259 related articles for article (PubMed ID: 7880443)
1. The Dfur2 gene of Drosophila melanogaster: genetic organization, expression during embryogenesis, and pro-protein processing activity of its translational product Dfurin2.
Roebroek AJ; Ayoubi TA; Creemers JW; Pauli IG; Van de Ven WJ
DNA Cell Biol; 1995 Mar; 14(3):223-34. PubMed ID: 7880443
[TBL] [Abstract][Full Text] [Related]
2. Cloning and functional expression of Dfurin2, a subtilisin-like proprotein processing enzyme of Drosophila melanogaster with multiple repeats of a cysteine motif.
Roebroek AJ; Creemers JW; Pauli IG; Kurzik-Dumke U; Rentrop M; Gateff EA; Leunissen JA; Van de Ven WJ
J Biol Chem; 1992 Aug; 267(24):17208-15. PubMed ID: 1512259
[TBL] [Abstract][Full Text] [Related]
3. Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases.
Van de Ven WJ; Roebroek AJ; Van Duijnhoven HL
Crit Rev Oncog; 1993; 4(2):115-36. PubMed ID: 8420571
[TBL] [Abstract][Full Text] [Related]
4. Processing specificity and biosynthesis of the Drosophila melanogaster convertases dfurin1, dfurin1-CRR, dfurin1-X, and dfurin2.
De Bie I; Savaria D; Roebroek AJ; Day R; Lazure C; Van de Ven WJ; Seidah NG
J Biol Chem; 1995 Jan; 270(3):1020-8. PubMed ID: 7836354
[TBL] [Abstract][Full Text] [Related]
5. Modulation of furin-mediated proprotein processing activity by site-directed mutagenesis.
Creemers JW; Siezen RJ; Roebroek AJ; Ayoubi TA; Huylebroeck D; Van de Ven WJ
J Biol Chem; 1993 Oct; 268(29):21826-34. PubMed ID: 8408037
[TBL] [Abstract][Full Text] [Related]
6. Furin: the prototype mammalian subtilisin-like proprotein-processing enzyme. Endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway.
Van de Ven WJ; Creemers JW; Roebroek AJ
Enzyme; 1991; 45(5-6):257-70. PubMed ID: 1843280
[TBL] [Abstract][Full Text] [Related]
7. Generation of structural and functional diversity in furin-like proteins in Drosophila melanogaster by alternative splicing of the Dfur1 gene.
Roebroek AJ; Creemers JW; Pauli IG; Bogaert T; Van de Ven WJ
EMBO J; 1993 May; 12(5):1853-70. PubMed ID: 8491178
[TBL] [Abstract][Full Text] [Related]
8. Proprotein processing activity and cleavage site selectivity of the Kex2-like endoprotease PACE4.
Creemers JW; Groot Kormelink PJ; Roebroek AJ; Nakayama K; Van de Ven WJ
FEBS Lett; 1993 Dec; 336(1):65-9. PubMed ID: 8262218
[TBL] [Abstract][Full Text] [Related]
9. cDNA sequence of a Drosophila melanogaster gene, Dfur1, encoding a protein structurally related to the subtilisin-like proprotein processing enzyme furin.
Roebroek AJ; Pauli IG; Zhang Y; van de Ven WJ
FEBS Lett; 1991 Sep; 289(2):133-7. PubMed ID: 1915835
[TBL] [Abstract][Full Text] [Related]
10. Preferred sequence requirements for cleavage of pro-von Willebrand factor by propeptide-processing enzymes.
Rehemtulla A; Kaufman RJ
Blood; 1992 May; 79(9):2349-55. PubMed ID: 1571548
[TBL] [Abstract][Full Text] [Related]
11. Gene organization of the mouse pro-hormone and pro-protein convertase PC1.
Ftouhi N; Day R; Mbikay M; Chrétien M; Seidah NG
DNA Cell Biol; 1994 Apr; 13(4):395-407. PubMed ID: 8011166
[TBL] [Abstract][Full Text] [Related]
12. Structure and tissue-specific expression of the Drosophila melanogaster organellar-type Ca(2+)-ATPase gene.
Magyar A; Bakos E; Váradi A
Biochem J; 1995 Sep; 310 ( Pt 3)(Pt 3):757-63. PubMed ID: 7575407
[TBL] [Abstract][Full Text] [Related]
13. Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease.
Tsuji A; Hine C; Tamai Y; Yonemoto K; Mori K; Yoshida S; Bando M; Sakai E; Mori K; Akamatsu T; Matsuda Y
J Biochem; 1997 Aug; 122(2):438-52. PubMed ID: 9378725
[TBL] [Abstract][Full Text] [Related]
14. Evolution of the aminoacyl-tRNA synthetase family and the organization of the Drosophila glutamyl-prolyl-tRNA synthetase gene. Intron/exon structure of the gene, control of expression of the two mRNAs, selective advantage of the multienzyme complex.
Cerini C; Semeriva M; Gratecos D
Eur J Biochem; 1997 Feb; 244(1):176-85. PubMed ID: 9063462
[TBL] [Abstract][Full Text] [Related]
15. Structure of the phenylalanine hydroxylase gene in Drosophila melanogaster and evidence of alternative promoter usage.
Ruiz-Vázquez P; Moulard M; Silva FJ
Biochem Biophys Res Commun; 1996 Aug; 225(1):238-42. PubMed ID: 8769124
[TBL] [Abstract][Full Text] [Related]
16. PACE4 is a member of the mammalian propeptidase family that has overlapping but not identical substrate specificity to PACE.
Rehemtulla A; Barr PJ; Rhodes CJ; Kaufman RJ
Biochemistry; 1993 Nov; 32(43):11586-90. PubMed ID: 8218226
[TBL] [Abstract][Full Text] [Related]
17. Differential coexpression of genes encoding prothyrotropin-releasing hormone (pro-TRH) and prohormone convertases (PC1 and PC2) in rat brain neurons: implications for differential processing of pro-TRH.
Pu LP; Ma W; Barker JL; Loh YP
Endocrinology; 1996 Apr; 137(4):1233-41. PubMed ID: 8625894
[TBL] [Abstract][Full Text] [Related]
18. cDNA and gene structure for a human subtilisin-like protease with cleavage specificity for paired basic amino acid residues.
Barr PJ; Mason OB; Landsberg KE; Wong PA; Kiefer MC; Brake AJ
DNA Cell Biol; 1991 Jun; 10(5):319-28. PubMed ID: 1713771
[TBL] [Abstract][Full Text] [Related]
19. Molecular cloning, genomic organization, and expression of a B-type (cricket-type) allatostatin preprohormone from Drosophila melanogaster.
Williamson M; Lenz C; Winther AM; Nässel DR; Grimmelikhuijzen CJ
Biochem Biophys Res Commun; 2001 Feb; 281(2):544-50. PubMed ID: 11181081
[TBL] [Abstract][Full Text] [Related]
20. Furin-mediated proprotein processing activity: involvement of negatively charged amino acid residues in the substrate binding region.
Roebroek AJ; Creemers JW; Ayoubi TA; Van de Ven WJ
Biochimie; 1994; 76(3-4):210-6. PubMed ID: 7819325
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]