{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T12:43:55Z","timestamp":1790772235686,"version":"4.1.0"},"reference-count":32,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2010,8,1]],"date-time":"2010-08-01T00:00:00Z","timestamp":1280620800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,7,16]],"date-time":"2013-07-16T00:00:00Z","timestamp":1373932800000},"content-version":"vor","delay-in-days":1080,"URL":"https:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2010,8]]},"DOI":"10.1016\/j.bpj.2010.06.002","type":"journal-article","created":{"date-parts":[[2010,8,18]],"date-time":"2010-08-18T06:16:23Z","timestamp":1282112183000},"page":"1192-1201","source":"Crossref","is-referenced-by-count":43,"title":["The Mechanism of VWF-Mediated Platelet GPIb\u03b1 Binding"],"prefix":"10.1016","volume":"99","author":[{"given":"Matthew","family":"Auton","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cheng","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miguel A.","family":"Cruz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bpj.2010.06.002_bib1","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1055\/s-0038-1657598","article-title":"Mechanisms initiating platelet thrombus formation","volume":"78","author":"Ruggeri","year":"1997","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.bpj.2010.06.002_bib2","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1146\/annurev.biochem.67.1.395","article-title":"Biochemistry and genetics of von Willebrand factor","volume":"67","author":"Sadler","year":"1998","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.bpj.2010.06.002_bib3","doi-asserted-by":"crossref","first-page":"19098","DOI":"10.1074\/jbc.M002292200","article-title":"Mapping the glycoprotein Ib-binding site in the Von Willebrand Factor A1 domain","volume":"275","author":"Cruz","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.bpj.2010.06.002_bib4","doi-asserted-by":"crossref","first-page":"23327","DOI":"10.1074\/jbc.M401659200","article-title":"Crystal structure of the wild-type Von Willebrand Factor A1-glycoprotein Ib\u03b1 complex reveals conformation differences with a complex bearing von Willebrand disease mutations","volume":"279","author":"Dumas","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpj.2010.06.002_bib5","doi-asserted-by":"crossref","first-page":"2939","DOI":"10.1182\/blood.V88.8.2939.bloodjournal8882939","article-title":"Shear-dependent changes in the three-dimensional structure of human von Willebrand factor","volume":"88","author":"Siedlecki","year":"1996","journal-title":"Blood"},{"key":"10.1016\/j.bpj.2010.06.002_bib6","doi-asserted-by":"crossref","first-page":"7899","DOI":"10.1073\/pnas.0608422104","article-title":"Shear-induced unfolding triggers adhesion of von Willebrand factor fibers","volume":"104","author":"Schneider","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2010.06.002_bib7","doi-asserted-by":"crossref","first-page":"3971","DOI":"10.1182\/blood-2001-11-0060","article-title":"Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex: studies using optical tweezers","volume":"99","author":"Arya","year":"2002","journal-title":"Blood"},{"key":"10.1016\/j.bpj.2010.06.002_bib8","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1016\/j.bpj.2009.05.009","article-title":"Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPI\u03b1","volume":"97","author":"Auton","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2010.06.002_bib9","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1016\/j.jmb.2006.10.067","article-title":"Conformational stability and domain unfolding of the Von Willebrand factor A domains","volume":"366","author":"Auton","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bpj.2010.06.002_bib10","first-page":"3195","article-title":"Platelet glycoprotein Ib\u03b1 forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF","volume":"118","author":"Yago","year":"2008","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bpj.2010.06.002_bib11","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1111\/j.1538-7836.2006.01742.x","article-title":"The interaction of von Willebrand factor-A1 domain with collagen: mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen","volume":"4","author":"Morales","year":"2006","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.bpj.2010.06.002_bib12","doi-asserted-by":"crossref","first-page":"9268","DOI":"10.1073\/pnas.95.16.9268","article-title":"Osmolyte-driven contraction of a random coil protein","volume":"95","author":"Qu","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2010.06.002_bib13","doi-asserted-by":"crossref","first-page":"2411","DOI":"10.1002\/pro.5560041120","article-title":"How to measure and predict the molar absorption coefficient of a protein","volume":"4","author":"Pace","year":"1995","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpj.2010.06.002_bib14","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"10.1016\/j.bpj.2010.06.002_bib15","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1002\/(SICI)1097-0134(19990515)35:3<307::AID-PROT4>3.0.CO;2-3","article-title":"Analyzing protein circular dichroism spectra for accurate secondary structures","volume":"35","author":"Johnson","year":"1999","journal-title":"Proteins"},{"key":"10.1016\/j.bpj.2010.06.002_bib16","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1006\/abio.2000.4880","article-title":"Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set","volume":"287","author":"Sreerama","year":"2000","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bpj.2010.06.002_bib17","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1110\/ps.8.2.370","article-title":"Estimation of the number of \u03b1-helical and \u03b2-strand segments in proteins using circular dichroism spectroscopy","volume":"8","author":"Sreerama","year":"1999","journal-title":"Protein Sci."