{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T09:30:09Z","timestamp":1790501409420,"version":"4.1.0"},"reference-count":44,"publisher":"American Society of Hematology","issue":"4","content-domain":{"domain":["ashpublications.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2001,2,15]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The study identified 10 patients from 6 families with prolonged bleeding time, decreased von Willebrand factor (vWF) ristocetin cofactor activity (RCoF) to vWF:Ag (antigen) ratio, and reduced ristocetin-induced platelet agglutination as well as ristocetin- or botrocetin-induced binding of plasma vWF to platelet glycoprotein Ib (GpIb). In addition, all patients showed a decrease of intermediate-molecular-weight (intermediate-MW) and high-molecular-weight (HMW) multimers of vWF. In the heterozygous state, a cysteine-to-threonine (C\u2009\u2192\u2009T) transversion was detected at nucleotide 4193 of the VWF gene of all patients and lead to the arginine (R)522C substitution in the A1 loop of vWF mature subunit (R1315C in the preprovWF). By in vitro mutagenesis of full-length complementary DNA (cDNA) of vWF and transient expression in COS-7 cells, the mutated C552 recombinant vWF (C552rvWF) was found to exhibit decreased expression, abnormal folding, and lack of intermediate-MW and HMW multimers. In addition, direct binding of botrocetin to C552rvWF, as well as ristocetin- and botrocetin-induced binding of C552rvWF to GpIb, was markedly decreased. Although being localized in an area of the A1 loop of vWF where most of the type 2B mutations that induce a gain-of-function have been identified, the R552C mutation induces a 2A-like phenotype with a decrease of intermediate-MW and HMW multimers as well as a loss-of-function of vWF in the presence of either ristocetin or botrocetin.<\/jats:p>","DOI":"10.1182\/blood.v97.4.952","type":"journal-article","created":{"date-parts":[[2002,7,27]],"date-time":"2002-07-27T12:46:47Z","timestamp":1027774007000},"page":"952-959","update-policy":"https:\/\/doi.org\/10.1182\/blood.2019cm0000","source":"Crossref","is-referenced-by-count":28,"title":["The arginine-552-cysteine (R1315C) mutation within the A1 loop of von Willebrand factor induces an abnormal folding with a loss of function resulting in type 2A\u2013like phenotype of von Willebrand disease: study of 10 patients and mutated recombinant von Willebrand factor"],"prefix":"10.1182","volume":"97","author":[{"given":"Anne-Sophie","family":"Ribba","sequence":"first","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lysiane","family":"Hilbert","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Maurice","family":"Lavergne","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edith","family":"Fressinaud","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catherine","family":"Boyer-Neumann","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catherine","family":"Ternisien","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ire\u0300ne","family":"Juhan-Vague","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jenny","family":"Goudemand","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jean-Pierre","family":"Girma","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Claudine","family":"Mazurier","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dominique","family":"Meyer","sequence":"additional","affiliation":[{"name":"From the Institut National de la Sante\u0301 et de la Recherche Me\u0301dicale (INSERM) U.143, Ho\u0302pital de Bice\u0302tre, Paris, France; the Laboratoire Franc\u0327ais du Fractionnement et des Biotechnologies and the Laboratoire d'He\u0301matologie CHU, Lille, France; the Laboratoire d'He\u0301matologie CHU, Nantes, France; the Laboratoire d'He\u0301mostase CHU, Angers, France; and the Laboratoire d'He\u0301matologie CHU, Marseilles, France."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"234","reference":[{"key":"2020021216434891100_B1","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":"Ann Rev Biochem."},{"key":"2020021216434891100_B2","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1055\/s-0038-1647310","article-title":"Ristocetin and botrocetin involve two distinct domains of von Willebrand Factor for binding to platelet membrane glycoprotein Ib.","volume":"64","author":"Girma","year":"1990","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B3","doi-asserted-by":"crossref","first-page":"18172","DOI":"10.1016\/S0021-9258(18)55251-0","article-title":"Identification of discontinuous von Willebrand factor sequences involved in complex formation with botrocetin: a model for the regulation of von Willebrand factor binding to platelet glycoprotein-Ib.","volume":"266","author":"Sugimoto","year":"1991","journal-title":"J Biol Chem."