Evidence map›Paper›PMID 26083915›Full record

ArticleBiophysical journal2015

Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions.

Jingjing Guo, Huan-Xiang Zhou

Abstract readLetter
In one paragraph

Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

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  4. Calculation of centralities in protein kinase A.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

2 authors.

Jingjing GuoDepartment of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida; School of Pharmacy, State Key Laboratory of Applied Organic Chemistry and Department of Chemistry, Lanzhou University, Lanzhou, China.
Huan-Xiang ZhouDepartment of Physics and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida. Electronic address: hzhou4@fsu.edu.

Funding

THEORY OF PROTEIN/PROTEIN ASSOCIATIONR01GM058187 · NIGMS · FLORIDA STATE UNIVERSITY · PI ZHOU, HUAN-XIANG · 1998 to 2016
$3.7M
NIGMS NIH HHS GM058187NIGMS NIH HHS R01 GM058187
6 · The paper itself

Abstract

There is considerable interest in the dynamic aspect of allosteric action, and in a growing list of proteins allostery has been characterized as being mediated predominantly by a change in dynamics, not a transition in conformation. For considering conformational dynamics, a protein molecule can be simplified into a number of relatively rigid microdomains connected by joints, corresponding to, e.g., communities and edges from a community network analysis. Binding of an allosteric activator strengthens intermicrodomain coupling, thereby quenching fast (e.g., picosecond to nanosecond) local motions but initiating slow (e.g., microsecond to millisecond), cross-microdomain correlated motions that are potentially of functional importance. This scenario explains allosteric effects observed in many unrelated proteins.

Indexed as

Allosteric SiteMolecular Dynamics SimulationAllosteric RegulationAmino Acid SequenceCatalytic DomainMolecular Sequence DataNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomeraseNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl Isomerase

Identifiers

PMID26083915
PMCPMC4472062

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.