Evidence map›Paper›PMID 33255942›Full record

SynthesisMolecules (Basel, Switzerland)2020

Deciphering the Role of Filamin B Calponin-Homology Domain in Causing the Larsen Syndrome, Boomerang Dysplasia, and Atelosteogenesis Type I Spectrum Disorders via a Computational Approach.

Udhaya Kumar S, Srivarshini Sankar, Salma Younes, Thirumal Kumar D, Muneera Naseer Ahmad, Sarah Samer Okashah, Balu Kamaraj, Abeer Mohammed Al-Subaie, George Priya Doss C, Hatem Zayed

Open access · goldAbstract readMeta-Analysis
In one paragraph

Synthesis in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 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

10 authors at 3 institutions in 3 countries.

Udhaya Kumar SSchool of Biosciences and Technology, Vellore Institute of Technology, Vellore, Tamil Nadu 632014, India.
Srivarshini SankarSchool of Biosciences and Technology, Vellore Institute of Technology, Vellore, Tamil Nadu 632014, India.
Salma YounesDepartment of Biomedical Sciences, College of Health and Sciences, Qatar University, QU Health, Doha 2713, Qatar.
Thirumal Kumar DSchool of Biosciences and Technology, Vellore Institute of Technology, Vellore, Tamil Nadu 632014, India.
Muneera Naseer AhmadDepartment of Biomedical Sciences, College of Health and Sciences, Qatar University, QU Health, Doha 2713, Qatar.
Sarah Samer OkashahDepartment of Biomedical Sciences, College of Health and Sciences, Qatar University, QU Health, Doha 2713, Qatar.
Balu KamarajDepartment of Neuroscience Technology, College of Applied Medical Sciences in Jubail, Imam Abdulrahman Bin Faisal University, Jubail 35816, Saudi Arabia.ORCID 0000-0002-9747-3984
Abeer Mohammed Al-SubaieDepartment of Clinical Laboratory Sciences, College of Applied Medical Sciences, Imam Abdulrahman Bin Faisal University, Dammam 31441, Saudi Arabia.
George Priya Doss CSchool of Biosciences and Technology, Vellore Institute of Technology, Vellore, Tamil Nadu 632014, India.
Hatem ZayedDepartment of Biomedical Sciences, College of Health and Sciences, Qatar University, QU Health, Doha 2713, Qatar.ORCID 0000-0001-8838-6638
Qatar University · QAVellore Institute of Technology University · INImam Abdulrahman Bin Faisal University · SA

Funding

Qatar University QUST-2-CHS-2020- 12
6 · The paper itself

Abstract

Filamins (FLN) are a family of actin-binding proteins involved in regulating the cytoskeleton and signaling phenomenon by developing a network with F-actin and FLN-binding partners. The FLN family comprises three conserved isoforms in mammals: FLNA, FLNB, and FLNC. FLNB is a multidomain monomer protein with domains containing an actin-binding N-terminal domain (ABD 1-242), encompassing two calponin-homology domains (assigned CH1 and CH2). Primary variants in FLNB mostly occur in the domain (CH2) and surrounding the hinge-1 region. The four autosomal dominant disorders that are associated with

Indexed as

Models, MolecularProtein DomainsCalcium-Binding ProteinsCalponinsChemical PhenomenaDwarfismEvolution, MolecularFaciesFilaminsGenetic VariationHumansMicrofilament ProteinsMolecular Dynamics SimulationMutationOsteochondrodysplasiasPolymorphism, Single NucleotideCalcium-Binding ProteinsCalponinsFilaminsMicrofilament ProteinsSolventsatelosteogenesis type Iboomerang dysplasiaCH2 domainFLNBLarsen syndromemolecular dynamics simulation (MDS)

Identifiers

PMID33255942
PMCPMC7730838
OpenAlexW3109848354

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.