{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,9]],"date-time":"2025-11-09T07:24:21Z","timestamp":1762673061118,"version":"build-2065373602"},"reference-count":28,"publisher":"Elsevier BV","issue":"1","license":[{"start":{"date-parts":[[2001,7,1]],"date-time":"2001-07-01T00:00:00Z","timestamp":993945600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2001,7,1]],"date-time":"2001-07-01T00:00:00Z","timestamp":993945600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["99R16701"],"award-info":[{"award-number":["99R16701"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2001,7]]},"DOI":"10.1006\/bbrc.2001.5118","type":"journal-article","created":{"date-parts":[[2002,9,16]],"date-time":"2002-09-16T09:50:03Z","timestamp":1032169803000},"page":"9-14","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":20,"title":["Force Measurement and Inhibitor Binding Assay of Monomer and Engineered Dimer of Bovine Carbonic Anhydrase B"],"prefix":"10.1006","volume":"285","author":[{"given":"Tong","family":"Wang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hideo","family":"Arakawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Atsushi","family":"Ikai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1006\/bbrc.2001.5118_RF1","doi-asserted-by":"crossref","first-page":"930","DOI":"10.1103\/PhysRevLett.56.930","article-title":"Atomic force microscope","volume":"56","author":"Binning","year":"1986","journal-title":"Phys. Rev. Lett."},{"key":"10.1006\/bbrc.2001.5118_RF2","doi-asserted-by":"crossref","first-page":"2226","DOI":"10.1016\/S0006-3495(95)80147-5","article-title":"Method for immobilizing microbial cells on gel surface for dynamic AFM studies","volume":"69","author":"Gad","year":"1995","journal-title":"Biophys. J."},{"key":"10.1006\/bbrc.2001.5118_RF3","doi-asserted-by":"crossref","first-page":"1672","DOI":"10.1016\/S0006-3495(95)80343-7","article-title":"Applications for atomic force microscopy of DNA","volume":"68","author":"Hansma","year":"1995","journal-title":"Biophys. J."},{"key":"10.1006\/bbrc.2001.5118_RF4","first-page":"75","article-title":"Measurement of mechanical properties of human chromosomes using atomic force microscopy","volume":"2","author":"Xu","year":"1997","journal-title":"Cell Eng."},{"key":"10.1006\/bbrc.2001.5118_RF5","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1038\/78929","article-title":"Observing single biomolecules at work with the atomic force microscope","volume":"7","author":"Engel","year":"2000","journal-title":"Nat. Struct. Biol."},{"key":"10.1006\/bbrc.2001.5118_RF6","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1038\/14907","article-title":"Single protein misfolding events captured by atomic force microscopy","volume":"6","author":"Oberhauser","year":"1999","journal-title":"Nat. Struct. Biol."},{"key":"10.1006\/bbrc.2001.5118_RF7","doi-asserted-by":"crossref","first-page":"3694","DOI":"10.1073\/pnas.96.7.3694","article-title":"Mechanical and chemical unfolding of a single protein: A comparison","volume":"96","author":"Carrion-Vazquez","year":"1999","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/bbrc.2001.5118_RF8","doi-asserted-by":"crossref","first-page":"3008","DOI":"10.1016\/S0006-3495(98)77741-0","article-title":"The mechanical stability of immunoglobulin and fibronection III domains in the muscle protein titin measured by atomic force microscope","volume":"75","author":"Rief","year":"1998","journal-title":"Biophys. J."},{"key":"10.1006\/bbrc.2001.5118_RF9","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1006\/jmbi.1998.2466","article-title":"Single molecule force microscopy of spectrin repeats: Low unfolding forces in helix bundles","volume":"286","author":"Rief","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1006\/bbrc.2001.5118_RF10","doi-asserted-by":"crossref","first-page":"6517","DOI":"10.1073\/pnas.120048697","article-title":"Atomic force microscopy reveals the mechanical design of a modular protein","volume":"97","author":"Li","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/bbrc.2001.5118_RF11","doi-asserted-by":"crossref","first-page":"5439","DOI":"10.1021\/bi9722756","article-title":"Direct force measurement of insulin monomer\u2013monomer interactions","volume":"37","author":"Yip","year":"1998","journal-title":"Biochemistry"},{"key":"10.1006\/bbrc.2001.5118_RF12","doi-asserted-by":"crossref","first-page":"763","DOI":"10.1093\/protein\/13.11.763","article-title":"Spring mechanics of \u03b1-helical polypeptide","volume":"13","author":"Alimjian","year":"2000","journal-title":"Protein Eng."},{"key":"10.1006\/bbrc.2001.5118_RF13","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/S0968-0004(99)01453-X","article-title":"The study of protein mechanics with the atomic force microscope","volume":"24","author":"Fisher","year":"1999","journal-title":"Trends Biochem. Sci."