernandez-Arriaga, L. E. Cybulski, A. C. Erazo, and D. de Mendoza, “Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis,” EMBO Journal, vol. 20, no. 7, pp. 1681–1691, 2001. View at Publisher · View at Google Scholar · View at PubMed
17. T. Suzuki, T. Nakayama, T. Kurihara, T. Nishino, and N. Esaki, “Cold-active lipolytic activity of psychrotrophic Acinetobacter sp. Strain no. 6,” Journal of Bioscience and Bioengineering, vol. 92, no. 2, pp. 144–148, 2001. View at Publisher · View at Google Scholar
18. R. Dutta, L. Qin, and M. Inouye, “Histidine kinases: diversity of domain organization,” Molecular Microbiology, vol. 34, no. 4, pp. 633–640, 1999. View at Publisher · View at Google Scholar
19. M. Mandal and R. R. Breaker, “Adenine riboswitches and gene activation by disruption of a transcription terminator,” Nature Structural and Molecular Biology, vol. 11, no. 1, pp. 29–35, 2004. View at Publisher · View at Google Scholar · View at PubMed
20. W. C. Winkler and R. R. Breaker, “Regulation of bacterial gene expression by riboswitches,” Annual Review of Microbiology, vol. 59, pp. 487–517, 2005. View at Publisher · View at Google Scholar · View at PubMed
21. C. Brunel, P. Romby, C. Sacerdot, et al., “Stabilised secondary structure at a ribosomal binding site enhances translational repression in E. coli,” Journal of Molecular Biology, vol. 253, no. 2, pp. 277–290, 1995. View at Publisher · View at Google Scholar · View at PubMed
22. R. Kaempfer, “RNA sensors: novel regulators of gene expression,” EMBO Reports, vol. 4, no. 11, pp. 1043–1047, 2003. View at Publisher · View at Google Scholar
23. B. J. Tucker and R. R. Breaker, “Riboswitches as versatile gene control elements,” Current Opinion in Structural Biology, vol. 15, no. 3, pp. 342–348, 2005. View at Publisher · View at Google Scholar · View at PubMed
24. J. Andersen, S. A. Forst, K. Zhao, M. Inouye, and N. Delihas, “The function of micF RNA. micF RNA is a major factor in the thermal regulation of OmpF protein in Escherichia coli,” Journal of Biological Chemistry, vol. 264, no. 30, pp. 17961–17970, 1989.
25. R. A. Lease and M. Belfort, “A trans-acting RNA as a control switch in Escherichia coli: DsrA modulates function by forming alternative structures,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 18, pp. 9919–9924, 2000. View at Publisher · View at Google Scholar · View at PubMed
26. J. Johansson, P. Mandin, A. Renzoni, C. Chiaruttini, M. Springer, and P. Cossart, “An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes,” Cell, vol. 110, no. 5, pp. 551–561, 2002. View at Publisher · View at Google Scholar
27. M. T. Morita, Y. Tanaka, T. S. Kodama, Y. Kyogoku, H. Yanagi, and T. Yura, “Translational induction of heat shock transcription factor ${\sigma }^{32}$: evidence for a built-in RNA thermosensor,” Genes & Development, vol. 13, no. 6, pp. 655–665, 1999. View at Publisher · View at Google Scholar
28. A. Nocker, T. Hausherr, S. Balsiger, N.-P. Krstulovic, H. Hennecke, and F. Narberhaus, “A mRNA-based thermosensor controls expression of rhizobial heat shock genes,” Nucleic Acids Research, vol. 29, no. 23, pp. 4800–4807, 2001. View at Publisher · View at Google Scholar
29. K. Yamanaka, “Cold shock response in Escherichia coli,” Journal of Molecular Microbiology and Biotechnology, vol. 1, no. 2, pp. 193–202, 1999.
30. C. J. Dorman, “Flexible response: DNA supercoiling, transcription and bacterial adaptation to environmental stress,” Trends in Microbiology, vol. 4, no. 6, pp. 214–216, 1996. View at Publisher · View at Google Scholar
31. C. J. Dorman, J. C. D. Hinton, and A. Free, “Domain organization and oligomerization among H-NS-like nucleoid-associated proteins in bacteria,” Trends in Microbiology, vol. 7, no. 3, pp. 124–128, 1999. View at Publisher · View at Google Scholar
32. C. J. Dorman, “DNA supercoiling and environmental regulation of gene expression in pathogenic bacteria,” Infection and Immunity, vol. 59, no. 3, pp. 745–749, 1991.
