Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Effects of different amino-acid substitutions in the leucine 694-proline 708 segment of recombinant von Willebrand factor.

British journal of haematology - 1 Dec 1995

Hilbert L, Gaucher C, Mazurier C

Abstract excerpt

Type 2B von Willebrand disease (vWD) is characterized by an increased affinity of von Willebrand factor (vWF) for binding to platelet glycoprotein Ib (GpIb). Most type 2B candidate mutations are clustered in the 509-695 disulphide loop but three of them (H505D, L697V and A698V) are outside this loop. We confirm here that the A698V mutation is a type 2B mutation by its expression in Cos-7 cells. As the L697V and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Base Sequence
Share to DNA Primers
Share to Molecular Sequence Data

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Pedigree

Share to Polymerase Chain Reaction

Share to Recombinant Proteins

Source

Identifiers

PMID: 8547152
DOI: 10.1111/j.1365-2141.1995.tb05423.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effects of different amino-acid substitutions in the leucine 694-proline 708 segment of recombinant von Willebrand factor.PMID 8547152Read ↗

Leu 697-->Val mutation in mature von Willebrand factor is responsible for type IIB von Willebrand disease.Semantic proximity Read ↗

A role for von Willebrand factor proline residues 702-704 in ristocetin-mediated binding to platelet glycoprotein Ib.Semantic proximity Read ↗

A new mutation, S1285F, within the A1 loop of von Willebrand factor induces a conformational change in A1 loop with abnormal binding to platelet GPIb and botrocetin causing type 2M von Willebrand disease.Semantic proximity Read ↗

Type IIB mutation His-505-->Asp implicates a new segment in the control of von Willebrand factor binding to platelet glycoprotein Ib.Semantic proximity Read ↗

Characterization of recombinant von Willebrand factor corresponding to mutations in type IIA and type IIB von Willebrand disease.Semantic proximity Read ↗

Recombinant von Willebrand factor Arg578-->Gln. A type IIB von Willebrand disease mutation affects binding to glycoprotein Ib but not to collagen or heparin.Semantic proximity Read ↗

Identification of new type 2B von Willebrand disease mutations: Arg543Gln, Arg545Pro and Arg578Leu.Semantic proximity Read ↗

von Willebrand disease type 1 mutation p.Arg1379Cys and the variant p.Ala1377Val synergistically determine a 2M phenotype in four Italian patients.Semantic proximity Read ↗

Effect of type IIB von Willebrand disease mutation Arg(545)Cys on platelet glycoprotein Ib binding--studies with recombinant von Willebrand factor.Semantic proximity Read ↗

Expression of the phenotypic abnormality of platelet-type von Willebrand disease in a recombinant glycoprotein Ib alpha fragment.Semantic proximity Read ↗

Molecular modeling of the seven tandem leucine-rich repeats within the ligand-binding region of platelet glycoprotein Ib alpha.Semantic proximity Read ↗

Gain of von Willebrand factor-binding function by mutagenesis of a species-conserved residue within the leucine-rich repeat region of platelet glycoprotein Ibalpha.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.