Evidence map›Paper›PMID 21477594›Full record

ArticleJournal of molecular biology2011

Differential interactions of fluorescent agonists and antagonists with the yeast G protein coupled receptor Ste2p.

Elizabeth Mathew, Anshika Bajaj, Sara M Connelly, Hasmik Sargsyan, Fa-Xiang Ding, Alexander G Hajduczok, Fred Naider, Mark E Dumont

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. A Paradigm for Peptide Hormone-GPCR Analyses.Molecules (Basel, Switzerland) · 2020
    Review
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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

8 authors at 3 institutions in 1 country.

Elizabeth MathewDepartment of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642, USA.
Anshika Bajaj
Sara M Connelly
Hasmik Sargsyan
Fa-Xiang Ding
Alexander G Hajduczok
Fred Naider
Mark E Dumont
University of Rochester · USCollege of Staten Island · USCity University of New York · US

Funding

PEPTIDE/CELL INTERACTIONS IN SACCHAROMYCES CEREVISIAER01GM022087 · NIGMS · UNIVERSITY OF TENNESSEE KNOXVILLE · PI BECKER, JEFFREY M., NAIDER, FRED R · 1985 to 2011
$4.9M
PEPTIDE-CELL INTERACTIONS IN SACCHAROMYCES CEREVISIAER01GM022086 · NIGMS · COLLEGE OF STATEN ISLD ST. GEORGE CAMPUS · PI NAIDER, FRED R · 1985 to 2006
$2.5M
G PROTEIN COUPLED RECEPTOR ACTIVATION STUDIED IN YEASTR01GM059357 · NIGMS · UNIVERSITY OF ROCHESTER · PI DUMONT, MARK E. · 1999 to 2009
$2.2M
Genetic Optimization of Membrane Protein Production for CrystallizationR01GM084083 · NIGMS · UNIVERSITY OF ROCHESTER · PI DUMONT, MARK E. · 2009 to 2012
$1.3M
Peptide-Cell Interactions in Saccharomyces cerevisiaeR56GM022086 · NIGMS · COLLEGE OF STATEN ISLAND · PI NAIDER, FRED R · 2007 to 2007
$371k
NIGMS NIH HHS GM059357NIGMS NIH HHS GM22086NIGMS NIH HHS R01 GM022086NIGMS NIH HHS R01 GM022087NIGMS NIH HHS R01 GM059357NIGMS NIH HHS R01 GM084083NIGMS NIH HHS R56 GM022086
6 · The paper itself

Abstract

We describe a rapid method to probe for mutations in cell surface ligand-binding proteins that affect the environment of bound ligand. The method uses fluorescence-activated cell sorting to screen randomly mutated receptors for substitutions that alter the fluorescence emission spectrum of environmentally sensitive fluorescent ligands. When applied to the yeast α-factor receptor Ste2p, a G protein-coupled receptor, the procedure identified 22 substitutions that red shift the emission of a fluorescent agonist, including substitutions at residues previously implicated in ligand binding and at additional sites. A separate set of substitutions, identified in a screen for mutations that alter the emission of a fluorescent α-factor antagonist, occurs at sites that are unlikely to contact the ligand directly. Instead, these mutations alter receptor conformation to increase ligand-binding affinity and provide signaling in response to antagonists of normal receptors. These results suggest that receptor--agonist interactions involve at least two sites, of which only one is specific for the activated conformation of the receptor.

Indexed as

MutationAmino Acid SequenceFlow CytometryFluorescent DyesLigandsMolecular Sequence DataProtein BindingProtein ConformationReceptors, Mating FactorSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsFluorescent DyesLigandsReceptors, Mating FactorSaccharomyces cerevisiae ProteinsSTE2 protein, S cerevisiae

Identifiers

PMID21477594
PMCPMC3104124
OpenAlexW2089029437

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.