Results 181 to 190 of about 18,044 (216)
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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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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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The prolyl isomerase Pin1 is a regulator of p53 in genotoxic response
Nature, 2002p53 is activated in response to various genotoxic stresses resulting in cell cycle arrest or apoptosis. It is well documented that DNA damage leads to phosphorylation and activation of p53 (refs 1-3), yet how p53 is activated is still not fully understood.
Hongwu, Zheng +9 more
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A human peptidyl–prolyl isomerase essential for regulation of mitosis
Nature, 1996The NIMA kinase is essential for progression through mitosis in Aspergillus nidulans, and there is evidence for a similar pathway in other eukaryotic cells. Here we describe the human protein Pin1, a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA.
K P, Lu, S D, Hanes, T, Hunter
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Interaction of p53 with prolyl isomerases: Healthy and unhealthy relationships
Biochimica et Biophysica Acta (BBA) - General Subjects, 2015The p53 protein family, comprising p53, p63 and p73, is primarily involved in preserving genome integrity and preventing tumor onset, and also affects a range of physiological processes. Signal-dependent modifications of its members and of other pathway components provide cells with a sophisticated code to transduce a variety of stress signaling into ...
Mantovani, Fiamma +3 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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A new family of peptidyl-prolyl isomerases
Trends in Biochemical Sciences, 1995K E, Rudd +5 more
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The mitotic peptidyl-prolyl isomerase, Pin1, interacts with Cdc25 and Plx1
EMBO Journal, 1998A R Means +2 more
exaly
Prolyl‐isomerase Pin1 controls normal and cancer stem cells of the breast
EMBO Molecular Medicine, 2014Alessandra Rustighi +2 more
exaly