33. R. Grau, D. Gardiol, G. C. Glikin, and D. de Mendoza, “DNA supercoiling and thermal regulation of unsaturated fatty acid synthesis in Bacillus subtilis,” Molecular Microbiology, vol. 11, no. 5, pp. 933–941, 1994. View at Publisher · View at Google Scholar
34. R. M. Williams and S. Rimsky, “Molecular aspects of the E. coli nucleoid protein, H-NS: a central controller of gene regulatory networks,” FEMS Microbiology Letters, vol. 156, no. 2, pp. 175–185, 1997. View at Publisher · View at Google Scholar
35. K. Drlica, “Control of bacterial DNA supercoiling,” Molecular Microbiology, vol. 6, no. 4, pp. 425–433, 1992. View at Publisher · View at Google Scholar
36. Y.-C. Tse-Dinh, H. Qi, and R. Menzel, “DNA supercoiling and bacterial adaptation: thermotolerance and thermoresistance,” Trends in Microbiology, vol. 5, no. 8, pp. 323–326, 1997. View at Publisher · View at Google Scholar
37. J. R. Lupski, S. J. Projan, L. S. Ozaki, and G. N. Godson, “A temperature-dependent pBR322 copy number mutant resulting from a Tn5 position effect,” Proceedings of the National Academy of Sciences of the United States of America, vol. 83, no. 19, pp. 7381–7385, 1986. View at Publisher · View at Google Scholar
38. O. Carmel-Harel and G. Storz, “Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress,” Annual Review of Microbiology, vol. 54, pp. 439–461, 2000. View at Publisher · View at Google Scholar · View at PubMed
39. L. Turner, A. D. Samuel, A. S. Stern, and H. C. Berg, “Temperature dependence of switching of the bacterial flagellar motor by the protein ${\text{CheY}}^{13\text{DK}106\text{YW}}$,” Biophysical Journal, vol. 77, no. 1, pp. 597–603, 1999.
40. U. Alon, L. Camarena, M. G. Surette, et al., “Response regulator output in bacterial chemotaxis,” EMBO Journal, vol. 17, no. 15, pp. 4238–4248, 1998. View at Publisher · View at Google Scholar · View at PubMed
41. J. Monod, J. Wyman, and J. P. Changeux, “On the nature of allosteric transitions: a plausible model,” Journal of Molecular Biology, vol. 12, pp. 88–118, 1965.
42. B. E. Scharf, K. A. Fahrner, L. Turner, and H. C. Berg, “Control of direction of flagellar rotation in bacterial chemotaxis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 1, pp. 201–206, 1998. View at Publisher · View at Google Scholar
43. T. Nara, L. Lee, and Y. Imae, “Thermosensing ability of Trg and Tap chemoreceptors in Escherichia coli,” Journal of Bacteriology, vol. 173, no. 3, pp. 1120–1124, 1991.
