{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T19:11:09Z","timestamp":1781205069842,"version":"3.54.1"},"reference-count":87,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2015,11,1]],"date-time":"2015-11-01T00:00:00Z","timestamp":1446336000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100002879","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["TGC114046"],"award-info":[{"award-number":["TGC114046"]}],"id":[{"id":"10.13039\/501100002879","id-type":"DOI","asserted-by":"publisher"}]},{"name":"MRC","award":["G1100135"],"award-info":[{"award-number":["G1100135"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"published-print":{"date-parts":[[2015,11]]},"DOI":"10.1016\/j.bbagen.2015.07.012","type":"journal-article","created":{"date-parts":[[2015,8,1]],"date-time":"2015-08-01T16:48:28Z","timestamp":1438447708000},"page":"2228-2238","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":12,"title":["Arginine-containing peptides as potent inhibitors of VIM-2 metallo-\u03b2-lactamase"],"prefix":"10.1016","volume":"1850","author":[{"given":"Caitlyn M.","family":"Rotondo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laura","family":"Marrone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valerie J.","family":"Goodfellow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ahmad","family":"Ghavami","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Genevi\u00e8ve","family":"Labb\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"Spencer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gary I.","family":"Dmitrienko","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefan","family":"Siemann","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbagen.2015.07.012_bb0005","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1021\/cr030102i","article-title":"Bacterial resistance to \u03b2-lactam antibiotics: compelling opportunism, compelling opportunity","volume":"105","author":"Fisher","year":"2005","journal-title":"Chem. Rev."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0010","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1038\/nrmicro2319","article-title":"Antibiotic resistance and its cost: is it possible to reverse resistance?","volume":"8","author":"Andersson","year":"2010","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0015","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1098\/rstb.1980.0049","article-title":"The structure of \u03b2-lactamases","volume":"289","author":"Ambler","year":"1980","journal-title":"Philos. Trans. R. Soc. Lond. Ser. B"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0020","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1021\/ar0400241","article-title":"Metallo-\u03b2-lactamases: novel weaponry for antibiotic resistance in bacteria","volume":"39","author":"Crowder","year":"2006","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0025","doi-asserted-by":"crossref","first-page":"576297","DOI":"10.1155\/2008\/576297","article-title":"The mechanisms of catalysis by metallo-\u03b2-lactamases","volume":"2008","author":"Page","year":"2008","journal-title":"Bioinorg. Chem. Appl."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0030","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1039\/c4mt00066h","article-title":"A variety of roles for versatile zinc in metallo-\u03b2-lactamases","volume":"6","author":"Karsisiotis","year":"2014","journal-title":"Metallomics"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0035","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1128\/AAC.45.3.660-663.2001","article-title":"Standard numbering scheme for class B \u03b2-lactamases","volume":"45","author":"Galleni","year":"2001","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0040","doi-asserted-by":"crossref","first-page":"2347","DOI":"10.1128\/AAC.48.7.2347-2349.2004","article-title":"Update of the standard numbering scheme for class B \u03b2-lactamases","volume":"48","author":"Garau","year":"2004","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0045","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1128\/CMR.18.2.306-325.2005","article-title":"Metallo-\u03b2-lactamases: the quiet before the storm?","volume":"18","author":"Walsh","year":"2005","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0050","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1177\/1060028014556652","article-title":"\u03b2-Lactam\/\u03b2-lactamase inhibitor combinations: from then to now","volume":"49","author":"Toussaint","year":"2015","journal-title":"Ann. Pharmacother."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0055","doi-asserted-by":"crossref","first-page":"651","DOI":"10.2165\/11318430-000000000-00000","article-title":"Current challenges in antimicrobial chemotherapy: focus on \u03b2-lactamase inhibition","volume":"70","author":"Bebrone","year":"2010","journal-title":"Drugs"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0060","doi-asserted-by":"crossref","first-page":"309","DOI":"10.3797\/scipharm.1302-08","article-title":"An update on the status of potent inhibitors of metallo-\u03b2-lactamases","volume":"81","author":"Faridoon","year":"2013","journal-title":"Sci. Pharm."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0065","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.2174\/15680266113139990011","article-title":"Metallo-\u03b2-lactamases: structural features, antibiotic recognition, inhibition, and inhibitor design","volume":"13","author":"Wang","year":"2013","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0070","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1128\/CMR.00037-09","article-title":"Three decades of \u03b2-lactamase inhibitors","volume":"23","author":"Drawz","year":"2010","journal-title":"Clin. Microbiol. Rev."