References
- Lindquist S, Craig EA. The Heat-Shock Proteins. Annu Rev Genet. 1988;22(1):631-77. https://doi.org/10.1146/annurev.ge.22.120188.003215
- Mestril R, Dillmann WH. Heat shock proteins and protection against myocardial ischemia. J Mol Cell Cardiol. 1995;27(1):45-52. https://doi.org/10.1016/S0022-2828(08)80006-5
- Basu N, Todgham AE, Ackerman PA, Bibeau MR, Nakano K, Schulte PM, et al. Heat shock protein genes and their functional significance in fish. Gene. 2002;295(2):173-83. https://doi.org/10.1016/S0378-1119(02)00687-X
- Yamashita M, Yabu T, Ojima N. Stress Protein HSP70 in Fish. Aqua-BioScience Monographs. 2010;3(4):111-41. https://doi.org/10.5047/absm.2010.00304.0111
- Basu N, Nakano T, Grau EG, Iwama GK. The Effects of Cortisol on Heat Shock Protein 70 Levels in Two Fish Species. Gen Comp Endocrinol. 2001;124(1):97-105. https://doi.org/10.1006/gcen.2001.7688
- Boutet I, Tanguy A, Rousseau S, Auffret M, Moraga D. Molecular identification and expression of heat shock cognate 70 (hsc70) and heat shock protein 70 (hsp70) genes in the Pacific oyster Crassostrea gigas. Cell Stress Chaperones. 2003;8(1):76-85. https://doi.org/10.1379/1466-1268(2003)8<76:MIAEOH>2.0.CO;2
- Ming J, Xie J, Xu P, Liu W, Ge X, Liu B, et al. Molecular cloning and expression of two HSP70 genes in the Wuchang bream (Megalobrama amblycephala Yih). Fish Shellfish Immunology. 2010;28(3):407-18. https://doi.org/10.1016/j.fsi.2009.11.018
- Iwama G, Thomas P, Forsyth R, Vijayan M. Heat shock protein expression in fish. Rev Fish Biol Fish. 1998;8(1):35-56. https://doi.org/10.1023/A:1008812500650
- Padmini E, Usha RM. Impact of seasonal variation on HSP70 expression quantitated in stressed fish hepatocytes. Comp Biochem Physiol B Biochem Mol Biol. 2008;151(3):278-85. https://doi.org/10.1016/j.cbpb.2008.07.011
- Welch W, Feramisco J. Disruption of the three cytoskeletal networks in mammalian cells does not affect transcription, translation, or protein translocation changes induced by heat shock. Mol Cell Biol. 1985;5(7):1571-81. https://doi.org/10.1128/MCB.5.7.1571
- Gething M-J, Sambrook J. Protein folding in the cell. Nature. 1992;355(6355):33-45. https://doi.org/10.1038/355033a0
- Wallin RP, Lundqvist A, More SH, Von Bonin A, Kiessling R, Ljunggren H-G. Heat-shock proteins as activators of the innate immune system. Trends Immunol. 2002;23(3):130-5. https://doi.org/10.1016/S1471-4906(01)02168-8
- Daugaard M, Rohde M, Jaattela M. The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions. FEBS Lett. 2007;581(19):3702-10. https://doi.org/10.1016/j.febslet.2007.05.039
- Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell. 1998;92(3):351-66. https://doi.org/10.1016/S0092-8674(00)80928-9
- Tutar Y, Song Y, Masison DC. Primate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae. Genetics. 2006;172(2):851-61. https://doi.org/10.1534/genetics.105.048926
- Luckstadt C, Schill RO, Focken U, Kohler H-R, Becker K. Stress protein HSP70 response of Nile Tilapia Oreochromis niloticus (Linnaeus, 1758) to induced hypoxia and recovery. Verhandlungen der Gesellschaft fur Ichthyologie Band. 2004;4:137-41.
- Yamashita M, Hojo M. Generation of a transgenic zebrafish model overexpressing heat shock protein HSP70. Mar Biotechnol. 2004;6:S1-7. https://doi.org/10.1007/s10126-002-0115-9
- Ojima N, Yamashita M, Watabe S. Comparative expression analysis of two paralogous Hsp70s in rainbow trout cells exposed to heat stress. Biochimica et Biophysica Acta (BBA)-Gene Structure and Expression. 2005;1681(2):99-106. https://doi.org/10.1016/j.bbaexp.2004.10.006
- Mu W, Wen H, Li J, He F. Cloning and expression analysis of a HSP70 gene from Korean rockfish (Sebastes schlegeli). Fish shellfish immunology. 2013;35(4):1111-21. https://doi.org/10.1016/j.fsi.2013.07.022
- Wang P, Zeng S, Xu P, Zhou L, Zeng L, Lu X, et al. Identification and expression analysis of two HSP70 isoforms in mandarin fish Siniperca chuatsi. Fish Sci. 2014;80(4):803-17. https://doi.org/10.1007/s12562-014-0747-5
- Zhou Z, Ren Z, Zeng H, Yao B. Apparent digestibility of various feedstuffs for bluntnose black bream Megalobrama amblycephala Yih. Aquac Nutr. 2008;14(2):153-65. https://doi.org/10.1111/j.1365-2095.2007.00515.x
- CAFS. Fishery Statistic Data: Chinese Academy of Fishery Sciences, Beijing. 2010.
