{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,22]],"date-time":"2026-01-22T09:06:11Z","timestamp":1769072771280,"version":"3.49.0"},"reference-count":39,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2004,4,1]],"date-time":"2004-04-01T00:00:00Z","timestamp":1080777600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2004,4]]},"DOI":"10.1016\/j.bbrc.2004.02.083","type":"journal-article","created":{"date-parts":[[2004,2,27]],"date-time":"2004-02-27T10:21:49Z","timestamp":1077877309000},"page":"559-564","source":"Crossref","is-referenced-by-count":9,"title":["The osmoprotectants glycine and its methyl derivatives prevent the thermal inactivation of protective antigen of Bacillus anthracis"],"prefix":"10.1016","volume":"316","author":[{"given":"Samer","family":"Singh","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mohd.Azhar","family":"Aziz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Puneet","family":"Khandelwal","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rajiv","family":"Bhat","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rakesh","family":"Bhatnagar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2004.02.083_BIB1","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/0264-410X(91)90237-Z","article-title":"Anthrax vaccines: past, present and future","volume":"9","author":"Turnbull","year":"1991","journal-title":"Vaccine"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB2","series-title":"Pharmacology of Bacterial Toxins","first-page":"381","article-title":"Anthrax toxin","author":"Stephen","year":"1986"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB3","series-title":"Handbook of Experimental Pharmacology: Bacterial Protein Toxins","first-page":"445","article-title":"Anthrax toxin","author":"Leppla","year":"2000"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB4","doi-asserted-by":"crossref","first-page":"1274","DOI":"10.1128\/JB.83.6.1274-1280.1962","article-title":"Rapid lethal effect in rats of a third component found upon fractionating the toxin of Bacillus anthracis","volume":"83","author":"Beall","year":"1962","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB5","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.1111\/j.1365-2958.1994.tb00500.x","article-title":"Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence, which is required for lethal toxin activity","volume":"13","author":"Klimpel","year":"1994","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB6","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1126\/science.280.5364.734","article-title":"Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor","volume":"280","author":"Duesbery","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB7","doi-asserted-by":"crossref","first-page":"706","DOI":"10.1006\/bbrc.1998.9040","article-title":"Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine\/threonine phosphorylation of MAPKs in cultured macrophages","volume":"248","author":"Vitale","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB8","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1042\/bj3520739","article-title":"Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor","volume":"352","author":"Vitale","year":"2000","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB9","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/0378-1119(88)90342-3","article-title":"Cloning and expression of the calmodulin-sensitive Bacillus anthracis adenylate cyclase in Escherichia coli","volume":"64","author":"Mock","year":"1988","journal-title":"Gene"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB10","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1016\/S0264-410X(98)80112-6","article-title":"Comparative efficacy of experimental anthrax vaccine candidates against inhalation anthrax in rhesus macaques","volume":"16","author":"Ivins","year":"1998","journal-title":"Vaccine"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB11","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1006\/prep.1999.1066","article-title":"Expression and purification of the recombinant protective antigen of Bacillus anthracis","volume":"16","author":"Gupta","year":"1999","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB12","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1006\/bbrc.2001.4777","article-title":"Constitutive expression of protective antigen gene of Bacillus anthracis in Escherichia coli","volume":"283","author":"Chauhan","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB13","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/0168-1656(96)01569-6","article-title":"Thermostabilization of protective antigen\u2014the binding component of anthrax lethal toxin","volume":"50","author":"Radha","year":"1996","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB14","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0378-5173(99)00152-0","article-title":"Instability, stabilization, and formulation of liquid protein pharmaceuticals","volume":"185","author":"Wang","year":"1999","journal-title":"Int. J. Pharm."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB15","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/S0021-9258(17)42341-6","article-title":"Deamidation and isoaspartate formation during in vitro aging of recombinant tissue plasminogen activator","volume":"269","author":"Paranandi","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB16","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1021\/js9700311","article-title":"Solid-state stability of human insulin. II. Effect of water on reactive intermediate partitioning in lyophiles from pH 2\u20135 solutions: stabilization against covalent dimer formation","volume":"86","author":"Strickley","year":"1997","journal-title":"J. Pharm. Sci."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB17","doi-asserted-by":"crossref","first-page":"15142","DOI":"10.1074\/jbc.M212180200","article-title":"Deamidations in recombinant human phenylalanine hydroxylase. Identification of labile asparagine residues and functional characterization of Asn\u2192Asp mutant forms","volume":"278","author":"Carvalho","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB18","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1096\/fasebj.10.1.8566551","article-title":"Forces contributing to the conformational stability of proteins","volume":"10","author":"Pace","year":"1996","journal-title":"FASEB J."