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0075","doi-asserted-by":"crossref","first-page":"1648","DOI":"10.1016\/j.bbapap.2013.04.024","article-title":"Metallo-\u03b2-lactamase: inhibitors and reporter substrates","volume":"1834","author":"Fast","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0080","doi-asserted-by":"crossref","first-page":"1846","DOI":"10.2174\/13895575113139990074","article-title":"\u03b2-Lactamase inhibitors: an update","volume":"13","author":"Chen","year":"2013","journal-title":"Mini Rev. Med. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0085","doi-asserted-by":"crossref","first-page":"689","DOI":"10.2174\/1389450115666140326094504","article-title":"Recent advances in the discovery of metallo-\u03b2-lactamase inhibitors for \u03b2-lactam antibiotic-resistant reversing agents","volume":"15","author":"Guo","year":"2014","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0090","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1128\/AAC.44.4.891-897.2000","article-title":"Characterization of VIM-2, a carbapenem-hydrolyzing metallo-\u03b2-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical isolate in France","volume":"44","author":"Poirel","year":"2000","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0095","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1073\/pnas.98.4.1427","article-title":"A 1.2-angstrom snapshot of the final step of bacterial cell wall biosynthesis","volume":"98","author":"Lee","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0100","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1128\/AAC.43.4.902","article-title":"Biochemical characterization of the Pseudomonas aeruginosa 101\/1477 metallo-\u03b2-lactamase IMP-1 produced by Escherichia coli","volume":"43","author":"Laraki","year":"1999","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0105","doi-asserted-by":"crossref","first-page":"40075","DOI":"10.1074\/jbc.M306466200","article-title":"The metalloproteolytic activity of the anthrax lethal factor is substrate-inhibited","volume":"278","author":"Tonello","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0110","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/0003-9861(59)90090-6","article-title":"Tissue sulfhydryl groups","volume":"82","author":"Ellman","year":"1959","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0115","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/0003-2697(79)90792-9","article-title":"Ellman's reagent: 5,5\u2032-dithiobis(2-nitrobenzoic acid) \u2014 a reexamination","volume":"94","author":"Riddles","year":"1979","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0120","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.ab.2015.06.032","article-title":"Assay for drug discovery: synthesis and testing of nitrocefin analogues for use as \u03b2-lactamase substrates","volume":"486","author":"Ghavami","year":"2015","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0125","doi-asserted-by":"crossref","first-page":"6945","DOI":"10.1021\/jm400769b","article-title":"Assay platform for clinically relevant metallo-\u03b2-lactamases","volume":"56","author":"van Berkel","year":"2013","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0130","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/0022-2836(86)90385-2","article-title":"Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes","volume":"189","author":"Studier","year":"1986","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0135","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/0076-6879(90)85008-C","article-title":"Use of T7 RNA polymerase to direct expression of cloned genes","volume":"185","author":"Studier","year":"1990","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0140","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1093\/jac\/dkg067","article-title":"On functional and structural heterogeneity of VIM-type metallo-\u03b2-lactamases","volume":"51","author":"Docquier","year":"2003","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0145","series-title":"Enzyme Kinetics: Behaviour and Analysis of Rapid Equilibrium and Steady-state Enzyme Systems","author":"Segel","year":"1993"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0150","series-title":"The Organic Chemistry of Enzyme-catalyzed Reactions","author":"Silverman","year":"2000"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0155","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1038\/418386a","article-title":"Screening inhibitors of anthrax lethal factor","volume":"418","author":"Tonello","year":"2002","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0160","doi-asserted-by":"crossref","first-page":"10013","DOI":"10.1021\/bi990356r","article-title":"On the mechanism of the metallo-\u03b2-lactamase from Bacteroides fragilis","volume":"38","author":"Wang","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0165","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1021\/bi9826512","article-title":"Kinetic mechanism of metallo-\u03b2-lactamase L1 from Stenotrophomonas maltophilia","volume":"38","author":"McManus-Munoz","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0170","doi-asserted-by":"crossref","first-page":"3839","DOI":"10.1021\/bi300056y","article-title":"Mechanistic and spectroscopic studies of metallo-\u03b2-lactamase NDM-1","volume":"51","author":"Yang","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0175","doi-asserted-by":"crossref","first-page":"4326","DOI":"10.1128\/AAC.04409-14","article-title":"Meropenem