ライフサイエンスコーパス: peptidylprolyl isomerase

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1 Peptidylprolyl isomerase 1 (Pin1), a protein overexpress

2 osphate dehydrogenase, alpha-enolase, actin, peptidylprolyl isomerase A, phosphatidylethanolamine-bin

3 ed FK506-binding immunophilin that possesses peptidylprolyl isomerase activity and a tetratricopeptid

4 t to cyclophilins is distinct from cis-trans-peptidylprolyl isomerase activity and is similar to that

5 compounds are shown to disrupt the cis-trans peptidylprolyl isomerase activity of FKBP12 with inhibit

6 Immunophilins are protein chaperones with peptidylprolyl isomerase activity that belong to one of

7 a wide range of tissues, and the protein has peptidylprolyl isomerase activity that is inhibited by F

8 atter effect being strongly dependent on the peptidylprolyl-isomerase activity and also on the TPR do

9 bitory action of FKBP51 requires neither the peptidylprolyl-isomerase activity of the immunophilin no

10 e and function are regulated by the cellular peptidylprolyl isomerase cyclophilin A (CyPA).

11 The peptidylprolyl isomerase, cyclophilin D (CypD, PPIF), is

12 Peptidylprolyl isomerase cyclophilins play critical role

13 Because the peptidylprolyl isomerase CYPA also interacts with HIV-1

14 57BL/6J mice (control) and mice deficient in peptidylprolyl isomerase D (cyclophilin D, encoded by Pp

15 22% identity with the central portion of the peptidylprolyl isomerase domain of human FKBP52.

16 atly reduced in cyclophilin D null [Ppif-/- (peptidylprolyl isomerase F)] mice.

17 FKBP8 is a member of the peptidylprolyl isomerase family that mediates the cis/tr

18 The peptidylprolyl isomerase FKBP12 interacts with FK506 for

19 the immunophilin-related co-chaperones: the peptidylprolyl isomerases FKBP51, FKBP52 or CyP40, or th

20 ion level or alteration of its activity by a peptidylprolyl isomerase inhibitor alter CFTR stability

21 Peptidylprolyl isomerase Pin1 regulates the function and

22 inhibitors of the phosphorylation-dependent peptidylprolyl isomerase Pin1, an essential regulator of

23 e characterized the backbone dynamics of the peptidylprolyl isomerase (Pin1) catalytic domain in the

24 By using the peptidylprolyl isomerase, Pin1, as a probe for proline-d

25 high molecular mass immunophilin possessing peptidylprolyl isomerase (PPIase) activity that is inhib

26 oth prokaryotes and eukaryotes, that exhibit peptidylprolyl isomerase (PPIase) activity.

27 teract either directly or indirectly via its peptidylprolyl isomerase (PPIase) domain with cytoplasmi

28 through the association of the immunophilin peptidylprolyl isomerase (PPIase) domain with dynamitin,

29 -binding immunophilins possess the signature peptidylprolyl isomerase (PPIase) domain, but no role fo

30 expressed fragment of FKBP52 comprising its peptidylprolyl isomerase (PPIase) domain.

31 Escherichia coli SlyD protein, a cis-trans peptidylprolyl isomerase (PPIase), copurifies with AC7 C

32 Current inhibitors of peptidylprolyl isomerases show no selectivity between th

33 associate with Pin1, a WW domain-containing peptidylprolyl isomerase that does not detectably bind t

34 romotes the association of Dab2 with Pin1, a peptidylprolyl isomerase that regulates the rate of Dab2

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