Role of fibrinogen alpha and gamma chain sites in platelet aggregation. - Wikidata - awgldk - TriplyDB

Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

http://www.wikidata.org/entity/Q37294912

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Structural recognition of a novel fibrinogen gamma chain sequence (117-133) by intercellular adhesion molecule-1 mediates leukocyte-endothelium interaction Structure and function of the platelet integrin alphaIIbbeta3 A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A.Fibrinogen-Related Proteins in Tissue Repair: How a Unique Domain with a Common Structure Controls Diverse Aspects of Wound Healing Structure of the fibrinogen γ-chain integrin binding and factor XIIIa cross-linking sites obtained through carrier protein driven crystallization Selection and structure of ion-selective ligands for platelet integrin alpha IIb(beta) 3 Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin α IIb β 3 A Structural Model of the Staphylococcus aureus ClfA–Fibrinogen Interaction Opens New Avenues for the Design of Anti-Staphylococcal Therapeutics Three-dimensional structure of the platelet integrin recognition segment of the fibrinogen gamma chain obtained by carrier protein-driven crystallization The primary fibrin polymerization pocket: three-dimensional structure of a 30-kDa C-terminal gamma chain fragment complexed with the peptide Gly-Pro-Arg-Pro Binding of a fibrinogen mimetic stabilizes integrin alphaIIbbeta3's open conformation The tryptase, mouse mast cell protease 7, exhibits anticoagulant activity in vivo and in vitro due to its ability to degrade fibrinogen in the presence of the diverse array of protease inhibitors in plasma Proteins, platelets, and blood coagulation at biomaterial interfaces Adhesive ligand binding to integrin alpha IIb beta 3 stimulates tyrosine phosphorylation of novel protein substrates before phosphorylation of pp125FAK Integrin alphaIIbbeta3:ligand interactions are linked to binding-site remodeling.Extracellular matrix molecules as targets for brown spider venom toxins.Fibrinogen and von Willebrand factor mediated platelet adhesion to polystyrene under flow conditions.The GPIIb/IIIa (integrin alphaIIbbeta3) odyssey: a technology-driven saga of a receptor with twists, turns, and even a bend.A new Ser472Asn (Cab2(a+)) polymorphism localized within the αIIb "thigh" domain is involved in neonatal thrombocytopenia.Liposomes bearing fibrinogen could potentially interfere with platelet interaction and procoagulant activity.The αIIb p.Leu841Met (Cab3(a+) ) polymorphism results in a new human platelet alloantigen involved in neonatal alloimmune thrombocytopenia.Preservation of hemostatic and structural properties of rehydrated lyophilized platelets: potential for long-term storage of dried platelets for transfusion Effects of the RGD loop and C-terminus of rhodostomin on regulating integrin αIIbβ3 recognition.DLBS1033, a protein extract from Lumbricus rubellus, possesses antithrombotic and thrombolytic activities.SdrG, a fibrinogen-binding bacterial adhesin of the microbial surface components recognizing adhesive matrix molecules subfamily from Staphylococcus epidermidis, targets the thrombin cleavage site in the Bbeta chain.Dynamics of platelet glycoprotein IIb-IIIa receptor expression and fibrinogen binding. II. Quantal activation parallels platelet capture in stir-associated microaggregation.Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase 1B (PTP-1B) in human platelets.Lotrafiban: an oral platelet glycoprotein IIb/IIIa blocker.Demystified...adhesion molecule deficiencies.Efficiency of platelet adhesion to fibrinogen depends on both cell activation and flow Alzheimer's disease peptide beta-amyloid interacts with fibrinogen and induces its oligomerization.The pharmacodynamics of parenteral glycoprotein IIb/IIIa inhibitors.Association of the platelet GPIIb/IIIa polymorphism with atherosclerotic plaque morphology: the Atherosclerosis Risk in Communities (ARIC) Study Delineating the roles of the GPIIb/IIIa and GP-Ib-IX-V platelet receptors in mediating platelet adhesion to adsorbed fibrinogen and albumin.The interaction of integrin αIIbβ3 with fibrin occurs through multiple binding sites in the αIIb β-propeller domain.Staphylococcus aureus induces platelet aggregation via a fibrinogen-dependent mechanism which is independent of principal platelet glycoprotein IIb/IIIa fibrinogen-binding domains Dynamic regulation of fibrinogen: integrin αIIbβ3 binding.The Platelet Integrin αIIbβ3 Differentially Interacts with Fibrin Versus Fibrinogen Identification of Serum Peptidome Signatures of Non-Small Cell Lung Cancer New circulating biomarkers for predicting cardiovascular death in healthy population.

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P2860

Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

http://www.wikidata.org/entity/Q37294912

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1992 nî lūn-bûn

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1992年の論文

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年学术文章

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1992年學術文章

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1992年學術文章

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1992年學術文章

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name

Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

@en

Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

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type

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Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

@en

Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

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prefLabel

Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

@en

Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

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PNAS.89.22.10729

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Role of fibrinogen alpha and gamma chain sites in platelet aggregation.

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P2093

D H Farrell

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D W Chung

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E W Davie

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P Thiagarajan

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P2860

gamma and alpha chains of human fibrinogen possess sites reactive with human platelet receptors

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Integrins: versatility, modulation, and signaling in cell adhesion

Integrins: a family of cell surface receptors

Platelet membrane glycoprotein IIb/IIIa: member of a family of Arg-Gly-Asp--specific adhesion receptors

Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule

Exposure of platelet fibrinogen receptors by ADP and epinephrine.

Platelets have more than one binding site for von Willebrand factor.

Arg-Gly-Asp: a versatile cell recognition signal.

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10729-10732

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10.1073/PNAS.89.22.10729

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