Evidence map›Paper›PMID 20826336›Full record

ArticleStructure (London, England : 1993)2010

Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators.

Joseph A Marsh, Barbara Dancheck, Michael J Ragusa, Marc Allaire, Julie D Forman-Kay, Wolfgang Peti

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
7.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

64 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Systematic identification of conditionally folded intrinsically disordered regions by AlphaFold2.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Intrinsic protein disorder uncouples affinity from binding specificity.Protein science : a publication of the Protein Society · 2022
    Article
  12. Article
  13. Lighting up Nobel Prize-winning studies with protein intrinsic disorder.Cellular and molecular life sciences : CMLS · 2022
    Review
  14. Article
  15. Article
  16. 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 · 2021
    Article
  17. Article
  18. Article
  19. The journal of physical chemistry. B · 2019
    Article
  20. Article

4 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 2 countries.

Joseph A MarshMolecular Structure & Function, Hospital for Sick Children, Toronto, ON M5G 1X8, Canada.
Barbara Dancheck
Michael J Ragusa
Marc Allaire
Julie D Forman-Kay
Wolfgang Peti
Brown University · USBrookhaven National Laboratory · USHospital for Sick Children · CAUniversity of Toronto · CA

Funding

TRAINING IN MOLECULAR &CELL BIOLOGY &BIOCHEMISTRYT32GM007601 · NIGMS · BROWN UNIVERSITY · PI MOWRY, KIMBERLY L. · 1985 to 2019
$6.4M
An 800 MHz NMR spectrometer for the Boston areaS10RR017269 · NCRR · BRANDEIS UNIVERSITY · PI POCHAPSKY, THOMAS CHARLES · 2003 to 2003
$2.0M
Structural and Functional Analysis of Signaling Proteins in Dendritic SpinesR01NS056128 · NINDS · BROWN UNIVERSITY · PI PETI, WOLFGANG · 2007 to 2011
$1.7M
CIHRNCRR NIH HHS S10 RR017269NIGMS NIH HHS T32 GM007601NINDS NIH HHS R01 NS056128NINDS NIH HHS R01NS056128
6 · The paper itself

Abstract

Complete folding is not a prerequisite for protein function, as disordered and partially folded states of proteins frequently perform essential biological functions. In order to understand their functions at the molecular level, we utilized diverse experimental measurements to calculate ensemble models of three nonhomologous, intrinsically disordered proteins: I-2, spinophilin, and DARPP-32, which bind to and regulate protein phosphatase 1 (PP1). The models demonstrate that these proteins have dissimilar propensities for secondary and tertiary structure in their unbound forms. Direct comparison of these ensemble models with recently determined PP1 complex structures suggests a significant role for transient, preformed structure in the interactions of these proteins with PP1. Finally, we generated an ensemble model of partially disordered I-2 bound to PP1 that provides insight into the relationship between flexibility and biological function in this dynamic complex.

Indexed as

Dopamine and cAMP-Regulated Phosphoprotein 32Microfilament ProteinsModels, MolecularNerve Tissue ProteinsNeurabinsProtein ConformationProtein FoldingProtein Phosphatase 1Protein Phosphatase Inhibitory ProteinsProteinsStructure-Activity RelationshipDopamine and cAMP-Regulated Phosphoprotein 32Microfilament ProteinsNerve Tissue ProteinsNeurabinsProtein Phosphatase 1protein phosphatase inhibitor-2Protein Phosphatase Inhibitory ProteinsProteins

Identifiers

PMID20826336
PMCPMC2936704
OpenAlexW2070958052

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.