Evidence map›Paper›PMID 36462455›Full record

ReviewCurrent opinion in chemical biology2023

Small-angle X-ray scattering studies of enzymes.

Amanda S Byer, Xiaokun Pei, Michael G Patterson, Nozomi Ando

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2023. 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
–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

15 citing papers in PubMed.

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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

4 authors.

Amanda S ByerDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Xiaokun PeiDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Michael G PattersonDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Nozomi AndoDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA. Electronic address: nozomi.ando@cornell.edu.

Funding

Protein Allostery and Catalysis Beyond Bragg DiffractionR35GM124847 · NIGMS · PRINCETON UNIVERSITY · PI Nozomi Ando · 2017 to 2026
$4.1M
Structural Studies of Alternating-site Reactivity in Nitrogenase-like OxidoreductasesF32GM140763 · NIGMS · CORNELL UNIVERSITY · PI BYER, AMANDA · 2021 to 2023
$210k
NIGMS NIH HHS F32 GM140763NIGMS NIH HHS R35 GM124847
6 · The paper itself

Abstract

Enzyme function requires conformational changes to achieve substrate binding, domain rearrangements, and interactions with partner proteins, but these movements are difficult to observe. Small-angle X-ray scattering (SAXS) is a versatile structural technique that can probe such conformational changes under solution conditions that are physiologically relevant. Although it is generally considered a low-resolution structural technique, when used to study conformational changes as a function of time, ligand binding, or protein interactions, SAXS can provide rich insight into enzyme behavior, including subtle domain movements. In this perspective, we highlight recent uses of SAXS to probe structural enzyme changes upon ligand and partner-protein binding and discuss tools for signal deconvolution of complex protein solutions.

Indexed as

ProteinsLigandsScattering, Small AngleX-Ray DiffractionX-RaysLigandsProteinsallosterydomain-domain interactionsEFAenzyme conformationsenzyme flexibilityoligomerizationprotein complexationprotein-protein interactionsREGALSSAXSSEC-SAXSsmall-angle X-ray scattering

Identifiers

PMID36462455
PMCPMC9992928

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.