Evidence map›Paper›PMID 28004021›Full record

ArticleData in brief2017

Data on evolution of intrinsically disordered regions of the human kinome and contribution of FAK1 IDRs to cytoskeletal remodeling.

Jaymin J Kathiriya, Ravi Ramesh Pathak, Alexandr Bezginov, Bin Xue, Vladimir N Uversky, Elisabeth R M Tillier, Vrushank Davé

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Data in brief, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
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 4 institutions in 3 countries.

Jaymin J KathiriyaMorsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, USA.
Ravi Ramesh PathakMorsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, USA.
Alexandr BezginovDepartment of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
Bin XueDepartment of Cell Biology, Microbiology and Molecular Biology, University of South Florida, Tampa, FL 33620, USA.
Vladimir N UverskyDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA; USF Health Byrd Alzheimer׳s Research Institute, University of South Florida, Tampa, FL 33612, USA; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russian Federation.
Elisabeth R M TillierDepartment of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
Vrushank DavéMorsani College of Medicine, Department of Pathology and Cell Biology, University of South Florida, Tampa, FL 33612, USA; Department of Cancer Biology and Evolution, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, USA.
University of South Florida · USUniversity of Toronto · CAInstitute of Cytology · RUMoffitt Cancer Center · US

Funding

Hypoxia Signaling and Spontaneous Pulmonary Fibrosis in a Novel Mouse ModelR21AG047473 · NIA · UNIVERSITY OF SOUTH FLORIDA · PI DAVE, VRUSHANK · 2015 to 2016
$426k
NIA NIH HHS R21 AG047473
6 · The paper itself

Abstract

We present data on the evolution of intrinsically disordered regions (IDRs) taking into account the entire human protein kinome. The evolutionary data of the IDRs with respect to the kinase domains (KDs) and kinases as a whole protein (WP) are reported. Further, we have reported its post translational modifications of FAK1 IDRs and their contribution to the cytoskeletal remodeling. We also report the data to build a protein-protein interaction (PPI) network of primary and secondary FAK1-interacting hybrid proteins. Detailed analysis of the data and its effect on FAK1-related functions have been described in "Structural pliability adjacent to the kinase domain highlights contribution of FAK1 IDRs to cytoskeletal remodeling" (Kathiriya et. al., 2016) [1].

Indexed as

Cytoskeletal remodelingEvolution of intrinsically disordered regionsFocal adhesion Kinase-1Protein kinases

Identifiers

PMID28004021
PMCPMC5157709
OpenAlexW2560372296

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.