Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Erhard Ralf Schönbrunner"'
Autor:
Nobuhiro Takahashi, Erhard Ralf Schönbrunner, Maximilian Tropschug, Franz X. Schmid, Gunter Fischer, Sabine Mayer
Publikováno v:
Journal of Biological Chemistry. 266:3630-3635
Cyclophilins are a class of ubiquitous proteins with yet unknown function. They were originally discovered as the major binding proteins for the immunosuppressant cyclosporin A. The only known catalytic function of these proteins in vitro is the cis/
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e420f0218d6d8531e1705a628659332a
https://doi.org/10.1016/s0021-9258(19)67841-5
https://doi.org/10.1016/s0021-9258(19)67841-5
Publisher Summary This chapter discusses the function of prolyl isomerases in protein folding. The importance of prolyl isomerization reactions as slow, rate-limiting steps of folding, and their interdependence with other events in protein folding ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea5736f213e5c5f54fa4f1e7d1d1cf84
https://doi.org/10.1016/s0065-3233(08)60563-x
https://doi.org/10.1016/s0065-3233(08)60563-x
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 89(10)
The cis-trans isomerization of prolyl peptide bonds and the formation of disulfide bonds are both slow steps in protein folding. By using ribonuclease T1 as a model system, we show that these two processes can become linked in the oxidative folding o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c33f60d29e4b8a42e2dc2e3c677af85
https://pubmed.ncbi.nlm.nih.gov/1584784
https://pubmed.ncbi.nlm.nih.gov/1584784
Publikováno v:
Nature. 346(6285)
Slow protein-folding reactions are accelerated by a prolyl cis/trans isomerase isolated from porcine kidney which is identical to cyclophilin, a protein that is probably the cellular receptor for the immunosuppressant cyclosporin A. Catalysis probabl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ba0afd0349fc043e526682f95581e5c
https://pubmed.ncbi.nlm.nih.gov/1696687
https://pubmed.ncbi.nlm.nih.gov/1696687