148 related articles for article (PubMed ID: 3922369)
1. A putative prohormone processing protease in bovine adrenal medulla specifically cleaving in between Lys-Arg sequences.
Mizuno K; Kojima M; Matsuo H
Biochem Biophys Res Commun; 1985 Apr; 128(2):884-91. PubMed ID: 3922369
[TBL] [Abstract][Full Text] [Related]
2. Proenkephalin processing enzyme with specificity toward paired basic residues purified from bovine adrenal chromaffin granules.
Mizuno K; Matsuo H
Neuropeptides; 1985 Feb; 5(4-6):489-92. PubMed ID: 3889695
[TBL] [Abstract][Full Text] [Related]
3. A putative processing enzyme for proenkephalin in bovine adrenal chromaffin granule membranes. Purification and properties.
Shen FS; Roberts SF; Lindberg I
J Biol Chem; 1989 Sep; 264(26):15600-5. PubMed ID: 2768280
[TBL] [Abstract][Full Text] [Related]
4. Arginine and lysine aminopeptidase activities in chromaffin granules of bovine adrenal medulla: relevance to prohormone processing.
Yasothornsrikul S; Toneff T; Hwang SR; Hook VY
J Neurochem; 1998 Jan; 70(1):153-63. PubMed ID: 9422358
[TBL] [Abstract][Full Text] [Related]
5. Purification and characterization of a putative proenkephalin cleaving enzyme.
Paik SR; Lewis RV
Arch Biochem Biophys; 1992 Aug; 296(2):617-29. PubMed ID: 1632649
[TBL] [Abstract][Full Text] [Related]
6. Purification and characteristics of the candidate prohormone processing proteases PC2 and PC1/3 from bovine adrenal medulla chromaffin granules.
Azaryan AV; Krieger TJ; Hook VY
J Biol Chem; 1995 Apr; 270(14):8201-8. PubMed ID: 7713926
[TBL] [Abstract][Full Text] [Related]
7. Purification and characterization of a novel thiol protease involved in processing the enkephalin precursor.
Krieger TJ; Hook VY
J Biol Chem; 1991 May; 266(13):8376-83. PubMed ID: 2022653
[TBL] [Abstract][Full Text] [Related]
8. Prohormone thiol protease and enkephalin precursor processing: cleavage at dibasic and monobasic sites.
Krieger TJ; Mende-Mueller L; Hook VY
J Neurochem; 1992 Jul; 59(1):26-31. PubMed ID: 1613503
[TBL] [Abstract][Full Text] [Related]
9. A unique proenkephalin-converting enzyme purified from bovine adrenal chromaffin granules.
Mizuno K; Miyata A; Kangawa K; Matsuo H
Biochem Biophys Res Commun; 1982 Oct; 108(3):1235-42. PubMed ID: 6758772
[No Abstract] [Full Text] [Related]
10. Alpha1-antichymotrypsin-like proteins I and II purified from bovine adrenal medulla are enriched in chromaffin granules and inhibit the proenkephalin processing enzyme "prohormone thiol protease".
Hook VY; Tezapsidis N; Hwang SR; Sei C; Byrne M; Yasothornsrikul S
J Neurochem; 1999 Jul; 73(1):59-69. PubMed ID: 10386955
[TBL] [Abstract][Full Text] [Related]
11. Purification of an endopeptidase from bovine adrenal medulla granules which cleaves in vitro at paired but not at single basic residues.
Maret GE; Fauchère JL
Anal Biochem; 1988 Jul; 172(1):248-58. PubMed ID: 3056095
[TBL] [Abstract][Full Text] [Related]
12. Molecular cloning of endopin 1, a novel serpin localized to neurosecretory vesicles of chromaffin cells. Inhibition of basic residue-cleaving proteases by endopin 1.
Hwang SR; Steineckert B; Yasothornsrikul S; Sei CA; Toneff T; Rattan J; Hook VY
J Biol Chem; 1999 Nov; 274(48):34164-73. PubMed ID: 10567388
[TBL] [Abstract][Full Text] [Related]
13. Distinct properties of prohormone thiol protease (PTP) compared to cathepsins B, L, and H: evidence for PTP as a novel cysteine protease.
Azaryan AV; Hook VY
Arch Biochem Biophys; 1994 Oct; 314(1):171-7. PubMed ID: 7944391
[TBL] [Abstract][Full Text] [Related]
14. Characterization of proenkephalin-cleaving proteinases in bovine adrenal chromaffin granules using [35S]proenkephalin copolymerized into sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
Roberts SF; Irvine JW; Lindberg I
J Neurochem; 1992 Feb; 58(2):593-9. PubMed ID: 1729404
[TBL] [Abstract][Full Text] [Related]
15. The prohormone processing activity is enriched in a low-density subpopulation of chromaffin granules.
Maret GE; Fauchère JL
FEBS Lett; 1986 Jan; 195(1-2):258-60. PubMed ID: 3510903
[TBL] [Abstract][Full Text] [Related]
16. Kex2-like proteolytic activity in adrenal medullary chromaffin granules.
Azaryan AV; Hook VY
Biochem Biophys Res Commun; 1992 May; 185(1):398-403. PubMed ID: 1599477
[TBL] [Abstract][Full Text] [Related]
17. A "trypsin-like" enzyme in adrenal chromaffin granules: a proenkephalin processing enzyme.
Evangelista R; Ray P; Lewis RV
Biochem Biophys Res Commun; 1982 Jun; 106(3):895-902. PubMed ID: 7115385
[No Abstract] [Full Text] [Related]
18. Further characterization of an enkephalin-generating enzyme from adrenal medullary chromaffin granules.
Lindberg I; Yang HY; Costa E
J Neurochem; 1984 May; 42(5):1411-9. PubMed ID: 6368750
[TBL] [Abstract][Full Text] [Related]
19. Selective cleavage of proenkephalin-derived peptides (less than 23,300 daltons) by plasma kallikrein.
Metters KM; Rossier J; Paquin J; Chrétien M; Seidah NG
J Biol Chem; 1988 Sep; 263(25):12543-53. PubMed ID: 3410851
[TBL] [Abstract][Full Text] [Related]
20. Purification and characterization of alpha 1-antichymotrypsin-like protease inhibitor that regulates prohormone thiol protease involved in enkephalin precursor processing.
Hook VY; Purviance RT; Azaryan AV; Hubbard G; Krieger TJ
J Biol Chem; 1993 Sep; 268(27):20570-7. PubMed ID: 8376411
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