and chromacef intermediates observed in IMP-25 metallo-\u03b2-lactamase-catalyzed hydrolysis","volume":"59","author":"Oelschlaeger","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0180","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1042\/BJ20140364","article-title":"Targeting metallo-carbapenemases via modulation of electronic properties of cephalosporins","volume":"464","author":"Yang","year":"2014","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0185","doi-asserted-by":"crossref","first-page":"9125","DOI":"10.1021\/bi200839h","article-title":"Structural and kinetic studies on metallo-\u03b2-lactamase IMP-1","volume":"50","author":"Griffin","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0190","doi-asserted-by":"crossref","first-page":"20824","DOI":"10.1074\/jbc.M414314200","article-title":"Probing the role of Asp-120(81) of metallo-\u03b2-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography","volume":"280","author":"Yamaguchi","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0195","doi-asserted-by":"crossref","first-page":"10753","DOI":"10.1021\/ja900296u","article-title":"Differential binding of Co(II) and Zn(II) to metallo-\u03b2-lactamase Bla2 from Bacillus anthracis","volume":"131","author":"Hawk","year":"2009","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0200","doi-asserted-by":"crossref","first-page":"507","DOI":"10.3998\/ark.5550190.0004.a47","article-title":"Mechanistic study of the hydrolysis of nitrocefin mediated by B. cereus metallo-\u03b2-lactamase","volume":"3","author":"Rasia","year":"2003","journal-title":"ARKIVOC"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0205","doi-asserted-by":"crossref","first-page":"7321","DOI":"10.1021\/bi500916y","article-title":"Biochemical, mechanistic, and spectroscopic characterization of metallo-\u03b2-lactamase VIM-2","volume":"53","author":"Aitha","year":"2014","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0210","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1128\/JB.181.3.823-832.1999","article-title":"Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations","volume":"181","author":"Mukherjee","year":"1999","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0215","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1111\/j.1432-1033.1997.0425a.x","article-title":"Vinblastine-induced formation of tubulin polymers is electrostatically regulated and nucleated","volume":"250","author":"Rai","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0220","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1016\/S0731-7085(97)00191-X","article-title":"Classical light scattering quantitation of protein aggregates: off-line spectroscopy versus HPLC detection","volume":"16","author":"Kunitani","year":"1997","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0225","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.febslet.2012.11.035","article-title":"Effect of pH on the catalytic function and zinc content of native and immobilized anthrax lethal factor","volume":"587","author":"Montpellier","year":"2013","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0230","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1007\/s13238-011-1027-0","article-title":"An unexpected similarity between antibiotic-resistant NDM-1 and \u03b2-lactamase II from Erythrobacter litoralis","volume":"2","author":"Zheng","year":"2011","journal-title":"Protein Cell"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0235","doi-asserted-by":"crossref","first-page":"4055","DOI":"10.1039\/c0cc05111j","article-title":"Molecular mechanisms of antibiotic resistance","volume":"47","author":"Wright","year":"2011","journal-title":"Chem. Commun."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0240","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/S0968-0896(00)00257-1","article-title":"Cysteinyl peptide inhibitors of Bacillus cereus zinc \u03b2-lactamase","volume":"9","author":"Bounaga","year":"2001","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0245","doi-asserted-by":"crossref","first-page":"5169","DOI":"10.1016\/j.bmcl.2006.07.001","article-title":"Homo-cysteinyl peptide inhibitors of the L1 metallo-\u03b2-lactamase, and SAR as determined by combinatorial library synthesis","volume":"16","author":"Sun","year":"2006","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0250","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1042\/BJ20121305","article-title":"Allosteric inhibition of VIM metallo-\u03b2-lactamases by a camelid nanobody","volume":"450","author":"Sohier","year":"2013","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0255","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S1473-3099(11)70056-1","article-title":"Metallo-\u03b2-lactamases: a last frontier for \u03b2-lactams?","volume":"11","author":"Cornaglia","year":"2011","journal-title":"Lancet Infect. Dis."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0260","doi-asserted-by":"crossref","DOI":"10.2807\/1560-7917.ES2013.18.28.20525","article-title":"Carbapenemase-producing Enterobacteriaceae in Europe: a survey among national experts from 39 countries, February 2013","volume":"18","author":"Glasner","year":"2013","journal-title":"Euro Surveill."