},{"key":"10.1016\/j.bpj.2010.06.002_bib18","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1111\/j.1538-7836.2007.02536.x","article-title":"Purified A2 domain of VWF binds to the active conformation of VWF and blocks the interaction with platelet GPIb\u03b1","volume":"5","author":"Martin","year":"2007","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.bpj.2010.06.002_bib19","doi-asserted-by":"crossref","first-page":"21238","DOI":"10.1016\/S0021-9258(19)36916-9","article-title":"The interaction of the von Willebrand factor-A1 domain with platelet glycoprotein Ib\/IX. The role of glycosylation and disulfide bonding in a monomeric recombinant A1 domain protein","volume":"268","author":"Cruz","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpj.2010.06.002_bib20","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1126\/science.347575","article-title":"Models for the specific adhesion of cells to cells","volume":"200","author":"Bell","year":"1978","journal-title":"Science"},{"key":"10.1016\/j.bpj.2010.06.002_bib21","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1529\/biophysj.105.066548","article-title":"Catch-bond model derived from allostery explains force-activated bacterial adhesion","volume":"90","author":"Thomas","year":"2006","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2010.06.002_bib22","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1073\/pnas.0810784105","article-title":"Structural basis for selectin mechanochemistry","volume":"106","author":"Springer","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2010.06.002_bib23","doi-asserted-by":"crossref","first-page":"4282","DOI":"10.1073\/pnas.0407499102","article-title":"Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins","volume":"102","author":"Whitten","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2010.06.002_bib24","doi-asserted-by":"crossref","first-page":"4391","DOI":"10.1529\/biophysj.104.046318","article-title":"Dynamic force spectroscopy of glycoprotein Ib-IX and von Willebrand factor","volume":"88","author":"Arya","year":"2005","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2010.06.002_bib25","doi-asserted-by":"crossref","first-page":"4099","DOI":"10.1016\/S0006-3495(03)74822-X","article-title":"Kinetics of GPIb\u03b1-vWF-A1 tether bond under flow: effect of GPIb\u03b1 mutations on the association and dissociation rates","volume":"85","author":"Kumar","year":"2003","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2010.06.002_bib26","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1182\/blood-2003-01-0072","article-title":"Alterations in the intrinsic properties of the GPIb\u03b1-VWF tether bond define the kinetics of the platelet-type von Willebrand disease mutation, Gly233Val","volume":"102","author":"Doggett","year":"2003","journal-title":"Blood"},{"key":"10.1016\/j.bpj.2010.06.002_bib27","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/S0006-3495(02)75161-8","article-title":"Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: the GPIb(\u03b1)-vWF tether bond","volume":"83","author":"Doggett","year":"2002","journal-title":"Biophys. J."},{"key":"10.1016\/j.bpj.2010.06.002_bib28","doi-asserted-by":"crossref","first-page":"6586","DOI":"10.1074\/jbc.274.10.6586","article-title":"Distinct structural attributes regulating von Willebrand factor A1 domain interaction with platelet glycoprotein Ib\u03b1 under flow","volume":"274","author":"Miyata","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpj.2010.06.002_bib29","doi-asserted-by":"crossref","first-page":"9046","DOI":"10.1074\/jbc.271.15.9046","article-title":"Conformational changes in the A1 domain of von Willebrand factor modulating the interaction with platelet glycoprotein Ib\u03b1","volume":"271","author":"Miyata","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bpj.2010.06.002_bib30","doi-asserted-by":"crossref","first-page":"1835","DOI":"10.1073\/pnas.0406938102","article-title":"Dynamics of unbinding of cell adhesion molecules: transition from catch to slip bonds","volume":"102","author":"Barsegov","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2010.06.002_bib31","doi-asserted-by":"crossref","first-page":"11281","DOI":"10.1073\/pnas.0401870101","article-title":"Mechanical switching and coupling between two dissociation pathways in a P-selectin adhesion bond","volume":"101","author":"Evans","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bpj.2010.06.002_bib32","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1073\/pnas.0810620105","article-title":"Transmission of allostery through the lectin domain in selectin-mediated cell adhesion","volume":"106","author":"Waldron","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349510007083?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349510007083?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,11,6]],"date-time":"2021-11-06T06:07:00Z","timestamp":1636178820000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349510007083"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2010,8]]},"references-count":32,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2010,8]]}},"alternative-id":["S0006349510007083"],"URL":"https:\/\/doi.org\/10.1016\/j.bpj.2010.06.002","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2010,8]]}}}