{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T05:33:57Z","timestamp":1790314437989,"version":"4.1.0"},"reference-count":59,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2010,12,1]],"date-time":"2010-12-01T00:00:00Z","timestamp":1291161600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2010,12,1]],"date-time":"2010-12-01T00:00:00Z","timestamp":1291161600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2010,12,1]],"date-time":"2010-12-01T00:00:00Z","timestamp":1291161600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2010,12,1]],"date-time":"2010-12-01T00:00:00Z","timestamp":1291161600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2010,12,1]],"date-time":"2010-12-01T00:00:00Z","timestamp":1291161600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2010,12,1]],"date-time":"2010-12-01T00:00:00Z","timestamp":1291161600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2010,12,1]],"date-time":"2010-12-01T00:00:00Z","timestamp":1291161600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["T90 DK070109-05"],"award-info":[{"award-number":["T90 DK070109-05"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2010,12]]},"DOI":"10.1016\/j.jmb.2010.10.008","type":"journal-article","created":{"date-parts":[[2010,10,17]],"date-time":"2010-10-17T04:13:53Z","timestamp":1287288833000},"page":"832-846","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":78,"title":["Multiple Global Suppressors of Protein Stability Defects Facilitate the Evolution of Extended-Spectrum TEM \u03b2-Lactamases"],"prefix":"10.1016","volume":"404","author":[{"given":"Nicholas G.","family":"Brown","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeanine M.","family":"Pennington","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wanzhi","family":"Huang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tulin","family":"Ayvaz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Timothy","family":"Palzkill","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2010.10.008_bb0005","doi-asserted-by":"crossref","first-page":"8801","DOI":"10.1073\/pnas.94.16.8801","article-title":"A natural polymorphism in beta-lactamase is a global suppressor","volume":"94","author":"Huang","year":"1997","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.10.008_bb0010","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1038\/84981","article-title":"Predicting the emergence of antibiotic resistance by directed evolution and structural analysis","volume":"8","author":"Orencia","year":"2001","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0015","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0022-2836(02)00400-X","article-title":"Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs","volume":"320","author":"Wang","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0020","doi-asserted-by":"crossref","first-page":"9995","DOI":"10.1073\/pnas.0901522106","article-title":"In the light of directed evolution: pathways of adaptive protein evolution","volume":"106","author":"Bloom","year":"2009","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.10.008_bb0025","doi-asserted-by":"crossref","first-page":"5869","DOI":"10.1073\/pnas.0510098103","article-title":"Protein stability promotes evolvability","volume":"103","author":"Bloom","year":"2006","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.10.008_bb0030","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1073\/pnas.0406744102","article-title":"Thermodynamic prediction of protein neutrality","volume":"102","author":"Bloom","year":"2005","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.10.008_bb0035","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1093\/protein\/gzp006","article-title":"Directed evolution of an extremely stable fluorescent protein","volume":"22","author":"Kiss","year":"2009","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.jmb.2010.10.008_bb0040","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1038\/nrm2805","article-title":"Exploring protein fitness landscapes by directed evolution","volume":"10","author":"Romero","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0045","doi-asserted-by":"crossref","first-page":"3714","DOI":"10.1529\/biophysj.105.062125","article-title":"Predicting the tolerance of proteins to random amino acid substitution","volume":"89","author":"Wilke","year":"2005","journal-title":"Biophys. J."