Evidence map›Paper›PMID 22683951›Full record

ReviewFEBS letters2012

SH3 domains come of age.

Brian K Kay

Open access · bronzeAbstract readReview
In one paragraph

Review in FEBS letters, 2012. 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
2.2field-weighted citation impact, top 13% 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, 28 citations in OpenAlex.

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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

1 author at 1 institution in 1 country.

Brian K KayDepartment of Biological Sciences, University of Illinois at Chicago, 845 W. Taylor St., 3240 SES - MC 066, Chicago, IL 60607-7060, USA. bkay@uic.edu
University of Illinois Chicago · US

Funding

Technology Development for Recombinant Affinity ReagentsU54DK093444 · NIDDK · UNIVERSITY OF ILLINOIS AT CHICAGO · PI KAY, BRIAN KENNETH · 2011 to 2013
$3.6M
NIDDK NIH HHS U54 DK093444
6 · The paper itself

Abstract

With the sequencing of an eukaryotic genome, it is possible to inventory the predicted proteome for proteins that carry one or more Src Homology 3 (SH3) domains. Due to the current ease of cloning and gene synthesis, these short domains can be readily overexpressed and manipulated for the purpose of characterizing their specificity and affinity for peptide ligands, as well as solving the three-dimensional structures of the domains. This information can be used to predict and confirm their cellular interacting partners, in the effort to understand the function of a eukaryotic protein by focusing on its SH3 domain. Finally, capitalizing on our mature understanding about protein-protein interacting modules, like the SH3 domain, it is possible to use directed evolution to enhance or change the specificity and affinity of an SH3 domain for the purpose of creating reagents to be used in biochemical purification or cell perturbation studies.

Indexed as

src Homology DomainsAnimalsBiochemistryCombinatorial Chemistry TechniquesComputational BiologyHumansLigandsPeptide LibraryPeptidesProlineProtein BindingProtein Interaction MappingProtein Structure, TertiaryProteomicsLigandsPeptide LibraryPeptidesProline

Identifiers

PMID22683951
PMCPMC3572761
OpenAlexW2112220065

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.