Evidence map›Paper›PMID 28548099›Full record

ArticleNature communications2017

Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.

Yang Chen, Lei Zhang, Laura Graf, Bing Yu, Yue Liu, Georg Kochs, Yongfang Zhao, Song Gao

Abstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Structural and functional characterization of the brain-specific dynamin superfamily member RNF112.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Antiviral Mx proteins have an ancient origin and widespread distribution among eukaryotes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Integrative modeling of guanylate binding protein dimers.Protein science : a publication of the Protein Society · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Quantification and demonstration of the collective constriction-by-ratchet mechanism in the dynamin molecular motor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

8 authors.

Yang ChenState Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center, Guangzhou 510060, China.
Lei ZhangNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Laura GrafInstitute of Virology, Medical Center, Faculty of Medicine, University of Freiburg, Freiburg 79008, Germany.
Bing YuState Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center, Guangzhou 510060, China.
Yue LiuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Georg KochsInstitute of Virology, Medical Center, Faculty of Medicine, University of Freiburg, Freiburg 79008, Germany.
Yongfang ZhaoNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0003-1751-7201
Song GaoState Key Laboratory of Oncology in South China, Collaborative Innovation Center for Cancer Medicine, Sun Yat-sen University Cancer Center, Guangzhou 510060, China.ORCID 0000-0001-7427-6681

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human myxovirus resistance protein 1 (MxA) restricts a wide range of viruses and is closely related to the membrane-remodelling GTPase dynamin. The functions of MxA rely on domain rearrangements coupled with GTP hydrolysis cycles. To gain insight into this process, we studied real-time domain dynamics of MxA by single-molecule fluorescence resonance energy transfer. We find that the GTPase domain-bundle-signalling-element (BSE) region can adopt either an 'open' or a 'closed' conformation in all nucleotide-loading conditions. Whereas the open conformation is preferred in nucleotide-free, GDP·AlF

Indexed as

Crystallography, X-RayDynaminsFluorescence Resonance Energy TransferGuanosine TriphosphateHEK293 CellsHumansMutationMyxovirus Resistance ProteinsProtein ConformationProtein DomainsProtein MultimerizationDynaminsGuanosine TriphosphateMX1 protein, humanMyxovirus Resistance Proteins

Identifiers

PMID28548099
PMCPMC5458555

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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.