Evidence map›Paper›PMID 28232900›Full record

ArticleIntrinsically disordered proteins2016

Intrinsic disorder in spondins and some of their interacting partners.

Oluwole Alowolodu, Gbemisola Johnson, Lamis Alashwal, Iqbal Addou, Irina V Zhdanova, Vladimir N Uversky

Open access · bronzeAbstract read
In one paragraph

Article in Intrinsically disordered proteins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.5field-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

9 citing papers in PubMed, 14 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

6 authors at 2 institutions in 2 countries.

Oluwole AlowoloduDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida , Tampa, FL, USA.
Gbemisola JohnsonDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida , Tampa, FL, USA.
Lamis AlashwalDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida , Tampa, FL, USA.
Iqbal AddouDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida , Tampa, FL, USA.
Irina V ZhdanovaDepartment of Anatomy & Neurobiology, Boston University School of Medicine , Boston, MA, USA.
Vladimir N UverskyDepartment of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA; USF Health Byrd Alzheimer Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.
University of South Florida · USBoston University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Spondins, which are proteins that inhibit and promote adherence of embryonic cells so as to aid axonal growth are part of the thrombospondin-1 family. Spondins function in several important biological processes, such as apoptosis, angiogenesis, etc. Spondins constitute a thrombospondin subfamily that includes F-spondin, a protein that interacts with Aβ precursor protein and inhibits its proteolytic processing; R-spondin, a 4-membered group of proteins that regulates Wnt pathway and have other functions, such as regulation of kidney proliferation, induction of epithelial proliferation, the tumor suppressant action; M-spondin that mediates mechanical linkage between the muscles and apodemes; and the SCO-spondin, a protein important for neuronal development. In this study, we investigated intrinsic disorder status of human spondins and their interacting partners, such as members of the LRP family, LGR family, Frizzled family, and several other binding partners in order to establish the existence and importance of disordered regions in spondins and their interacting partners by conducting a detailed analysis of their sequences, finding disordered regions, and establishing a correlation between their structure and biological functions.

Indexed as

intrinsically disordered proteinintrinsically disordered protein regionsposttranslational modificationsprotein functionprotein structurespondin

Identifiers

PMID28232900
PMCPMC5314907
OpenAlexW2566939916

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.