},{"key":"2020021216434891100_B4","doi-asserted-by":"crossref","first-page":"11144","DOI":"10.1021\/bi00160a027","article-title":"Identification of aspartic acid-514 through glutamic acid-542 as a glycoprotein-Ib-IX complex receptor recognition sequence in von Willebrand factor: mechanism of modulation of von Willebrand factor by ristocetin and botrocetin.","volume":"31","author":"Berndt","year":"1992","journal-title":"Biochemistry."},{"key":"2020021216434891100_B5","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1016\/S0021-9258(17)42483-5","article-title":"von Willebrand Factor: a reduced and alkylated 52\/48-kDa fragment beginning at amino acid residue 449 contains the domain interacting with platelet glycoprotein Ib.","volume":"261","author":"Fujimura","year":"1986","journal-title":"J Biol Chem."},{"key":"2020021216434891100_B6","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1111\/j.1432-1033.1991.tb15826.x","article-title":"Effect of deletion of the A1 domain of von Willebrand Factor on its binding to heparin, collagen and platelets in the presence of ristocetin.","volume":"196","author":"Sixma","year":"1991","journal-title":"Eur J Biochem."},{"key":"2020021216434891100_B7","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.","volume":"268","author":"Cruz","year":"1993","journal-title":"J Biol Chem."},{"key":"2020021216434891100_B8","doi-asserted-by":"crossref","first-page":"12185","DOI":"10.1016\/S0021-9258(19)50324-6","article-title":"Analysis of structure-function relationships in the platelet membrane glycoprotein Ib-binding domain of von Willebrand's factor by expression of deletion mutants.","volume":"268","author":"Sugimoto","year":"1993","journal-title":"J Biol Chem."},{"key":"2020021216434891100_B9","doi-asserted-by":"crossref","first-page":"13406","DOI":"10.1074\/jbc.270.22.13406","article-title":"Identification of amino acid residues essential for von Willebrand factor binding to platelet glycoprotein Ib: charged-to-alanine scanning mutagenesis of the A1 domain of human von Willebrand factor.","volume":"270","author":"Matsushita","year":"1995","journal-title":"J Biol Chem."},{"key":"2020021216434891100_B10","doi-asserted-by":"crossref","first-page":"13460","DOI":"10.1021\/bi9610313","article-title":"Analysis of the structure and function of the von Willebrand factor A1 domain using targeted deletions and alanine-scanning mutagenesis.","volume":"35","author":"Kroner","year":"1996","journal-title":"Biochemistry."},{"key":"2020021216434891100_B11","doi-asserted-by":"crossref","first-page":"11044","DOI":"10.1074\/jbc.275.15.11044","article-title":"Localization of von Willebrand factor-binding sites for platelet glycoprotein Ib and botrocetin by charged-to-alanine scanning mutagenesis.","volume":"275","author":"Matsushita","year":"2000","journal-title":"J Biol Chem."},{"key":"2020021216434891100_B12","doi-asserted-by":"crossref","first-page":"12763","DOI":"10.1074\/jbc.275.17.12763","article-title":"Modeling and functional analysis of the interaction between von Willebrand factor A1 domain and glycoprotein Ib alpha.","volume":"275","author":"Vasudevan","year":"2000","journal-title":"J Biol Chem."},{"key":"2020021216434891100_B13","doi-asserted-by":"crossref","first-page":"10396","DOI":"10.1074\/jbc.273.17.10396","article-title":"Crystal structure of the von Willebrand factor A1 domain and implications for the binding of platelet glycoprotein Ib.","volume":"273","author":"Emsley","year":"1998","journal-title":"J Biol Chem."},{"key":"2020021216434891100_B14","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1038\/nsb0398-189","article-title":"Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab.","volume":"5","author":"Celikel","year":"1998","journal-title":"Nature Struct Biol."},{"key":"2020021216434891100_B15","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1055\/s-0038-1651576","article-title":"von Willebrand disease: a database of point mutations, insertions, and deletions.","volume":"69","author":"Ginsburg","year":"1993","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B16","first-page":"34","article-title":"Molecular genetics of von Willebrand disease.","volume":"41","author":"Mazurier","year":"1998","journal-title":"Ann Genet."},{"key":"2020021216434891100_B17","doi-asserted-by":"crossref","first-page":"2559","DOI":"10.1182\/blood.V88.7.2559.bloodjournal8872559","article-title":"Type 2M:Milwaukee-1 von Willebrand disease: an in-frame deletion in the Cys509-Cys695 loop of the von Willebrand factor A1 domain causes deficient binding of von Willebrand factor to platelets.","volume":"88","author":"Mancuso","year":"1996","journal-title":"Blood."