Evidence map›Paper›PMID 34068055›Full record

ReviewCells2021

Novel Roles of SH2 and SH3 Domains in Lipid Binding.

Szabolcs Sipeki, Kitti Koprivanacz, Tamás Takács, Anita Kurilla, Loretta László, Virag Vas, László Buday

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

10 citing papers in PubMed, 19 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

7 authors at 2 institutions in 1 country.

Szabolcs SipekiDepartment of Molecular Biology, Institute of Biochemistry and Molecular Biology, Semmelweis University Medical School, 1094 Budapest, Hungary.
Kitti KoprivanaczInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Tamás TakácsInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Anita KurillaInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Loretta LászlóInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.
Virag VasInstitute of Enzymology, Research Centre for Natural Sciences, 1117 Budapest, Hungary.ORCID 0000-0001-7249-6816
László BudayDepartment of Molecular Biology, Institute of Biochemistry and Molecular Biology, Semmelweis University Medical School, 1094 Budapest, Hungary.
Institute of Molecular Life Sciences · HUSemmelweis University · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Signal transduction, the ability of cells to perceive information from the surroundings and alter behavior in response, is an essential property of life. Studies on tyrosine kinase action fundamentally changed our concept of cellular regulation. The induced assembly of subcellular hubs via the recognition of local protein or lipid modifications by modular protein interactions is now a central paradigm in signaling. Such molecular interactions are mediated by specific protein interaction domains. The first such domain identified was the SH2 domain, which was postulated to be a reader capable of finding and binding protein partners displaying phosphorylated tyrosine side chains. The SH3 domain was found to be involved in the formation of stable protein sub-complexes by constitutively attaching to proline-rich surfaces on its binding partners. The SH2 and SH3 domains have thus served as the prototypes for a diverse collection of interaction domains that recognize not only proteins but also lipids, nucleic acids, and small molecules. It has also been found that particular SH2 and SH3 domains themselves might also bind to and rely on lipids to modulate complex assembly. Some lipid-binding properties of SH2 and SH3 domains are reviewed here.

Indexed as

src Homology DomainsAnimalsBinding SitesHumansPhospholipidsPhosphorylationProtein BindingProtein Interaction Domains and MotifsSignal Transductionsrc-Family KinasesStructure-Activity RelationshipPhospholipidssrc-Family Kinaseslipid bindingproline-rich sequencesprotein tyrosine kinaseSH2 domainSH3 domainSrc

Identifiers

PMID34068055
PMCPMC8152464
OpenAlexW3163586240

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.