44. S. Eriksson, R. Hurme, and M. Rhen, “Low-temperature sensors in bacteria,” Philosophical Transactions of the Royal Society B, vol. 357, no. 1423, pp. 887–893, 2002. View at Publisher · View at Google Scholar · View at PubMed
45. C. Harteneck, T. D. Plant, and G. Schultz, “From worm to man: three subfamilies of TRP channels,” Trends in Neurosciences, vol. 23, no. 4, pp. 159–166, 2000. View at Publisher · View at Google Scholar
46. C. Montell, “The TRP superfamily of cation channels,” Science's STKE, vol. 2005, no. 272, re3 pages, 2005. View at Publisher · View at Google Scholar · View at PubMed
47. N. Kedei, T. Szabo, J. D. Lile, et al., “Analysis of the native quaternary structure of vanilloid receptor 1,” Journal of Biological Chemistry, vol. 276, no. 30, pp. 28613–28619, 2001. View at Publisher · View at Google Scholar · View at PubMed
48. M. J. Caterina, “Transient receptor potential ion channels as participants in thermosensation and thermoregulation,” American Journal of Physiology, vol. 292, no. 1, pp. R64–R76, 2007. View at Publisher · View at Google Scholar · View at PubMed
49. M. M. Moran, H. Xu, and D. E. Clapham, “TRP ion channels in the nervous system,” Current Opinion in Neurobiology, vol. 14, no. 3, pp. 362–369, 2004. View at Publisher · View at Google Scholar · View at PubMed
50. A. M. Peier, A. J. Reeve, D. A. Andersson, et al., “A heat-sensitive TRP channel expressed in keratinocytes,” Science, vol. 296, no. 5575, pp. 2046–2049, 2002. View at Publisher · View at Google Scholar · View at PubMed
51. D. D. McKemy, “How cold is it? TRPM8 and TRPA1 in the molecular logic of cold sensation,” Molecular Pain, vol. 1, article 16, 2005. View at Publisher · View at Google Scholar · View at PubMed
52. G. M. Story, A. M. Peier, A. J. Reeve, et al., “ANKTM1, a TRP-like channel expressed in nociceptive neurons, is activated by cold temperatures,” Cell, vol. 112, no. 6, pp. 819–829, 2003. View at Publisher · View at Google Scholar
53. B. Liu, K. Hui, and F. Qin, “Thermodynamics of heat activation of single capsaicin ion channels VR1,” Biophysical Journal, vol. 85, no. 5, pp. 2988–3006, 2003.
54. S. Brauchi, P. Orio, and R. Latorre, “Clues to understanding cold sensation: thermodynamics and electrophysiological analysis of the cold receptor TRPM8,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 43, pp. 15494–15499, 2004. View at Publisher · View at Google Scholar · View at PubMed
55. S. Brauchi, G. Orta, M. Salazar, E. Rosenmann, and R. Latorre, “A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels,” Journal of Neuroscience, vol. 26, no. 18, pp. 4835–4840, 2006. View at Publisher · View at Google Scholar · View at PubMed
56. H. W. Huang, “Allosteric linkage and phase transition,” Physiological Chemistry and Physics, vol. 8, no. 2, pp. 143–150, 1976.
57. L. J. DeLucas, K. M. Moore, and M. M. Long, “Protein crystal growth and the International Space Station,” Gravitational and Space Biology Bulletin, vol. 12, no. 2, pp. 39–45, 1999.
58. G. M. Artmann, Ch. Kelemen, D. Porst, G. Büldt, and S. Chien, “Temperature transitions of protein properties in human red blood cells,” Biophysical Journal, vol. 75, no. 6, pp. 3179–3183, 1998.
59. S. H. Ip and G. K. Ackers, “Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer tetramer association constants for oxygenated and unliganded hemoglobins,” Journal of Biological Chemistry, vol. 252, no. 1, pp. 82–87, 1977.
60. R. Valdes, Jr. and G. K. Ackers, “Thermodynamic studies on subunit assembly in human hemoglobin. Calorimetric measurements on the reconstitution of oxyhemoglobin from isolated chains,” Journal of Biological Chemistry, vol. 252, no. 1, pp. 88–91, 1977.
