Evidence map›Paper›PMID 22057126›Full record

ArticleNature chemical biology2011

Structural basis of p38α regulation by hematopoietic tyrosine phosphatase.

Dana M Francis, Bartosz Różycki, Dorothy Koveal, Gerhard Hummer, Rebecca Page, Wolfgang Peti

Open access · hybridAbstract read
In one paragraph

Article in Nature chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

44 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Linear motif specificity in signaling through p38α and ERK2 mitogen-activated protein kinases.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  4. Review
  5. Article
  6. Mapping the deformability of natural and designed cellulosomes in solution.Biotechnology for biofuels and bioproducts · 2022
    Article
  7. Comprehensive analysis ofFrontiers in genetics · 2022
    Article
  8. The interaction of p38 with its upstream kinase MKK6.Protein science : a publication of the Protein Society · 2021
    Article
  9. The methylJournal of biomolecular NMR · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Efficient Ensemble Refinement by Reweighting.Journal of chemical theory and computation · 2019
    Article
  16. Article
  17. Review
  18. Dynamic activation and regulation of the mitogen-activated protein kinase p38.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Dana M FrancisDepartment of Molecular Pharmacology, Physiology and Biotechnology, Brown University, Providence, Rhode Island, USA.
Bartosz Różycki
Dorothy Koveal
Gerhard Hummer
Rebecca Page
Wolfgang Peti
Brown University · USNational Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

TRAINING IN MOLECULAR &CELL BIOLOGY &BIOCHEMISTRYT32GM007601 · NIGMS · BROWN UNIVERSITY · PI MOWRY, KIMBERLY L. · 1985 to 2019
$6.4M
STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
Theory and simulation of protein dynamics, folding, and functionZIADK029033 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI HUMMER, GERHARD · 2009 to 2013
$3.3M
An 800 MHz NMR spectrometer for the Boston areaS10RR017269 · NCRR · BRANDEIS UNIVERSITY · PI POCHAPSKY, THOMAS CHARLES · 2003 to 2003
$2.0M
Dynamics & energetics of p38a kinase regulation by ligandsR01GM100910 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI PETI, WOLFGANG, WAND, A. JOSHUA · 2013 to 2016
$1.3M
Intramural NIH HHSNCRR NIH HHS S10 RR017269NCRR NIH HHS S10-RR017269NIGMS NIH HHS R01 GM100910NIGMS NIH HHS T32 GM007601NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

MAP kinases regulate essential cellular events, including cell growth, differentiation and inflammation. The solution structure of a complete MAPK-MAPK-regulatory protein complex, p38α-HePTP, was determined, enabling a comprehensive investigation of the molecular basis of specificity and fidelity in MAPK regulation. Structure determination was achieved by combining NMR spectroscopy and small-angle X-ray scattering data with a new ensemble calculation-refinement procedure. We identified 25 residues outside of the HePTP kinase interaction motif necessary for p38α recognition. The complex adopts an extended conformation in solution and rarely samples the conformation necessary for kinase deactivation. Complex formation also does not affect the N-terminal lobe, the activation loop of p38α or the catalytic domain of HePTP. Together, these results show how the downstream tyrosine phosphatase HePTP regulates p38α and provide for fundamentally new insights into MAPK regulation and specificity.

Indexed as

Amino Acid SequenceMitogen-Activated Protein Kinase 14Models, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein Tyrosine Phosphatase, Non-Receptor Type 6Structure-Activity RelationshipSubstrate SpecificityMitogen-Activated Protein Kinase 14Protein Tyrosine Phosphatase, Non-Receptor Type 6

Identifiers

PMID22057126
PMCPMC3657131
OpenAlexW2080285527

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.