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1                                              Tripeptidyl peptidase 1 (TPP1) deficiency causes CLN2 di
2 atients with nonsense mutations in the TPP1 (tripeptidyl peptidase 1), DMD (dystrophin), SMARCAL1 (SW
3 ed by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
4                                              Tripeptidyl peptidase I (TPP I) is the first mammalian r
5 y mutations in CLN2, which encodes lysosomal tripeptidyl peptidase I (TPP1).
6 used by a deficiency in the lysosomal enzyme tripeptidyl peptidase I, which results in aberrant lysos
7                                              Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-ca
8 , which encodes a lysosomal serine protease, tripeptidyl-peptidase I (TPP I), result in an autosomal
9 N2, the gene encoding the lysosomal protease tripeptidyl-peptidase I (TPP I).
10                                              Tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysos
11                                              Tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysos
12                                        Human tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysos
13 , where the defective gene is Cln2, encoding tripeptidyl-peptidase I (TPP1).
14 fuscinosis encodes a lysosomal protease with tripeptidyl-peptidase I activity.
15 lly and stoichiometrically reacts with CLN2p/tripeptidyl-peptidase I at Ser475, demonstrating that th
16  C-terminal hexahistidine-tagged human CLN2p/tripeptidyl-peptidase I produced from insect cells trans
17 (Leu196) corresponds to that of mature CLN2p/tripeptidyl-peptidase I purified from human brain.
18 been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10).
19 terization, cloning, and genetic analysis of tripeptidyl peptidase II (TPP II) from Drosophila melano
20                                              Tripeptidyl peptidase II (TPP II) is an exopeptidase of
21        Now it appears that another protease, tripeptidyl peptidase II (TPP II), plays a critical role
22 t showed a homozygous frameshift mutation in tripeptidyl peptidase II (TPP2) abolishing protein expre
23                                     Although tripeptidyl peptidase II (TPPII) exhibited limited activ
24                                              Tripeptidyl peptidase II (TPPII) is a eukaryotic proteas
25                                              Tripeptidyl peptidase II (TPPII) is a large cytosolic pr
26 sates and cultured cells have suggested that tripeptidyl peptidase II (TPPII) plays a role in creatin
27                     We demonstrate here that tripeptidyl peptidase II (TPPII), a cytoplasmic, high-mo
28  (IC50 = 7 nM) of the serine protease enzyme tripeptidyl peptidase II (TPPII), an endogenous protease
29  immunosenescence arising from deficiency in tripeptidyl peptidase II (TPPII).
30 -chloromethylketone, a specific inhibitor of tripeptidyl peptidase II activity.
31 ticularly a large proteolytic complex with a tripeptidyl peptidase II activity.
32 t in part, on nonproteasomal protease(s), 2) tripeptidyl peptidase II does not substitute for the pro
33 resentation after leucine aminopeptidase and tripeptidyl peptidase II knockdown.
34 -fold at 10 days without changes in MAFbx or tripeptidyl peptidase II mRNA, but all decreased between
35 osolic peptidases leucine aminopeptidase and tripeptidyl peptidase II, as evidenced by increased pp65
36 , one important intermediate exopeptidase is tripeptidyl peptidase (TPP)II, which digests peptide pro
37 an palmitoyl protein thioesterase (PPT1) and tripeptidyl peptidase (TPP1) in dried blood spots from n
38                Recent reports concluded that tripeptidyl peptidase (TPPII) is essential for MHC class

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