Evidence map›Paper›PMID 20164644›Full record

ArticleActa crystallographica. Section A, Foundations of crystallography2010

Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches.

Sebastian Westenhoff, Elena Nazarenko, Erik Malmerberg, Jan Davidsson, Gergely Katona, Richard Neutze

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section A, Foundations of crystallography, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Protein folding from heterogeneous unfolded state revealed by time-resolved X-ray solution scattering.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  5. Article
  6. Estimating the difference between structure-factor amplitudes using multivariate Bayesian inference.Acta crystallographica. Section A, Foundations and advances · 2016
    Article
  7. Article
  8. Article
  9. Article
  10. Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014
    Review
  11. Review
  12. NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. Review
  14. Article
  15. Article
  16. Pathway and mechanism of drug binding to G-protein-coupled receptors.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  17. Article
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

6 authors at 2 institutions in 1 country.

Sebastian WestenhoffDepartment of Chemistry, Biochemistry and Biophysics, University of Gothenburg, Box 462, SE-40530 Gothenburg, Sweden.
Elena Nazarenko
Erik Malmerberg
Jan Davidsson
Gergely Katona
Richard Neutze
University of Gothenburg · SEUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins undergo conformational changes during their biological function. As such, a high-resolution structure of a protein's resting conformation provides a starting point for elucidating its reaction mechanism, but provides no direct information concerning the protein's conformational dynamics. Several X-ray methods have been developed to elucidate those conformational changes that occur during a protein's reaction, including time-resolved Laue diffraction and intermediate trapping studies on three-dimensional protein crystals, and time-resolved wide-angle X-ray scattering and X-ray absorption studies on proteins in the solution phase. This review emphasizes the scope and limitations of these complementary experimental approaches when seeking to understand protein conformational dynamics. These methods are illustrated using a limited set of examples including myoglobin and haemoglobin in complex with carbon monoxide, the simple light-driven proton pump bacteriorhodopsin, and the superoxide scavenger superoxide reductase. In conclusion, likely future developments of these methods at synchrotron X-ray sources and the potential impact of emerging X-ray free-electron laser facilities are speculated upon.

Indexed as

Computer SimulationCrystallography, X-RayKineticsLasersModels, MolecularProtein ConformationProteinsTime FactorsX-Ray DiffractionProteins

Identifiers

PMID20164644
PMCPMC2824530
OpenAlexW2014378919

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.