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Journal Abstract Search

178 related items for PubMed ID: 15733845

  • 1. 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
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  • 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
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  • 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 24; 268(3):904-8. PubMed ID: 10679303
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  • 6. [Tripeptidyl-peptidase I--distribution, biogenesis, and mechanisms of activation].
    Gołabek AA.
    Postepy Biochem; 2006 Feb 24; 52(1):16-23. PubMed ID: 16869297
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  • 13. 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 19; 276(3):2249-55. PubMed ID: 11054422
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  • 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 19; 18(2):165. PubMed ID: 11462245
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  • 18. 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 13; 283(24):16497-504. PubMed ID: 18411270
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  • 20. 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 Jun 13; 5 Suppl A():73-9. PubMed ID: 11589013
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