Evidence map›Paper›PMID 11909967›Full record

ArticleMolecular and cellular biology2002

Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase.

Gaohua Liu, Cristina D Guibao, Jie Zheng

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
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  5. Article
  6. Review
  7. FAK Signaling in Rhabdomyosarcoma.International journal of molecular sciences · 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

3 authors at 2 institutions in 1 country.

Gaohua LiuDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
Cristina D Guibao
Jie Zheng
St. Jude Children's Research Hospital · USUniversity of Tennessee Health Science Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase whose focal adhesion targeting (FAT) domain interacts with other focal adhesion molecules in integrin-mediated signaling. Localization of activated FAK to focal adhesions is indispensable for its function. Here we describe a solution structure of the FAT domain bound to a peptide derived from paxillin, a FAK-binding partner. The FAT domain is composed of four helices that form a "right-turn" elongated bundle; the globular fold is mainly maintained by hydrophobic interactions. The bound peptide further stabilizes the structure. Certain signaling events such as phosphorylation and molecule interplay may induce opening of the helix bundle. Such conformational change is proposed to precede departure of FAK from focal adhesions, which starts focal adhesion turnover.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsBinding SitesChickensCytoskeletal ProteinsFocal Adhesion Protein-Tyrosine KinasesIn Vitro TechniquesMacromolecular SubstancesModels, MolecularMolecular Sequence DataPaxillinPhosphoproteinsProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryCytoskeletal ProteinsFocal Adhesion Protein-Tyrosine KinasesMacromolecular SubstancesPaxillinPhosphoproteinsProtein-Tyrosine KinasesRecombinant Proteins

Identifiers

PMID11909967
PMCPMC133741
OpenAlexW2052639416

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.