Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Peptidyl prolyl cis-trans-isomerase activity associated with the lumen of the endoplasmic reticulum.

Literature DB >> 8010971

Peptidyl prolyl cis-trans-isomerase activity associated with the lumen of the endoplasmic reticulum.

Abstract

Peptidyl prolyl cis-trans-isomerase (PPI) activity was detected in microsomal fractions from bovine and rat liver. Extensive washing, proteinase and sonication treatments indicated that although some of this activity was due to adsorbed cytosolic enzymes, there was also an active but latent microsomal PPI activity. Density-gradient subfractionation indicated that activity was associated with vesicles derived from both the rough and the smooth endoplasmic reticulum (ER), suggesting that the activity was located within the ER lumen. The luminal PPI activity was inhibited by cyclosporin A and was active towards an unfolded protein substrate as well as towards the standard peptide substrate.

Entities: Chemical Species

Mesh：

Substances：

Year: 1994 PMID： 8010971 PMCID： PMC1138245 DOI： 10.1042/bj3000865

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

32 in total

1. Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A binding protein).

Authors: S Schneuwly; R D Shortridge; D C Larrivee; T Ono; M Ozaki; W L Pak
Journal: Proc Natl Acad Sci U S A Date: 1989-07 Impact factor: 11.205

Review 2. Protein oligomerization in the endoplasmic reticulum.

Authors: S M Hurtley; A Helenius
Journal: Annu Rev Cell Biol Date: 1989

Review 3. The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.

Authors: G Fischer; F X Schmid
Journal: Biochemistry Date: 1990-03-06 Impact factor: 3.162

4. Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A.

Authors: J Liu; C T Walsh
Journal: Proc Natl Acad Sci U S A Date: 1990-06 Impact factor: 11.205

5. Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding.

Authors: T Kiefhaber; H P Grunert; U Hahn; F X Schmid
Journal: Biochemistry Date: 1990-07-10 Impact factor: 3.162

6. The latency of rat liver microsomal protein disulphide-isomerase.

Authors: N Lambert; R B Freedman
Journal: Biochem J Date: 1985-06-15 Impact factor: 3.857

7. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.

Authors: G Fischer; B Wittmann-Liebold; K Lang; T Kiefhaber; F X Schmid
Journal: Nature Date: 1989-02-02 Impact factor: 49.962

8. The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein.

Authors: B H Shieh; M A Stamnes; S Seavello; G L Harris; C S Zuker
Journal: Nature Date: 1989-03-02 Impact factor: 49.962

9. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin.

Authors: N Takahashi; T Hayano; M Suzuki
Journal: Nature Date: 1989-02-02 Impact factor: 49.962

10. [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides].

Authors: G Fischer; H Bang; C Mech
Journal: Biomed Biochim Acta Date: 1984

9 in total

6. Chaperones contribute to G protein coupled receptor oligomerization, but do not participate in assembly of the G protein with the receptor signaling complex.

Authors: Maha M Hammad; Denis J Dupré
Journal: J Mol Signal Date: 2010-09-24

Peptidyl prolyl cis-trans-isomerase activity associated with the lumen of the endoplasmic reticulum.

1. Drosophila ninaA gene encodes an eye-specific cyclophilin (cyclosporine A binding protein).

Review 2. Protein oligomerization in the endoplasmic reticulum.

Review 3. The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.

4. Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A.

5. Replacement of a cis proline simplifies the mechanism of ribonuclease T1 folding.

6. The latency of rat liver microsomal protein disulphide-isomerase.

7. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins.

8. The ninaA gene required for visual transduction in Drosophila encodes a homologue of cyclosporin A-binding protein.

9. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin.

10. [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides].

1. Protein folding in the secretory pathway of animal cells.

2. The characterization of a cyclophilin-type peptidyl prolyl cis-trans-isomerase from the endoplasmic-reticulum lumen.

3. Mitochondrial and Cell Death Mechanisms in Neurodegenerative Diseases.

Review 4. Biology of mitochondria in neurodegenerative diseases.

5. Purification and characterization of cytosolic and microsomal cyclophilins from maize (Zea mays).

6. Chaperones contribute to G protein coupled receptor oligomerization, but do not participate in assembly of the G protein with the receptor signaling complex.

7. The mitochondrial permeability transition pore in motor neurons: involvement in the pathobiology of ALS mice.

8. Cyclophilin-40: evidence for a dimeric complex with hsp90.

Review 9. The mitochondrial permeability transition pore: a molecular target for amyotrophic lateral sclerosis therapy.