Evidence map›Paper›PMID 34667558›Full record

ArticleChemical science2021

State-selective frustration as a key driver of allosteric pluripotency.

Jung Ah Byun, Bryan VanSchouwen, Nishi Parikh, Madoka Akimoto, Eric Tyler McNicholl, Giuseppe Melacini

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. 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 1 institution in 1 country.

Jung Ah ByunDepartment of Biochemistry and Biomedical Sciences, McMaster University Hamilton ON L8S 4M1 Canada melacin@mcmaster.ca.ORCID https://orcid.org/0000-0001-7814-7326
Bryan VanSchouwenDepartment of Chemistry and Chemical Biology, McMaster University Hamilton ON L8S 4M1 Canada.
Nishi ParikhDepartment of Chemistry and Chemical Biology, McMaster University Hamilton ON L8S 4M1 Canada.
Madoka AkimotoDepartment of Chemistry and Chemical Biology, McMaster University Hamilton ON L8S 4M1 Canada.
Eric Tyler McNichollDepartment of Chemistry and Chemical Biology, McMaster University Hamilton ON L8S 4M1 Canada.
Giuseppe MelaciniDepartment of Biochemistry and Biomedical Sciences, McMaster University Hamilton ON L8S 4M1 Canada melacin@mcmaster.ca.ORCID https://orcid.org/0000-0003-1164-2853
McMaster University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Allosteric pluripotency arises when an allosteric effector switches from agonist to antagonist depending on the experimental conditions. For example, the Rp-cAMPS ligand of Protein Kinase A (PKA) switches from agonist to antagonist as the MgATP concentration increases and/or the kinase substrate affinity or concentration decreases. Understanding allosteric pluripotency is essential to design effective allosteric therapeutics with minimal side effects. Allosteric pluripotency of PKA arises from divergent allosteric responses of two homologous tandem cAMP-binding domains, resulting in a free energy landscape for the Rp-cAMPS-bound PKA regulatory subunit R1a in which the ground state is kinase inhibition-incompetent and the kinase inhibition-competent state is excited. The magnitude of the free energy difference between the ground non-inhibitory and excited inhibitory states (Δ

Identifiers

PMID34667558
PMCPMC8447923
OpenAlexW3179310865

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.