Zobrazeno 1 - 10
of 65
pro vyhledávání: '"C Valcarce"'
Publikováno v:
The Journal Of Prevention of Alzheimer's Disease. :1-6
Increasing evidence supports the role of the Receptor for Advanced Glycation Endproducts (RAGE) in the pathology of Alzheimer’s disease. Azeliragon (TTP488) is an orally bioavailable small molecule inhibitor of RAGE in Phase 3 development as a pote
Publikováno v:
European Journal of Biochemistry. 260:200-207
Various human body fluids and secretions contain a soluble form of the epidermal growth factor (EGF) precursor. The EGF precursor molecule contains eight EGF modules in addition to EGF itself. Using monoclonal antibodies specific for the EGF modules
Akademický článek
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Publikováno v:
Journal of Biological Chemistry. 269:26011-26016
The N-terminal epidermal growth factor (EGF)-like module in factor X binds a single Ca2+ with low affinity (Kd = 2.2 mM). When it is linked to the gamma-carboxyglutamic acid (Gla)-containing module, however, the affinity increases approximately 20-fo
Autor:
Ingemar Björk, Torbjörn Drakenberg, M Selander-Sunnerhagen, C Valcarce, Johan Stenflo, A M Tämlitz
Publikováno v:
Journal of Biological Chemistry. 268:26673-26678
The NH2-terminal epidermal growth factor (EGF)-like module of vitamin K-dependent coagulation factors IX and X and protein C each has one calcium binding site. This module (residues 45-86) from factor X has been isolated previously and found to bind
Publikováno v:
Journal of Biological Chemistry. 266:2453-2458
Factor Xa is the enzymatically active constituent of the prothrombinase complex, which catalyzes the conversion of prothrombin to thrombin. We have isolated fragments, from tryptic digests of factor X, that consists of the gamma-carboxyglutamic acid
Publikováno v:
The Journal of biological chemistry. 269(42)
The N-terminal epidermal growth factor (EGF)-like module in factor X binds a single Ca2+ with low affinity (Kd = 2.2 mM). When it is linked to the gamma-carboxyglutamic acid (Gla)-containing module, however, the affinity increases approximately 20-fo
Publikováno v:
The Journal of biological chemistry. 268(35)
The NH2-terminal epidermal growth factor (EGF)-like module of vitamin K-dependent coagulation factors IX and X and protein C each has one calcium binding site. This module (residues 45-86) from factor X has been isolated previously and found to bind
Publikováno v:
Current Aspects of Blood Coagulation, Fibrinolysis, and Platelets ISBN: 9784431701231
Blood coagulation results form a series of activations of zymogens of serine proteases by limited proteolytic cleavage. These reactions form what is commonly referred to as a procoagulant cascade. The final zymogen activation is the conversion of pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::14eab708b9fd3f46939c1d550d10992e
https://doi.org/10.1007/978-4-431-68323-0_1
https://doi.org/10.1007/978-4-431-68323-0_1
Publisher Summary Factors IX and X and protein C are zymogens of vitamin K-dependent serine proteases. The active form of factor IX, factor IXa, is part of the macromolecular complex (factor IXa, factor VIIIa, phospholipid, and calcium ions) that act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b20b2d23dac8652330aeb1e284b762d0
https://doi.org/10.1016/0076-6879(93)22027-d
https://doi.org/10.1016/0076-6879(93)22027-d