Evidence map›Paper›PMID 28202679›Full record

ArticleBiochemical Society transactions2017

From molecular chaperones to membrane motors: through the lens of a mass spectrometrist.

Carol V Robinson

Abstract read
In one paragraph

Article in Biochemical Society transactions, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Allostery revealed within lipid binding events to membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. 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

1 author.

Carol V RobinsonDepartment of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QY, U.K. carol.robinson@chem.ox.ac.uk.

Funding

Medical Research Council 98101Medical Research Council G1000819Medical Research Council MR/N020413/1Wellcome TrustWellcome Trust WT008150Wellcome Trust WT099141
6 · The paper itself

Abstract

Twenty-five years ago, we obtained our first mass spectra of molecular chaperones in complex with protein ligands and entered a new field of gas-phase structural biology. It is perhaps now time to pause and reflect, and to ask how many of our initial structure predictions and models derived from mass spectrometry (MS) datasets were correct. With recent advances in structure determination, many of the most challenging complexes that we studied over the years have become tractable by other structural biology approaches enabling such comparisons to be made. Moreover, in the light of powerful new electron microscopy methods, what role is there now for MS? In considering these questions, I will give my personal view on progress and problems as well as my predictions for future directions.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsCell MembraneChaperonin 60Mass SpectrometryMembrane ProteinsMicroscopy, ElectronModels, MolecularMolecular ChaperonesMolecular Motor ProteinsProtein ConformationRibosomesThermus thermophilusTime FactorsAdenosine TriphosphatasesBacterial ProteinsChaperonin 60Membrane ProteinsMolecular ChaperonesMolecular Motor Proteinsion mobilitymass spectrometrymembrane proteinsmolecular chaperones

Identifiers

PMID28202679
PMCPMC5310722

What OpenQuestion holds

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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.