Evidence map›Paper›PMID 34175665›Full record

ReviewCurrent opinion in structural biology2021

Time-resolved X-ray scattering studies of proteins.

Hyun Sun Cho, Friedrich Schotte, Valentyn Stadnytskyi, Philip Anfinrud

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2021. 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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  16. Evolving Experimental Techniques for Structure-Based Drug Design.The journal of physical chemistry. B · 2022
    Review
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.

Hyun Sun ChoLaboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, MD, 20892-0520, USA.
Friedrich SchotteLaboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, MD, 20892-0520, USA.
Valentyn StadnytskyiLaboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, MD, 20892-0520, USA.
Philip AnfinrudLaboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, MD, 20892-0520, USA. Electronic address: anfinrud@nih.gov.

Funding

Ultrafast Biophysical Studies of Proteins: Time-resolved Laue crystallographyZIADK029058 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ANFINRUD, PHILIP · 2009 to 2025
$9.3M
Ultrafast Biophysical Studies Of ProteinsZIADK029031 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ANFINRUD, PHILIP · 2009 to 2025
$7.1M
Electric Field-stimulated Protein MechanicsP41GM118217 · NIGMS · UNIVERSITY OF CHICAGO · PI RANGANATHAN, RAMA · 2019 to 2021
$5.3M
Ultrafast Biophysical Studies of Proteins: Time-resolved WAXS StudiesZIADK029059 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ANFINRUD, PHILIP · 2009 to 2017
$2.8M
Developing Picosecond Time-Resolved X-ray Infrastructure at the APSZIADK029060 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ANFINRUD, PHILIP · 2009 to 2016
$2.4M
Developing Picosecond Time-Resolved X-ray Infrastructure at the APSZ01DK029060 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ANFINRUD, PHILIP · 2007 to 2008
$542k
Ultrafast Biophysical Studies of Proteins: Time-resolved WAXS StudiesZ01DK029059 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ANFINRUD, PHILIP · 2007 to 2008
$542k
Ultrafast Biophysical Studies Of ProteinsZ01DK029031 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI ANFINRUD, PHILIP A · 1999 to 2008
$542k
Intramural NIH HHS Z01 DK029031Intramural NIH HHS Z01 DK029059Intramural NIH HHS Z01 DK029060Intramural NIH HHS ZIA DK029031Intramural NIH HHS ZIA DK029058Intramural NIH HHS ZIA DK029059Intramural NIH HHS ZIA DK029060NIGMS NIH HHS P41 GM118217
6 · The paper itself

Abstract

Time-resolved small- and wide-angle X-ray scattering studies of proteins in solution based on the pump-probe approach unveil structural information from intermediates over a broad range of length and time scales. In spite of the promise of this methodology, only a fraction of the wealth of information encoded in scattering data has been extracted in studies performed thus far. Here, we discuss the methodology, summarize results from recent time-resolved X-ray scattering studies, and examine the potential to extract additional information from these scattering curves.

Indexed as

ProteinsScattering, Small AngleX-Ray DiffractionX-RaysProteinsProtein structure dynamicsSAXSTime-resolvedWAXS

Identifiers

PMID34175665
PMCPMC8530917

What OpenQuestion 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 OpenQuestion graph.