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2 atients with nonsense mutations in the TPP1 (tripeptidyl peptidase 1), DMD (dystrophin), SMARCAL1 (SW
6 used by a deficiency in the lysosomal enzyme tripeptidyl peptidase I, which results in aberrant lysos
8 , which encodes a lysosomal serine protease, tripeptidyl-peptidase I (TPP I), result in an autosomal
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
19 terization, cloning, and genetic analysis of tripeptidyl peptidase II (TPP II) from Drosophila melano
22 t showed a homozygous frameshift mutation in tripeptidyl peptidase II (TPP2) abolishing protein expre
26 sates and cultured cells have suggested that tripeptidyl peptidase II (TPPII) plays a role in creatin
28 (IC50 = 7 nM) of the serine protease enzyme tripeptidyl peptidase II (TPPII), an endogenous protease
32 t in part, on nonproteasomal protease(s), 2) tripeptidyl peptidase II does not substitute for the pro
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
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