Evidence map›Paper›PMID 24778185›Full record

ArticleThe Journal of biological chemistry2014

Tyrosine phosphorylation of Dbl regulates GTPase signaling.

Meghana Gupta, Xiaojun Qi, Varsha Thakur, Danny Manor

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Regulating Rho GTPases and their regulators.Nature reviews. Molecular cell biology · 2016
    Review
  10. Article
  11. 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

4 authors at 1 institution in 1 country.

Meghana GuptaFrom the Departments of Pharmacology, and Nutrition, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
Xiaojun QiNutrition, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
Varsha ThakurNutrition, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
Danny ManorFrom the Departments of Pharmacology, and Nutrition, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106 dxm178@case.edu.
Case Western Reserve University · US

Funding

Cell Transformation by Dbl-like onco-proteinsR01CA082391 · NCI · CORNELL UNIVERSITY ITHACA · PI MANOR, DANNY · 2002 to 2006
$1.3M
CELL TRANSFORMATION BY DBL LIKE ONCOPROTEINSR55CA082391 · NCI · CORNELL UNIVERSITY ITHACA · PI MANOR, DANNY · 1999 to 1999
–
NCI NIH HHS CA082391NCI NIH HHS R01 CA082391NCI NIH HHS R55 CA082391
6 · The paper itself

Abstract

Rho GTPases are molecular "switches" that cycle between "on" (GTP-bound) and "off" (GDP-bound) states and regulate numerous cellular activities such as gene expression, protein synthesis, cytoskeletal rearrangements, and metabolic responses. Dysregulation of GTPases is a key feature of many diseases, especially cancers. Guanine nucleotide exchange factors (GEFs) of the Dbl family are activated by mitogenic cell surface receptors and activate the Rho family GTPases Cdc42, Rac1, and RhoA. The molecular mechanisms that regulate GEFs from the Dbl family are poorly understood. Our studies reveal that Dbl is phosphorylated on tyrosine residues upon stimulation by growth factors and that this event is critical for the regulated activation of the GEF. These findings uncover a novel layer of complexity in the physiological regulation of this protein.

Indexed as

Protein Processing, Post-TranslationalSignal TransductionAnimalscdc42 GTP-Binding ProteinChlorocebus aethiopsCHO CellsCOS CellsCricetinaeCricetulusGuanine Nucleotide Exchange FactorsHEK293 CellsHumansIntercellular Signaling Peptides and ProteinsMiceNIH 3T3 CellsPhosphorylationcdc42 GTP-Binding ProteinGuanine Nucleotide Exchange FactorsIntercellular Signaling Peptides and Proteinsrac1 GTP-Binding ProteinrhoA GTP-Binding ProteinTyrosineGuanine Nucleotide Exchange Factor (GEF)PhosphorylationPhosphotyrosineRho GTPasesSmall GTPase

Identifiers

PMID24778185
PMCPMC4059160
OpenAlexW2003289800

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.