ArticleStructure (London, England : 1993)2015
Negative Regulation of Peptidyl-Prolyl Isomerase Activity by Interdomain Contact in Human Pin1.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- Mapping Phosphorylation-Specific Pin1-CRMP2 Interactions Using an Integrated Mass Spectrometry Approach.ACS chemical biology · 2026Article
- A tethering mechanism underlies Pin1-catalyzed prolineProceedings of the National Academy of Sciences of the United States of America · 2025Article
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- Article
- Regulation of eukaryotic protein kinases by Pin1, a peptidyl-prolyl isomerase.Advances in biological regulation · 2023Article
- Ligand-specific conformational change drives interdomain allostery in Pin1.Nature communications · 2022Article
- Structure analysis suggests Ess1 isomerizes the carboxy-terminal domain of RNA polymerase II via a bivalent anchoring mechanism.Communications biology · 2021Article
- Coupled intra- and interdomain dynamics support domain cross-talk in Pin1.The Journal of biological chemistry · 2020Article
- Activity and Affinity of Pin1 Variants.Molecules (Basel, Switzerland) · 2019Review
- Molecular Mechanism of the Pin1-Histone H1 Interaction.Biochemistry · 2019Article
- Mutational effects of Cys113 on structural dynamics of Pin1.Biophysics and physicobiology · 2019Article
- Enhanced Sampling of Interdomain Motion Using Map-Restrained Langevin Dynamics and NMR: Application to Pin1.Journal of molecular biology · 2018Article
- Hinge-Shift Mechanism Modulates Allosteric Regulations in Human Pin1.The journal of physical chemistry. B · 2018Article
- The Exact Nuclear Overhauser Enhancement: Recent Advances.Molecules (Basel, Switzerland) · 2017Review
- Fine-tuning the extent and dynamics of binding cleft opening as a potential general regulatory mechanism in parvulin-type peptidyl prolyl isomerases.Scientific reports · 2017Article
- Neighboring phosphoSer-Pro motifs in the undefined domain of IRAK1 impart bivalent advantage for Pin1 binding.The FEBS journal · 2016Article
- Intrinsic protein disorder could be overlooked in cocrystallization conditions: An SRCD case study.Protein science : a publication of the Protein Society · 2016Article
- Kinetic Insights into the Binding between the nSH3 Domain of CrkII and Proline-Rich Motifs in cAbl.Biophysical journal · 2016Article
- Protein Allostery and Conformational Dynamics.Chemical reviews · 2016Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Pin1 is a modular peptidyl-prolyl isomerase specific for phosphorylated Ser/Thr-Pro (pS/T-P) motifs, typically within intrinsically disordered regions of signaling proteins. Pin1 consists of two flexibly linked domains: an N-terminal WW domain for substrate binding and a larger C-terminal peptidyl-prolyl isomerase (PPIase) domain. Previous studies showed that binding of phosphopeptide substrates to Pin1 could alter Pin1 interdomain contact, strengthening or weakening it depending on the substrate sequence. Thus, substrate-induced changes in interdomain contact may act as a trigger within the Pin1 mechanism. Here, we investigate this possibility via nuclear magnetic resonance studies of several Pin1 mutants. Our findings provide new mechanistic insights for those substrates that reduce interdomain contact. Specifically, the reduced interdomain contact can allosterically enhance PPIase activity relative to that when the contact is sustained. These findings suggest Pin1 interdomain contact can negatively regulate its activity.
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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.