Evidence map›Paper›PMID 18596064›Full record

ArticleMolecular & cellular proteomics : MCP2008

A proteomics analysis of yeast Mot1p protein-protein associations: insights into mechanism.

Diana R Arnett, Jennifer L Jennings, David L Tabb, Andrew J Link, P Anthony Weil

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2008. 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
1.4field-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

13 citing papers in PubMed, 17 citations in OpenAlex.

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  12. The dynamic personality of TATA-binding protein.Trends in biochemical sciences · 2009
    Article
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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

5 authors at 1 institution in 1 country.

Diana R ArnettDepartment of Molecular Physiology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0615, USA.
Jennifer L Jennings
David L Tabb
Andrew J Link
P Anthony Weil
Vanderbilt University · US

Funding

TISSUE CoreP50CA098131 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI PARK, BEN HO, PIETENPOL, JENNIFER A · 2003 to 2024
$48.7M
T Lymphocyte based functional genomics of inflammationP01HL068744 · NHLBI · VANDERBILT UNIVERSITY · PI MOORE, JASON H. · 2002 to 2006
$9.9M
MOLECULAR GENETIC ANALYSIS OF YEAST TAFSR01GM052461 · NIGMS · VANDERBILT UNIVERSITY · PI WEIL, PETER ANTHONY · 1995 to 2011
$6.2M
Proteomic Analysis of Eukaryotic Protein SynthesisR01GM064779 · NIGMS · VANDERBILT UNIVERSITY · PI LINK, ANDREW J. · 2002 to 2010
$3.0M
Proteomic Construction of Stress Regulated NetworksR01ES011993 · NIEHS · VANDERBILT UNIVERSITY · PI WEIL, PETER ANTHONY · 2002 to 2005
$2.0M
New Proteomic Algorithms to Identify Mutant or Modified ProteinsR01CA126218 · NCI · VANDERBILT UNIVERSITY · PI TABB, DAVID L · 2006 to 2010
$1.8M
Molecular Genetic Analysis of Yeast TAFsR56GM052461 · NIGMS · VANDERBILT UNIVERSITY · PI WEIL, PETER ANTHONY · 2007 to 2007
$500k
NCI NIH HHS P50 CA098131NCI NIH HHS R01 CA126218NHLBI NIH HHS HL68744NHLBI NIH HHS P01 HL068744NIAID NIH HHS N01 AI040079NIEHS NIH HHS ES11993NIEHS NIH HHS R01 ES011993NIGMS NIH HHS GM52461NIGMS NIH HHS GM64779NIGMS NIH HHS R01 GM052461NIGMS NIH HHS R01 GM064779NIGMS NIH HHS R56 GM052461PHS HHS HHSN266200400079C
6 · The paper itself

Abstract

Yeast Mot1p, a member of the Snf2 ATPase family of proteins, is a transcriptional regulator that has the unusual ability to both repress and activate mRNA gene transcription. To identify interactions with other proteins that may assist Mot1p in its regulatory processes, Mot1p was purified from replicate yeast cell extracts, and Mot1p-associated proteins were identified by coupled multidimensional liquid chromatography and tandem mass spectrometry. Using this approach we generated a catalog of Mot1p-interacting proteins. Mot1p interacts with a range of transcriptional co-regulators as well as proteins involved in chromatin remodeling. We propose that interaction with such a wide range of proteins may be one mechanism through which Mot1p subserves its roles as a transcriptional activator and repressor.

Indexed as

Adenosine TriphosphatasesBase SequenceChromatin Assembly and DisassemblyDNA, FungalDNA HelicasesModels, MolecularMolecular WeightMultiprotein ComplexesPlasmidsProtein Interaction Domains and MotifsProtein Interaction MappingProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTandem Mass SpectrometryTATA-Binding Protein Associated FactorsAdenosine TriphosphatasesDNA, FungalDNA HelicasesMOT1 protein, S cerevisiaeMultiprotein ComplexesSaccharomyces cerevisiae ProteinsTATA-Binding Protein Associated Factors

Identifiers

PMID18596064
PMCPMC2577210
OpenAlexW2105831706

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.