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB19","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/S0958-1669(02)00325-7","article-title":"Selection of mutations for increased protein stability","volume":"13","author":"van den Burg","year":"2002","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB20","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/MMBR.65.1.1-43.2001","article-title":"Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability","volume":"65","author":"Vieille","year":"2001","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB21","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1016\/S0006-291X(02)02049-1","article-title":"Gln277 and Phe554 residues are involved in thermal inactivation of protective antigen of Bacillus anthracis","volume":"296","author":"Singh","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB22","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/S0141-0229(03)00160-1","article-title":"Enzyme stabilization\u2014recent experimental progress","volume":"33","author":"Fagain","year":"2003","journal-title":"Enzyme Microb. Technol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB23","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1126\/science.7112124","article-title":"Living with water stress: evolution of osmolyte systems","volume":"217","author":"Yancey","year":"1982","journal-title":"Science"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB24","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1007\/s002030050649","article-title":"Uptake and synthesis of compatible solutes as microbial stress responses to high-osmolality environments","volume":"170","author":"Kempf","year":"1998","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB25","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/S0065-3233(08)60656-7","article-title":"Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated","volume":"51","author":"Timasheff","year":"1998","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB26","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/0003-9861(83)90201-1","article-title":"Preferential interactions of proteins with solvent components in aqueous amino acid solutions","volume":"224","author":"Arakawa","year":"1983","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB27","doi-asserted-by":"crossref","first-page":"12884","DOI":"10.1021\/bi00039a051","article-title":"The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes","volume":"34","author":"Liu","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB28","doi-asserted-by":"crossref","first-page":"5278","DOI":"10.1021\/bi00138a006","article-title":"Increased thermal stability of proteins in the presence of naturally occurring osmolytes","volume":"31","author":"Santoro","year":"1992","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB29","doi-asserted-by":"crossref","first-page":"2769","DOI":"10.1039\/ft9938902769","article-title":"Effect of osmoregulatory solutes on the stability of proteins","volume":"89","author":"Gopal","year":"1993","journal-title":"J. Chem. Soc., Faraday Trans."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB30","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/S0065-3233(08)60460-X","article-title":"Stability of proteins: small globular proteins","volume":"33","author":"Privalov","year":"1979","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB31","doi-asserted-by":"crossref","first-page":"4176","DOI":"10.1073\/pnas.88.10.4176","article-title":"Protein stability: electrostatics and compact denatured states","volume":"88","author":"Stigter","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2004.02.083_BIB32","first-page":"117","article-title":"An overview of the role and diversity of compatible solutes in Bacteria and Archaea","volume":"61","author":"da Costa","year":"1998","journal-title":"Adv. Biochem. Eng. Biotechnol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB33","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1007\/s00203-001-0368-0","article-title":"Biology of extremophilic and extremotolerant methanotrophs","volume":"177","author":"Trotsenko","year":"2002","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB34","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1007\/BF00590161","article-title":"The salt relations of marine and halophilic species of the unicellular green alga: Dunaliella. The role of glycerol as a compatible solute","volume":"96","author":"Borowitzka","year":"1974","journal-title":"Arch. Microbiol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB35","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1002\/jez.1402080202","article-title":"Solute compatibility with enzyme function and structure: rationales for the selection of osmotic agents and end-products of anaerobic metabolism in marine invertebrates","volume":"208","author":"Bowlus","year":"1979","journal-title":"J. Exp. Zool."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB36","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1016\/S0006-3495(96)79410-9","article-title":"Effect of proline on lactate dehydrogenase activity: testing the generality and scope of the compatibility paradigm","volume":"71","author":"Wang","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB37","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1016\/S0167-7799(98)01251-7","article-title":"Thermotolerance in Saccharomyces cerevisiae: the Yin and Yang of trehalose","volume":"16","author":"Singer","year":"1998","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB38","first-page":"253","article-title":"Solvent stabilization of protein structure","volume":"40","author":"Timasheff","year":"1995","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.bbrc.2004.02.083_BIB39","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1006\/jmbi.2001.4819","article-title":"The osmophobic effect: natural selection of a thermodynamic force in protein folding","volume":"310","author":"Bolen","year":"2001","journal-title":"J. Mol. Biol."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X04003444?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X04003444?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,6,14]],"date-time":"2021-06-14T22:30:25Z","timestamp":1623709825000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X04003444"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2004,4]]},"references-count":39,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2004,4]]}},"alternative-id":["S0006291X04003444"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2004.02.083","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2004,4]]}}}