Evidence map›Paper›PMID 25271401›Full record

ArticleBiochemistry2014

Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: insights for cGMP-dependent protein kinase agonist design.

Gilbert Y Huang, Oksana O Gerlits, Matthew P Blakeley, Banumathi Sankaran, Andrey Y Kovalevsky, Choel Kim

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Structures of the cGMP-dependent protein kinase in malaria parasites reveal a unique structural relay mechanism for activation.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  6. Article
  7. Article
  8. Large-scale crystallization and neutron crystallographic analysis of HSP70 in complex with ADP.Acta crystallographica. Section F, Structural biology communications · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Mechanism of cAMP Partial Agonism in Protein Kinase G (PKG).The Journal of biological chemistry · 2015
    Article
  16. Review
  17. 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 4 institutions in 2 countries.

Gilbert Y HuangVerna and Mars McClean Department of Biochemistry and Molecular Biology, Baylor College of Medicine , One Baylor Plaza, Houston, Texas 77004, United States.
Oksana O Gerlits
Matthew P Blakeley
Banumathi Sankaran
Andrey Y Kovalevsky
Choel Kim
Baylor College of Medicine · USOak Ridge National Laboratory · USInstitut Laue-Langevin · FRLawrence Berkeley National Laboratory · US

Funding

HOUSTON AREA MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008280 · NIGMS · RICE UNIVERSITY · PI WENSEL, THEODORE G · 1988 to 2023
$8.0M
Targeting mechanisms of cGMP dependent protein kinases by peptide arrays and crysR01GM090161 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI KIM, CHOEL WOONG · 2010 to 2018
$2.9M
NIGMS NIH HHS R01 GM090161NIGMS NIH HHS R01GM090161NIGMS NIH HHS T32 GM008280NIGMS NIH HHS T32GM008280
6 · The paper itself

Abstract

High selectivity of cyclic-nucleotide binding (CNB) domains for cAMP and cGMP are required for segregating signaling pathways; however, the mechanism of selectivity remains unclear. To investigate the mechanism of high selectivity in cGMP-dependent protein kinase (PKG), we determined a room-temperature joint X-ray/neutron (XN) structure of PKG Iβ CNB-B, a domain 200-fold selective for cGMP over cAMP, bound to cGMP (2.2 Å), and a low-temperature X-ray structure of CNB-B with cAMP (1.3 Å). The XN structure directly describes the hydrogen bonding interactions that modulate high selectivity for cGMP, while the structure with cAMP reveals that all these contacts are disrupted, explaining its low affinity for cAMP.

Indexed as

NeutronsScattering, RadiationAnimalsCyclic AMPCyclic GMPCyclic GMP-Dependent Protein Kinase Type IDrug DesignEnzyme ActivationEnzyme ActivatorsHumansHydrogen BondingCyclic AMPCyclic GMPCyclic GMP-Dependent Protein Kinase Type IEnzyme ActivatorsPRKG1 protein, human

Identifiers

PMID25271401
PMCPMC4222537
OpenAlexW2317265306

What OpenQuestion holds

Textmetadata
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.