Unique disulfide bonds in epidermal growth factor (EGF) domains of β3 affect structure and function of αIIbβ3 and αvβ3 integrins in different manner.
about
From structure to redox: The diverse functional roles of disulfides and implications in disease.Congenital platelet disorders and understanding of platelet function.αIIbβ3 variants defined by next-generation sequencing: predicting variants likely to cause Glanzmann thrombasthenia.Cytoskeletal perturbation leads to platelet dysfunction and thrombocytopenia in variant forms of Glanzmann thrombastheniaGlanzmann thrombasthenia: state of the art and future directions.Thiol isomerases in thrombus formation.Protein disulfide isomerase in thrombosis and vascular inflammationThe importance of N-glycosylation on β3 integrin ligand binding and conformational regulationA single disulfide bond disruption in the β3 integrin subunit promotes thiol/disulfide exchange, a molecular dynamics study.Molecular dynamics analysis of a novel β3 Pro189Ser mutation in a patient with glanzmann thrombasthenia differentially affecting αIIbβ3 and αvβ3 expression.Context-Dependent Sensitivity to Mutations Disrupting the Structural Integrity of Individual EGF Repeats in the Mouse Notch Ligand DLL1.C560Rβ3 caused platelet integrin αII b β3 to bind fibrinogen continuously, but resulted in a severe bleeding syndrome and increased murine mortalityPlatelet-derived ERp57 mediates platelet incorporation into a growing thrombus by regulation of the αIIbβ3 integrin.Control of blood proteins by functional disulfide bonds.Understanding the genetic basis of Glanzmann thrombasthenia: implications for treatment.Immunoregulation through membrane proteins modified by reducing conditions induced by immune reactions.Redox-relevant aspects of the extracellular matrix and its cellular contacts via integrinsRedox regulation of cancer metastasis: molecular signaling and therapeutic opportunities.RUBCN/rubicon and EGFR regulate lysosomal degradative processes in the retinal pigment epithelium (RPE) of the eye.Linkage disequilibrium amongst ITGA2B and ITGB3 gene variants in patients with Glanzmann thrombasthenia confirms that most disease-causing mutations are recent.Expanding the Mutation Spectrum Affecting αIIbβ3 Integrin in Glanzmann Thrombasthenia: Screening of the ITGA2B and ITGB3 Genes in a Large International Cohort.Reduction of leucocyte cell surface disulfide bonds during immune activation is dynamic as revealed by a quantitative proteomics workflow (SH-IQ)
P2860
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P2860
Unique disulfide bonds in epidermal growth factor (EGF) domains of β3 affect structure and function of αIIbβ3 and αvβ3 integrins in different manner.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Unique disulfide bonds in epid ...... integrins in different manner.
@en
Unique disulfide bonds in epidermal growth factor
@nl
type
label
Unique disulfide bonds in epid ...... integrins in different manner.
@en
Unique disulfide bonds in epidermal growth factor
@nl
prefLabel
Unique disulfide bonds in epid ...... integrins in different manner.
@en
Unique disulfide bonds in epidermal growth factor
@nl
P2093
P2860
P356
P1476
Unique disulfide bonds in epid ...... integrins in different manner.
@en
P2093
Ehud Zelzion
Nurit Rosenberg
Ronit Mor-Cohen
Uri Seligsohn
Wissam Mansour
Yulia Averbukh
Yulia Einav
P2860
P304
P356
10.1074/JBC.M111.311043
P407
P577
2012-02-03T00:00:00Z