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Peptidyl prolyl cis-trans

Takahashi, N., Hayano, T., Suzuki, M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A binding protein cyclophilin. Nature 337 473-475, 1989. [Pg.120]

Peptidyl-prolyl cis-trans isomerase A (Rotamase) P05092 3X 2X... [Pg.236]

Peptidyl-prolyl cis-trans isomerase (PPI, cyclophilins/FKBPs) (EC5.3.4.1)... [Pg.185]

Bachinger, H.P. (1987) The influence of peptidyl-prolyl cis-trans isomerase on the in vitro folding of type III collagens. Journal of Biobgical Chemistry 262, 17144-17148. [Pg.194]

Gothel, S.F. and Marahiel, M.A. (1999) Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cellular and Molecular Life Sciences 55, 423-436. [Pg.196]

Schonbranner, E.R. and Schmid, F.X. (1992) Peptidyl-prolyl cis-trans isomerase improves the efficiency of protein disulfide isomerase as a catalyst of protein folding. Proceedings of the National Academy of Sciences USA 89, 4510-4513. [Pg.199]

Steinmann, B., Bruckner, P. and Superti-Furga, A. (1991) Cyclosporin A slows collagen triple-helix formation in vivo indirect evidence for a physiological role of peptidyl prolyl cis-trans isomer use. Journal ofBiological Chemistry 266,1299-1303. [Pg.200]

Disulfide bond formation within the individual propeptides precedes folding and trimers are then formed by association of the C-terminal propeptides." Disulfide bonds between the chains are then formed and this formation is most likely catalyzed by PDI." As triple helix formation proceeds, the rate-limiting step in this process is the cis—trans isomerization of peptidyl-Pro bonds. This process can be catalyzed by peptidyl-prolyl cis—trans isomerases (cyclophilins and FKBPs). This activity is required to convert the proline residues to the trans form required for triple helix formation." " " ... [Pg.500]

Smet, C., Sambo, A.V., Wieruszeski, J.M., et al. (2004) The peptidyl prolyl cis/trans-isomer-ase Pinl recognizes the phospho-Thr212-Pro213 site on Tau. Biochemistry, 43, 2032-2040. [Pg.335]

The protein phosphatase calcineurin was of particular interest since it mediates the immunosuppressive effect of the pharmaceuticals cyclosporin and FK506, often used in organ and tissue transplantations. The biochemical point of application of both pharmaceuticals was unclear for a long time. In initial experiments, it was found that cyclosporin and FK506 bind specifically to two proteins known as cyclophilin and FK506 binding protein, respectively. Both proteins function as peptidyl prolyl cis/trans isome-rases (review Fischer, 1994). [Pg.271]

Fischer, G. fiber Peptidyl-Prolyl-cis/trans-Isomerasen and ihre Effektoren (1994) Angew.Chem. 106, 1479-1501... [Pg.283]

Proteins spontaneously fold into their native conformation, with the primary structure of the protein dictating its three-dimensional structure. Protein folding is driven primarily by hydrophobic forces and proceeds through an ordered set of pathways. Accessory proteins, including protein disulfide isomerases, peptidyl prolyl cis-trans isomerases, and molecular chaperones, assist proteins to fold correctly in the cell. [Pg.27]

The peptidyl-prolyl cis/trans isomerase Pin 1 isomerizes the peptide bond of a phos-phorylated serine or phosphorylated threonine followed by a proline. Through isomerization of pSer-Pro or PThr-Pro, Pinl regulates a number of proteins. Together with its ability to regulate phosphorylation and conformation of tau proteins. Pin 1 is considered a potential neuroprotective function against AD. [Pg.645]

Koltin, Y., Faucette, L., Bergsma, D.J., Levy, M.A., Cafferkey, R., Koser, P.L., Johnson, R.K., and Livi, G.P. (1991). Rapamycin sensitivity in Saccharomyces cerevisiae is mediated by a peptidyl prolyl cis-trans isomerase related to human FK506-binding protein. A/o/. Cell. Biol. 11, 1718 1723. [Pg.163]

It was a surprise to discover that all of the cyclo-philins and FK506-binding proteins are peptidyl prolyl cis-trans isomerases or rotamases. They all catalyze the following simple and reversible reaction of a prolyl peptide linkage ... [Pg.488]

Jordens J, Janssens V, Longin S et al (2006) The protein phosphatase 2A phosphatase activator is a novel peptidyl-prolyl cis/ trans-isomerase. J Biol Chem 281 6349-6357... [Pg.298]

Peptidyl prolyl cis-trans isomerases (PPIases) are able to catalyze the folding or unfolding reaction. [Pg.182]

Par14i (PIN4,13810 Da) Q9Y237, NP 006214 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (Isoform)... [Pg.211]

See other pages where Peptidyl prolyl cis-trans is mentioned: [Pg.734]    [Pg.508]    [Pg.185]    [Pg.493]    [Pg.494]    [Pg.510]    [Pg.309]    [Pg.734]    [Pg.35]    [Pg.590]    [Pg.591]    [Pg.595]    [Pg.190]    [Pg.552]    [Pg.83]    [Pg.159]    [Pg.6]    [Pg.3]    [Pg.283]    [Pg.120]    [Pg.303]    [Pg.196]   


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Isomerases peptidyl prolyl cis-trans

Peptidyl

Peptidyl prolyl cis/trans isomerases (PPIases

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