},{"key":"10.1016\/j.jmb.2010.10.008_bb0050","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.tim.2006.07.008","article-title":"The beta-lactamase threat in Enterobacteriaceae, Pseudomonas and Acinetobacter","volume":"14","author":"Livermore","year":"2006","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0055","series-title":"Enzyme Structure and Mechanism","author":"Fersht","year":"1985"},{"key":"10.1016\/j.jmb.2010.10.008_bb0060","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1111\/j.1365-2958.1995.tb02404.x","article-title":"Beta-lactamases and bacterial resistance to antibiotics","volume":"16","author":"Frere","year":"1995","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0065","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1128\/CMR.18.4.657-686.2005","article-title":"Extended-spectrum beta-lactamases: a clinical update","volume":"18","author":"Paterson","year":"2005","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.jmb.2010.10.008_bb0070","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.resmic.2004.02.009","article-title":"Characteristics, epidemiology and clinical importance of emerging strains of Gram-negative bacilli producing extended-spectrum beta-lactamases","volume":"155","author":"Shah","year":"2004","journal-title":"Res. Microbiol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0075","first-page":"853","article-title":"Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism","volume":"266","author":"Christensen","year":"1990","journal-title":"Biochem. J."},{"key":"10.1016\/j.jmb.2010.10.008_bb0080","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/S0966-842X(98)01317-1","article-title":"Beta-lactamases: protein evolution in real time","volume":"6","author":"Petrosino","year":"1998","journal-title":"Trends Microbiol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0085","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1128\/CMR.00037-09","article-title":"Three decades of beta-lactamase inhibitors","volume":"23","author":"Drawz","year":"2010","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.jmb.2010.10.008_bb0090","doi-asserted-by":"crossref","first-page":"2593","DOI":"10.1128\/AAC.39.12.2593","article-title":"Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure","volume":"39","author":"Knox","year":"1995","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jmb.2010.10.008_bb0095","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.jmb.2009.11.005","article-title":"Structural bases for stability\u2013function tradeoffs in antibiotic resistance","volume":"396","author":"Thomas","year":"2010","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0100","first-page":"4","article-title":"How protein stability and new functions trade off","volume":"e1000002","author":"Tokuriki","year":"2008","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0105","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1073\/pnas.92.2.452","article-title":"A relationship between protein stability and protein function","volume":"92","author":"Shoichet","year":"1995","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.10.008_bb0110","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1002\/prot.10016","article-title":"Why are proteins marginally stable?","volume":"46","author":"Taverna","year":"2002","journal-title":"Proteins"},{"key":"10.1016\/j.jmb.2010.10.008_bb0115","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1016\/j.jmb.2008.04.024","article-title":"Intense neutral drifts yield robust and evolvable consensus proteins","volume":"379","author":"Bershtein","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0120","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.jmb.2008.09.009","article-title":"Genetic and structural characterization of an L201P global suppressor substitution in TEM-1 beta-lactamase","volume":"384","author":"Marciano","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0125","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1126\/science.1648264","article-title":"Global suppression of protein folding defects and inclusion body formation","volume":"253","author":"Mitraki","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.jmb.2010.10.008_bb0130","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1093\/genetics\/110.4.539","article-title":"Genetic analysis of staphylococcal nuclease: identification of three intragenic \u201cglobal\u201d suppressors of nuclease-minus mutations","volume":"110","author":"Shortle","year":"1985","journal-title":"Genetics"},{"key":"10.1016\/j.jmb.2010.10.008_bb0135","doi-asserted-by":"crossref","first-page":"596","DOI":"10.1016\/j.sbi.2009.08.003","article-title":"Stability effects of mutations and protein evolvability","volume":"19","author":"Tokuriki","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0140","first-page":"283","article-title":"A secondary drug resistance mutation of TEM-1 beta-lactamase that suppresses misfolding and aggregation","volume":"98","author":"Sideraki","year":"2001","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.jmb.2010.10.008_bb0145","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.jmb.2008.07.082","article-title":"Increased folding stability of TEM-1 beta-lactamase by in vitro selection","volume":"383","author":"Kather","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0150","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1111\/j.1574-6976.2010.00222.x","article-title":"Natural evolution of TEM-1 beta-lactamase: experimental reconstruction and clinical