Evidence map›Paper›PMID 28602821›Full record

ArticleStructure (London, England : 1993)2017

Timing and Reset Mechanism of GTP Hydrolysis-Driven Conformational Changes of Atlastin.

John P O'Donnell, Richard B Cooley, Carolyn M Kelly, Kurt Miller, Olaf S Andersen, Radda Rusinova, Holger Sondermann

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. 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
1.8field-weighted citation impact, top 17% 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, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Exploring switch II pocket conformation of KRAS(G12D) with mutant-selective monobody inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  7. A role for endoplasmic reticulum dynamics in the cellular distribution of microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Review
  10. Article
  11. Review
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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

7 authors at 2 institutions in 1 country.

John P O'DonnellDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Richard B CooleyDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Carolyn M KellyDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Kurt MillerDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
Olaf S AndersenDepartment of Physiology and Biophysics, Weill Cornell Medicine, New York, NY 10065, USA.
Radda RusinovaDepartment of Physiology and Biophysics, Weill Cornell Medicine, New York, NY 10065, USA.
Holger SondermannDepartment of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA. Electronic address: hs293@cornell.edu.
Cornell University · USWeill Cornell Medicine · US

Funding

Overall (pp. 40-62)P41GM103485 · NIGMS · CORNELL UNIVERSITY · PI CERIONE, RICHARD A. · 2012 to 2018
$15.5M
Energetics of Channel-Bilayer InteractionsR01GM021342 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI ANDERSEN, OLAF S. · 1985 to 2021
$9.9M
CHEMISTRY OF BIOLOGICAL SYSTEMST32GM008500 · NIGMS · CORNELL UNIVERSITY ITHACA · PI LIN, HENING · 1996 to 2020
$5.4M
NIGMS NIH HHS P41 GM103485NIGMS NIH HHS R01 GM021342NIGMS NIH HHS T32 GM008500
6 · The paper itself

Abstract

The endoplasmic reticulum (ER) forms a branched, dynamic membrane tubule network that is vital for cellular function. Branching arises from membrane fusion facilitated by the GTPase atlastin (ATL). Many metazoan genomes encode for three ATL isoforms that appear to fulfill partially redundant function despite differences in their intrinsic GTPase activity and localization within the ER; however, the underlying mechanistic differences between the isoforms are poorly understood. Here, we identify discrete temporal steps in the catalytic cycle for the two most dissimilar isoforms, ATL1 and ATL3, revealing an overall conserved progression of molecular events from nucleotide binding and hydrolysis to ATL dimerization and phosphate release. A crystal structure of ATL3 suggests a mechanism for the displacement of the catalytic Mg

Indexed as

Catalytic DomainGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateHumansMagnesiumMembrane ProteinsProtein BindingATL1 protein, humanATL3 protein, humanGTP-Binding ProteinsGTP PhosphohydrolasesGuanosine TriphosphateMagnesiumMembrane Proteinsdynamin-related proteinsenzyme mechanismGTPasemembrane fusionnucleotide exchange

Identifiers

PMID28602821
PMCPMC5516944
OpenAlexW2623903988

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.