Results 161 to 170 of about 18,044 (216)

Prolyl isomerase Pin1: a promoter of cancer and a target for therapy. [PDF]

Cell Death Dis, 2018
Chen Y, Wu YR, Yang HY, Li XZ, Jie MM, Hu CJ, Wu YY, Yang SM, Yang YB.   +8 more
europepmc   +1 more source

Peptidyl-Prolyl Isomerase ppiB Is Essential for Proteome Homeostasis and Virulence in Burkholderia pseudomallei. [PDF]

Infect Immun, 2019
Bzdyl NM, Scott NE, Norville IH, Scott AE, Atkins T, Pang S, Sarovich DS, Coombs G, Inglis TJJ, Kahler CM, Sarkar-Tyson M.   +10 more
europepmc   +1 more source

Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD

Biological Chemistry, 2013
SlyD is a bacterial two-domain protein that functions as a molecular chaperone, a prolyl cis/trans isomerase, and a nickel-binding protein. This review summarizes recent findings about the molecular enzyme mechanism of SlyD.
Michael Kovermann, Franz X Schmid, Jochen Balbach   +2 more
exaly   +2 more sources

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Prolyl isomerases in yeast

Frontiers in Bioscience, 2004
Prolyl isomerases are enzymes that catalyze cis-trans isomerization of peptidyl-prolyl bonds and span three structurally unrelated protein families: the cyclophilins, FKBPs, and parvulins. The genome of the budding yeast Saccharomyces cerevisiae encodes eight different cyclophilins (Cpr1 to Cpr8), four FKBPs (Fpr1 to Fpr4), and a single parvulin (Ess1).
Miguel, Arevalo-Rodriguez, Xiaoyun, Wu, Steven D, Hanes, Joseph, Heitman   +3 more
openaire   +2 more sources

Peptidyl‐prolyl isomerase inhibitors

Peptide Science, 2005
AbstractDesigned peptidyl‐prolyl isomerase (PPIase) inhibitors of Pin1, cyclophilin (CyP), and FK506 binding protein (FKBP) are reviewed. Emphasis is placed on the design, structure, and biological activity of the inhibitors. While CyP and FKBP inhibitors have been explored fairly thoroughly, inhibitors of the relatively new Pin1 cell cycle regulator ...
Xiaodong J, Wang, Felicia A, Etzkorn
openaire   +2 more sources

Periplasmic Chaperones and Prolyl Isomerases

EcoSal Plus, 2018
The biogenesis of periplasmic and outer membrane proteins (OMPs) in Escherichia coli is assisted by a variety of processes that help with their folding and transport to their final destination in the cellular envelope.
Stull, Frederick, Betton, Jean-Michel, Bardwell, James C.A.   +2 more
openaire   +3 more sources

Catalysis of protein folding by prolyl isomerase

Nature, 1987
Rates of protein folding reactions vary considerably. Some denatured proteins regain the native conformation within milliseconds or seconds, whereas others refold very slowly in the time range of minutes or hours. Varying folding rates are observed not only for different proteins, but can also be detected for single polypeptide species. This originates
K, Lang, F X, Schmid, G, Fischer
openaire   +2 more sources

Isomerase and Chaperone Activity of Prolyl Isomerase in the Folding of Carbonic Anhydrase

Science, 1992
Several proteins have been discovered that either catalyze slow protein-folding reactions or assist folding in the cell. Prolyl isomerase, which has been shown to accelerate rate-limiting cis-trans peptidyl-proline isomerization steps in the folding pathway, can also participate in the protein-folding process as a ...
P O, Freskgård, N, Bergenhem, B H, Jonsson, M, Svensson, U, Carlsson   +4 more
openaire   +2 more sources

The major peptidyl-prolyl isomerase activity in thylakoid lumen of plant chloroplasts belongs to a novel cyclophilin TLP20

FEBS Letters, 2003
Fractionation of proteins from the thylakoid lumen of spinach chloroplasts combined with peptidyl-prolyl cis/trans isomerase (PPIase) measurements revealed a major isomerase activity that was ascribed to a novel enzyme TLP20 (thylakoid lumen PPIase of 20
Alexander V Vener, Bertil Andersson
exaly   +2 more sources