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ACS Chem.","volume":"4","author":"AW Puri","year":"2009","journal-title":"Biol"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"4617","DOI":"10.1073\/pnas.0900191106","article-title":"Identifying the proteins to which small-molecule probes and drugs bind in cells.","volume":"106","author":"SE Ong","year":"2009","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref3","article-title":"Review of reported cholera outbreaks worldwide 1995\u20132005.","volume":"973\u2013977","author":"DC Griffith","year":"2006","journal-title":"Am J Trop Med Hyg 75;"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1128\/CMR.8.1.48","article-title":"Cholera.","volume":"8","author":"JB Kaper","year":"1995","journal-title":"Clin Microbiol Rev"},{"key":"ref5","article-title":"in Enteric Infections and Immunity, New York: Plenum Press, p","volume":"37","author":"MM Waldor","year":"1996"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1126\/science.1116739","article-title":"Small-molecule inhibitor of <italic>Vibrio cholerae<\/italic> virulence and intestinal colonization.","volume":"310","author":"DT Hung","year":"2005","journal-title":"Science"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"2372","DOI":"10.1073\/pnas.0611643104","article-title":"Virstatin inhibits dimerization of the transcriptional activator ToxT.","volume":"104","author":"EA Shakhnovich","year":"2007","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"6974","DOI":"10.1128\/jb.174.21.6974-6980.1992","article-title":"The virulence gene activator ToxT from <italic>Vibrio cholerae<\/italic> is a member of the AraC family of transcriptional activators.","volume":"174","author":"DE Higgins","year":"1992","journal-title":"J Bacteriol"},{"key":"ref9","first-page":"2962","article-title":"Accessory cholera enterotoxin, Ace, from <italic>Vibrio cholerae<\/italic>: structure, unfolding, and virstatin binding.","author":"T Chatterjee","year":"2011"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1248\/bpb.25.695","article-title":"Practical aspects of the ligand-binding and enzymatic properties of human serum albumin.","volume":"25","author":"U Kragh-Hansen","year":"2002","journal-title":"Biol Pharm Bull"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1126\/science.2374930","article-title":"Structure of human serum albumin.","volume":"249","author":"DC Carter","year":"1990","journal-title":"Science"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0065-3233(08)60640-3","article-title":"Structure of serum albumin.","volume":"45","author":"DC Carter","year":"1994","journal-title":"Adv Protein Chem"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"3042","DOI":"10.1074\/jbc.275.5.3042","article-title":"Conformational transitions of the three recombinant domains of human serum albumin depending on pH.","volume":"275","author":"M Dockal","year":"2000","journal-title":"J Biol Chem"},{"key":"ref14","first-page":"209","article-title":"Atomic structure and chemistry of human serum albumin, Nature","volume":"358","author":"XM He","year":"1992"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1126\/science.2727704","article-title":"Three-dimensional structure of human serum albumin.","volume":"244","author":"DC Carter","year":"1989","journal-title":"Science"},{"key":"ref16","first-page":"1984","article-title":"A structural transformation in bovine and human plasma albumins in alkaline solution as revealed by rotatory dispersion studies, J Biol. Chem.","volume":"238","author":"WJ Leonard","year":"1963"},{"key":"ref17","doi-asserted-by":"crossref","DOI":"10.1016\/B978-0-08-019603-9.50010-7","article-title":"Some aspects of the structure and conformational properties of serum albumin,","author":"JF Foster","year":"1977"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1042\/bj1630477","article-title":"Physical and binding properties of large fragments of human serum albumin.","volume":"163","author":"MJ Geisow","year":"1977","journal-title":"Biochem J"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1042\/bj2360307","article-title":"Direct evidence for the involvement of domain III in the N-F transition of bovine serum albumin.","volume":"236","author":"MY Khan","year":"1986","journal-title":"Biochem J"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/S0167-4838(99)00098-9","article-title":"Interactive binding to the two principal ligand binding sites of human serum albumin: effect of the neutral-to-base transition.","volume":"1432","author":"K Yamasaki","year":"1999","journal-title":"Biochim Biophys