Evidence map›Paper›PMID 38326645›Full record

ArticleNature chemistry2024

Characterizing ATP processing by the AAA+ protein p97 at the atomic level.

Mikhail Shein, Manuel Hitzenberger, Tat Cheung Cheng, Smruti R Rout, Kira D Leitl, Yusuke Sato, Martin Zacharias, Eri Sakata, Anne K Schütz

Abstract read
In one paragraph

Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing 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

24 citing papers in PubMed.

  1. Article
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  11. Molecular Mechanism of ATP Hydrolysis Catalyzed by p97: A QM/MM Study.Journal of chemical theory and computation · 2025
    Article
  12. A genome-scale drug discovery pipeline uncovers therapeutic targets and a unique p97 allosteric binding site inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. SNARE disassembly requires Sec18/NSF side loading.Nature structural & molecular biology · 2025
    Article
  14. Article
  15. Review
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  17. SNARE disassembly requires Sec18/NSF side-loading.bioRxiv : the preprint server for biology · 2025
    Article
  18. Article
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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

9 authors.

Mikhail Shein *Faculty for Chemistry and Pharmacy, Ludwig-Maximilians-Universität München, München, Germany.
Manuel Hitzenberger *Physics Department and Center of Protein Assemblies, Technical University of Munich, Garching, Germany. manuel.hitzenberger@tum.de.ORCID 0000-0001-9726-2370
Tat Cheung Cheng *Institute for Neuropathology, University Medical Center Göttingen, Göttingen, Germany.ORCID 0000-0003-2801-3084
Smruti R RoutMultiscale Bioimaging: from Molecular Machines to Networks of Excitable Cells (MBExC), University of Göttingen, Göttingen, Germany.
Kira D LeitlFaculty for Chemistry and Pharmacy, Ludwig-Maximilians-Universität München, München, Germany.ORCID 0000-0001-8438-7369
Yusuke SatoCenter for Research on Green Sustainable Chemistry, Graduate School of Engineering, Tottori University, Tottori, Japan.ORCID 0000-0001-8495-8950
Martin ZachariasPhysics Department and Center of Protein Assemblies, Technical University of Munich, Garching, Germany. martin.zacharias@ph.tum.de.ORCID 0000-0001-5163-2663
Eri SakataMultiscale Bioimaging: from Molecular Machines to Networks of Excitable Cells (MBExC), University of Göttingen, Göttingen, Germany. eri.sakata@med.uni-goettingen.de.ORCID 0000-0002-8580-3683
Anne K SchützFaculty for Chemistry and Pharmacy, Ludwig-Maximilians-Universität München, München, Germany. anne.schuetz@cup.lmu.de.ORCID 0000-0001-6398-5757

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 154113120Deutsche Forschungsgemeinschaft (German Research Foundation) 201302640Deutsche Forschungsgemeinschaft (German Research Foundation) 394455587Deutsche Forschungsgemeinschaft (German Research Foundation) EXC 2067/1-390729940
6 · The paper itself

Abstract

The human enzyme p97 regulates various cellular pathways by unfolding hundreds of protein substrates in an ATP-dependent manner, making it an essential component of protein homeostasis and an impactful pharmacological target. The hexameric complex undergoes substantial conformational changes throughout its catalytic cycle. Here we elucidate the molecular motions that occur at the active site in the temporal window immediately before and after ATP hydrolysis by merging cryo-EM, NMR spectroscopy and molecular dynamics simulations. p97 populates a metastable reaction intermediate, the ADP·P

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateHumansMolecular Dynamics SimulationValosin Containing ProteinAdenosine TriphosphatasesAdenosine TriphosphateValosin Containing Protein

Identifiers

PMID38326645
PMCPMC10914628

What OpenQuestion holds

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Registered trials

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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.