Evidence map›Paper›PMID 30906862›Full record

ArticleScience advances2019

Zooming in on protons: Neutron structure of protein kinase A trapped in a product complex.

Oksana Gerlits, Kevin L Weiss, Matthew P Blakeley, Gianluigi Veglia, Susan S Taylor, Andrey Kovalevsky

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Protein Kinase Structure and Dynamics: Role of the αC-β4 Loop.bioRxiv : the preprint server for biology · 2023
    Article
  7. Article
  8. Article
  9. Review
  10. Molecular-dynamics simulation methods for macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2023
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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 5 institutions in 2 countries.

Oksana GerlitsBredesen Center, University of Tennessee, Knoxville, TN 37996, USA.ORCID 0000-0002-0836-826X
Kevin L WeissNeutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.ORCID 0000-0002-6486-8007
Matthew P BlakeleyLarge Scale Structures Group, Institut Laue-Langevin, Grenoble Cedex 9, 38042, France.ORCID 0000-0002-6412-4358
Gianluigi VegliaDepartment of Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.
Susan S TaylorDepartment of Pharmacology, University of California at San Diego, La Jolla, CA 92093, USA.ORCID 0000-0002-7702-6108
Andrey KovalevskyNeutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.ORCID 0000-0003-4459-9142
Oak Ridge National Laboratory · USInstitut Laue-Langevin · FRUniversity of California San Diego · USUniversity of Minnesota · USUniversity of Tennessee at Knoxville · US

Funding

Lessons Learned from PKA: Assembly of Dynamic Macromolecular SwitchesR35GM130389 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI SUSAN S. TAYLOR · 2019 to 2026
$5.7M
Mapping Allosteric Cooperativity in Protein KinasesR01GM100310 · NIGMS · UNIVERSITY OF MINNESOTA · PI VEGLIA, GIANLUIGI · 2012 to 2019
$4.3M
Protein Kinase: Primary Structure and cAMP InteractionsR01GM019301 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI TAYLOR, SUSAN S. · 1985 to 2013
$3.4M
PROTEIN KINASE: PRIMARY STRUCTURE AND CAMP INTERACTIONR37GM019301 · NIGMS · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI TAYLOR, SUSAN S · 1995 to 2004
$2.0M
NIGMS NIH HHS R01 GM019301NIGMS NIH HHS R01 GM100310NIGMS NIH HHS R35 GM130389NIGMS NIH HHS R37 GM019301
6 · The paper itself

Abstract

The question vis-à-vis the chemistry of phosphoryl group transfer catalyzed by protein kinases remains a major challenge. The neutron diffraction structure of the catalytic subunit of cAMP-dependent protein kinase (PKA-C) provides a more complete chemical portrait of key proton interactions at the active site. By using a high-affinity protein kinase substrate (PKS) peptide, we captured the reaction products, dephosphorylated nucleotide [adenosine diphosphate (ADP)] and phosphorylated PKS (pPKS), bound at the active site. In the complex, the phosphoryl group of the peptide is protonated, whereas the carboxyl group of the catalytic Asp

Indexed as

NeutronsAdenosine DiphosphateAmidesAmino Acid SequenceAnimalsBinding SitesCatalysisCatalytic DomainCrystallography, X-RayCyclic AMP-Dependent Protein KinasesMagnetic Resonance SpectroscopyMiceModels, MolecularNucleotidesPeptidesPhosphorylationAdenosine DiphosphateAmidesCyclic AMP-Dependent Protein KinasesNucleotidesPeptidesProtein Kinase CProtonsWater

Identifiers

PMID30906862
PMCPMC6426457
OpenAlexW2924353062

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.