Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIa
about
Novel Family of Insect Salivary Inhibitors Blocks Contact Pathway Activation by Binding to Polyphosphate, Heparin, and Dextran SulfateEvaluation of imaging plates as recording medium for images of negatively stained single particles and electron diffraction patterns of two-dimensional crystals.The mechanism underlying activation of factor IX by factor XIa.Structure and function of factor XIAllosteric inhibition of human factor XIa: discovery of monosulfated benzofurans as a class of promising inhibitorsSite-specific N-glycosylation analysis of human factor XI: Identification of a noncanonical NXC glycosite.Blood clot formation under flow: the importance of factor XI depends strongly on platelet count.Productive recognition of factor IX by factor XIa exosites requires disulfide linkage between heavy and light chains of factor XIa.A sequential mechanism for exosite-mediated factor IX activation by factor XIaThe dimeric structure of factor XI and zymogen activationEvolution of the contact phase of vertebrate blood coagulation.Update on the physiology and pathology of factor IX activation by factor XIa.Factor XI anion-binding sites are required for productive interactions with polyphosphate.Structural and functional features of factor XI.Molecular characterization of FXI deficiency.The many faces of the contact pathway and their role in thrombosis.The activation peptide of coagulation factor XIII is vital for its expression and stability.An update on factor XI structure and function.Molecular genetic analysis of the F11 gene in 14 Turkish patients with factor XI deficiency: identification of novel and recurrent mutations and their inheritance within families.
P2860
Q27680138-FCC43EB6-A24D-4238-A313-D8A95AD53E07Q33488790-73982866-F843-4A58-BC32-33EE34AE1E13Q33597260-5B398BE5-F563-456B-909D-E5131BD79D90Q34095400-BFACABEA-AE1B-46C9-A6E7-5FE24522C92DQ35049040-6BA0DF3D-314F-4BC7-B770-39E3EBFA6336Q35219258-4A08FFBD-DF46-4EB5-8FCB-10309E255A4CQ35649582-45D54DE3-3A8D-4C1B-BF47-112E795028EDQ35838920-4B94C79C-609A-4A1F-B25D-5842F812F589Q36368312-8471B60B-1F8A-41E1-AD72-60802ABEC68BQ36833564-ECA8E218-A470-4753-AC05-282DD6DB3B67Q37153442-CCF391A1-7285-4775-9680-18538D33B446Q37318613-53FC8B78-B5A3-41B4-8A24-70312762BEB9Q37398521-095C05BB-E489-42D7-AE74-0D6BA8251119Q37561457-A6894635-6D7E-4631-B79C-282E3E14D1ABQ37716295-64C2B941-6A26-4A60-8AF4-EFC1AF365705Q37853060-0118DB5E-8492-4E21-A6EE-07550AEFC6CBQ40827724-D3A70CD3-0283-4769-A645-D54C74865776Q47311661-3A0CDC59-4555-4F95-8439-F5E5721409E4Q49273922-F0492C55-45CE-4653-A0F0-54FB02A2051C
P2860
Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIa
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@ast
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@en
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@nl
type
label
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@ast
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@en
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@nl
prefLabel
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@ast
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@en
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@nl
P2093
P2860
P356
P1476
Factor XI homodimer structure ...... XIIa, thrombin, and factor XIa
@en
P2093
Calvin K Yip
Dipali Sinha
James D Lear
Paul C Billings
Peter N Walsh
Sergei Shikov
Thomas Walz
P2860
P304
P356
10.1074/JBC.M802275200
P407
P577
2008-07-04T00:00:00Z