186 related articles for article (PubMed ID: 14609438)
1. A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidases.
Wlodawer A; Durell SR; Li M; Oyama H; Oda K; Dunn BM
BMC Struct Biol; 2003 Nov; 3():8. PubMed ID: 14609438
[TBL] [Abstract][Full Text] [Related]
2. Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis.
Rawlings ND; Barrett AJ
Biochim Biophys Acta; 1999 Jan; 1429(2):496-500. PubMed ID: 9989235
[TBL] [Abstract][Full Text] [Related]
3. Characterization and chromosomal mapping of a mouse ortholog of the late-infantile ceroid-lipofuscinosis gene CLN2.
Katz ML; Liu PC; Grob-Nunn SE; Shibuya H; Johnson GS
Mamm Genome; 1999 Nov; 10(11):1050-3. PubMed ID: 10556422
[TBL] [Abstract][Full Text] [Related]
4. Biochemical characterization of a lysosomal protease deficient in classical late infantile neuronal ceroid lipofuscinosis (LINCL) and development of an enzyme-based assay for diagnosis and exclusion of LINCL in human specimens and animal models.
Sohar I; Sleat DE; Jadot M; Lobel P
J Neurochem; 1999 Aug; 73(2):700-11. PubMed ID: 10428067
[TBL] [Abstract][Full Text] [Related]
5. 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; 268(3):904-8. PubMed ID: 10679303
[TBL] [Abstract][Full Text] [Related]
6. The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH.
Lin L; Sohar I; Lackland H; Lobel P
J Biol Chem; 2001 Jan; 276(3):2249-55. PubMed ID: 11054422
[TBL] [Abstract][Full Text] [Related]
7. 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; 13(20):2483-91. PubMed ID: 15317752
[TBL] [Abstract][Full Text] [Related]
8. A mouse model of classical late-infantile neuronal ceroid lipofuscinosis based on targeted disruption of the CLN2 gene results in a loss of tripeptidyl-peptidase I activity and progressive neurodegeneration.
Sleat DE; Wiseman JA; El-Banna M; Kim KH; Mao Q; Price S; Macauley SL; Sidman RL; Shen MM; Zhao Q; Passini MA; Davidson BL; Stewart GR; Lobel P
J Neurosci; 2004 Oct; 24(41):9117-26. PubMed ID: 15483130
[TBL] [Abstract][Full Text] [Related]
9. Structural organization and sequence of CLN2, the defective gene in classical late infantile neuronal ceroid lipofuscinosis.
Liu CG; Sleat DE; Donnelly RJ; Lobel P
Genomics; 1998 Jun; 50(2):206-12. PubMed ID: 9653647
[TBL] [Abstract][Full Text] [Related]
10. Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme.
Golabek AA; Dolzhanskaya N; Walus M; Wisniewski KE; Kida E
J Biol Chem; 2008 Jun; 283(24):16497-504. PubMed ID: 18411270
[TBL] [Abstract][Full Text] [Related]
11. Two novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosis.
Lam CW; Poon PM; Tong SF; Ko CH
Am J Med Genet; 2001 Mar; 99(2):161-3. PubMed ID: 11241479
[No Abstract] [Full Text] [Related]
12. 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; 15(11):1131-54. PubMed ID: 15610613
[TBL] [Abstract][Full Text] [Related]
13. New families of carboxyl peptidases: serine-carboxyl peptidases and glutamic peptidases.
Oda K
J Biochem; 2012 Jan; 151(1):13-25. PubMed ID: 22016395
[TBL] [Abstract][Full Text] [Related]
14. Late infantile neuronal ceroid lipofuscinosis is due to splicing mutations in the CLN2 gene.
Hartikainen JM; Ju W; Wisniewski KE; Moroziewicz DN; Kaczmarski AL; McLendon L; Zhong D; Suarez CT; Brown WT; Zhong N
Mol Genet Metab; 1999 Jun; 67(2):162-8. PubMed ID: 10356316
[TBL] [Abstract][Full Text] [Related]
15. Rapid detection of the two most common CLN2 mutations causing classical late infantile neuronal ceroid lipofuscinosis.
Bodzioch M; Aslanidis C; Kacinski M; Zhong N; Wisniewski KE; Schmitz G
Clin Chem; 2000 Oct; 46(10):1696-9. PubMed ID: 11017954
[No Abstract] [Full Text] [Related]
16. Production and characterization of recombinant human CLN2 protein for enzyme-replacement therapy in late infantile neuronal ceroid lipofuscinosis.
Lin L; Lobel P
Biochem J; 2001 Jul; 357(Pt 1):49-55. PubMed ID: 11415435
[TBL] [Abstract][Full Text] [Related]
17. 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; 18(2):165. PubMed ID: 11462245
[TBL] [Abstract][Full Text] [Related]
18. Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
Pal A; Kraetzner R; Gruene T; Grapp M; Schreiber K; Grønborg M; Urlaub H; Becker S; Asif AR; Gärtner J; Sheldrick GM; Steinfeld R
J Biol Chem; 2009 Feb; 284(6):3976-84. PubMed ID: 19038966
[TBL] [Abstract][Full Text] [Related]
19. Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
Guhaniyogi J; Sohar I; Das K; Stock AM; Lobel P
J Biol Chem; 2009 Feb; 284(6):3985-97. PubMed ID: 19038967
[TBL] [Abstract][Full Text] [Related]
20. Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity.
Tsiakas K; Steinfeld R; Storch S; Ezaki J; Lukacs Z; Kominami E; Kohlschütter A; Ullrich K; Braulke T
Glycobiology; 2004 Apr; 14(4):1C-5C. PubMed ID: 14736728
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
