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

Role of the leucine-rich domain of platelet GPIbalpha in correct post-translational processing--the Nancy I Bernard-Soulier mutation expressed on CHO cells.

Thrombosis and haemostasis - 1 Jul 2000

Ulsemer P, Lanza F, Baas M J, Schwartz A, Ravanat C, Briquel M E, Cranmer S, Jackson S, Cazenave J P, de la Salle C

Abstract excerpt

The mechanisms governing the biosynthesis and surface expression of platelet adhesive receptors on parent megakaryocytes are as yet poorly understood. In particular, the assembly and processing of the multisubunit glycoprotein (GP) Ib-IX-V complex, a receptor for von Willebrand factor (vWf) is not fully understood. In the present work, these questions were addressed by reproducing a natural mutation of GPIbalpha...

Read the complete abstract on PubMed

Topics

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

Share to Bernard-Soulier Syndrome
Share to Cricetulus

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

Share to Leucine

Share to Molecular Weight

Share to Platelet Adhesiveness

Share to Platelet Glycoprotein GPIb-IX Complex

Share to Tunicamycin

Share to von Willebrand Factor

Source

Identifiers

PMID: 10928479

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

Role of the leucine-rich domain of platelet GPIbalpha in correct post-translational processing--the Nancy I Bernard-Soulier mutation expressed on CHO cells.PMID 10928479Read ↗

Naturally occurring mutations in glycoprotein Ibalpha that result in defective ligand binding and synthesis of a truncated protein.Semantic proximity Read ↗

A novel homozygous 8-base pair deletion mutation in the glycoprotein Ibalpha gene in a patient with Bernard-Soulier syndrome.Semantic proximity Read ↗

Biosynthesis and intracellular post-translational processing of normal and mutant platelet glycoprotein GPIb-IX.Semantic proximity Read ↗

A novel hemizygous Bernard-Soulier Syndrome (BSS) mutation in the amino terminal domain of glycoprotein (GP)Ibbeta--platelet characterization and transfection studies.Semantic proximity Read ↗

The Critical Interaction of Glycoprotein (GP) Ibβ With GPIX—A Genetic Cause of Bernard-Soulier SyndromeSemantic proximity Read ↗

Surface expression of glycoprotein ib alpha is dependent on glycoprotein ib beta: evidence from a novel mutation causing Bernard-Soulier syndrome.Semantic proximity Read ↗

Compound heterozygosity of the GPIbalpha gene associated with Bernard-Soulier syndrome.Semantic proximity Read ↗

Amelioration of the macrothrombocytopenia associated with the murine Bernard-Soulier syndromeSemantic proximity Read ↗

Modularity of the oncoprotein-like properties of platelet glycoprotein Ibalpha.Semantic proximity Read ↗

Role of the transmembrane domain of glycoprotein IX in assembly of the glycoprotein Ib-IX complex.Semantic proximity Read ↗

Juxtamembrane basic residues in glycoprotein Ibbeta cytoplasmic domain are required for assembly and surface expression of glycoprotein Ib-IX complex.Semantic proximity Read ↗

Bernard-Soulier syndrome Karlstad: Trp 498-->Stop mutation resulting in a truncated glycoprotein Ib alpha that contains part of the transmembranous domain.Semantic proximity Read ↗

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