ライフサイエンスコーパス: yapsin

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1 A C-terminally truncated form of yapsin 1 (yeast aspartic protease 3), the first member o

2 as specificity for basic residues similar to yapsin 1 and might provide the basis for the prevention

3 gent greatly facilitates the purification of yapsin 1 and should also enable the identification of ne

4 ence of a cholecystokinin(13-33) analog that yapsin 1 cleaved with an efficiency of 5.2 x 10(5) m(-1)

5 Molecular modeling of yapsin 1 identified the active-site cleft to have negati

6 netics and generated an intermediate form of yapsin 1 or pseudo-yapsin 1.

7 We report that yapsin 1 preferentially cleaves a CCK13-33 substrate wit

8 arose beads were successfully used to purify yapsin 1 to apparent homogeneity from conditioned medium

9 he apparent K(i) of Y1 for the inhibition of yapsin 1 was determined to be 64.5 nm, and the mechanism

10 Furthermore, the cleavage efficiency of yapsin 1 was enhanced for CCK13-33 analogues with argini

11 Yapsin 1, a novel aspartic protease with unique specific

12 on of six residues close to the S1 pocket in yapsin 1, relative to rhizopuspepsin and other aspartic

13 ic residue-specific yeast aspartyl protease, yapsin 1, was synthesized and characterized.

14 d an intermediate form of yapsin 1 or pseudo-yapsin 1.

15 hat it can affect the primary specificity of yapsin 1.

16 the predictions from the molecular model of yapsin 1.

17 esignated here as alpha and beta, similar to yapsin 1.

18 ogeneity, yielding approximately 1 microg of yapsin 1/g of wet yeast.

19 glycosylphosphatidylinositol-linked form of yapsin 2 (Mkc7p) was purified to homogeneity from the me

20 These results suggest that yapsin 2 is a monobasic amino acid-specific protease tha

21 Purified yapsin 2 migrated diffusely in SDS-polyacrylamide gel el

22 leavage of beta amyloid precursor protein by yapsin 2 when expressed in yeast.

23 hat the high-osmolarity glycerol pathway and yapsins are required for virulence of C. glabrata in thi

24 teases, Mkc7p and Yap3p (collectively termed yapsin), are responsible for alpha-secretase-type cleava

25 Unexpectedly, yapsins do not appear to be required to counteract the c

26 tease that belongs to the recently described yapsin family of processing enzymes.

27 should also enable the identification of new yapsin-like enzymes from mammalian and nonmammalian sour

28 ecificity for basic residues (designated the Yapsins), was overexpressed and purified to apparent hom

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