ReviewEMBO reports2007
Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail?
Review in EMBO reports, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 68 citations in OpenAlex.
- Domain acquisition enabled functional expansion of the TFIIS transcription factor family.Cell & bioscience · 2025Review
- Inhibition of the prolyl isomerase Pin1 improves endothelial function and attenuates vascular remodelling in pulmonary hypertension by inhibiting TGF-β signalling.Angiogenesis · 2022Article
- Pinning Down the Transcription: A Role for Peptidyl-ProlylFrontiers in cell and developmental biology · 2020Review
- Novel polysaccharide binding to the N-terminal tail of galectin-3 is likely modulated by proline isomerization.Glycobiology · 2017Article
- Neighboring phosphoSer-Pro motifs in the undefined domain of IRAK1 impart bivalent advantage for Pin1 binding.The FEBS journal · 2016Article
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- Molecular dynamics of the proline switch and its role in Crk signaling.The journal of physical chemistry. B · 2014Article
- Cross-talk of phosphorylation and prolyl isomerization of the C-terminal domain of RNA Polymerase II.Molecules (Basel, Switzerland) · 2014Review
- The cellular peptidyl-prolyl cis/trans isomerase Pin1 regulates reactivation of Kaposi's sarcoma-associated herpesvirus from latency.Journal of virology · 2014Article
- The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.Biochimica et biophysica acta · 2014Review
- ERK phosphorylation of MED14 in promoter complexes during mitogen-induced gene activation by Elk-1.Nucleic acids research · 2013Article
- The peptidyl-prolyl isomerase Pin1 up-regulation and proapoptotic function in dopaminergic neurons: relevance to the pathogenesis of Parkinson disease.The Journal of biological chemistry · 2013Article
- Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5, and Ser7 within the carboxyl-terminal domain repeat.The Journal of biological chemistry · 2013Article
- Sequence characterization, in silico mapping and cytosine methylation analysis of markers linked to apospory in Paspalum notatum.Genetics and molecular biology · 2012Article
- The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination.Molecular and cellular biology · 2012Article
- Prolyl isomerase Pin1 regulates neuronal differentiation via β-catenin.Molecular and cellular biology · 2012Article
- Ser-634 and Ser-636 of Kaposi's Sarcoma-Associated Herpesvirus RTA are Involved in Transactivation and are Potential Cdk9 Phosphorylation Sites.Frontiers in microbiology · 2012Article
- cis-Proline-mediated Ser(P)5 dephosphorylation by the RNA polymerase II C-terminal domain phosphatase Ssu72.The Journal of biological chemistry · 2011Article
- Systematic identification of novel, essential host genes affecting bromovirus RNA replication.PloS one · 2011Article
- Phosphorylation stabilizes Nanog by promoting its interaction with Pin1.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Eukaryotic transcription is regulated predominantly by the post-translational modification of the participating components. One such modification is the cis-trans isomerization of peptidyl-prolyl bonds, which results in a conformational change in the protein involved. Enzymes that carry out this reaction include the yeast peptidyl-prolyl cis/trans isomerase Ess1 and its human counterpart Pin1, both of which recognize phosphorylated target motifs exclusively. Consequently, they operate together with proline-directed serine-threonine kinases and phosphatases. High-profile client proteins involved in transcription include steroid hormone receptors, cell-cycle regulators and immune mediators. Other key targets are elements of the transcription machinery, including the multiply phosphorylated carboxy-terminal domain of RNA polymerase II. Changes in isomerase activity have been shown to alter the transactivation potential, protein stability or intracellular localization of these client proteins. The resulting disruption to developmental processes and cell proliferation has been linked, in some cases, to human cancers.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.