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Peptidyl Prolyl Isomerase Inhibitors
2011Publisher 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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Catalysis of protein folding by prolyl isomerase
Nature, 1987Rates 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
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A miniaturized peptidyl-prolyl isomerase enzyme assay
Analytical Biochemistry, 2017Prolyl-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 +10 more
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Multidomain Peptidyl Prolyl cis/trans Isomerases
Biochimica et Biophysica Acta (BBA) - General Subjects, 2015Peptidyl 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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Prolyl cis/trans isomerase signalling pathways in cancer
Current Opinion in Pharmacology, 2011It is an emerging view that in many cases cell signalling relies on slow conformational interconversions of the backbone of key proteins as exemplified by the prolyl cis/trans isomerization, and that prolyl cis/trans isomerases (PPIases), such as cyclophilins, FK506-binding proteins and the parvulin-like Pin1, serve to integrate temporally and ...
Martin, Theuerkorn +2 more
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The peptidyl-prolyl isomerase Pin1.
Progress in cell cycle research, 2003The phospho-Ser/Thr-Pro specific prolyl-isomerase Pin1 has been implicated in multiple aspects of cell cycle regulation. It has been suggested that Pin1 function is required for both normal mitotic progression and reentry into the cell cycle from quiescence.
James D, Joseph +4 more
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Prolyl isomerases do not catalyze isomerization of non-prolyl peptide bonds.
Biological chemistry, 1998Prolyl isomerases accelerate the cis trans isomerization of prolyl peptide bonds during protein folding and probably also in folded proteins. We asked whether this catalytic function is in fact restricted to prolyl bonds or whether the isomerizations of 'normal' non-prolyl peptide bonds are catalyzed as well.
C, Scholz +5 more
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Periplasmic Chaperones and Peptidyl-Prolyl Isomerases
2014The cellular functions of molecular chaperones include protecting newly synthesized polypeptides from misfolding or aggregation, and promoting disaggregation and refolding of stress-denaturated proteins. It was debated whether periplasmic chaperones might exist that could associate with newly exported polypeptides emerging at the translocation sites to
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Integrative oncology: Addressing the global challenges of cancer prevention and treatment
Ca-A Cancer Journal for Clinicians, 2022Jun J Mao,, Msce +2 more
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