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3 omparisons of the propeptides indicated that cathepsin F and cathepsin W may form a new cathepsin sub
6 1.7A structure of the mature domain of human cathepsin F associated with an irreversible vinyl sulfon
8 wn cathepsins, the open reading frame of the cathepsin F cDNA did not encode a signal sequence, thus
9 an papain-like cysteine protease, designated cathepsin F, has been cloned from a lambdagt10-skeletal
13 rley plants silencing or over-expressing the cathepsin F-like HvPap-1 Cys protease show differential
14 , one of the proteinaceous inhibitors of the cathepsin F-like protease, also has important effects on
15 odds ratio [OR] = 1.07, p-value = 6.80E-06), cathepsin F (OR = 1.10, p-value = 7.16E-05), and serine
16 e precursor polypeptide of human recombinant cathepsin F, produced in Pichia pastoris, was processed
17 structure provides a basis for understanding cathepsin F's substrate specificity, and suggests ways o
19 CLIP from Ii-MHC class II complexes, whereas cathepsin F was as efficient as cathepsin S in CLIP gene