High molecular weight kininogen binds to unstimulated platelets
about
Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and factor XII: identity with the receptor that binds to the globular "heads" of C1q (gC1q-R)Identification of cytokeratin 1 as a binding protein and presentation receptor for kininogens on endothelial cellsPhospholipid binding plasma proteins required for antiphospholipid antibody detection--an overview.Heat shock protein 90 catalyzes activation of the prekallikrein-kininogen complex in the absence of factor XII.Bradykinin metabolism and hypotensive transfusion reactions.Human neutrophils contain and bind high molecular weight kininogen.Antiphospholipid antibodies and kininogens in pathologic pregnancies: a review.Regulation of factor XIa activity by platelets and alpha 1-protease inhibitor.High molecular weight kininogen inhibits fibrinogen binding to cytoadhesins of neutrophils and plateletsThe sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependent binding to an anionic surface.Assembly, activation, and physiologic influence of the plasma kallikrein/kinin system.Inhibition of cell adhesion by high molecular weight kininogen.The kinin-kallikrein system: physiological roles, pathophysiology and its relationship to cancer biomarkers.Incidence of hypotension and acute hypotensive transfusion reactions following platelet concentrate transfusions.Physiologic activities of the contact activation system.Mesothelial cells activate the plasma kallikrein-kinin system during pleural inflammation.The assembly and activation of kinin-forming systems on the surface of human U-937 macrophage-like cells.Cleavage of high-molecular-weight kininogen by elastase and tryptase is inhibited by ferritin.The beta A4 amyloid protein precursor in human circulation.Kinetics of inhibition of platelet calpain II by human kininogensActivation of the plasma kallikrein-kinin system on human lung epithelial cells.Assembly and activation of HK-PK complex on endothelial cells results in bradykinin liberation and NO formation.Thrombin-induced platelet aggregation is inhibited by the heptapeptide Leu271-Ala277 of domain 3 in the heavy chain of high molecular weight kininogen.Assembly, activation, and signaling by kinin-forming proteins on human vascular smooth muscle cells.
P2860
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P2860
High molecular weight kininogen binds to unstimulated platelets
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
High molecular weight kininogen binds to unstimulated platelets
@ast
High molecular weight kininogen binds to unstimulated platelets
@en
type
label
High molecular weight kininogen binds to unstimulated platelets
@ast
High molecular weight kininogen binds to unstimulated platelets
@en
prefLabel
High molecular weight kininogen binds to unstimulated platelets
@ast
High molecular weight kininogen binds to unstimulated platelets
@en
P2093
P2860
P356
P1476
High molecular weight kininogen binds to unstimulated platelets
@en
P2093
A H Schmaier
D Schutsky
E J Gustafson
L C Knight
P2860
P304
P356
10.1172/JCI112567
P407
P577
1986-07-01T00:00:00Z