Evidence map›Paper›PMID 11967834›Full record

ArticleYeast (Chichester, England)2002

Isolation and mapping of self-assembling protein domains encoded by the Saccharomyces cerevisiae genome using lambda repressor fusions.

Leonardo Mariño-Ramírez, James C Hu

Open access · greenAbstract read
In one paragraph

Article in Yeast (Chichester, England), 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Sec7 regulatory domains scaffold autoinhibited and active conformations.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  8. The oligomerization of CynR in Escherichia coli.Protein science : a publication of the Protein Society · 2009
    Article
  9. The oligomerization of OxyR in Escherichia coli.Protein science : a publication of the Protein Society · 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

2 authors at 1 institution in 1 country.

Leonardo Mariño-RamírezDepartment of Biochemistry and Biophysics, Center for Advanced Biomolecular Research, Texas A&M University, College Station, TX 77843-2128, USA.
James C Hu
Texas A&M University · US

Funding

Protein Self-Assembly in Model MicroorganismsR01GM063652 · NIGMS · TEXAS A&M UNIVERSITY SYSTEM · PI HU, JAMES C · 2001 to 2004
$1.1M
Intramural NIH HHS Z99 LM999999NIGMS NIH HHS R01 GM063652
6 · The paper itself

Abstract

Understanding how proteins are able to form stable complexes is of fundamental interest from the perspective of protein structure and function. Here we show that lambda repressor fusions can be used to identify and characterize homotypic interaction domains encoded by the genome of Saccharomyces cerevisiae, using a selection for polypeptides that can drive the assembly of the DNA binding domain of bacteriophage lambda repressor. Three high complexity libraries were constructed by cloning random fragments of S. cerevisiae DNA as lambda repressor fusions. Repressor fusions encoding homotypic interactions were recovered, identifying oligomerization units in 35 yeast proteins. Seventeen of these interaction domains have not been previously reported, while the other 18 represent homotypic interactions that have been characterized at varying levels of detail. The novel interactions include several predicted coiled-coils as well as domains of unknown structure. With the availability of genomic sequences it should be possible to apply this approach, which provides information about protein-protein interactions that is complementary to that obtained from yeast two-hybrid screens, on a genome-wide scale in yeast or other organisms where large-scale protein-protein interaction data is not available.

Indexed as

Artificial Gene FusionDNA-Binding ProteinsProtein Interaction MappingAmino Acid SequenceBacteriophage lambdaBase SequenceGenomic LibraryMolecular Sequence DataOpen Reading FramesPeptidesRepressor ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Tagged SitesViral ProteinsViral Regulatory and Accessory ProteinsDNA-Binding ProteinsPeptidesphage repressor proteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsViral ProteinsViral Regulatory and Accessory Proteins

Identifiers

PMID11967834
PMCPMC1955323
OpenAlexW2079997671

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.