ReviewBiochemical Society transactions2012
Regulation of protein phosphatase 1 by intrinsically disordered proteins.
Review in Biochemical Society transactions, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 55 citations in OpenAlex.
- Coronavirus genome packaging and nucleocapsid assembly.Journal of virology · 2026Review
- All-Trans Retinoic Acid Impacts Early Palatal Shelves Development via the Wnt and TGF-β Signaling Pathways.Biomedicines · 2025Article
- From Crypts to Cancer: A Holistic Perspective on Colorectal Carcinogenesis and Therapeutic Strategies.International journal of molecular sciences · 2024Review
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- PHI-1, an Endogenous Inhibitor Protein for Protein Phosphatase-1 and a Pan-Cancer Marker, Regulates Raf-1 Proteostasis.Biomolecules · 2023Article
- Leishmania PNUTS discriminates between PP1 catalytic subunits through an RVxF-ΦΦ-F motif and polymorphisms in the PP1 C-tail and catalytic domain.The Journal of biological chemistry · 2023Article
- Phosphomimetics at Ser199/Ser202/Thr205 in Tau Impairs Axonal Transport in Rat Hippocampal Neurons.Molecular neurobiology · 2023Article
- PPP1R14B is a diagnostic prognostic marker in patients with uterine corpus endometrial carcinoma.Journal of cellular and molecular medicine · 2023Article
- Article
- The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs.Cell reports · 2022Article
- Comparison of rule- and ordinary differential equation-based dynamic model of DARPP-32 signalling network.PeerJ · 2022Article
- Frontotemporal Lobar Dementia Mutant Tau Impairs Axonal Transport through a Protein Phosphatase 1γ-Dependent Mechanism.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Dynamics in Fip1 regulate eukaryotic mRNA 3' end processing.Genes & development · 2021Article
- Evolutionary crossroads of cell signaling: PP1 and PP2A substrate sites in intrinsically disordered regions.Biochemical Society transactions · 2021Review
- PPP1R14B Is a Prognostic and Immunological Biomarker in Pan-Cancer.Frontiers in genetics · 2021Article
- Prevention of mitochondrial impairment by inhibition of protein phosphatase 1 activity in amyotrophic lateral sclerosis.Cell death & disease · 2020Article
- Protein Phosphatase PP1 Negatively Regulates IRF3 in Response to GCRV Infection in Grass Carp (Frontiers in immunology · 2020Article
- SDS22 selectively recognizes and traps metal-deficient inactive PP1.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis.Structure (London, England : 1993) · 2019Article
- NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins.Journal of biomolecular NMR · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
PP1 (protein phosphatase 1) is an essential serine/threonine phosphatase that plays a critical role in a broad range of biological processes, from muscle contraction to memory formation. PP1 achieves its biological specificity by forming holoenzymes with more than 200 known regulatory proteins. Interestingly, most of these regulatory proteins (≥ 70%) belong to the class of IDPs (intrinsically disordered proteins). Thus structural studies highlighting the interaction of these IDP regulatory proteins with PP1 are an attractive model system because it allows general parameters for a group of diverse IDPs that interact with the same binding partner to be identified, while also providing fundamental insights into PP1 biology. The present review provides a brief overview of our current understanding of IDP-PP1 interactions, including the importance of pre-formed secondary and tertiary structures for PP1 binding, as well as changes of IDP dynamics upon interacting with PP1.
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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.