Evidence map›Paper›PMID 26972107›Full record

ReviewBiopolymers2016

Invited review: Small GTPases and their GAPs.

Ashwini K Mishra, David G Lambright

Open access · greenAbstract readReview
In one paragraph

Review in Biopolymers, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.0field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Assessing the mechanism of fast-cycling cancer-associated mutations of Rac1 small Rho GTPase.Protein science : a publication of the Protein Society · 2024
    Article
  12. Mechanism-Based Redesign of GAP to Activate Oncogenic Ras.Journal of the American Chemical Society · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Editorial: Signaling by Small GTPases in Metastatic Disease.Frontiers in cell and developmental biology · 2022
    Article
  17. Article
  18. Article
  19. The Role of the Guanosine Nucleotide-Binding Protein in the Corpus Luteum.Animals : an open access journal from MDPI · 2021
    Review
  20. The Ras dimer structure.Chemical science · 2021
    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

2 authors at 1 institution in 1 country.

Ashwini K MishraProgram in Molecular Medicine and Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA, 01605.
David G LambrightProgram in Molecular Medicine and Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA, 01605.
University of Massachusetts Chan Medical School · US

Funding

STRUCTURAL BASIS OF G PROTEIN MEDIATED SIGNALINGR01GM056324 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LAMBRIGHT, DAVID G · 1998 to 2018
$6.2M
NIGMS NIH HHS R01 GM056324
6 · The paper itself

Abstract

Widespread utilization of small GTPases as major regulatory hubs in many different biological systems derives from a conserved conformational switch mechanism that facilitates cycling between GTP-bound active and GDP-bound inactive states under control of guanine nucleotide exchange factors (GEFs) and GTPase activating proteins (GAPs), which accelerate slow intrinsic rates of activation by nucleotide exchange and deactivation by GTP hydrolysis, respectively. Here we review developments leading to current understanding of intrinsic and GAP catalyzed GTP hydrolytic reactions in small GTPases from structural, molecular and chemical mechanistic perspectives. Despite the apparent simplicity of the GTPase cycle, the structural bases underlying the hallmark hydrolytic reaction and catalytic acceleration by GAPs are considerably more diverse than originally anticipated. Even the most fundamental aspects of the reaction mechanism have been challenging to decipher. Through a combination of experimental and in silico approaches, the outlines of a consensus view have begun to emerge for the best studied paradigms. Nevertheless, recent observations indicate that there is still much to be learned. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 431-448, 2016.

Indexed as

AnimalsCatalysisCell CycleGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsGuanosine TriphosphateHumansHydrolysisGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsGuanosine TriphosphateGAPGTPasehydrolysismechanismstructure

Identifiers

PMID26972107
PMCPMC5439442
OpenAlexW2415918635

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.