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Ould-Abeih MB, Petit-Topin I, Zidane N, Baron B, Bedouelle H (June 2012). “Multiple folding states and disorder of ribosomal protein SA, a membrane receptor for laminin, anticarcinogens, and pathogens”. Biochemistry51 (24): 4807–21. doi:10.1021/bi300335r. PMID22640394.
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Sharma, Vivek; Kaila, Ville R.I.; Annila, Arto (2009). “Protein folding as an evolutionary process”. Physica A: Statistical Mechanics and Its Applications388 (6): 851–62. Bibcode: 2009PhyA..388..851S. doi:10.1016/j.physa.2008.12.004.
Zhang, Gong; Ignatova, Zoya (2011-02-01). “Folding at the birth of the nascent chain: coordinating translation with co-translational folding”. Current Opinion in Structural Biology21 (1): 25–31. doi:10.1016/j.sbi.2010.10.008. ISSN0959-440X. PMID21111607.
Pace CN, Shirley BA, McNutt M, Gajiwala K (January 1996). “Forces contributing to the conformational stability of proteins”. FASEB Journal10 (1): 75–83. doi:10.1096/fasebj.10.1.8566551. PMID8566551.
Cui D, Ou S, Patel S (December 2014). “Protein-spanning water networks and implications for prediction of protein-protein interactions mediated through hydrophobic effects”. Proteins82 (12): 3312–26. doi:10.1002/prot.24683. PMID25204743.
Hartl FU, Bracher A, Hayer-Hartl M (July 2011). “Molecular chaperones in protein folding and proteostasis”. Nature475 (7356): 324–32. doi:10.1038/nature10317. PMID21776078.
Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU (2013). “Molecular chaperone functions in protein folding and proteostasis”. Annual Review of Biochemistry82: 323–55. doi:10.1146/annurev-biochem-060208-092442. PMID23746257.
Shortle D (January 1996). “The denatured state (the other half of the folding equation) and its role in protein stability”. FASEB Journal10 (1): 27–34. doi:10.1096/fasebj.10.1.8566543. PMID8566543.
Lee S, Tsai FT (2005). “Molecular chaperones in protein quality control”. Journal of Biochemistry and Molecular Biology38 (3): 259–65. doi:10.5483/BMBRep.2005.38.3.259. PMID15943899.
Chaudhuri TK, Paul S (April 2006). “Protein-misfolding diseases and chaperone-based therapeutic approaches”. The FEBS Journal273 (7): 1331–49. doi:10.1111/j.1742-4658.2006.05181.x. PMID16689923.
Soto C, Estrada L, Castilla J (March 2006). “Amyloids, prions and the inherent infectious nature of misfolded protein aggregates”. Trends in Biochemical Sciences31 (3): 150–5. doi:10.1016/j.tibs.2006.01.002. PMID16473510.
Johnson SM, Wiseman RL, Sekijima Y, Green NS, Adamski-Werner SL, Kelly JW (December 2005). “Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses”. Accounts of Chemical Research38 (12): 911–21. doi:10.1021/ar020073i. PMID16359163.
Bedouelle H (February 2016). “Principles and equations for measuring and interpreting protein stability: From monomer to tetramer”. Biochimie121: 29–37. doi:10.1016/j.biochi.2015.11.013. PMID26607240.
Monsellier E, Bedouelle H (September 2005). “Quantitative measurement of protein stability from unfolding equilibria monitored with the fluorescence maximum wavelength”. Protein Engineering, Design & Selection18 (9): 445–56. doi:10.1093/protein/gzi046. PMID16087653.
Park YC, Bedouelle H (July 1998). “Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions”. The Journal of Biological Chemistry273 (29): 18052–9. doi:10.1074/jbc.273.29.18052. PMID9660761.
Ould-Abeih MB, Petit-Topin I, Zidane N, Baron B, Bedouelle H (June 2012). “Multiple folding states and disorder of ribosomal protein SA, a membrane receptor for laminin, anticarcinogens, and pathogens”. Biochemistry51 (24): 4807–21. doi:10.1021/bi300335r. PMID22640394.
Royer CA (May 2006). “Probing protein folding and conformational transitions with fluorescence”. Chemical Reviews106 (5): 1769–84. doi:10.1021/cr0404390. PMID16683754.
Bu Z, Cook J, Callaway DJ (September 2001). “Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin”. Journal of Molecular Biology312 (4): 865–73. doi:10.1006/jmbi.2001.5006. PMID11575938.
Park C, Marqusee S (March 2005). “Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding”. Nature Methods2 (3): 207–12. doi:10.1038/nmeth740. PMID15782190.
Mashaghi A, Kramer G, Lamb DC, Mayer MP, Tans SJ (January 2014). “Chaperone action at the single-molecule level”. Chemical Reviews114 (1): 660–76. doi:10.1021/cr400326k. PMID24001118.
Compiani M, Capriotti E (December 2013). “Computational and theoretical methods for protein folding”. Biochemistry52 (48): 8601–24. doi:10.1021/bi4001529. PMID24187909.
Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (March 1995). “Funnels, pathways, and the energy landscape of protein folding: a synthesis”. Proteins21 (3): 167–95. arXiv:chem-ph/9411008. doi:10.1002/prot.340210302. PMID7784423.
Robson, Barry; Vaithilingam, Andy (2008). “Protein Folding Revisited”. Molecular Biology of Protein Folding, Part B. Progress in Molecular Biology and Translational Science. 84. pp. 161–202. doi:10.1016/S0079-6603(08)00405-4. ISBN978-0-12-374595-8. PMID19121702
Schaefer M, Bartels C, Karplus M (December 1998). “Solution conformations and thermodynamics of structured peptides: molecular dynamics simulation with an implicit solvation model”. Journal of Molecular Biology284 (3): 835–48. doi:10.1006/jmbi.1998.2172. PMID9826519.
Kmiecik S, Gront D, Kolinski M, Wieteska L, Dawid AE, Kolinski A (July 2016). “Coarse-Grained Protein Models and Their Applications”. Chemical Reviews116 (14): 7898–936. doi:10.1021/acs.chemrev.6b00163. PMID27333362.
Zhang, Gong; Ignatova, Zoya (2011-02-01). “Folding at the birth of the nascent chain: coordinating translation with co-translational folding”. Current Opinion in Structural Biology21 (1): 25–31. doi:10.1016/j.sbi.2010.10.008. ISSN0959-440X. PMID21111607.