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0265","doi-asserted-by":"crossref","first-page":"317","DOI":"10.2217\/fmb.11.13","article-title":"Epidemiology and genetics of VIM-type metallo-\u03b2-lactamases in Gram-negative bacilli","volume":"6","author":"Zhao","year":"2011","journal-title":"Future Microbiol"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0270","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1016\/j.jinorgbio.2014.06.009","article-title":"High metal substitution tolerance of anthrax lethal factor and characterization of its active copper-substituted analogue","volume":"140","author":"Lo","year":"2014","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0275","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1093\/jac\/dkh550","article-title":"A specific peptide inhibitor of the class B metallo-\u03b2-lactamase L-1 from Stenotrophomonas maltophilia identified using phage display","volume":"55","author":"Sanschagrin","year":"2005","journal-title":"J. Antimicrob. Chemother."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0280","doi-asserted-by":"crossref","first-page":"1712","DOI":"10.1021\/jm010533y","article-title":"A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening","volume":"45","author":"McGovern","year":"2002","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0285","doi-asserted-by":"crossref","first-page":"4477","DOI":"10.1021\/jm030191r","article-title":"Identification and prediction of promiscuous aggregating inhibitors among known drugs","volume":"46","author":"Seidler","year":"2003","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0290","doi-asserted-by":"crossref","first-page":"9606","DOI":"10.1021\/ja802977h","article-title":"Stoichiometry and physical chemistry of promiscuous aggregate-based inhibitors","volume":"130","author":"Coan","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0295","doi-asserted-by":"crossref","first-page":"2067","DOI":"10.1021\/jm801605r","article-title":"Promiscuous aggregate-based inhibitors promote enzyme unfolding","volume":"52","author":"Coan","year":"2009","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0300","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/S0003-2697(03)00059-9","article-title":"Detection and prevention of protein aggregation before, during, and after purification","volume":"316","author":"Bondos","year":"2003","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0305","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1016\/S0006-3495(01)75786-4","article-title":"Fluctuations and the Hofmeister effect","volume":"81","author":"Neagu","year":"2001","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0310","doi-asserted-by":"crossref","first-page":"2056","DOI":"10.1016\/S0006-3495(96)79404-3","article-title":"How Hofmeister ion interactions affect protein stability","volume":"71","author":"Baldwin","year":"1996","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0315","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1017\/S0033583500005369","article-title":"The Hofmeister effect and the behaviour of water at interfaces","volume":"18","author":"Collins","year":"1985","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0320","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1016\/j.jmb.2007.11.012","article-title":"The three-dimensional structure of VIM-2, a Zn-\u03b2-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form","volume":"375","author":"Garcia-Saez","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0325","doi-asserted-by":"crossref","first-page":"4288","DOI":"10.1021\/bi992569m","article-title":"Crystal structure of the IMP-1 metallo-\u03b2-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: binding determinants of a potent, broad-spectrum inhibitor","volume":"39","author":"Concha","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0330","doi-asserted-by":"crossref","first-page":"1248","DOI":"10.1128\/AAC.01486-09","article-title":"Biochemical and structural characterization of the subclass B1 metallo-\u03b2-lactamase VIM-4","volume":"55","author":"Lassaux","year":"2011","journal-title":"Antimicrob. Agents Chemother."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0335","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.jmb.2011.05.035","article-title":"Structural and computational investigations of VIM-7: insights into the substrate specificity of vim metallo-\u03b2-lactamases","volume":"411","author":"Borra","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0340","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1111\/febs.13200","article-title":"Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-\u03b2-lactamases","volume":"282","author":"Leiros","year":"2015","journal-title":"FEBS J."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0345","doi-asserted-by":"crossref","first-page":"2352","DOI":"10.1111\/febs.13283","article-title":"The three-dimensional structure of VIM-31 \u2014 a metallo-\u03b2-lactamase from Enterobacter cloacae in its native and oxidized form","volume":"282","author":"Kupper","year":"2015","journal-title":"FEBS J."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0350","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.jmb.2007.10.036","article-title":"Structural insights into the design of inhibitors for the L1 metallo-\u03b2-lactamase from Stenotrophomonas maltophilia","volume":"375","author":"Nauton","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0355","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/S0969-2126(96)00089-5","article-title":"Crystal structure of the wide-spectrum binuclear zinc \u03b2-lactamase from Bacteroides fragilis","volume":"4","author":"Concha","year":"1996","journal-title":"Structure"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0360","doi-asserted-by":"crossref","first-page":"4557","DOI":"10.1073\/pnas.0735920100","article-title":"The hydration structure of guanidinium and thiocyanate ions: implications for protein