The role of beta-hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX
about
Molecular characterization of a gene of the 'EGF family' expressed in undifferentiated human NTERA2 teratocarcinoma cellsVitamin C: update on physiology and pharmacologyStructure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium bindingThe three-dimensional structure of the first EGF-like module of human factor IX: Comparison with EGF and TGF-αTwo non-contiguous regions contribute to nidogen binding to a single EGF-like motif of the laminin gamma 1 chainAmino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for laminin, collagen IV and cellsMolecular pathology of haemophilia BAspartyl beta-hydroxylase: in vitro hydroxylation of a synthetic peptide based on the structure of the first growth factor-like domain of human factor IX.C1q receptors.Characterization of recombinant human factor IX expressed in transgenic mice and in derived trans-immortalized hepatic cell lines.Cloning and expression of a protective antigen from the cattle tick Boophilus microplus.First epidermal growth factor-like domain of human blood coagulation factor IX is required for its activation by factor VIIa/tissue factor but not by factor XIa.Missense mutations and evolutionary conservation of amino acids: evidence that many of the amino acids in factor IX function as "spacer" elementsAmino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor.A GPI-anchored sea urchin sperm membrane protein containing EGF domains is related to human uromodulinMUP-4 is a novel transmembrane protein with functions in epithelial cell adhesion in Caenorhabditis elegansFibrillin-containing microfibrils are key signal relay stations for cell function.Fibulin-1 purification from human plasma using affinity chromatography on Factor H-SepharoseAntibody-probed conformational transitions in the protease domain of human factor IX upon calcium binding and zymogen activation: putative high-affinity Ca(2+)-binding site in the protease domainThe interaction between complement component C4b-binding protein and the vitamin K-dependent protein S forms a link between blood coagulation and the complement systemReplacing the first epidermal growth factor-like domain of factor IX with that of factor VII enhances activity in vitro and in canine hemophilia B.Molecular insights of Gas6/TAM in cancer development and therapy.Surface-loop residue Lys316 in blood coagulation Factor IX is a major determinant for Factor X but not antithrombin recognition.The first EGF-like domain from human factor IX contains a high-affinity calcium binding site.The first EGF domain of coagulation factor IX attenuates cell adhesion and induces apoptosis.Non-Linear and Flexible Regions of the Human Notch1 Extracellular Domain Revealed by High-Resolution Structural Studies.Direct detection of point mutations by mismatch analysis: application to haemophilia B.Recombinant human protein C derivatives: altered response to calcium resulting in enhanced activation by thrombinRegions 301-303 and 333-339 in the catalytic domain of blood coagulation factor IX are factor VIII-interactive sites involved in stimulation of enzyme activity.Replacement of isoleucine-397 by threonine in the clotting proteinase factor IXa (Los Angeles and Long Beach variants) affects macromolecular catalysis but not L-tosylarginine methyl ester hydrolysis. Lack of correlation between the ox brain prothroCoagulation Factor IX for Hemophilia B Therapy.
P2860
Q24567485-EE7750DF-5909-441B-BA61-056657C81526Q24654791-D4413825-97EA-429A-B4B0-FBDCB4E798D0Q24673741-12FA93EB-E7C8-45C7-8762-E9FD89583D07Q27642047-B71CF3B8-6405-4D09-88E4-DCBB8526CDA2Q30448484-39F8607E-1E1C-4F1B-8051-CB031B95B1EBQ33557514-F95408AE-B220-4CB2-A9D3-C49EF8EFD550Q33562603-6BE6B0CD-5FE8-4A48-9AB3-C89C9A79DD99Q33856789-0FC4E0FA-D18D-4B13-935C-37E8D9724BA6Q33938158-7154D53E-4B35-4211-8813-1B3C4EEC31A3Q34077417-5A507788-9941-46E5-9610-A703C1D870C0Q34324585-4D4068C2-3A80-4EE9-9213-D4731EF1EDB3Q35183792-EF47E053-BDBB-44C4-B965-1895342B8270Q35196882-90D83DAD-70BA-4ACE-A6BF-A79F8A411476Q36221099-CEB85D75-CBDD-4E37-AF95-8AB242BC82AAQ36232958-9F79A5A1-D03D-4BA4-8625-BD68B8A16925Q36293940-59D1D356-C08C-4641-BA67-A99C94ACBF6AQ36470965-BFDA8765-6405-470A-9554-2A391A35FDC3Q36717079-366ECAC2-331A-4279-A662-9221C93B10DFQ36761241-D0FC3F8C-6BCE-4C61-B8D4-8554B0EFA562Q37099581-A7A2D39D-0C36-4530-BEE0-EEB4CDAB1289Q37371257-73373C83-5C3F-482E-95E2-3A4174205B82Q37745358-6FF15B55-7AF2-4FEA-8E0E-B03C46B0F83CQ38308725-AE0CB4ED-0678-422B-A5CC-31191784A6B7Q38342074-ABFBB176-D649-4276-87D8-5F295A3534ECQ39809447-DB2337AE-B192-4A7C-9625-720F77DF6672Q39903567-08425F8D-8076-4D31-BE7B-E068CFAA35AAQ40449237-0A8D7846-F366-45B6-A28C-88A5E5A40472Q41240571-DA827A0C-D2D4-4F5E-A57A-5C8C122560AAQ41788714-342E2111-8D21-4299-BFA9-F1E849A112E6Q41999331-943B0978-440B-4138-8CA5-BA5FBDBE1D10Q42256024-7F858D8F-FF84-4322-8AB0-F13B1AAD0ABD
P2860
The role of beta-hydroxyaspartate and adjacent carboxylate residues in the first EGF domain of human factor IX
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
The role of beta-hydroxyaspart ...... EGF domain of human factor IX
@ast
The role of beta-hydroxyaspart ...... EGF domain of human factor IX
@en
type
label
The role of beta-hydroxyaspart ...... EGF domain of human factor IX
@ast
The role of beta-hydroxyaspart ...... EGF domain of human factor IX
@en
prefLabel
The role of beta-hydroxyaspart ...... EGF domain of human factor IX
@ast
The role of beta-hydroxyaspart ...... EGF domain of human factor IX
@en
P2093
P2860
P1433
P1476
The role of beta-hydroxyaspart ...... EGF domain of human factor IX
@en
P2093
P2860
P304
P407
P577
1988-07-01T00:00:00Z