Results 101 to 110 of about 9,490 (159)

Three-dimensional model of human platelet Integrin αIIbβ3 in solution obtained by small angle neutron scattering

open access: yes, 2013
Integrin αIIbβ3 is the major membrane protein and adhesion receptor at the surface of blood platelets, which after activation plays a key role in platelet plug formation in hemostasis and thrombosis.
Callow, Phil   +5 more
core   +1 more source

A Glanzmann Thrombasthenia-like Phenotype Caused by a Defect in Inside-Out Signaling through the Integrin αIIbβ3

open access: yes, 1998
SummaryActivation of the platelet integrin αIIbβ3, an essential step in platelet aggregation, is regulated by intracellular signal pathways (inside-out signaling). In this study, we characterize a 35-year-old Japanese female, HM, with a life-long history
Yoshiaki Tomiyama   +6 more
core   +1 more source

A Disease Mechanism Underlying Bleeding in Wiskott-Aldrich Syndrome

open access: yesClinical Medicine Insights: Blood Disorders, 2008
The Wiskott-Aldrich Syndrome (WAS) is an × chromosome-linked immunodeficiency disorder. The most common symptom in WAS is bleeding. Several clinical investigations indicate that low platelet counts and defective platelet aggregation are the major causes ...
Shigeru Tsuboi
doaj   +1 more source

Integrin αIIbβ3 outside-in signaling

open access: yes, 2017
Integrin αIIbβ3 is a highly abundant heterodimeric platelet receptor that can transmit information bidirectionally across the plasma membrane, and plays a critical role in hemostasis and thrombosis. Upon platelet activation, inside-out signaling pathways
Marion T. van den Bosch   +2 more
core   +1 more source

Integrin Priming Dynamics: Mechanisms of Integrin Antagonist-Promoted αIIbβ3:PAC-1 Molecular Recognition

open access: yes, 2016
This investigation addressed the paradox that disintegrins and small RGD-ligands readily bind to the resting αIIbβ3 integrin, while macromolecules with similar integrin recognition motifs require an activated, or primed, receptor.
Mary C. Stahle (2255554)   +1 more
core   +1 more source

The lateral diffusion and fibrinogen induced clustering of platelet integrin αIIbβ3 reconstituted into physiologically mimetic GUVs

open access: yes, 2015
Platelet integrin αIIbβ3 is a key mediator of platelet activation and thrombosis. Upon activation αIIbβ3 undergoes significant conformational rearrangement, inducing complex bidirectional signalling and protein recruitment leading to platelet activation.
Keyes, Tia E.   +5 more
core   +1 more source

Modulating Integrin αIIbβ3 Activity through Mutagenesis of Allosterically Regulated Intersubunit Contacts

open access: yes, 2019
Integrin αIIbβ3, a transmembrane heterodimer, mediates platelet aggregation when it switches from an inactive to an active ligand-binding conformation following platelet stimulation.
William F. DeGrado (276486)   +7 more
core   +1 more source

Синтез та антиагрегаційна активність антагоніста αIIbβ3--рецепторів на основі 2-(4-піперазин-1-іл)-3Н-хіназолін-4-ону

open access: yesДоповiдi Нацiональної академiї наук України
Синтезовано нове похідне 2-(4-піперазин-1-іл)-хіназолін-4-ону, що є антагоністом αIIbβ3-рецепторів закритої форми. Досліджено антиагрегаційну активність сполуки на збагаченій тромбоцитами плазмі крові людини в досліді in vitro.
S.A. Andronati   +6 more
doaj   +1 more source

Abnormal cytoplasmic extensions associated with active αIIbβ3 are probably the cause for macrothrombocytopenia in Glanzmann thrombasthenia-like syndrome

open access: yes, 2015
Mutations in the ITGA2B or ITGB3 genes that encode for the αIIbβ3 platelet integrin usually cause Glanzmann thrombasthenia, a severe autosomal recessive bleeding disorder characterized by absence of platelet aggregation, but normal platelet number and ...
Seligsohn, Uri   +6 more
core   +1 more source

A Novel αIIbβ3 Antagonist from Snake Venom Prevents Thrombosis without Causing Bleeding

open access: yes, 2019
Life-threatening thrombocytopenia and bleeding, common side effects of clinically available αIIbβ3 antagonists, are associated with the induction of ligand-induced integrin conformational changes and exposure of ligand-induced binding sites (LIBSs).
Ching-Hu Chung   +4 more
core   +1 more source

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