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232 related items for PubMed ID: 15158442
1. The lysosomal degradation of neuromedin B is dependent on tripeptidyl peptidase-I: evidence for the impairment of neuropeptide degradation in late-infantile neuronal ceroid lipofuscinosis. Kopan S, Sivasubramaniam U, Warburton MJ. Biochem Biophys Res Commun; 2004 Jun 18; 319(1):58-65. PubMed ID: 15158442 [Abstract] [Full Text] [Related]
2. Lysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on tripeptidyl peptidase-I: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis. Bernardini F, Warburton MJ. Biochem J; 2002 Sep 01; 366(Pt 2):521-9. PubMed ID: 12038963 [Abstract] [Full Text] [Related]
3. Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes. Steinfeld R, Steinke HB, Isbrandt D, Kohlschütter A, Gärtner J. Hum Mol Genet; 2004 Oct 15; 13(20):2483-91. PubMed ID: 15317752 [Abstract] [Full Text] [Related]
4. Characterization of endopeptidase activity of tripeptidyl peptidase-I/CLN2 protein which is deficient in classical late infantile neuronal ceroid lipofuscinosis. Ezaki J, Takeda-Ezaki M, Oda K, Kominami E. Biochem Biophys Res Commun; 2000 Feb 24; 268(3):904-8. PubMed ID: 10679303 [Abstract] [Full Text] [Related]
5. [Tripeptidyl-peptidase I--distribution, biogenesis, and mechanisms of activation]. Gołabek AA. Postepy Biochem; 2006 Feb 24; 52(1):16-23. PubMed ID: 16869297 [Abstract] [Full Text] [Related]
6. AAV2-mediated CLN2 gene transfer to rodent and non-human primate brain results in long-term TPP-I expression compatible with therapy for LINCL. Sondhi D, Peterson DA, Giannaris EL, Sanders CT, Mendez BS, De B, Rostkowski AB, Blanchard B, Bjugstad K, Sladek JR, Redmond DE, Leopold PL, Kaminsky SM, Hackett NR, Crystal RG. Gene Ther; 2005 Nov 24; 12(22):1618-32. PubMed ID: 16052206 [Abstract] [Full Text] [Related]
7. Tripeptidyl-peptidase I in health and disease. Golabek AA, Kida E. Biol Chem; 2006 Aug 24; 387(8):1091-9. PubMed ID: 16895480 [Abstract] [Full Text] [Related]
8. Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase. Ezaki J, Takeda-Ezaki M, Kominami E. J Biochem; 2000 Sep 24; 128(3):509-16. PubMed ID: 10965052 [Abstract] [Full Text] [Related]
9. Tripeptidyl peptidase-I is essential for the degradation of sulphated cholecystokinin-8 (CCK-8S) by mouse brain lysosomes. Warburton MJ, Bernardini F. Neurosci Lett; 2002 Oct 11; 331(2):99-102. PubMed ID: 12361850 [Abstract] [Full Text] [Related]
10. Diagnosis of late-infantile neuronal ceroid lipofuscinosis: a new sensitive method to assay lysosomal pepstatin-insensitive proteinase activity in human and animal specimens by capillary electrophoresis. Viglio S, Marchi E, Wisniewski K, Casado B, Cetta G, Iadarola P. Electrophoresis; 2001 Jul 11; 22(11):2343-50. PubMed ID: 11504071 [Abstract] [Full Text] [Related]
11. Rat tripeptidyl peptidase I: molecular cloning, functional expression, tissue localization and enzymatic characterization. Du PG, Kato S, Li YH, Maeda T, Yamane T, Yamamoto S, Fujiwara M, Yamamoto Y, Nishi K, Ohkubo I. Biol Chem; 2001 Dec 11; 382(12):1715-25. PubMed ID: 11843185 [Abstract] [Full Text] [Related]
12. Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates. Steinfeld R, Fuhrmann JC, Gärtner J. J Histochem Cytochem; 2006 Sep 11; 54(9):991-6. PubMed ID: 16782851 [Abstract] [Full Text] [Related]
13. Tripeptidyl-peptidase I in neuronal ceroid lipofuscinoses and other lysosomal storage disorders. Wisniewski KE, Kida E, Walus M, Wujek P, Kaczmarski W, Golabek AA. Eur J Paediatr Neurol; 2001 Sep 11; 5 Suppl A():73-9. PubMed ID: 11589013 [Abstract] [Full Text] [Related]
14. Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I. Vines DJ, Warburton MJ. FEBS Lett; 1999 Jan 25; 443(2):131-5. PubMed ID: 9989590 [Abstract] [Full Text] [Related]
15. Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations. Lin L, Lobel P. Hum Mutat; 2001 Aug 25; 18(2):165. PubMed ID: 11462245 [Abstract] [Full Text] [Related]
16. Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I. Golabek AA, Kida E, Walus M, Wujek P, Mehta P, Wisniewski KE. J Biol Chem; 2003 Feb 28; 278(9):7135-45. PubMed ID: 12488460 [Abstract] [Full Text] [Related]
17. Clinical protocol. Administration of a replication-deficient adeno-associated virus gene transfer vector expressing the human CLN2 cDNA to the brain of children with late infantile neuronal ceroid lipofuscinosis. Crystal RG, Sondhi D, Hackett NR, Kaminsky SM, Worgall S, Stieg P, Souweidane M, Hosain S, Heier L, Ballon D, Dinner M, Wisniewski K, Kaplitt M, Greenwald BM, Howell JD, Strybing K, Dyke J, Voss H. Hum Gene Ther; 2004 Nov 28; 15(11):1131-54. PubMed ID: 15610613 [Abstract] [Full Text] [Related]
18. R208X mutation in CLN2 gene associated with reduced cerebrospinal fluid pterins in a girl with classic late infantile neuronal ceroid lipofuscinosis. Barisić N, Logan P, Pikija S, Skarpa D, Blau N. Croat Med J; 2003 Aug 28; 44(4):489-93. PubMed ID: 12950156 [Abstract] [Full Text] [Related]
19. The substrate range of tripeptidyl-peptidase I. Bernardini F, Warburton MJ. Eur J Paediatr Neurol; 2001 Aug 28; 5 Suppl A():69-72. PubMed ID: 11589011 [Abstract] [Full Text] [Related]
20. Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I. Walus M, Kida E, Wisniewski KE, Golabek AA. FEBS Lett; 2005 Feb 28; 579(6):1383-8. PubMed ID: 15733845 [Abstract] [Full Text] [Related] Page: [Next] [New Search]