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1                                              Tripeptidyl peptidase 1 (TPP1) deficiency causes CLN2 di
2      Cerliponase alfa is a recombinant human tripeptidyl peptidase 1 (TPP1) enzyme replacement therap
3 atients with nonsense mutations in the TPP1 (tripeptidyl peptidase 1), DMD (dystrophin), SMARCAL1 (SW
4 nt therapy (ERT) involving recombinant human tripeptidyl peptidase 1, known as cerliponase alfa (Brin
5 rder caused by loss-of-function mutations in tripeptidyl-peptidase 1 (TPP1), we used the capsid to pa
6 ed by a deficiency in the lysosomal protease tripeptidyl-peptidase 1 (TPP1).
7 cies in palmitoyl protein thioesterase-1 and tripeptidyl peptidase-1, respectively.
8 lthough endopeptidase, dipeptidyl peptidase, tripeptidyl peptidase, and acylaminoacyl peptidase activ
9      In 2017, cerliponase alfa (Brineura), a tripeptidyl peptidase enzyme replacement therapy, became
10                                              Tripeptidyl peptidase I (TPP I) is the first mammalian r
11 y mutations in CLN2, which encodes lysosomal tripeptidyl peptidase I (TPP1).
12 used by a deficiency in the lysosomal enzyme tripeptidyl peptidase I, which results in aberrant lysos
13                                              Tripeptidyl-peptidase I (TPP I) is a lysosomal serine-ca
14 , which encodes a lysosomal serine protease, tripeptidyl-peptidase I (TPP I), result in an autosomal
15 N2, the gene encoding the lysosomal protease tripeptidyl-peptidase I (TPP I).
16                                              Tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysos
17                                              Tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysos
18                                        Human tripeptidyl-peptidase I (TPP I, CLN2 protein) is a lysos
19 , where the defective gene is Cln2, encoding tripeptidyl-peptidase I (TPP1).
20 fuscinosis encodes a lysosomal protease with tripeptidyl-peptidase I activity.
21 lly and stoichiometrically reacts with CLN2p/tripeptidyl-peptidase I at Ser475, demonstrating that th
22  C-terminal hexahistidine-tagged human CLN2p/tripeptidyl-peptidase I produced from insect cells trans
23 (Leu196) corresponds to that of mature CLN2p/tripeptidyl-peptidase I purified from human brain.
24 been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10).
25 terization, cloning, and genetic analysis of tripeptidyl peptidase II (TPP II) from Drosophila melano
26                                              Tripeptidyl peptidase II (TPP II) is an exopeptidase of
27        Now it appears that another protease, tripeptidyl peptidase II (TPP II), plays a critical role
28 t showed a homozygous frameshift mutation in tripeptidyl peptidase II (TPP2) abolishing protein expre
29                                     Although tripeptidyl peptidase II (TPPII) exhibited limited activ
30                                              Tripeptidyl peptidase II (TPPII) is a eukaryotic proteas
31                                              Tripeptidyl peptidase II (TPPII) is a large cytosolic pr
32 sates and cultured cells have suggested that tripeptidyl peptidase II (TPPII) plays a role in creatin
33                     We demonstrate here that tripeptidyl peptidase II (TPPII), a cytoplasmic, high-mo
34  (IC50 = 7 nM) of the serine protease enzyme tripeptidyl peptidase II (TPPII), an endogenous protease
35  immunosenescence arising from deficiency in tripeptidyl peptidase II (TPPII).
36 -chloromethylketone, a specific inhibitor of tripeptidyl peptidase II activity.
37 ticularly a large proteolytic complex with a tripeptidyl peptidase II activity.
38 t in part, on nonproteasomal protease(s), 2) tripeptidyl peptidase II does not substitute for the pro
39 resentation after leucine aminopeptidase and tripeptidyl peptidase II knockdown.
40 -fold at 10 days without changes in MAFbx or tripeptidyl peptidase II mRNA, but all decreased between
41 osolic peptidases leucine aminopeptidase and tripeptidyl peptidase II, as evidenced by increased pp65
42 , one important intermediate exopeptidase is tripeptidyl peptidase (TPP)II, which digests peptide pro
43 an palmitoyl protein thioesterase (PPT1) and tripeptidyl peptidase (TPP1) in dried blood spots from n
44                Recent reports concluded that tripeptidyl peptidase (TPPII) is essential for MHC class