Evidence map›Paper›PMID 23409238›Full record

ArticleScientific reports2013

Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry.

Qian Zhang, Jin Chen, Kunihiro Kuwajima, Hui-Min Zhang, Feng Xian, Nicolas L Young, Alan G Marshall

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Pih1p-Tah1p Puts a Lid on Hexameric AAA+ ATPases Rvb1/2p.Structure (London, England : 1993) · 2017
    Article
  5. Conformational dynamics of 1-deoxy-d-xylulose 5-phosphate synthase on ligand binding revealed by H/D exchange MS.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  6. Article
  7. Assessing heterogeneity in oligomeric AAA+ machines.Cellular and molecular life sciences : CMLS · 2017
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Analytical Aspects of Hydrogen Exchange Mass Spectrometry.Annual review of analytical chemistry (Palo Alto, Calif.) · 2015
    Review
  14. Article
  15. 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

7 authors at 4 institutions in 2 countries.

Qian ZhangFlorida State University, Department of Chemistry, Tallahassee, FL 32306, USA.
Jin Chen
Kunihiro Kuwajima
Hui-Min Zhang
Feng Xian
Nicolas L Young
Alan G Marshall
National High Magnetic Field Laboratory · USFlorida State University · USNational Institutes of Natural Sciences · JPOkazaki Institute for Integrative Bioscience · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here we employ hydrogen/deuterium exchange mass spectrometry (HDX-MS) to access E. coli chaperonin GroEL conformation. The ~800 kDa tetradecameric GroEL plays an essential role in the proper folding of many proteins. Previous studies of the structural dynamics of GroEL upon ATP binding have been inconsistent, showing either minimal or major allosteric changes. Our results, based on the native, non-mutated, protein under physiological conditions in solution demonstrate substantial changes in conformation and/or flexibility upon ATP binding. We capture the pivotal step in its functional cycle by use of a non-hydrolyzable ATP analog, ATPγS, to mimic the ATP-bound GroEL state. Comparison of HDX-MS results for apo GroEL and GroEL-ATPγS enables the characterization of the nucleotide-regulated conformational changes throughout the entire protein with high sequence resolution. The 14-mer GroEL complex is the largest protein assembly yet accessed by HDX-MS, with sequence resolution of segments of as few as five amino acids.

Indexed as

Adenosine TriphosphateAmino Acid SequenceChaperonin 60Deuterium Exchange MeasurementEscherichia coliMass SpectrometryMolecular Sequence DataProtein BindingProtein Structure, TertiaryAdenosine TriphosphateChaperonin 60

Identifiers

PMID23409238
PMCPMC3570780
OpenAlexW2010734518

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.