Acta"},{"key":"ref21","first-page":"291","article-title":"The role of albumin conformation in the binding of diazepam to human serum albumin, Biochim. Biophys.","volume":"626","author":"J Wilting","year":"1980","journal-title":"Acta"},{"key":"ref22","author":"Biochemistry Peters T All about Albumin:","year":"1980"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1002\/(SICI)1099-1352(199901\/02)12:1<3::AID-JMR441>3.0.CO;2-6","article-title":"Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition.","volume":"12","author":"I Jelesarov","year":"1999","journal-title":"J Mol Recognit"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/0958-1669(94)90046-9","article-title":"Acquisition and use of calorimetric data for prediction of the thermodynamics of ligand-binding and folding reactions of proteins.","volume":"5","author":"PR Connelly","year":"1994","journal-title":"Curr Opin Biotechnol"},{"key":"ref25","article-title":"PatchDock and SymmDock: servers for rigid and symmetric docking.","volume":"363\u2013367","author":"D Schneidman-Duhovny","year":"2005","journal-title":"Nucl Acids Res 33 : W"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1006\/jmbi.1996.0897","article-title":"Development and validation of a genetic algorithm for flexible docking.","volume":"267","author":"G Jones","year":"1997","journal-title":"J Mol Biol"},{"key":"ref27","first-page":"777","article-title":"Satisfying hydrogen bonding potential in proteins, J Mol Biol","volume":"238","author":"IK McDonald","year":"1994"},{"key":"ref28","article-title":"NACCESS: Program for Calculating Accessibilities.","author":"SJ Hubbard","year":"1992"},{"key":"ref29","article-title":"Principles of fluorescence spectroscopy, New York.","author":"JR Lakowicz","year":"1983"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"1431","DOI":"10.1016\/j.bmc.2005.09.066","article-title":"Human serum albumin interaction with formononetin studied using fluorescence anisotropy, FT-IR spectroscopy, and molecular modeling methods.","volume":"14","author":"Y Li","year":"2006","journal-title":"Bioorg Med Chem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0167-4838(99)00226-5","article-title":"Anion-induced refolding of human serum albumin under low pH conditions.","volume":"1476","author":"M Salman","year":"2000","journal-title":"Biochim Biophys Acta"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1021\/js960142k","article-title":"Interaction of small ligands with human serum albumin IIIA Subdomain. How to determine the affinity constant using an easy steady state fluorescence method.","volume":"85","author":"LA Bagatolli","year":"1996","journal-title":"J Pharm Sci"},{"key":"ref33","article-title":"Stereo-selectivity of human serum albumin to enantiomeric and isoelectronic pollutants dissected by spectroscopy, calorimetry and bioinformatics.","volume":"e26186","author":"E Ahmad","year":"2011","journal-title":"Plos one 6,"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"3096","DOI":"10.1021\/bi00514a017","article-title":"Thermodynamics of protein association reactions: forces contributing to stability.","volume":"20","author":"PD Ross","year":"1981","journal-title":"Biochemistry"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1016\/S0026-895X(25)10691-3","article-title":"The characterization of two specific drug binding sites on human serum albumin.","volume":"11","author":"G Sudlow","year":"1975","journal-title":"Mol Pharmacol"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S0026-895X(25)14614-2","article-title":"Characterization of an important drug binding area on human serum albumin including the high-affinity binding sites of warfarin and azapropazone.","volume":"21","author":"KJ Fehske","year":"1981","journal-title":"Mol Pharmacol"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"2876","DOI":"10.1038\/nprot.2006.202","article-title":"Using circular dichroism spectra to estimate protein secondary structure.","volume":"1","author":"NJ Greenfield","year":"2006","journal-title":"Nat Protoc"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S0167-4838(96)00190-2","article-title":"The application of circular dichroism to studies of protein folding and unfolding.","volume":"1338","author":"SM Kelly","year":"1997","journal-title":"Biochim Biophys Acta"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"1350","DOI":"10.1021\/bm050996b","article-title":"Effect of albumin conformation on the binding of ciprofloxacin to human serum albumin: a novel approach directly assigning binding site.","volume":"7","author":"B Ahmad","year":"2006","journal-title":"Biomacromolecules"},{"key":"ref40","article-title":"Advances