stability in aqueous solution","volume":"100","author":"Mason","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0365","doi-asserted-by":"crossref","first-page":"7346","DOI":"10.1021\/ja069232+","article-title":"Interactions between hydrophobic and ionic solutes in aqueous guanidinium chloride and urea solutions: lessons for protein denaturation mechanism","volume":"129","author":"O'Brien","year":"2007","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0370","doi-asserted-by":"crossref","first-page":"L04","DOI":"10.1529\/biophysj.107.108290","article-title":"The interaction of guanidinium ions with a model peptide","volume":"93","author":"Mason","year":"2007","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0375","doi-asserted-by":"crossref","first-page":"11462","DOI":"10.1021\/ja040034x","article-title":"The structure of aqueous guanidinium chloride solutions","volume":"126","author":"Mason","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0380","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/0014-5793(86)80730-X","article-title":"Amino\u2013aromatic interactions in proteins","volume":"203","author":"Burley","year":"1986","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0385","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1006\/jmbi.1994.1022","article-title":"Planar stacking interactions of arginine and aromatic side-chains in proteins","volume":"235","author":"Flocco","year":"1994","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0390","doi-asserted-by":"crossref","first-page":"2246","DOI":"10.1021\/jp906976q","article-title":"Unfolding of hydrophobic polymers in guanidinium chloride solutions","volume":"114","author":"Godawat","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0395","doi-asserted-by":"crossref","first-page":"2445","DOI":"10.1002\/cmdc.201402249","article-title":"Diaryl-substituted azolylthioacetamides: inhibitor discovery of New Delhi metallo-\u03b2-lactamase-1 (NDM-1)","volume":"9","author":"Zhang","year":"2014","journal-title":"ChemMedChem"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0400","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1021\/ml500534c","article-title":"Azolylthioacetamide: a highly promising scaffold for the development of metallo-\u03b2-lactamase inhibitors","volume":"6","author":"Yang","year":"2015","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0405","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1038\/nature13445","article-title":"Aspergillomarasmine A overcomes metallo-\u03b2-lactamase antibiotic resistance","volume":"510","author":"King","year":"2014","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0410","doi-asserted-by":"crossref","first-page":"9543","DOI":"10.1039\/C5CC02594J","article-title":"Ebselen as a potent covalent inhibitor of New Delhi metallo-\u03b2-lactamase (NDM-1)","volume":"51","author":"Chiou","year":"2015","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1016\/j.bbagen.2015.07.012_bb0415","doi-asserted-by":"crossref","first-page":"3626","DOI":"10.1021\/jm501844d","article-title":"Approved drugs containing thiols as inhibitors of metallo-\u03b2-lactamases: strategy to combat multidrug-resistant bacteria","volume":"58","author":"Klingler","year":"2015","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0420","doi-asserted-by":"crossref","first-page":"5809","DOI":"10.2174\/13816128113199990003","article-title":"Small cationic antimicrobial peptidomimetics: emerging candidate for the development of potential anti-infective agents","volume":"19","author":"Lohan","year":"2013","journal-title":"Curr. Pharm. Des."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0425","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.2174\/1389557511313070010","article-title":"Recent approaches in design of peptidomimetics for antimicrobial drug discovery research","volume":"13","author":"Lohan","year":"2013","journal-title":"Mini Rev. Med. Chem."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0430","doi-asserted-by":"crossref","first-page":"229","DOI":"10.2147\/IDR.S49229","article-title":"Peptidomimetics as a new generation of antimicrobial agents: current progress","volume":"7","author":"M\u00e9ndez-Samperio","year":"2014","journal-title":"Infect. Drug Resist."},{"key":"10.1016\/j.bbagen.2015.07.012_bb0435","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1517\/13543776.2013.788645","article-title":"Biological activities of guanidine compounds, 2008\u20132012 update","volume":"23","author":"S\u0105czewski","year":"2013","journal-title":"Expert Opin. Ther. Pat."}],"container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416515002081?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416515002081?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,5,19]],"date-time":"2022-05-19T21:00:31Z","timestamp":1652994031000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0304416515002081"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,11]]},"references-count":87,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2015,11]]}},"alternative-id":["S0304416515002081"],"URL":"https:\/\/doi.org\/10.1016\/j.bbagen.2015.07.012","relation":{},"ISSN":["0304-4165"],"issn-type":[{"value":"0304-4165","type":"print"}],"subject":[],"published":{"date-parts":[[2015,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Arginine-containing peptides as potent inhibitors of VIM-2 metallo-\u03b2-lactamase","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - General Subjects","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbagen.2015.07.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}