},{"key":"2020021216434891100_B18","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1055\/s-0038-1657568","article-title":"Gene defects in 150 unrelated French cases with type 2 von Willebrand disease: from the patient to the gene.","volume":"78","author":"Meyer","year":"1997","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B19","doi-asserted-by":"crossref","first-page":"1572","DOI":"10.1182\/blood.V91.5.1572","article-title":"Type 2M von Willebrand disease: F606I and I662F mutations in the glycoprotein Ib binding domain selectively impair ristocetin\u2014but not botrocetin-mediated binding of von Willebrand factor to platelets.","volume":"91","author":"Hillery","year":"1998","journal-title":"Blood."},{"key":"2020021216434891100_B20","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1111\/j.1365-2141.1992.tb04595.x","article-title":"Defects in type 2A von Willebrand disease: a cysteine 509 to arginine substitution in the mature von Willebrand Factor disrupts a disulphide loop involved in the interaction with platelet glycoprotein Ib-IX.","volume":"82","author":"Lavergne","year":"1992","journal-title":"Br J Haematol."},{"key":"2020021216434891100_B21","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1182\/blood.V83.3.833.833","article-title":"Discrepancy between 2A-phenotype and 2B-genotype in a patient with a variant of von Willebrand disease.","volume":"83","author":"Ribba","year":"1994","journal-title":"Blood."},{"key":"2020021216434891100_B22","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1055\/s-0038-1653829","article-title":"Diagnosis of subtype 2B von Willebrand disease in a patient with 2A phenotype of plasma von Willebrand factor.","volume":"73","author":"Gaucher","year":"1995","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B23","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1182\/blood.V79.8.2048.2048","article-title":"Expressed full-length von Willebrand Factor containing missense mutations linked to type-2B von Willebrand Disease shows enhanced binding to platelets.","volume":"79","author":"Kroner","year":"1992","journal-title":"Blood."},{"key":"2020021216434891100_B24","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1055\/s-0038-1649725","article-title":"Effect of type 2B von Willebrand disease mutation Arg(545)Cys on platelet glycoprotein Ib binding-studies with recombinant von Willebrand Factor.","volume":"70","author":"Inbal","year":"1993","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B25","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1055\/s-0038-1650599","article-title":"Characterization of recombinant von Willebrand factors mutated on cysteine 509 or 695.","volume":"76","author":"Siguret","year":"1996","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B26","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1007\/s005990050046","article-title":"Laboratory diagnosis of von Willebrand disease.","volume":"28","author":"Veyradier","year":"1998","journal-title":"Intern J Clin Lab Res."},{"key":"2020021216434891100_B27","first-page":"a631","article-title":"Usefulness of a functional test based on the von Willebrand Factor: collagen binding to classify von Willebrand patients.","volume":"suppl","author":"Caron","year":"1997","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B28","doi-asserted-by":"crossref","first-page":"1382","DOI":"10.1055\/s-0037-1614779","article-title":"Estimation of the von Willebrand factor-cleaving protease in plasma using monoclonal antibodies to VWF.","volume":"82","author":"Obert","year":"1999","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B29","doi-asserted-by":"crossref","first-page":"1010","DOI":"10.1182\/blood.V86.3.1010.1010","article-title":"Identification of two mutations (Arg611Cys and Arg611His) in the A1 loop of von Willebrand factor (VWF) responsible for type 2 von Willebrand disease with decreased platelet-dependent function of VWF.","volume":"86","author":"Hilbert","year":"1995","journal-title":"Blood."},{"key":"2020021216434891100_B30","doi-asserted-by":"crossref","first-page":"1542","DOI":"10.1182\/blood.V83.6.1542.1542","article-title":"Leu 697\u2212\u2192Val mutation in mature von Willebrand factor is responsible for type 2B von Willebrand disease.","volume":"83","author":"Hilbert","year":"1994","journal-title":"Blood."},{"key":"2020021216434891100_B31","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1111\/j.1365-2141.1994.tb04879.x","article-title":"Fine epitope mapping of monoclonal antibodies to the NH2-terminal part of von Willebrand factor (VWF) by using recombinant and synthetic peptides: interest for the localization of the factor VIII binding domain.","volume":"87","author":"Jorieux","year":"1994","journal-title":"Br J Haematol."},{"key":"2020021216434891100_B32","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1055\/s-0038-1642524","article-title":"Epitope mapping of inhibitory monoclonal antibodies to human von Willebrand factor by using recombinant cDNA libraries.","volume":"71","author":"Pietu","year":"1994","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B33","doi-asserted-by":"crossref","first-page":"1738","DOI":"10.1182\/blood.V78.7.1738.1738","article-title":"Duplication of a methionine within the glycoprotein Ib binding domain of von Willebrand Factor detected by denaturing gradient gel electrophoresis in a patient with type-2B von Willebrand Disease.","volume":"78","author":"Ribba","year":"1991","journal-title":"Blood."