relevance","volume":"34","author":"Salverda","year":"2010","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.jmb.2010.10.008_bb0155","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1002\/prot.340230108","article-title":"Stability of TEM beta-lactamase mutants hydrolyzing third generation cephalosporins","volume":"23","author":"Raquet","year":"1995","journal-title":"Proteins"},{"key":"10.1016\/j.jmb.2010.10.008_bb0160","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1098\/rstb.1980.0049","article-title":"The structure of beta-lactamases","volume":"289","author":"Ambler","year":"1980","journal-title":"Philos. Trans. R. Soc. London Ser. B"},{"key":"10.1016\/j.jmb.2010.10.008_bb0165","doi-asserted-by":"crossref","first-page":"12640","DOI":"10.1021\/bi0501885","article-title":"Structural perturbation and compensation by directed evolution at physiological temperature leads to thermostabilization of \u03b2-lactamase","volume":"44","author":"Hecky","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.10.008_bb0170","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1002\/(SICI)1097-0290(20000405)68:1<121::AID-BIT15>3.0.CO;2-X","article-title":"Rapid in vivo evolution of a \u03b2-lactamase using phagemids","volume":"68","author":"Long-McGie","year":"2000","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.jmb.2010.10.008_bb0175","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1093\/protein\/15.6.463","article-title":"Improving a circularly permuted TEM-1 beta-lactamase by directed evolution","volume":"15","author":"Osuna","year":"2002","journal-title":"Protein. Eng."},{"key":"10.1016\/j.jmb.2010.10.008_bb0180","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1093\/jac\/43.4.447","article-title":"Inhibitor-resistant TEM beta-lactamases: phenotypic, genetic and biochemical characteristics","volume":"43","author":"Chaibi","year":"1999","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.jmb.2010.10.008_bb0185","doi-asserted-by":"crossref","first-page":"4557","DOI":"10.1021\/bi9003292","article-title":"The role of a second-shell residue in modifying substrate and inhibitor interactions in the SHV beta-lactamase: a study of Ambler position Asn276","volume":"48","author":"Drawz","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.10.008_bb0190","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1093\/jac\/43.1.23","article-title":"Aspartic acid for asparagine substitution at position 276 reduces susceptibility to mechanism-based inhibitors in SHV-1 and SHV-5 beta-lactamases","volume":"43","author":"Giakkoupi","year":"1999","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.jmb.2010.10.008_bb0195","doi-asserted-by":"crossref","first-page":"2080","DOI":"10.1002\/pro.220","article-title":"Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamase","volume":"18","author":"Marciano","year":"2009","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2010.10.008_bb0200","doi-asserted-by":"crossref","first-page":"18240","DOI":"10.1074\/jbc.270.31.18240","article-title":"The asparagine to aspartic acid substitution at position 276 of TEM-35 and TEM-36 is involved in the beta-lactamase resistance to clavulanic acid","volume":"270","author":"Saves","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.10.008_bb0205","doi-asserted-by":"crossref","first-page":"9330","DOI":"10.1021\/bi0502700","article-title":"Structural consequences of the inhibitor-resistant Ser130Gly substitution in TEM beta-lactamase","volume":"44","author":"Thomas","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.10.008_bb0210","doi-asserted-by":"crossref","first-page":"17676","DOI":"10.1074\/jbc.M611548200","article-title":"Thermodynamic investigation of the role of contact residues of beta-lactamase-inhibitory protein for binding to TEM-1 beta-lactamase","volume":"282","author":"Wang","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.10.008_bb0215","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1002\/prot.10058","article-title":"Noncovalent interaction energies in covalent complexes: TEM-1 beta-lactamase and beta-lactams","volume":"47","author":"Wang","year":"2002","journal-title":"Proteins"},{"key":"10.1016\/j.jmb.2010.10.008_bb0220","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1002\/prot.340160406","article-title":"Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8\u00a0\u00c5 resolution","volume":"16","author":"Jelsch","year":"1993","journal-title":"Proteins"},{"key":"10.1016\/j.jmb.2010.10.008_bb0225","doi-asserted-by":"crossref","first-page":"9570","DOI":"10.1021\/bi990758z","article-title":"X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid","volume":"38","author":"Swaren","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2010.10.008_bb0230","doi-asserted-by":"crossref","first-page":"2266","DOI":"10.1128\/AAC.38.10.2266","article-title":"Effect of threonine-to-methionine substitution at position 265 on structure and function of TEM-1 beta-lactamase","volume":"38","author":"Huang","year":"1994","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jmb.2010.10.008_bb0235","doi-asserted-by":"crossref","first-page":"1323","DOI":"10.1128\/AAC.42.6.1323","article-title":"Phenotypic study of resistance of beta-lactamase-inhibitor-resistant TEM enzymes which differ by naturally occurring variations and by site-directed substitution at Asp276","volume":"42","author":"Canica","year":"1998","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.jmb.2010.10.008_bb0240","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1110\/ps.9.5.1035","article-title":"Temperature-sensitive suppressor mutations of the Escherichia coli DNA gyrase B protein","volume":"9","author":"Blance","year":"2000","journal-title":"Protein Sci."