Evidence map›Paper›PMID 33335680›Full record

ReviewComputational and structural biotechnology journal2020

Allosteric inhibition explained through conformational ensembles sampling distinct "mixed" states.

Jung Ah Byun, Bryan VanSchouwen, Madoka Akimoto, Giuseppe Melacini

Open access · goldAbstract readReview
In one paragraph

Review in Computational and structural biotechnology journal, 2020. 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
2.6field-weighted citation impact, top 9% 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, 45 citations in OpenAlex.

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  16. Allosteric regulation of autoinhibition and activation of c-Abl.Computational and structural biotechnology journal · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Atomic-scale insights into allosteric inhibition and evolutional rescue mechanism ofComputational and structural biotechnology journal · 2021
    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

4 authors at 1 institution in 1 country.

Jung Ah ByunDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
Bryan VanSchouwenDepartment of Chemistry and Chemical Biology, McMaster University, Hamilton, Ontario, Canada.
Madoka AkimotoDepartment of Chemistry and Chemical Biology, McMaster University, Hamilton, Ontario, Canada.
Giuseppe MelaciniDepartment of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, Ontario, Canada.
McMaster University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Allosteric modulation provides an effective avenue for selective and potent enzyme inhibition. Here, we summarize and critically discuss recent advances on the mechanisms of allosteric partial agonists for three representative signalling enzymes activated by cyclic nucleotides: the cAMP-dependent protein kinase (PKA), the cGMP-dependent protein kinase (PKG), and the exchange protein activated by cAMP (EPAC). The comparative analysis of partial agonism in PKA, PKG and EPAC reveals a common emerging theme,

Indexed as

AgonismAllosteric pluripotencyAllosteryAntagonismcAMPcGMPEPACPKAPKG

Identifiers

PMID33335680
PMCPMC7720024
OpenAlexW3101130800

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.