Evidence map›Paper›PMID 35872562›Full record

ReviewCurrent opinion in structural biology2022

Functional roles of enzyme dynamics in accelerating active site chemistry: Emerging techniques and changing concepts.

Shuaihua Gao, Judith P Klinman

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

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  15. Enzyme dynamics-a brief review.Biophysical reviews · 2023
    Article
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  18. Review
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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.

Shuaihua GaoDepartment of Chemistry, University of California, Berkeley, CA, 94720, United States; California Institute for Quantitative Biosciences, University of California, Berkeley, CA, 94720, United States. Electronic address: https://twitter.com/S_H_Gao.
Judith P KlinmanDepartment of Chemistry, University of California, Berkeley, CA, 94720, United States; California Institute for Quantitative Biosciences, University of California, Berkeley, CA, 94720, United States; Department of Molecular and Cell Biology, University of California, Berkeley, CA, 94720, United States. Electronic address: klinman@berkeley.edu.

Funding

Looking in New Directions for Origins and Cryptic Mechanisms of Enzyme CatalysisR35GM118117 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 2016 to 2025
$7.5M
NIGMS NIH HHS R35 GM118117
6 · The paper itself

Abstract

With the growing acceptance of the contribution of protein conformational ensembles to enzyme catalysis and regulation, research in the field of protein dynamics has shifted toward an understanding of the atomistic properties of protein dynamical networks and the mechanisms and time scales that control such behavior. A full description of an enzymatic reaction coordinate is expected to extend beyond the active site and include site-specific networks that communicate with the protein/water interface. Advances in experimental tools for the spatial resolution of thermal activation pathways are being complemented by biophysical methods for visualizing dynamics in real time. An emerging multidimensional model integrates the impacts of bound substrate/effector on the distribution of protein substates that are in rapid equilibration near room temperature with reaction-specific protein embedded heat transfer conduits.

Indexed as

ProteinsBiophysicsCatalysisCatalytic DomainProtein ConformationProteins

Identifiers

PMID35872562
PMCPMC9901422

What OpenQuestion holds

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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.