About: Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells

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description	artículu científicu espublizáu en 1988 (ast) vědecký článek publikovaný v roce 1988 (cs) наукова стаття, опублікована в жовтні 1988 (uk) 1988 թվականի հոտեմբերին հրատարակված գիտական հոդված (hy) 1988 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած (hyw) article scientifique publié en 1988 (fr) scientific journal article (en) im Oktober 1988 veröffentlicher wissenschaftlicher Artikel (de) wetenschappelijk artikel (gepubliceerd op 1988/10/04) (nl) vedecký článok (publikovaný 1988/10/04) (sk) مقالة علمية (نشرت في 4-10-1988) (ar)
publication date	wds:Q28646327-30CB60D9-EC78-425D-87F7-E0C0FC6A4B79
publication date	1988-10-04 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28646327-498E579E-BB51-42BB-AEB4-A3B0BF1B0901
language of work or name	English
author name string	wds:Q28646327-10E4E650-5B96-4FD9-BE7E-2AFC4E522C32 wds:Q28646327-2CE6DBA3-49DF-47C0-BBB0-FAC7E0280EF7 wds:Q28646327-485763C9-35E3-42CA-80E3-DE9514654D7F wds:Q28646327-6D61D26A-823C-451D-8CFC-1AF7EA438AF5 wds:Q28646327-965C157A-5709-49A9-B760-BC562FCE187F wds:Q28646327-9C2BE8AD-78BE-4E28-928C-CF24DE0665CE wds:Q28646327-FDE29B16-8984-4C7D-BB75-CACC9B04535E
author name string	A. H. Pedersen E. M. Nicolaisen L. Thim M. Christensen S. Bjoern T. Lund-Hansen U. Hedner
rdfs:label	Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (en) Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (nl) Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (ast)
skos:prefLabel	Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (en) Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (nl) Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (ast)
name	Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (en) Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (nl) Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (ast)
title	wds:Q28646327-16916BE9-CDE3-4ACE-84AF-5CF06C0201F6
title	Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells (en)
page(s)	wds:Q28646327-D732BD4B-3FCB-4983-A543-0B317E4C2B7C
page(s)	7785–7793
instance of	wds:Q28646327-7A424381-5FF1-4092-9BE9-9C237045F1CC
instance of	scholarly article
PubMed ID	wds:Q28646327-241EC84F-4192-43D9-A0FC-D866935C8118
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3264725
PubMed ID	3264725
published in	wds:Q28646327-3DEEFB4D-C39A-4820-8697-2350C3395399
published in	Biochemistry
issue	wds:Q28646327-65AD9F9B-4922-4036-9D44-F616C838E8BD
volume	wds:Q28646327-7BB84A46-59A1-41C4-BC8C-692D75E01E4E
issue	20
volume	27
DOI	wds:Q28646327-CFD5040A-7C89-41EB-861E-EFF244740166
DOI	http://dx.doi.org/10.1021/BI00420A030
DOI	10.1021/BI00420A030
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28646327
is cites work of	Production of multidomain complement glycoproteins in insect cells. Preparation of vitamin K-dependent proteins, such as clotting factors II, VII, IX and X and clotting inhibitor protein C. High-dose factor VIIa increases initial thrombin generation and mediates faster platelet activation in thrombocytopenia-like conditions in a cell-based model system. Hepsin, a putative membrane-associated serine protease, activates human factor VII and initiates a pathway of blood coagulation on the cell surface leading to thrombin formation Contribution of tryptophan residues to the CD spectrum of the extracellular domain of human tissue factor: application in folding studies and prediction of secondary structure The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency. The hydroxy amino acid in an Asn-X-Ser/Thr sequon can influence N-linked core glycosylation efficiency and the level of expression of a cell surface glycoprotein The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor Biological Insights into Therapeutic Protein Modifications throughout Trafficking and Their Biopharmaceutical Applications Post-translational modifications in the context of therapeutic proteins Oxygen-dependent asparagine hydroxylation Calcium-binding EGF-like modules in coagulation proteinases: function of the calcium ion in module interactions The activation of factor X and prothrombin by recombinant factor VIIa in vivo is mediated by tissue factor Ca2+ binding to the first epidermal growth factor module of coagulation factor VIIa is important for cofactor interaction and proteolytic function Involvement of the hydrophobic stack residues 39-44 of factor VIIa in tissue factor interactions Catabolism of factor VIIa bound to tissue factor in fibroblasts in the presence and absence of tissue factor pathway inhibitor Pharmacokinetics and safety of FFR-rFVIIa after single doses in healthy subjects Antibody-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 domain Effect of recombinant factor VIIa (Novoseven) on thrombocytopenia-like conditions in vitro Rational combinatorial chemistry-based selection, synthesis and evaluation of an affinity adsorbent for recombinant human clotting factor VII. Effect of recombinant factor VIIa on the hemostatic defect in dogs with hemophilia A, hemophilia B, and von Willebrand disease Transcriptional program induced by factor VIIa-tissue factor, PAR1 and PAR2 in MDA-MB-231 cells Tissue factor-factor VIIa-specific up-regulation of IL-8 expression in MDA-MB-231 cells is mediated by PAR-2 and results in increased cell migration Activated factor VII: my story Mechanism of the Ca2+-induced Enhancement of the Intrinsic Factor VIIa Activity Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity. Site-directed mutagenesis but not gamma-carboxylation of Glu-35 in factor VIIa affects the association with tissue factor. Incorporation of an active site inhibitor in factor VIIa alters the affinity for tissue factor Augmented intrinsic activity of Factor VIIa by replacement of residues 305, 314, 337 and 374: evidence of two unique mutational mechanisms of activity enhancement Structural changes in factor VIIa induced by Ca2+ and tissue factor studied using circular dichroism spectroscopy Assignment of molecular properties of a superactive coagulation factor VIIa variant to individual amino acid changes. High affinity Ca(2+)-binding site in the serine protease domain of human factor VIIa and its role in tissue factor binding and development of catalytic activity Allosteric activation of coagulation factor VIIa visualized by hydrogen exchange Analysis of the site-specific asparagine-linked glycosylation of recombinant human coagulation factor VIIa by glycosidase digestions, liquid chromatography, and mass spectrometry Mutagenesis of the gamma-carboxyglutamic acid domain of human factor VII to generate maximum enhancement of the membrane contact site Mass spectrometric characterization of N- and O-glycans of plasma-derived coagulation factor VII. FVIIa derivatives obtained by autolytic and controlled cathepsin G mediated cleavage Spin and fluorescent probing of the binding interface between tissue factor and factor VIIa at multiple sites. Factor VIIa-induced p44/42 mitogen-activated protein kinase activation requires the proteolytic activity of factor VIIa and is independent of the tissue factor cytoplasmic domain Recombinant activated factor VII in the treatment of bleeding episodes in patients with inherited and acquired bleeding disorders. Effect of activated prothrombin complex concentrate or recombinant factor VIIa on the bleeding time and thrombus formation during anticoagulation with a direct thrombin inhibitor Mammalian recombinant coagulation proteins: structure and function

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