},{"key":"2020021216434891100_B34","doi-asserted-by":"crossref","first-page":"4800","DOI":"10.1093\/nar\/19.17.4800","article-title":"Characterization of 98 alleles in 105 unrelated individuals in the F8VWF gene.","volume":"19","author":"Mercier","year":"1991","journal-title":"Nucleic Acids Res."},{"key":"2020021216434891100_B35","doi-asserted-by":"crossref","first-page":"1024","DOI":"10.1182\/blood.V84.4.1024.1024","article-title":"Characterization of von Willebrand factor gene defects in two unrelated patients with IIC von Willebrand disease.","volume":"84","author":"Gaucher","year":"1994","journal-title":"Blood."},{"key":"2020021216434891100_B36","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1016\/0006-291X(78)91322-0","article-title":"Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1, 3, 4, 6- tetrachloro-3a, 6a-diphenylglycoluril.","volume":"80","author":"Fraker","year":"1978","journal-title":"Biochem Biophys Res Commun."},{"key":"2020021216434891100_B37","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1111\/j.1365-2141.1995.tb03400.x","article-title":"A monoclonal antibody (B724) to von Willebrand factor recognizing an epitope within the A1 disulphide loop (Cys509-Cys695) discriminates between type 2A and type 2B von Willebrand disease.","volume":"90","author":"Christophe","year":"1995","journal-title":"Br J Haematol."},{"key":"2020021216434891100_B38","doi-asserted-by":"crossref","first-page":"3553","DOI":"10.1182\/blood.V83.12.3553.3553","article-title":"Influence of mutations and size of multimers in type II von Willebrand disease upon the function of von Willebrand factor.","volume":"83","author":"Christophe","year":"1994","journal-title":"Blood."},{"key":"2020021216434891100_B39","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1055\/s-0038-1642471","article-title":"A revised classification of von Willebrand disease.","volume":"71","author":"Sadler","year":"1994","journal-title":"Thromb Haemost."},{"key":"2020021216434891100_B40","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1002\/(SICI)1096-8652(199809)59:1<57::AID-AJH11>3.0.CO;2-Z","article-title":"Search for mutations in a segment of the exon 28 of the human von Willebrand factor gene: new mutations, R1315C and R1341W, associated with type 2M and 2B variants.","volume":"59","author":"Casana","year":"1998","journal-title":"Am J Hematol."},{"key":"2020021216434891100_B41","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1172\/JCI115376","article-title":"Heterogeneity of plasma von Willebrand-Factor multimers resulting from proteolysis of the constituent subunit.","volume":"88","author":"Dent","year":"1991","journal-title":"J Clin Invest."},{"key":"2020021216434891100_B42","doi-asserted-by":"crossref","first-page":"4424","DOI":"10.1016\/S0021-9258(18)42852-9","article-title":"Impaired intracellular transport produced by a subset of type-2A von Willebrand disease mutations.","volume":"267","author":"Lyons","year":"1992","journal-title":"J Biol Chem."},{"key":"2020021216434891100_B43","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1111\/j.1365-2141.1992.tb04594.x","article-title":"Type 2B von Willebrand's disease: gene mutations and clinical presentation in nine families from Denmark, Germany and Sweden.","volume":"82","author":"Donner","year":"1992","journal-title":"Br J Haematol."},{"key":"2020021216434891100_B44","doi-asserted-by":"crossref","first-page":"2322","DOI":"10.1182\/blood.V87.6.2322.bloodjournal8762322","article-title":"Comparative analysis of type 2B von Willebrand disease mutations: implications for the mechanism of von Willebrand factor binding to platelets.","volume":"87","author":"Cooney","year":"1996","journal-title":"Blood."}],"container-title":["Blood"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/ashpublications.org\/blood\/article-pdf\/97\/4\/952\/1671346\/h8040100952.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/ashpublications.org\/blood\/article-pdf\/97\/4\/952\/1671346\/h8040100952.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,5,26]],"date-time":"2021-05-26T09:15:43Z","timestamp":1622020543000},"score":1,"resource":{"primary":{"URL":"https:\/\/ashpublications.org\/blood\/article\/97\/4\/952\/53088\/The-arginine552cysteine-R1315C-mutation-within-the"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,2,15]]},"references-count":44,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2001,2,15]]}},"URL":"https:\/\/doi.org\/10.1182\/blood.v97.4.952","relation":{},"ISSN":["1528-0020","0006-4971"],"issn-type":[{"value":"1528-0020","type":"electronic"},{"value":"0006-4971","type":"print"}],"subject":[],"published":{"date-parts":[[2001,2,15]]}}}