Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule.
about
Tryptase 4, a new member of the chromosome 17 family of mouse serine proteases.The toxoplasma micronemal protein MIC4 is an adhesin composed of six conserved apple domains.Mapping of the discontinuous H-kininogen binding site of plasma prekallikrein. Evidence for a critical role of apple domain-2.The PAN module: the N-terminal domains of plasminogen and hepatocyte growth factor are homologous with the apple domains of the prekallikrein family and with a novel domain found in numerous nematode proteins.Structure and function of factor XIAnalysis of the factor XI variant Arg184Gly suggests a structural basis for factor IX binding to factor XIaActivation of factor XI by products of prothrombin activationCharacterization of a core binding site for ADAMTS-13 in the A2 domain of von Willebrand factor.The dimeric structure of factor XI and zymogen activationEvolution of the contact phase of vertebrate blood coagulation.Factor XI anion-binding sites are required for productive interactions with polyphosphate.Molecular characterization of FXI deficiency.A new type of plasma prekallikrein deficiency associated with homozygosity for Gly104Arg and Asn124Ser in apple domain 2 of the heavy-chain region.Mapping of the discontinuous kininogen binding site of prekallikrein. A distal binding segment is located in the heavy chain domain A4.T-SP1: a novel serine protease-like protein predominantly expressed in testis.Characterization of the H-kininogen-binding site on factor XI: a comparison of factor XI and plasma prekallikrein.Identification and characterization of an escorter for two secretory adhesins in Toxoplasma gondii.Identification of amino acids in the factor XI apple 3 domain required for activation of factor IX.Molecular cloning and biochemical characterization of rabbit factor XI.The factor IX gamma-carboxyglutamic acid (Gla) domain is involved in interactions between factor IX and factor XIa.Plasma prekallikrein/kallikrein processing by lysosomal cysteine proteases.A pair of receptor-like kinases is responsible for natural variation in shoot growth response to mannitol treatment in Arabidopsis thaliana.An update on factor XI structure and function.Cloning and structural analysis of leydin, a novel human serine protease expressed by the Leydig cells of the testis.S cysteine-rich (SCR) binding domain analysis of the Brassica self-incompatibility S-locus receptor kinase.
P2860
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P2860
Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule.
description
1991 nî lūn-bûn
@nan
1991 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
name
Location of the disulfide bond ...... minal portion of the molecule.
@ast
Location of the disulfide bond ...... minal portion of the molecule.
@en
type
label
Location of the disulfide bond ...... minal portion of the molecule.
@ast
Location of the disulfide bond ...... minal portion of the molecule.
@en
prefLabel
Location of the disulfide bond ...... minal portion of the molecule.
@ast
Location of the disulfide bond ...... minal portion of the molecule.
@en
P2093
P356
P1433
P1476
Location of the disulfide bond ...... minal portion of the molecule.
@en
P2093
P304
P356
10.1021/BI00222A007
P407
P577
1991-02-01T00:00:00Z