61. B. E. Bowler, “Thermodynamics of protein denatured states,” Molecular BioSystems, vol. 3, no. 2, pp. 88–99, 2007. View at Publisher · View at Google Scholar · View at PubMed
62. Y. Levy and J. N. Onuchic, “Water mediation in protein folding and molecular recognition,” Annual Review of Biophysics and Biomolecular Structure, vol. 35, pp. 389–415, 2006. View at Publisher · View at Google Scholar · View at PubMed
63. B. Nilius, K. Talavera, G. Owsianik, J. Prenen, G. Droogmans, and T. Voets, “Gating of TRP channels: a voltage connection?,” Journal of Physiology, vol. 567, no. 1, pp. 35–44, 2005. View at Publisher · View at Google Scholar · View at PubMed
64. B. Nilius, G. Owsianik, T. Voets, and J. A. Peters, “Transient receptor potential cation channels in disease,” Physiological Reviews, vol. 87, no. 1, pp. 165–217, 2007. View at Publisher · View at Google Scholar · View at PubMed
65. G. Zaccai and B. Jacrot, “Small angle neutron scattering,” Annual Review of Biophysics and Bioengineering, vol. 12, pp. 139–157, 1983. View at Publisher · View at Google Scholar · View at PubMed
66. G. Zaccai, F. Cendrin, Y. Haik, N. Borochov, and H. Eisenberg, “Stabilization of halophilic malate dehydrogenase,” Journal of Molecular Biology, vol. 208, no. 3, pp. 491–500, 1989. View at Publisher · View at Google Scholar
67. G. Zaccai and H. Eisenberg, “Halophilic proteins and the influence of solvent on protein stabilization,” Trends in Biochemical Sciences, vol. 15, no. 9, pp. 333–337, 1990. View at Publisher · View at Google Scholar
68. G. Zaccai, “The effect of water on protein dynamics,” Philosophical Transactions of the Royal Society of London B, vol. 359, no. 1448, pp. 1269–1275, 2004. View at Publisher · View at Google Scholar · View at PubMed
69. J. C. Smith, F. Merzel, A.-N. Bondar, A. Tournier, and S. Fischer, “Structure, dynamics and reactions of protein hydration water,” Philosophical Transactions of the Royal Society B, vol. 359, no. 1448, pp. 1181–1190, 2004. View at Publisher · View at Google Scholar · View at PubMed
70. V. Réat, R. Dunn, M. Ferrand, J. L. Finney, R. M. Daniel, and J. C. Smith, “Solvent dependence of dynamic transitions in protein solutions,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 18, pp. 9961–9966, 2000. View at Publisher · View at Google Scholar
71. O. P. Hamill and B. Martinac, “Molecular basis of mechanotransduction in living cells,” Physiological Reviews, vol. 81, no. 2, pp. 685–740, 2001.
72. F. Sachs and C. E. Morris, “Mechanosensitive ion channels in nonspecialized cells,” Reviews of Physiology, Biochemistry and Pharmacology, vol. 132, pp. 1–77, 1998. View at Publisher · View at Google Scholar
73. T. Rohacs and B. Nilius, “Regulation of transient receptor potential (TRP) channels by phosphoinositides,” Pflugers Archiv European Journal of Physiology, vol. 455, no. 1, pp. 157–168, 2007. View at Publisher · View at Google Scholar · View at PubMed
74. T. Rohacs, “Teaching resources. TRP channels,” Science's STKE, vol. 2005, no. 282, tr14 pages, 2005.
75. D. D. McKemy, “Temperature sensing across species,” Pflügers Archiv European Journal of Physiology, vol. 454, no. 5, pp. 777–791, 2007. View at Publisher · View at Google Scholar · View at PubMed
76. G. M. Artmann, L. Burns, J. M. Canaves, et al., “Circular dichroism spectra of human hemoglobin reveal a reversible structural transition at body temperature,” European Biophysics Journal, vol. 33, no. 6, pp. 490–496, 2004. View at Publisher · View at Google Scholar · View at PubMed
77. I. Digel, Ch. Maggakis-Kelemen, K. F. Zerlin, et al., “Body temperature-related structural transitions of monotremal and human hemoglobin,” Biophysical Journal, vol. 91, no. 8, pp. 3014–3021, 2006. View at Publisher · View at Google Scholar · View at PubMed
78. K. F. Zerlin, N. Kasischke, I. Digel, et al., “Structural transition temperature of hemoglobins correlates with species' body temperature,” European Biophysics Journal, vol. 37, no. 1, pp. 1–10, 2007. View at Publisher · View at Google Scholar · View at PubMed
79. R. E. Weber and S. N. Vinogradov, “Nonvertebrate hemoglobins: functions and molecular adaptations,” Physiological Reviews, vol. 81, no. 2, pp. 569–628, 2001.
80. H. Frauenfelder, G. A. Petsko, and D. Tsernoglou, “Temperature-dependent X-ray diffraction as a probe of protein structural dynamics,” Nature, vol. 280, no. 5723, pp. 558–563, 1979. View at Publisher · View at Google Scholar