Evidence map›Paper›PMID 31197034›Full record

ArticleThe Journal of biological chemistry2019

The chaperone SmgGDS-607 has a dual role, both activating and inhibiting farnesylation of small GTPases.

Desirée García-Torres, Carol A Fierke

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Post-translational modification of RAS proteins.Current opinion in structural biology · 2021
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Splice switching an oncogenic ratio of SmgGDS isoforms as a strategy to diminish malignancy.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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.

Desirée García-TorresProgram in Chemical Biology, University of Michigan, Ann Arbor, Michigan 48109.
Carol A FierkeDepartment of Chemistry, University of Michigan, Ann Arbor, Michigan 48109 fierke@umich.edu.

Funding

STRUCTURE/FUNCTION OF ZINC METALLOPROTEINSR01GM040602 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FIERKE, CAROL A · 1993 to 2017
$6.0M
MICHIGAN CHEMISTRY-BIOLOGY INTERFACE TRAINING PROGRAMT32GM008597 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MONTGOMERY, JOHN · 1996 to 2018
$5.0M
NIGMS NIH HHS R01 GM040602NIGMS NIH HHS T32 GM008597
6 · The paper itself

Abstract

Ras family small GTPases undergo prenylation (such as farnesylation) for proper localization to the plasma membrane, where they can initiate oncogenic signaling pathways. Small GTP-binding protein GDP-dissociation stimulator (SmgGDS) proteins are chaperones that bind and traffic small GTPases, although their exact cellular function is unknown. Initially, SmgGDS proteins were classified as guanine nucleotide exchange factors, but recent findings suggest that SmgGDS proteins also regulate prenylation of small GTPases

Indexed as

Alkyl and Aryl TransferasesAmino Acid MotifsBiocatalysisGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsHumansKineticsMonomeric GTP-Binding ProteinsMutagenesis, Site-DirectedProtein BindingProtein PrenylationProto-Oncogene Proteins p21(ras)Recombinant ProteinsSubstrate SpecificityThermodynamicsTumor Suppressor ProteinsAlkyl and Aryl TransferasesDIRAS1 protein, humanGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsKRAS protein, humanMonomeric GTP-Binding Proteinsp21(ras) farnesyl-protein transferaseProto-Oncogene Proteins p21(ras)RAP1GDS1 protein, humanRecombinant ProteinsTumor Suppressor Proteinscancercell signalingenzyme kineticsGTPase Kras (KRAS)post-translational modification (PTM)protein farnesylationprotein prenylationRas proteinsmall GTPasesmall GTP-binding protein GDP-dissociation stimulator (SmgGDS)

Identifiers

PMID31197034
PMCPMC6682747

What OpenQuestion holds

Textmetadata
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.