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301 related items for PubMed ID: 10360939
1. Evidence for the proenkephalin processing enzyme prohormone thiol protease (PTP) as a multicatalytic cysteine protease complex: activation by glutathione localized to secretory vesicles. Yasothornsrikul S, Aaron W, Toneff T, Hook VY. Biochemistry; 1999 Jun 08; 38(23):7421-30. PubMed ID: 10360939 [Abstract] [Full Text] [Related]
2. Evidence for functional localization of the proenkephalin-processing enzyme, prohormone thiol protease, to secretory vesicles of chromaffin cells. Hook VY, Noctor S, Sei CA, Toneff T, Yasothornsrikul S, Kang YH. Endocrinology; 1999 Aug 08; 140(8):3744-54. PubMed ID: 10433235 [Abstract] [Full Text] [Related]
3. 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 08; 314(1):171-7. PubMed ID: 7944391 [Abstract] [Full Text] [Related]
4. 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 08; 73(1):59-69. PubMed ID: 10386955 [Abstract] [Full Text] [Related]
5. Stimulation of "prohormone thiol protease" (PTP) and [Met]enkephalin by forskolin. Blockade of elevated [Met]enkephalin by a cysteine protease inhibitor of PTP. Tezapsidis N, Noctor S, Kannan R, Krieger TJ, Mende-Mueller L, Hook VY. J Biol Chem; 1995 Jun 02; 270(22):13285-90. PubMed ID: 7768928 [Abstract] [Full Text] [Related]
6. Purification and characterization of a novel thiol protease involved in processing the enkephalin precursor. Krieger TJ, Hook VY. J Biol Chem; 1991 May 05; 266(13):8376-83. PubMed ID: 2022653 [Abstract] [Full Text] [Related]
7. "Prohormone thiol protease" (PTP) processing of recombinant proenkephalin. Schiller MR, Mende-Mueller L, Moran K, Meng M, Miller KW, Hook VY. Biochemistry; 1995 Jun 27; 34(25):7988-95. PubMed ID: 7794912 [Abstract] [Full Text] [Related]
8. Thiol and aspartyl proteolytic activities in secretory vesicles of bovine pituitary. Toomim CS, Hook VY. Biochem Biophys Res Commun; 1992 Mar 16; 183(2):449-55. PubMed ID: 1550554 [Abstract] [Full Text] [Related]
9. Primary sequence characterization of catestatin intermediates and peptides defines proteolytic cleavage sites utilized for converting chromogranin a into active catestatin secreted from neuroendocrine chromaffin cells. Lee JC, Taylor CV, Gaucher SP, Toneff T, Taupenot L, Yasothornsrikul S, Mahata SK, Sei C, Parmer RJ, Neveu JM, Lane WS, Gibson BW, O'Connor DT, Hook VY. Biochemistry; 2003 Jun 17; 42(23):6938-46. PubMed ID: 12795588 [Abstract] [Full Text] [Related]
10. The processing proteases prohormone thiol protease, PC1/3 and PC2, and 70-kDa aspartic proteinase show preferences among proenkephalin, proneuropeptide Y, and proopiomelanocortin substrates. Hook VY, Schiller MR, Azaryan AV. Arch Biochem Biophys; 1996 Apr 01; 328(1):107-14. PubMed ID: 8638918 [Abstract] [Full Text] [Related]
11. The kunitz protease inhibitor form of the amyloid precursor protein (KPI/APP) inhibits the proneuropeptide processing enzyme prohormone thiol protease (PTP). Colocalization of KPI/APP and PTP in secretory vesicles. Hook VY, Sei C, Yasothornsrikul S, Toneff T, Kang YH, Efthimiopoulos S, Robakis NK, Van Nostrand W. J Biol Chem; 1999 Jan 29; 274(5):3165-72. PubMed ID: 9915856 [Abstract] [Full Text] [Related]
12. High-level expression of the prohormones proenkephalin, pro-neuropeptide Y, proopiomelanocortin, and beta-protachykinin for in vitro prohormone processing. Hook VY, Moran K, Kannan R, Kohn A, Lively MO, Azaryan A, Schiller M, Miller K. Protein Expr Purif; 1997 Jun 29; 10(1):80-8. PubMed ID: 9179294 [Abstract] [Full Text] [Related]
13. Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter. Yasothornsrikul S, Greenbaum D, Medzihradszky KF, Toneff T, Bundey R, Miller R, Schilling B, Petermann I, Dehnert J, Logvinova A, Goldsmith P, Neveu JM, Lane WS, Gibson B, Reinheckel T, Peters C, Bogyo M, Hook V. Proc Natl Acad Sci U S A; 2003 Aug 05; 100(16):9590-5. PubMed ID: 12869695 [Abstract] [Full Text] [Related]
14. 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 26; 274(48):34164-73. PubMed ID: 10567388 [Abstract] [Full Text] [Related]
15. Secretory vesicle aminopeptidase B related to neuropeptide processing: molecular identification and subcellular localization to enkephalin- and NPY-containing chromaffin granules. Hwang SR, O'Neill A, Bark S, Foulon T, Hook V. J Neurochem; 2007 Mar 26; 100(5):1340-50. PubMed ID: 17241125 [Abstract] [Full Text] [Related]
17. 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 07; 270(14):8201-8. PubMed ID: 7713926 [Abstract] [Full Text] [Related]
18. 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 07; 58(2):593-9. PubMed ID: 1729404 [Abstract] [Full Text] [Related]
19. 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 25; 268(27):20570-7. PubMed ID: 8376411 [Abstract] [Full Text] [Related]
20. Proenkephalin-processing enzymes in chromaffin granules: model for neuropeptide biosynthesis. Hook VY, Schiller MR, Azaryan AV, Tezapsidis N. Ann N Y Acad Sci; 1996 Mar 22; 780():121-33. PubMed ID: 8602725 [Abstract] [Full Text] [Related] Page: [Next] [New Search]