Results 171 to 180 of about 18,044 (216)

Prolyl Isomerases: Role in Protein Folding

1993
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 are described.
F X, Schmid, L M, Mayr, M, Mücke, E R, Schönbrunner   +3 more
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Unraveling the Role of Peptidyl-Prolyl Isomerases in Neurodegeneration

Molecular Neurobiology, 2011
Immunophilins are a family of highly conserved proteins with a peptidyl-prolyl isomerase activity that binds immunosuppressive drugs such as FK506, cyclosporin A, and rapamycin. Immunophilins can be divided into two subfamilies, the cyclophilins, and the FK506 binding proteins (FKBPs).
Melanie, Gerard, Angélique, Deleersnijder, Jonas, Demeulemeester, Zeger, Debyser, Veerle, Baekelandt   +4 more
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Requirement of the Prolyl Isomerase Pin1 for the Replication Checkpoint

Science, 2000
The peptidyl-prolyl isomerase Pin1 has been implicated in regulating cell cycle progression. Pin1 was found to be required for the DNA replication checkpoint in Xenopus laevis . Egg extracts depleted of Pin1 inappropriately transited from the G 2 to the M phase of the cell cycle in the ...
K E, Winkler, K I, Swenson, S, Kornbluth, A R, Means   +3 more
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Characterization of folding intermediates using prolyl isomerase

Biochemistry, 1994
Structure-reactivity relationships of human peptidyl prolyl cis-trans isomerase (PPI) toward the two slow folding reactions of yeast iso-2 cytochrome c have been used to characterize the structure of folding intermediates in the vicinity of critical prolines. We propose that the relative catalytic efficiency of PPI for the protein substrate relative to
S, Veeraraghavan, B T, Nall
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Peptidyl Prolyl Isomerase Inhibitors

2011
Publisher Summary This chapter presents the biochemistry of the peptidyl prolyl isomerases (PPIs) with an emphasis on their overall biological relevance, mechanism, and possible therapeutic utility. PPIs such as cis–trans PPIs catalyze the conversion of nascent protein strands containing cis -proline residues to the more stable transproline ...
Patrick T. Flaherty, Prashi Jain
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Targeting carcinogenesis: A role for the prolyl isomerase Pin1?

Molecular Carcinogenesis, 2006
AbstractPhosphorylation of proteins on serine or threonine residues that immediately precede proline (pSer/Thr‐Pro) is a central signaling mechanism in cell proliferation and transformation. Recent studies indicate that certain pSer/Thr‐Pro motifs in native proteins exist in two completely distinct conformations, cis and trans, whose conversion is ...
Kun Ping, Lu, Futoshi, Suizu, Xiao Zhen, Zhou, Greg, Finn, Prudence, Lam, Gerburg, Wulf   +5 more
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A miniaturized peptidyl-prolyl isomerase enzyme assay

Analytical Biochemistry, 2017
Prolyl-peptidyl isomerases (PPIases) are enzymes that are found in all living organisms. They form an essential part of the cellular protein folding homeostasis machinery. PPIases are associated with many important human diseases, e.g. cardiovascular disease, cancer and Alzheimer's.
Mirella Vivoli, Julien Renou, Arnaud Chevalier, Isobel H. Norville, Suraya Diaz, Christina Juli, Helen Atkins, Ulrike Holzgrabe, Pierre-Yves Renard, Mitali Sarkar-Tyson, Nicholas J. Harmer   +10 more
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Crosstalk of Prolyl Isomerases, Pin1/Ess1, and Cyclophilin A

Biochemical and Biophysical Research Communications, 2001
Previous studies have indicated that Ess1/Pin1, a gene in the parvulin family of peptidyl-prolyl isomerases (PPIases), plays an important role in regulating the G(2)/M transition of the cell cycle by binding cell-cycle-regulating proteins in eukaryotic cells.
F, Fujimori, W, Gunji, J, Kikuchi, T, Mogi, Y, Ohashi, T, Makino, A, Oyama, K, Okuhara, T, Uchida, Y, Murakami   +9 more
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Archaeal peptidyl prolyl cis-trans isomerases (PPIases)

Frontiers in Bioscience, 2000
PPIases are ubiquitous in living organisms. While 3 families of PPIases, cyclophilin (CyP), FK506 binding protein (FKBP) and parvulin (Pvn), have been studied in detail in Eukarya and Bacteria (eubacteria), little is known about archaeal PPIases. Among 2 cyclophilins found in Archaea, only Halobacterium cyclophilin (HcCyP19) has been characterized.
T, Maruyama, M, Furutani
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Multidomain Peptidyl Prolyl cis/trans Isomerases

Biochimica et Biophysica Acta (BBA) - General Subjects, 2015
Peptidyl prolyl cis/trans isomerases (PPIases) assist the folding and restructuring of client proteins by catalysis of the slow rotational motion of peptide bonds preceding a proline residue. Catalysis is performed by relatively small, distinct protein domains of 10 to 18kDa for all PPIase families.
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