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Article

Biosynthesis and intracellular post-translational processing of normal and mutant platelet glycoprotein GPIb-IX.

The Biochemical journal - 1 Sept 2001

Ulsemer P, Strassel C, Baas M J, Salamero J, Chasserot-Golaz S, Cazenave J P, De La Salle C, Lanza F

Abstract excerpt

The multisubunit leucine-rich glycoprotein (GP) Ib-IX-V complex mediates von Willebrand factor-dependent platelet adhesion at sites of blood-vessel injury. Molecular defects of this receptor are reported to cause the Bernard-Soulier haemorrhagic disorder. To gain insight into the mechanisms controlling expression of normal and defective receptors, we performed pulse-chase metabolic studies and detailed analysis...

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Identifiers

PMID: 11513727
DOI: 10.1042/0264-6021:3580295
PMCID: PMC1222061

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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.

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Biosynthesis and intracellular post-translational processing of normal and mutant platelet glycoprotein GPIb-IX.PMID 11513727Read ↗

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Posttranslational N-glycosylation takes place during the normal processing of human coagulation factor VII.Semantic proximity Read ↗

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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 ↗

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Identification of a novel 14-3-3zeta binding site within the cytoplasmic domain of platelet glycoprotein Ibalpha that plays a key role in regulating the von Willebrand factor binding function of glycoprotein Ib-IX.Semantic proximity Read ↗

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