About: Propeptide of human protein C is necessary for .gamma.-carboxylation

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scientific article published on 01 November 1987

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в листопаді 1987 (uk) article scientifique publié en 1987 (fr) artículu científicu espublizáu en payares de 1987 (ast) scientific article published on 01 November 1987 (en) im November 1987 veröffentlicher wissenschaftlicher Artikel (de)
publication date	wds:Q61314310-AC794FDA-2987-4DA9-A5B4-C05D088527F5
publication date	1987-11-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q61314310-48AC4990-5B47-4B8D-9D77-66C9E681FE19
language of work or name	English
author name string	wds:Q61314310-057BB583-86B8-4953-B024-5816B501F052 wds:Q61314310-0A644A44-B59D-4D02-8296-B88E734A017D wds:Q61314310-177771CD-F9D0-4B51-970E-0B226BED3548 wds:Q61314310-19AC8737-9759-477C-9EE8-7EE2FD7AC5E7 wds:Q61314310-7D3DA263-43F6-4E0A-93F4-FFE20971A3A1 wds:Q61314310-87002468-6194-4B21-AA08-AD251F99AEC3 wds:Q61314310-ACE9AEB1-2B91-4F03-9D51-E2FA0B3C1356 wds:Q61314310-B199EAA9-7669-426F-BA9D-04360D9E2838
author name string	C A Sprecher E W Davie F S Hagen D C Foster A A Kumar B G Schach M S Rudinski M Y Insley
rdfs:label	Propeptide of human protein C is necessary for .gamma.-carboxylation (en) Propeptide of human protein C is necessary for .gamma.-carboxylation (nl)
skos:prefLabel	Propeptide of human protein C is necessary for .gamma.-carboxylation (en) Propeptide of human protein C is necessary for .gamma.-carboxylation (nl)
name	Propeptide of human protein C is necessary for .gamma.-carboxylation (en) Propeptide of human protein C is necessary for .gamma.-carboxylation (nl)
author	wds:Q61314310-D7FA9550-D4D9-4736-BA1D-7636FB2FA1DC
author	Kathleen L Berkner
title	wds:Q61314310-360A91B0-F6D6-425C-AE51-49B2B3180344
title	Propeptide of human protein C is necessary for gamma-carboxylation (en)
page(s)	wds:Q61314310-67F0116A-6D7B-4B91-A9BA-37DB1627E44C
page(s)	7003-7011
instance of	wds:Q61314310-4A445228-6055-40B7-BF37-43902B3D8635
instance of	scholarly article
PubMed ID	wds:Q61314310-9E4032CF-BD55-42BF-9747-DB448C14035C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3427056
PubMed ID	3427056
published in	wds:Q61314310-1CC37774-2B2B-47E6-AAFC-74D659A9029D
published in	Biochemistry
issue	wds:Q61314310-EBDD976F-1AB5-4953-9AE3-99323CACD299
volume	wds:Q61314310-8ABA5311-8CAB-4CA4-B9F4-5E6CB1841AF6
issue	22
volume	26
DOI	wds:Q61314310-833A0000-ABFD-4E2B-9F15-CC0713B9A35C
DOI	http://dx.doi.org/10.1021/BI00396A022
DOI	10.1021/BI00396A022
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q61314310
is cites work of	Identification of two novel transmembrane gamma-carboxyglutamic acid proteins expressed broadly in fetal and adult tissues Profactor IX propeptide and glutamate substrate binding sites on the vitamin K-dependent carboxylase identified by site-directed mutagenesis The propeptides of the vitamin K-dependent proteins possess different affinities for the vitamin K-dependent carboxylase Vitamin K-dependent gamma-glutamylcarboxylation: an ancient posttranslational modification Recombinant ob protein reduces feeding and body weight in the ob/ob mouse Beta protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites Molecular pathology of haemophilia B Protein C and protein S Proline-rich Gla protein 2 is a cell-surface vitamin K-dependent protein that binds to the transcriptional coactivator Yes-associated protein Cloning and expression of murine thrombopoietin cDNA and stimulation of platelet production in vivo Characterization and novel purification of recombinant human protein C from three mammalian cell lines Gamma-carboxyglutamate-containing proteins and the vitamin K-dependent carboxylase Evolution of prothrombin: isolation and characterization of the cDNAs encoding chicken and hagfish prothrombin Vitamin K-dependent carboxylation of the carboxylase Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state Purification of vitamin K-dependent carboxylase from cultured cells Nucleotide sequence of prothrombin gene in abnormal prothrombin-producing hepatocellular carcinoma cell lines Human thrombopoietin: gene structure, cDNA sequence, expression, and chromosomal localization Role of N-linked glycosylation in human osteonectin. Effect of carbohydrate removal by N-glycanase and site-directed mutagenesis on structure and binding of type V collagen Purification and identification of bovine liver gamma-carboxylase Expression of recombinant human plasminogen in mammalian cells is augmented by suppression of plasmin activity Identification of sequences within the gamma-carboxylase that represent a novel contact site with vitamin K-dependent proteins and that are required for activity Mammalian expression of the human sex steroid-binding protein of plasma (SBP or SHBG) and testis (ABP). Characterization of the recombinant protein beta-Hydroxyaspartic acid and beta-hydroxyasparagine residues in recombinant human protein S are not required for anticoagulant cofactor activity or for binding to C4b-binding protein The gamma-carboxylation recognition site is sufficient to direct vitamin K-dependent carboxylation on an adjacent glutamate-rich region of thrombin in a propeptide-thrombin chimera. Structural integrity of the gamma-carboxyglutamic acid domain of human blood coagulation factor IXa Is required for its binding to cofactor VIIIa The active site region of the vitamin K-dependent carboxylase includes both the amino-terminal hydrophobic and carboxy-terminal hydrophilic domains of the protein Vitamin K-dependent carboxylase: affinity purification from bovine liver by using a synthetic propeptide containing the gamma-carboxylation recognition site Modeling zymogen protein C. Identification and computationally-based structural interpretation of naturally occurring variants of human protein C Genetic background analysis of protein C deficiency demonstrates a recurrent mutation associated with venous thrombosis in Chinese population Molecular biology of factor X. Impaired secretion of the elongated mutant of protein C (protein C-Nagoya). Molecular and cellular basis for hereditary protein C deficiency Thrombin activation of protein C requires prior processing by a liver proprotein convertase. Purification of protein C from canine plasma Mechanisms of vitamin K antagonism
is cites work of	wds:Q36674600-8B416C69-412B-4497-A0ED-F05CE3AE2666 wds:Q35738080-DC9321FA-4B4B-45C9-AA42-A7F74A5A201A wds:Q41137813-E6C9A83D-E53D-4288-AE91-110A2347A9F4 wds:Q73674227-9B53E13B-0786-48D1-981F-4B663DBEF97E wds:Q71144055-A3BD01AD-FC67-420E-AAE0-30B5CD5F8AF1 wds:Q77841219-268A2224-BAFD-46C9-9B97-05193AF503D1 wds:Q34302852-A36983C4-6E74-4515-BC6D-5398AE74121F wds:Q28116089-D6C7A172-431D-45C8-A98D-03C7A822859C wds:Q34251221-079437FC-F93A-4E93-B77D-4A957973D8F0 wds:Q36018621-CCC00A0D-CA37-4114-8E1A-C7D58C5481F4

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