},{"key":"10.1006\/bbrc.2001.5118_RF14","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0079-6107(00)00017-1","article-title":"Mechanical design of proteins studied of single-molecule force spectroscopy and protein engineering","volume":"74","author":"Carrion-Vaqzuez","year":"2000","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1006\/bbrc.2001.5118_RF15","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0079-6107(00)00014-6","article-title":"Single molecule force spectroscopy in biology using the atomic force microscope","volume":"74","author":"Zlatanova","year":"2000","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1006\/bbrc.2001.5118_RF16","doi-asserted-by":"crossref","first-page":"3912","DOI":"10.1143\/JJAP.38.3912","article-title":"Protein stretching. III. Force\u2013extension curves of tethered bovine carbonic anhydrase B to the silicon substrate under native, intermediate and denaturing conditions","volume":"38","author":"Wang","year":"1999","journal-title":"Jpn. J. Appl. Phys."},{"key":"10.1006\/bbrc.2001.5118_RF17","doi-asserted-by":"crossref","first-page":"3784","DOI":"10.1143\/JJAP.39.3784","article-title":"Protein stretching. IV. Analysis of force extension curves","volume":"39","author":"Ikai","year":"2000","journal-title":"Jpn. J. Appl. Phys."},{"key":"10.1006\/bbrc.2001.5118_RF18","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1126\/science.288.5463.143","article-title":"Unfolding pathways of individual bacteriorhodopsius","volume":"288","author":"Oesterhelt","year":"2000","journal-title":"Science"},{"key":"10.1006\/bbrc.2001.5118_RF19","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/0014-5793(91)80922-P","article-title":"Folding around the C-terminus of human carbonic anhydrase II kinetic characterization by use of a chemically reactive SH-group introduced by protein","volume":"289","author":"Freskg\u00e5rd","year":"1991","journal-title":"FEBS Lett."},{"key":"10.1006\/bbrc.2001.5118_RF20","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1111\/j.1399-3011.1989.tb00199.x","article-title":"Evidence for an initial fast nucleation process in the folding of human carbonic anhydrase I","volume":"33","author":"Bergenhem","year":"1989","journal-title":"Int. J. Peptide Protein Res."},{"key":"10.1006\/bbrc.2001.5118_RF21","unstructured":"Saito, R, Ikai, A, and, Tanaka, N. 2001, To be published."},{"key":"10.1006\/bbrc.2001.5118_RF22","doi-asserted-by":"crossref","first-page":"2785","DOI":"10.1016\/S0021-9258(19)44075-1","article-title":"Monocarboxamidomethyl carbonic anhydrase purified by affinity chromatography","volume":"248","author":"Whitney","year":"1973","journal-title":"J. Biol. Chem."},{"key":"10.1006\/bbrc.2001.5118_RF23","doi-asserted-by":"crossref","first-page":"5813","DOI":"10.1016\/S0021-9258(18)99374-9","article-title":"Combination of bovine carbonic anhydrase with a fluorescent sulfonamide","volume":"242","author":"Chen","year":"1967","journal-title":"J. Biol. Chem."},{"key":"10.1006\/bbrc.2001.5118_RF24","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1038\/360719a0","article-title":"Evidence of a transition temperature for the optimum deposition of grafted monolayer coatings","volume":"360","author":"Brzoska","year":"1992","journal-title":"Nature"},{"key":"10.1006\/bbrc.2001.5118_RF25","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.1063\/1.1143970","article-title":"Calibration of atomic force microscopy tips","volume":"64","author":"Hutter","year":"1993","journal-title":"Rev. Sci. Instrum."},{"key":"10.1006\/bbrc.2001.5118_RF26","doi-asserted-by":"crossref","first-page":"S121","DOI":"10.1007\/s003390100650","article-title":"Protein stretching. V. Two forms of carbonic dehydratase detected by force microscopy","volume":"72","author":"Alam","year":"2000","journal-title":"Appl. Phys. A"},{"key":"10.1006\/bbrc.2001.5118_RF27","doi-asserted-by":"crossref","first-page":"5918","DOI":"10.1021\/bi00266a029","article-title":"Detection and characterization using circular dichroism and fluorescence spectroscopy of a stable intermediate conformation formed in the denaturation of bovine carbonic anhydrase with guanidinium chloride","volume":"21","author":"Henkers","year":"1982","journal-title":"Biochemistry"},{"key":"10.1006\/bbrc.2001.5118_RF28","doi-asserted-by":"crossref","first-page":"2658","DOI":"10.1021\/bi00280a011","article-title":"Nitrogen-15 nuclear magnetic resonance study of benzensulfonamide and cyanate binding to carbonic anhydrase","volume":"22","author":"Kanamori","year":"1983","journal-title":"Biochemistry"}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X01951186?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X01951186?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,2]],"date-time":"2025-11-02T14:06:27Z","timestamp":1762092387000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X01951186"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,7]]},"references-count":28,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2001,7]]}},"alternative-id":["S0006291X01951186"],"URL":"https:\/\/doi.org\/10.1006\/bbrc.2001.5118","relation":{},"ISSN":["0006-291X"],"issn-type":[{"type":"print","value":"0006-291X"}],"subject":[],"published":{"date-parts":[[2001,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Force Measurement and Inhibitor Binding Assay of Monomer and Engineered Dimer of Bovine Carbonic Anhydrase B","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1006\/bbrc.2001.5118","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"converted-article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2001 Academic Press. All rights reserved.","name":"copyright","label":"Copyright"}]}}