in Protein Chemistry, C.A. Anfinsen, J.T. Edsall, F.M. Richards (Eds.), New York, Academic Press 37: p","author":"T Peters","year":"1985"},{"key":"ref41","first-page":"333","article-title":"Binding of genistein to human serum albumin demonstrated using tryptophan fluorescence quenching. Int J Biol Macro","volume":"34","author":"Q Bian","year":"2004"},{"key":"ref42","first-page":"153","article-title":"Interaction of cisplatin with human serum albumin. Drug binding mode and protein secondary structure. Biochim. Biophys.","volume":"1384","author":"JF Neault","year":"1998","journal-title":"Acta"},{"key":"ref43","first-page":"69","article-title":"Spectroscopic studies on the effect of temperature on pH-induced folded states of human serum albumin, Photochem Photobiol B","volume":"90","author":"AK Shaw","year":"2008"},{"key":"ref44","first-page":"263","article-title":"Differential scanning calorimetric studies on bovine serum albumin: I. Effects of pH and ionic strength. Int. J. Biol. Macromol.","volume":"12","author":"M Yamasaki","year":"1990"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.bpc.2004.04.005","article-title":"Vibrational circular dichroism spectra of protein films: thermal denaturation of bovine serum albumin.","volume":"111","author":"G Shanmugam","year":"2004","journal-title":"Biophys Chem"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/0167-4838(88)90107-0","article-title":"New insight into protein secondary structure from resolution-enhanced infrared spectra.","volume":"952","author":"WK Surewicz","year":"1988","journal-title":"Biochim Biophys Acta"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1002\/(SICI)1520-6343(1998)4:2<93::AID-BSPY2>3.0.CO;2-T","article-title":"Predictions of protein secondary structures using factor analysis on Fourier transform infrared spectra: effect of Fourier self-deconvolution of the amide I and amide II bands<bold>.<\/bold>","volume":"4","author":"S Wi","year":"1998","journal-title":"Biospectroscopy"},{"key":"ref48","article-title":"Secondary structure determination of proteins in aqueous solution by infrared spectroscopy: a comparison of multivariate data analysis methods. Anal. Biochem.","volume":"5\u201313","author":"K Rahmelow","year":"1996","journal-title":"241 (1996)"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"113638","DOI":"10.1021\/bi970332p","article-title":"Rigidity of human alpha-fetoprotein tertiary structure is under ligand control.","volume":"36","author":"VN Uversky","year":"1997","journal-title":"Biochemistry"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1399-3011.1990.tb00714.x","article-title":"Structural transition of bovine plasma albumin in the alkaline region\u2013the N-B transition.","volume":"35","author":"S Era","year":"1990","journal-title":"Int J Pept Protein Res"},{"key":"ref51","first-page":"263","article-title":"Circular dichroic and fluoropolarimetric studies on tryptophyl residues in acid-induced isomerization of bovine plasma albumin. Int. J. Pept. Protein Res.","volume":"19","author":"M Sogami","year":"1982"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"3042","DOI":"10.1074\/jbc.275.5.3042","article-title":"Conformational transitions of the three recombinant domains of human serum albumin depending on pH.","volume":"275","author":"M Dockal","year":"2000","journal-title":"J Biol Chem"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"e17230","DOI":"10.1371\/journal.pone.0017230","article-title":"Elimination of endogenous toxin, creatinine from blood plasma depends on albumin conformation: site specific uremic toxicity and impaired drug binding.","volume":"6","author":"A Varshney","year":"2011","journal-title":"Plos One"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"1806","DOI":"10.1093\/bioinformatics\/btr284","article-title":"Evaluation of drug-human serum albumin binding interactions with support vector machine aided online automated docking.","volume":"27","author":"F Zsila","year":"2011","journal-title":"Bioinformatics,"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0037468","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,3,28]],"date-time":"2025-03-28T18:13:32Z","timestamp":1743185612000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0037468"}},"subtitle":[],"editor":[{"given":"Eugene A.","family":"Permyakov","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2012,5,23]]},"references-count":54,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2012,5,23]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0037468","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,5,23]]}}}