- MAPRC. Chinese fisheries yearbook: Chinese Agricultural Press, Beijing. 2010.
- Marti-Renom MA, Stuart AC, Fiser A, Sanchez R, Melo F, Sali A. Comparative Protein Structure Modeling of Genes and Genomes. Annu Rev Biophys Biomol Struct. 2000;29(1):291-325. https://doi.org/10.1146/annurev.biophys.29.1.291
- Skolnick J, Fetrow JS, Kolinski A. Structural genomics and its importance for gene function analysis. Nat Biotechnol. 2000;18(3):283-7. https://doi.org/10.1038/73723
- Teichmann SA, Murzin AG, Chothia C. Determination of protein function, evolution and interactions by structural genomics. Curr Opin Struct Biol. 2001;11(3):354-63. https://doi.org/10.1016/S0959-440X(00)00215-3
- Radivojac P, Clark WT, Oron TR, Schnoes AM, Wittkop T, Sokolov A, et al. A large-scale evaluation of computational protein function prediction. Nat Methods. 2013;10(3):221-7. https://doi.org/10.1038/nmeth.2340
- Gasteiger E, Hoogland C, Gattiker A, Wilkins MR, Appel RD, Bairoch A. Protein identification and analysis tools on the ExPASy server. In: The proteomics protocols handbook: Springer. 2005. p. 571-607.
- Hirokawa T, Boon-Chieng S, Mitaku S. SOSUI: classification and secondary structure prediction system for membrane proteins. Bioinformatics. 1998;14(4):378-9. https://doi.org/10.1093/bioinformatics/14.4.378
- Schwede T, Kopp J, Guex N, Peitsch MC. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 2003;31(13):3381-5. https://doi.org/10.1093/nar/gkg520
- Arnold K, Bordoli L, Kopp J, Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics. 2006;22(2):195-201. https://doi.org/10.1093/bioinformatics/bti770
- Fiser A. Template-based protein structure modeling. In: Fenyo D, editor. Computational Biology: Humana Press. 2004.
- Cristobal S, Zemla A, Fischer D, Rychlewski L, Elofsson A. A study of quality measures for protein threading models. BMC bioinformatics. 2001;2(1):5. https://doi.org/10.1186/1471-2105-2-5
- Sippl MJ. Recognition of errors in three-dimensional structures of proteins. Proteins: Structure Function, and Bioinformatics. 1993;17(4):355-62. https://doi.org/10.1002/prot.340170404
- Wiederstein M, Sippl MJ. ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. Nucleic Acids Res. 2007;35 suppl 2:W407-10. https://doi.org/10.1093/nar/gkm290
- Guex N, Peitsch MC. SWISS-MODEL and the Swiss-Pdb Viewer: An environment for comparative protein modeling. ELECTROPHORESIS. 1997;18(15):2714-23. https://doi.org/10.1002/elps.1150181505
- Zhang Y, Skolnick J. TM-align: a protein structure alignment algorithm based on the TM-score. Nucleic Acids Res. 2005;33(7):2302-9. https://doi.org/10.1093/nar/gki524
- Zhang Y. I-TASSER server for protein 3D structure prediction. BMC bioinformatics. 2008;9(1):40. https://doi.org/10.1186/1471-2105-9-40
- Roy A, Kucukural A, Zhang Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc. 2010;5(4):725-38. https://doi.org/10.1038/nprot.2010.5
- Yang J, Yan R, Roy A, Xu D, Poisson J, Zhang Y. The I-TASSER Suite: protein structure and function prediction. Nat Methods. 2015;12(1):7-8. https://doi.org/10.1038/nmeth.3213
- Guruprasad K, Reddy BB, Pandit MW. Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Eng. 1990;4(2):155-61. https://doi.org/10.1093/protein/4.2.155
- Ikai A. Thermostability and aliphatic index of globular proteins. J Biochem. 1980;88(6):1895-8.
- Hogg PJ. Disulfide bonds as switches for protein function. Trends Biochem Sci. 2003;28(4):210-4. https://doi.org/10.1016/S0968-0004(03)00057-4
- Ramachandran G, Ramakrishnan C, Sasisekhran V. Stereochemistry of polypeptide chain configuarations. J Mol Biol. 1963;7:95-9. https://doi.org/10.1016/S0022-2836(63)80023-6
- Liithy R, Bowie J, Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature. 1992;356(6364):83-5. https://doi.org/10.1038/356083a0
- Colovos C, Yeates TO. Verification of protein structures: patterns of nonbonded atomic interactions. Protein Sci. 1993;2(9):1511-9. https://doi.org/10.1002/pro.5560020916
- Vorobiev S, Strokopytov B, Drubin D, Frieden C, Ono S, Condeelis J, et al. The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism. Proc Natl Acad Sci. 2003;100(10):5760-5. https://doi.org/10.1073/pnas.0832273100
- Zhang Z, Cellitti J, Teriete P, Pellecchia M, Stec B. New crystal structures of HSC-70 ATP binding domain confirm the role of individual binding pockets and suggest a new method of inhibition. Biochimie. 2015;108:186-92. https://doi.org/10.1016/j.biochi.2014.11.012
- Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, et al. The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange. Structure. 2010;18(3):309-19. https://doi.org/10.1016/j.str.2010.01.004