Evidence map›Paper›PMID 34932909›Full record

ReviewAnnual review of biophysics2022

Mapping Enzyme Landscapes by Time-Resolved Crystallography with Synchrotron and X-Ray Free Electron Laser Light.

Mark A Wilson

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of biophysics, 2022. 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, 42 citations in OpenAlex.

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  7. Structural Biology for Target Identification and Validation.Methods in molecular biology (Clifton, N.J.) · 2025
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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

1 author at 1 institution in 1 country.

Mark A WilsonDepartment of Biochemistry and Redox Biology Center, University of Nebraska, Lincoln, Nebraska, USA; email: mwilson13@unl.edu.
University of Nebraska–Lincoln · US

Funding

Time-Resolved X-ray Crystallography of Dynamics in Cysteine-Dependent EnzymesR01GM139978 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI WILSON, MARK A. · 2020 to 2023
$1.2M
NIGMS NIH HHS R01 GM139978
6 · The paper itself

Abstract

Directly observing enzyme catalysis in real time at the molecular level has been a long-standing goal of structural enzymology. Time-resolved serial crystallography methods at synchrotron and X-ray free electron laser (XFEL) sources have enabled researchers to follow enzyme catalysis and other nonequilibrium events at ambient conditions with unprecedented time resolution. X-ray crystallography provides detailed information about conformational heterogeneity and protein dynamics, which is enhanced when time-resolved approaches are used. This review outlines the ways in which information about the underlying energy landscape of a protein can be extracted from X-ray crystallographic data, with an emphasis on new developments in XFEL and synchrotron time-resolved crystallography. The emerging view of enzyme catalysis afforded by these techniques can be interpreted as enzymes moving on a time-dependent energy landscape. Some consequences of this view are discussed, including the proposal that irreversible enzymes or enzymes that use covalent catalytic mechanisms may commonly exhibit catalysis-activated motions.

Indexed as

ElectronsSynchrotronsCrystallography, X-RayLasersX-Raysconformational ensemblesfluctuation–dissipation relationnonequilibrium protein dynamicstime-resolved crystallographyXFELX-ray free electron laser

Identifiers

PMID34932909
PMCPMC9132212
OpenAlexW4200611562

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.