Evidence map›Paper›PMID 36584678›Full record

ReviewStructure (London, England : 1993)2023

Frozen in time: analyzing molecular dynamics with time-resolved cryo-EM.

Sascha Josef Amann, Demian Keihsler, Tatyana Bodrug, Nicholas G Brown, David Haselbach

Abstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Microfluidic Devices for High-Throughput In Situ Serial Crystallography.Advances in biochemical engineering/biotechnology · 2026
    Review
  6. Review
  7. Review
  8. A Bright and Dynamic Future in Structural Biology.Advances in experimental medicine and biology · 2026
    Review
  9. Article
  10. Article
  11. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Structural Chemistry of Helicase Inhibition.Journal of medicinal chemistry · 2025
    Review
  19. Article
  20. 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

5 authors.

Sascha Josef AmannIMP - Research Institute of Molecular Pathology, Campus-Vienna-Biocenter 1, 1030 Vienna, Austria; Vienna BioCenter PhD Program, a Doctoral School of the University of Vienna and Medical University of Vienna, A-1030 Vienna, Austria.
Demian KeihslerIMP - Research Institute of Molecular Pathology, Campus-Vienna-Biocenter 1, 1030 Vienna, Austria.
Tatyana BodrugIMP - Research Institute of Molecular Pathology, Campus-Vienna-Biocenter 1, 1030 Vienna, Austria; Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Nicholas G BrownDepartment of Pharmacology and Lineberger Comprehensive Cancer Center, University of North Carolina School of Medicine, Chapel Hill, NC 27599, USA.
David HaselbachIMP - Research Institute of Molecular Pathology, Campus-Vienna-Biocenter 1, 1030 Vienna, Austria; Institute for Physical Chemistry, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg, Germany. Electronic address: david.haselbach@imp.ac.at.

Funding

Spindle Assembly Checkpoint SilencingR35GM128855 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Nicholas Gene Brown · 2018 to 2026
$4.1M
NIGMS NIH HHS R35 GM128855
6 · The paper itself

Abstract

Molecular machines, such as polymerases, ribosomes, or proteasomes, fulfill complex tasks requiring the thermal energy of their environment. They achieve this by restricting random motion along a path of possible conformational changes. These changes are often directed through engagement with different cofactors, which can best be compared to a Brownian ratchet. Many molecular machines undergo three major steps throughout their functional cycles, including initialization, repetitive processing, and termination. Several of these major states have been elucidated by cryogenic electron microscopy (cryo-EM). However, the individual steps for these machines are unique and multistep processes themselves, and their coordination in time is still elusive. To measure these short-lived intermediate events by cryo-EM, the total reaction time needs to be shortened to enrich for the respective pre-equilibrium states. This approach is termed time-resolved cryo-EM (trEM). In this review, we sum up the methodological development of trEM and its application to a range of biological questions.

Indexed as

Molecular Dynamics SimulationRibosomesCryoelectron MicroscopyMotionTimemolecular machinesSPAtime-resolved cryo-EM

Identifiers

PMID36584678
PMCPMC9825670

What OpenQuestion holds

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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.