Evidence map›Paper›PMID 38386706›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2024

Perturbative diffraction methods resolve a conformational switch that facilitates a two-step enzymatic mechanism.

Jack B Greisman, Kevin M Dalton, Dennis E Brookner, Margaret A Klureza, Candice J Sheehan, In-Sik Kim, Robert W Henning, Silvia Russi, Doeke R Hekstra

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

15 citing papers in PubMed, 16 citations in OpenAlex.

  1. Chaperonin recognition of protein dynamics drives drug resistance.bioRxiv : the preprint server for biology · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Jack B GreismanDepartment of Molecular & Cellular Biology, Harvard University, Cambridge, MA 02138.ORCID 0000-0002-6394-2658
Kevin M DaltonDepartment of Molecular & Cellular Biology, Harvard University, Cambridge, MA 02138.ORCID 0000-0001-9396-085X
Dennis E BrooknerDepartment of Molecular & Cellular Biology, Harvard University, Cambridge, MA 02138.ORCID 0000-0003-2827-4743
Margaret A KlurezaDepartment of Chemistry & Chemical Biology, Harvard University, Cambridge, MA 02138.ORCID 0000-0001-5774-1297
Candice J SheehanDepartment of Molecular & Cellular Biology, Harvard University, Cambridge, MA 02138.
In-Sik KimBioCARS, Argonne National Laboratory, The University of Chicago, Lemont, IL 60439.
Robert W HenningBioCARS, Argonne National Laboratory, The University of Chicago, Lemont, IL 60439.ORCID 0000-0003-4404-0189
Silvia RussiStanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA 94025.ORCID 0000-0002-9666-1465
Doeke R HekstraDepartment of Molecular & Cellular Biology, Harvard University, Cambridge, MA 02138.ORCID 0000-0003-2332-9223
Harvard University · USArgonne National Laboratory · USSLAC National Accelerator Laboratory · US

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Electric Field-stimulated Protein MechanicsP41GM118217 · NIGMS · UNIVERSITY OF CHICAGO · PI RANGANATHAN, RAMA · 2019 to 2021
$5.3M
Identifying Principles of Protein Mechanics by Applying Force and Observing MotionDP2GM141000 · NIGMS · HARVARD UNIVERSITY · PI HEKSTRA, DOEKE ROMKE · 2020 to 2020
$2.4M
NIGMS NIH HHS DP2 GM141000NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41 GM118217
6 · The paper itself

Abstract

Enzymes catalyze biochemical reactions through precise positioning of substrates, cofactors, and amino acids to modulate the transition-state free energy. However, the role of conformational dynamics remains poorly understood due to poor experimental access. This shortcoming is evident with

Indexed as

Amino AcidsElectricityCatalysisEscherichia coliMolecular ConformationTetrahydrofolate DehydrogenaseAmino AcidsTetrahydrofolate DehydrogenaseallosteryDHFRenzyme catalysisprotein dynamicsX-ray crystallography

Identifiers

PMID38386706
PMCPMC10907320
OpenAlexW4392028361

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.