Extracellular protein disulfide isomerase regulates feedback activation of platelet thrombin generation via modulation of coagulation factor binding (Q84963105)

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scientific article published on 01 November 2011

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English	Extracellular protein disulfide isomerase regulates feedback activation of platelet thrombin generation via modulation of coagulation factor binding	scientific article published on 01 November 2011

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13 February 2020

Extracellular protein disulfide isomerase regulates feedback activation of platelet thrombin generation via modulation of coagulation factor binding (English)

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13 February 2020

physiological feedback

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12 December 2024

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J-R Nofer

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13 February 2020

K. Jurk

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J. Lahav

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H. VAN Aken

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M. F. Brodde

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B. E. Kehrel

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1 November 2011

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November 2011

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https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1538-7836.2011.04509.x

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10.1111/J.1538-7836.2011.04509.X

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12 December 2024

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https://api.elsevier.com/content/article/PII:S1538783622074578?httpAccept=text/plain

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http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1538-7836.2011.04509.x/fullpdf

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10.1111/J.1538-7836.2011.04509.X

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Journal of Thrombosis and Haemostasis

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2278-2290

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13 February 2020

Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively

1 reference

30 December 2023

https://opencitations.net/index/api/v1/citations/10.1074/JBC.M306925200

Platelets and thrombin generation

1

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Role of the extrinsic pathway of blood coagulation in hemostasis and thrombosis

2

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Thrombin functions during tissue factor-induced blood coagulation

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A cell-based model of thrombin generation

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Platelet coagulation-protein interactions

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Variability in platelet procoagulant activity in healthy volunteers

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Scott syndrome, a bleeding disorder caused by defective scrambling of membrane phospholipids

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The Physical Exchange of Factor VIII (FVIII) between von Willebrand Factor and Activated Platelets and the Effect of the FVIII B-Domain on Platelet Binding

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A thrombin receptor function for platelet glycoprotein Ib-IX unmasked by cleavage of glycoprotein V.

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The glycoprotein Ib-IX-V complex contributes to tissue factor-independent thrombin generation by recombinant factor VIIa on the activated platelet surface

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Protease-activated receptors 1 and 4 mediate activation of human platelets by thrombin

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Networking in the hemostatic system. Integrin alphaiibbeta3 binds prothrombin and influences its activation

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Effector cell protease receptor-1, a platelet activation-dependent membrane protein, regulates prothrombinase-catalyzed thrombin generation

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Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation

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A critical role for extracellular protein disulfide isomerase during thrombus formation in mice

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Oxidative protein folding in eukaryotes: mechanisms and consequences

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Characterization of protein disulphide isomerase released from activated platelets

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Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane

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Contribution of allosteric disulfide bonds to regulation of hemostasis.

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A role for the thiol isomerase protein ERP5 in platelet function

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Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation

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Protein disulfide isomerase mediates integrin-dependent adhesion

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Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1.

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Sustained integrin ligation involves extracellular free sulfhydryls and enzymatically catalyzed disulfide exchange

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Protein disulphide isomerase mediates platelet aggregation and secretion

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Immunological and functional analyses of the extracellular domain of human tissue factor

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Platelets in patients with acute ischemic stroke are exhausted and refractory to thrombin, due to cleavage of the seven-transmembrane thrombin receptor (PAR-1).

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Native high-density lipoproteins inhibit platelet activation via scavenger receptor BI: role of negatively charged phospholipids.

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Calibrated automated thrombin generation measurement in clotting plasma

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Optimally functional fluorescein isothiocyanate-labelled fibrinogen for quantitative studies of binding to activated platelets and platelet aggregation

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Characterization of redox state and reductase activity of protein disulfide isomerase under different redox environments using a sensitive fluorescent assay

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Extracellular disulfide exchange and the regulation of cellular function

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Physical proximity and functional association of glycoprotein 1balpha and protein-disulfide isomerase on the platelet plasma membrane

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The platelet integrin alpha IIbbeta 3 has an endogenous thiol isomerase activity.

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Disulfide locked variants of factor VIIa with a restricted beta-strand conformation have enhanced enzymatic activity

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Structure-function relationships of human factor VIII complex studied by thioredoxin dependent disulfide reduction

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Conformation of Factor VIIa Stabilized by a Labile Disulfide Bond (Cys-310–Cys-329) in the Protease Domain Is Essential for Interaction with Tissue Factor

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Important role of the cys-191 cys-220 disulfide bond in thrombin function and allostery

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A catalytic domain exosite (Cys527-Cys542) in factor XIa mediates binding to a site on activated platelets

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Prothrombin carora: hypoprothrombinaemia caused by substitution of Tyr-44 by Cys

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Identifiers

10.1111/J.1538-7836.2011.04509.X

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21929690%20AND%20SRC:MED&resulttype=core&format=json

13 February 2020

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21929690%20AND%20SRC:MED&resulttype=core&format=json

13 February 2020

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