Apple four in human blood coagulation factor XI mediates dimer formation.
about
Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIaDimer dissociation and unfolding mechanism of coagulation factor XI apple 4 domain: spectroscopic and mutational analysisA role for factor XIIa-mediated factor XI activation in thrombus formation in vivoThe mechanism underlying activation of factor IX by factor XIa.Mapping of the discontinuous H-kininogen binding site of plasma prekallikrein. Evidence for a critical role of apple domain-2.Activated factor V is a cofactor for the activation of factor XI by thrombin in plasma.The maternal nudel protein of Drosophila has two distinct roles important for embryogenesis.Structure and function of factor XIA classification system for cross-reactive material-negative factor XI deficiencyThe dimeric structure of factor XI and zymogen activationCharacterization of Novel Forms of Coagulation Factor XIa: independence of factor XIa subunits in factor IX activation.Why factor XI deficiency is a clinical concern.Evolution of the contact phase of vertebrate blood coagulation.Platelets express three different splice variants of ApoER2 that are all involved in signaling.Mapping of the discontinuous kininogen binding site of prekallikrein. A distal binding segment is located in the heavy chain domain A4.Factor XI deficiency: a review.Characterization of the H-kininogen-binding site on factor XI: a comparison of factor XI and plasma prekallikrein.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.Noncovalent interactions of the Apple 4 domain that mediate coagulation factor XI homodimerization.Factor IX oligomerization underlies reduced activity upon disruption of physiological conditions.Three dominant-negative mutations in factor XI-deficient patients.An update on factor XI structure and function.A binding site for heparin in the apple 3 domain of factor XI.Factor 11 single-nucleotide variants in women with heavy menstrual bleeding.
P2860
Q24649797-A0F73FAA-84F5-44EC-AB14-5CE8A5F776C0Q24680521-D658299F-3270-4FD0-BFA6-5B356F748568Q28748458-31A22A5D-0AED-416E-AEFA-058ADFA9E1C2Q33597260-8521C7C6-7A09-4CD6-8AE4-00C1431B7790Q33872348-43476F96-A9B9-47CF-A357-1BACF489749DQ33927262-1AA96DDB-81F3-4E51-B8A2-6AFA8883B3C7Q33968119-B1FDD4BA-F586-4EE4-B680-DFB0FC4480D8Q34095400-5B58D5CE-4273-4909-A98D-19600B1E387BQ35847443-EFB96B37-6571-4650-8112-D2E945D6955DQ36833564-1AD9446C-A1BA-4CB9-923F-F00778F6D5BFQ37078887-FE2B06E5-CA22-4C7E-8CD8-09B1E4DA3606Q37108888-484C71F6-E27B-4042-A275-999447305D8FQ37153442-F91FEC7C-D72F-4720-A00C-4B17F144182CQ38302213-5C216271-B74A-41ED-9BDD-DC6EFC5B8350Q38357483-F8BC6CCA-08D8-428D-B501-4E78855712BCQ38841881-D9A9B899-17D4-4847-BE0C-4165517EBACEQ40762400-DFA97D00-60F6-4415-AD93-CF66EB73AB94Q40912856-DB9FD66A-77F1-48D8-840B-F2019702C3B2Q43002210-B7CBCE72-EA03-463A-86EB-4A858013DAE4Q43510603-21F634F9-77F6-428C-B3AC-2924FC41E650Q45861473-54FDDEA7-3F93-4305-8E91-AD96ADE23CCAQ45868983-D2A30A01-15AC-444B-95EF-C9471CD23F64Q47311661-71927110-ED76-4736-BD80-6A1ED499FAC6Q47954505-3511FF8A-9237-45C7-B31B-6B356F11516EQ54790631-42CC6427-634F-4AA5-B8C5-3F6FF31C5CB6
P2860
Apple four in human blood coagulation factor XI mediates dimer formation.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh
1992年學術文章
@zh-hant
name
Apple four in human blood coagulation factor XI mediates dimer formation.
@en
type
label
Apple four in human blood coagulation factor XI mediates dimer formation.
@en
prefLabel
Apple four in human blood coagulation factor XI mediates dimer formation.
@en
P2093
P356
P1433
P1476
Apple four in human blood coagulation factor XI mediates dimer formation.
@en
P2093
P304
P356
10.1021/BI00134A021
P407
P577
1992-05-01T00:00:00Z