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3 ing cyclophilin A (CYPA, also known as PPIA, peptidylprolyl isomerase A) to the so-called CYPA-bindin
4 osphate dehydrogenase, alpha-enolase, actin, peptidylprolyl isomerase A, phosphatidylethanolamine-bin
6 ed FK506-binding immunophilin that possesses peptidylprolyl isomerase activity and a tetratricopeptid
7 t to cyclophilins is distinct from cis-trans-peptidylprolyl isomerase activity and is similar to that
8 compounds are shown to disrupt the cis-trans peptidylprolyl isomerase activity of FKBP12 with inhibit
10 a wide range of tissues, and the protein has peptidylprolyl isomerase activity that is inhibited by F
11 atter effect being strongly dependent on the peptidylprolyl-isomerase activity and also on the TPR do
12 bitory action of FKBP51 requires neither the peptidylprolyl-isomerase activity of the immunophilin no
17 57BL/6J mice (control) and mice deficient in peptidylprolyl isomerase D (cyclophilin D, encoded by Pp
18 sion of QTL-linked genes, we nominated Ppid (peptidylprolyl isomerase D, a member of the tetratricope
20 E. coli SurA comprises a core domain and two peptidylprolyl isomerase domains (P1 and P2), but its me
22 ild-type mice and knockout mice deficient in peptidylprolyl isomerase F (Ppif) or deficient in both P
26 the immunophilin-related co-chaperones: the peptidylprolyl isomerases FKBP51, FKBP52 or CyP40, or th
27 ion level or alteration of its activity by a peptidylprolyl isomerase inhibitor alter CFTR stability
29 inhibitors of the phosphorylation-dependent peptidylprolyl isomerase Pin1, an essential regulator of
30 e characterized the backbone dynamics of the peptidylprolyl isomerase (Pin1) catalytic domain in the
32 high molecular mass immunophilin possessing peptidylprolyl isomerase (PPIase) activity that is inhib
34 teract either directly or indirectly via its peptidylprolyl isomerase (PPIase) domain with cytoplasmi
35 through the association of the immunophilin peptidylprolyl isomerase (PPIase) domain with dynamitin,
36 -binding immunophilins possess the signature peptidylprolyl isomerase (PPIase) domain, but no role fo
38 herichia coli SurA has a core domain and two peptidylprolyl isomerase (PPIase) domains, the role(s) o
39 Escherichia coli SlyD protein, a cis-trans peptidylprolyl isomerase (PPIase), copurifies with AC7 C
42 associate with Pin1, a WW domain-containing peptidylprolyl isomerase that does not detectably bind t
43 romotes the association of Dab2 with Pin1, a peptidylprolyl isomerase that regulates the rate of Dab2