},{"key":"10.1016\/j.jmb.2010.10.008_bb0245","doi-asserted-by":"crossref","first-page":"11640","DOI":"10.1016\/S0021-9258(18)99005-8","article-title":"Identification of global suppressors for temperature-sensitive folding mutations of the P22 tailspike protein","volume":"266","author":"Fane","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.10.008_bb0250","doi-asserted-by":"crossref","first-page":"23191","DOI":"10.1016\/S0021-9258(18)54482-3","article-title":"Molecular properties of global suppressors of temperature-sensitive folding mutations in P22 tailspike endorhamnosidase","volume":"266","author":"Lee","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.10.008_bb0255","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1093\/emboj\/19.3.370","article-title":"Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations","volume":"19","author":"Nikolova","year":"2000","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2010.10.008_bb0260","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.bpc.2009.08.008","article-title":"Molecular mechanisms of functional rescue mediated by p53 tumor suppressor mutations","volume":"145","author":"Tan","year":"2009","journal-title":"Biophys. Chem."},{"key":"10.1016\/j.jmb.2010.10.008_bb0265","doi-asserted-by":"crossref","first-page":"688","DOI":"10.1006\/jmbi.1996.0279","article-title":"Amino acid sequence determinants of beta-lactamase structure and activity","volume":"258","author":"Huang","year":"1996","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0270","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1002\/prot.340140106","article-title":"Probing beta-lactamase structure and function using random replacement mutagenesis","volume":"14","author":"Palzkill","year":"1992","journal-title":"Proteins"},{"key":"10.1016\/j.jmb.2010.10.008_bb0275","doi-asserted-by":"crossref","first-page":"1330","DOI":"10.1126\/science.2466339","article-title":"Receptor and antibody epitopes in human growth hormone identified by homolog-scanning mutagenesis","volume":"243","author":"Cunningham","year":"1989","journal-title":"Science"},{"key":"10.1016\/j.jmb.2010.10.008_bb0280","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1006\/prep.2000.1243","article-title":"Overexpression and biosynthetic deuterium enrichment of TEM-1 beta-lactamase for structural characterization by magnetic resonance methods","volume":"19","author":"Sosa-Peinado","year":"2000","journal-title":"Protein Expression Purif."},{"key":"10.1016\/j.jmb.2010.10.008_bb0285","doi-asserted-by":"crossref","first-page":"29144","DOI":"10.1074\/jbc.272.46.29144","article-title":"Cephalosporin substrate specificity determinants of TEM-1 beta-lactamase","volume":"272","author":"Cantu","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2010.10.008_bb0290","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1007\/978-1-60327-058-8_28","article-title":"Automated structure solution with the PHENIX suite","volume":"426","author":"Zwart","year":"2008","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jmb.2010.10.008_bb0295","doi-asserted-by":"crossref","first-page":"1948","DOI":"10.1107\/S0907444902016657","article-title":"PHENIX: building new software for automated crystallographic structure determination","volume":"58","author":"Adams","year":"2002","journal-title":"Acta Crystallogr. Sect. D"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283610011058?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283610011058?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T06:11:35Z","timestamp":1762668695000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283610011058"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,12]]},"references-count":59,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2010,12]]}},"alternative-id":["S0022283610011058"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2010.10.008","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2010,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Multiple Global Suppressors of Protein Stability Defects Facilitate the Evolution of Extended-Spectrum TEM \u03b2-Lactamases","name":"articletitle","label":"Article Title"},{"value":"Journal of Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jmb.2010.10.008","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2010 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}