Evidence map›Paper›PMID 27658684›Full record

ReviewTrends in biochemical sciences2016

ATPase and GTPase Tangos Drive Intracellular Protein Transport.

Shu-Ou Shan

Open access · bronzeAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-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

21 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
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  6. Structures of theProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Membrane fusion byMolecular biology of the cell · 2022
    Article
  11. Review
  12. Article
  13. Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum.International journal of molecular sciences · 2021
    Review
  14. 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

1 author at 1 institution in 1 country.

Shu-Ou ShanDivision of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA. Electronic address: sshan@caltech.edu.
California Institute of Technology · US

Funding

Molecular Mechanism of Protein Targeting by the Signal Recognition ParticleR01GM078024 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI SHAN, SHU-OU · 2007 to 2020
$4.4M
Molecular mechanisms of post-translational targeting of tail-anchored proteins.R01GM107368 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI SHAN, SHU-OU · 2014 to 2019
$2.1M
NIGMS NIH HHS R01 GM078024NIGMS NIH HHS R01 GM107368
6 · The paper itself

Abstract

The GTPase superfamily of proteins provides molecular switches to regulate numerous cellular processes. The 'GTPase switch' paradigm, in which external regulatory factors control the switch of a GTPase between 'on' and 'off' states, has been used to interpret the regulatory mechanism of many GTPases. However, recent work unveiled a class of nucleotide hydrolases that do not adhere to this classical paradigm. Instead, they use nucleotide-dependent dimerization cycles to regulate key cellular processes. In this review article, recent studies of dimeric GTPases and ATPases involved in intracellular protein targeting are summarized. It is suggested that these proteins can use the conformational plasticity at their dimer interface to generate multiple points of regulation, thereby providing the driving force and spatiotemporal coordination of complex cellular pathways.

Indexed as

Evolution, MolecularAdenosine TriphosphatasesAnimalsArchaeaBacteriaGene ExpressionGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsHumansNucleotidasesPhylogenyProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein MultimerizationAdenosine TriphosphatasesGet3 protein, S cerevisiaeGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsnucleotidaseNucleotidasesSaccharomyces cerevisiae ProteinsATPasesGet3GTPasesmolecular recognition and regulationprotein targetingsignal recognition particle

Identifiers

PMID27658684
PMCPMC5627767
OpenAlexW2522870155

What OpenQuestion holds

Textmetadata
LicenceTDM
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.