204 related articles for article (PubMed ID: 9353278)
1. 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.
Furie BC; Ratcliffe JV; Tward J; Jorgensen MJ; Blaszkowsky LS; DiMichele D; Furie B
J Biol Chem; 1997 Nov; 272(45):28258-62. PubMed ID: 9353278
[TBL] [Abstract][Full Text] [Related]
2. Enhanced gamma-carboxylation of recombinant factor X using a chimeric construct containing the prothrombin propeptide.
Camire RM; Larson PJ; Stafford DW; High KA
Biochemistry; 2000 Nov; 39(46):14322-9. PubMed ID: 11087381
[TBL] [Abstract][Full Text] [Related]
3. Identification of amino acids in the gamma-carboxylation recognition site on the propeptide of prothrombin.
Huber P; Schmitz T; Griffin J; Jacobs M; Walsh C; Furie B; Furie BC
J Biol Chem; 1990 Jul; 265(21):12467-73. PubMed ID: 2373701
[TBL] [Abstract][Full Text] [Related]
4. Vitamin K-dependent carboxylation. A synthetic peptide based upon the gamma-carboxylation recognition site sequence of the prothrombin propeptide is an active substrate for the carboxylase in vitro.
Ulrich MM; Furie B; Jacobs MR; Vermeer C; Furie BC
J Biol Chem; 1988 Jul; 263(20):9697-702. PubMed ID: 3133366
[TBL] [Abstract][Full Text] [Related]
5. Biosynthesis of prothrombin: intracellular localization of the vitamin K-dependent carboxylase and the sites of gamma-carboxylation.
Bristol JA; Ratcliffe JV; Roth DA; Jacobs MA; Furie BC; Furie B
Blood; 1996 Oct; 88(7):2585-93. PubMed ID: 8839851
[TBL] [Abstract][Full Text] [Related]
6. Identification of sequences within the gamma-carboxylase that represent a novel contact site with vitamin K-dependent proteins and that are required for activity.
Pudota BN; Hommema EL; Hallgren KW; McNally BA; Lee S; Berkner KL
J Biol Chem; 2001 Dec; 276(50):46878-86. PubMed ID: 11591726
[TBL] [Abstract][Full Text] [Related]
7. Vitamin K-dependent carboxylation. In vitro modification of synthetic peptides containing the gamma-carboxylation recognition site.
Hubbard BR; Jacobs M; Ulrich MM; Walsh C; Furie B; Furie BC
J Biol Chem; 1989 Aug; 264(24):14145-50. PubMed ID: 2569466
[TBL] [Abstract][Full Text] [Related]
8. Role of the propeptide and gamma-glutamic acid domain of factor IX for in vitro carboxylation by the vitamin K-dependent carboxylase.
Stanley TB; Wu SM; Houben RJ; Mutucumarana VP; Stafford DW
Biochemistry; 1998 Sep; 37(38):13262-8. PubMed ID: 9748333
[TBL] [Abstract][Full Text] [Related]
9. Profactor IX propeptide and glutamate substrate binding sites on the vitamin K-dependent carboxylase identified by site-directed mutagenesis.
Sugiura I; Furie B; Walsh CT; Furie BC
J Biol Chem; 1996 Jul; 271(30):17837-44. PubMed ID: 8663364
[TBL] [Abstract][Full Text] [Related]
10. Multi-site-specificity of the vitamin K-dependent carboxylase: in vitro carboxylation of des-gamma-carboxylated bone Gla protein and Des-gamma-carboxylated pro bone Gla protein.
Benton ME; Price PA; Suttie JW
Biochemistry; 1995 Jul; 34(29):9541-51. PubMed ID: 7626624
[TBL] [Abstract][Full Text] [Related]
11. Propeptide recognition by the vitamin K-dependent carboxylase in early processing of prothrombin and factor X.
Wallin R; Turner R
Biochem J; 1990 Dec; 272(2):473-8. PubMed ID: 2268273
[TBL] [Abstract][Full Text] [Related]
12. Conantokin-G precursor and its role in gamma-carboxylation by a vitamin K-dependent carboxylase from a Conus snail.
Bandyopadhyay PK; Colledge CJ; Walker CS; Zhou LM; Hillyard DR; Olivera BM
J Biol Chem; 1998 Mar; 273(10):5447-50. PubMed ID: 9488665
[TBL] [Abstract][Full Text] [Related]
13. In vitro gamma-carboxylation of a 59-residue recombinant peptide including the propeptide and the gamma-carboxyglutamic acid domain of coagulation factor IX. Effect of mutations near the propeptide cleavage site.
Wu SM; Soute BA; Vermeer C; Stafford DW
J Biol Chem; 1990 Aug; 265(22):13124-9. PubMed ID: 2198285
[TBL] [Abstract][Full Text] [Related]
14. Recognition site directing vitamin K-dependent gamma-carboxylation resides on the propeptide of factor IX.
Jorgensen MJ; Cantor AB; Furie BC; Brown CL; Shoemaker CB; Furie B
Cell; 1987 Jan; 48(2):185-91. PubMed ID: 3802193
[TBL] [Abstract][Full Text] [Related]
15. Effect of propeptide amino acid substitution in γ-carboxylation, activity and expression of recombinant human coagulation factor IX.
Vatandoost J; Zarei Sani O
Biotechnol Prog; 2018 Mar; 34(2):515-520. PubMed ID: 29086495
[TBL] [Abstract][Full Text] [Related]
16. Hydrophobic amino acids define the carboxylation recognition site in the precursor of the gamma-carboxyglutamic-acid-containing conotoxin epsilon-TxIX from the marine cone snail Conus textile.
Bush KA; Stenflo J; Roth DA; Czerwiec E; Harrist A; Begley GS; Furie BC; Furie B
Biochemistry; 1999 Nov; 38(44):14660-6. PubMed ID: 10545191
[TBL] [Abstract][Full Text] [Related]
17. Structural features of the kringle domain determine the intracellular degradation of under-gamma-carboxylated prothrombin: studies of chimeric rat/human prothrombin.
Wu W; Bancroft JD; Suttie JW
Proc Natl Acad Sci U S A; 1997 Dec; 94(25):13654-60. PubMed ID: 9391081
[TBL] [Abstract][Full Text] [Related]
18. Effect of propeptide mutations on post-translational processing of factor IX. Evidence that beta-hydroxylation and gamma-carboxylation are independent events.
Rabiet MJ; Jorgensen MJ; Furie B; Furie BC
J Biol Chem; 1987 Nov; 262(31):14895-8. PubMed ID: 3667614
[TBL] [Abstract][Full Text] [Related]
19. The propeptides of the vitamin K-dependent proteins possess different affinities for the vitamin K-dependent carboxylase.
Stanley TB; Jin DY; Lin PJ; Stafford DW
J Biol Chem; 1999 Jun; 274(24):16940-4. PubMed ID: 10358041
[TBL] [Abstract][Full Text] [Related]
20. Binding of the factor IX gamma-carboxyglutamic acid domain to the vitamin K-dependent gamma-glutamyl carboxylase active site induces an allosteric effect that may ensure processive carboxylation and regulate the release of carboxylated product.
Lin PJ; Straight DL; Stafford DW
J Biol Chem; 2004 Feb; 279(8):6560-6. PubMed ID: 14660587
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]