Evidence map›Paper›PMID 26910532›Full record

ReviewCurrent genetics2016

Regulation of TORC1 by ubiquitin through non-covalent binding.

Yu Jiang

Abstract readReview
In one paragraph

Review in Current genetics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Express yourself: how PP2A-B55Current genetics · 2018
    Review
  8. Article
  9. Review
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.

Yu JiangDepartment of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15213, USA. yuj5@pitt.edu.
University of Pittsburgh · US

Funding

The role of arachidonic acid in estrogen mediated mTOR activationR21CA169186 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JIANG, YU · 2013 to 2014
$361k
NCI NIH HHS R21 CA169186
6 · The paper itself

Abstract

Ubiquitin (Ub) regulates numerous cellular processes through covalent attachment to other proteins in the forms of poly- and mono-ubiquitination. A recent study in yeast shows that ubiquitin controls TORC1 through a noncovalent binding with Kog1, a regulatory subunit of TORC1. The binding stabilizes Kog1 and prevents its degradation under stress conditions. This finding unveils a novel role of Ub in TORC1 function and implicates a unique mechanism that attributes the action of Ub in cell signaling.

Indexed as

Mechanistic Target of Rapamycin Complex 1Multiprotein ComplexesProtein BindingSignal TransductionTOR Serine-Threonine KinasesUbiquitinUbiquitinationMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesTOR Serine-Threonine KinasesUbiquitinKog1RapamycinTORUbiquitinWD40 repeats

Identifiers

PMID26910532
PMCPMC4930378
OpenAlexW2274479436

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.