1 y identified lysosomal pepstatin-insensitive acid protease.

2 he cDNA of human procathepsin L, a lysosomal acid protease.

3 ta indicate that GPR is an atypical aspartic acid protease.

4 ion, and the activation of cysteine aspartic acid proteases.

5  over the physiologically important aspartic acid proteases.

6 c residues and propeptide lysine of aspartic acid proteases.

7 ction in the expression of cathepsin D or in acid protease activity.

8 t binds to a specific pocket of the aspartic acid protease, beta-secretase (BACE-1).

9                                          The acid protease cathepsin D generated fragments of 31-33.5

10 ling process in the presence of barbel crude acid protease extract.

11                                           An acid protease in the anther extract converted the inacti

12 opic agent chloroquine or with inhibitors of acid proteases inhibits processing and presentation of t

13 or but not inhibitors of cysteine proteases, acid proteases, metalloproteases, or aminopeptidases abo

14 some, lysosomal cysteine proteases, aspartic acid proteases, or metalloproteases.

15 roximately 7.5 mM) of the mammalian aspartic acid protease pepsin.

16 we have cloned and characterized a 188-amino acid, protease-resistant, carboxy-terminal fragment (C17

17 equires the CTD and residues within an amino acid protease-sensitive segment that joins the CTD to th

18 isive role for a family of cysteine aspartic acid proteases, termed caspases, as mediators of neurona