Evidence map›Paper›PMID 23009691›Full record

ArticleBMC research notes2012

Structural attributes for the recognition of weak and anomalous regions in coiled-coils of myosins and other motor proteins.

Margaret S Sunitha, Anu G Nair, Amol Charya, Kamalakar Jadhav, Sami Mukhopadhyay, Ramanathan Sowdhamini

Open access · goldAbstract read
In one paragraph

Article in BMC research notes, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

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  6. Molecular mechanisms and structural features of cardiomyopathy-causing troponin T mutants in the tropomyosin overlap region.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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 1 institution in 1 country.

Margaret S SunithaNational Centre for Biological Sciences (TIFR), UAS-GKVK Campus, Bellary Road, Bangalore 560 065, India.
Anu G Nair
Amol Charya
Kamalakar Jadhav
Sami Mukhopadhyay
Ramanathan Sowdhamini
National Centre for Biological Sciences · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundCoiled-coils are found in different proteins like transcription factors, myosin tail domain, tropomyosin, leucine zippers and kinesins. Analysis of various structures containing coiled-coils has revealed the importance of electrostatic and hydrophobic interactions. In such domains, regions of different strength of interactions need to be identified since they could be biologically relevant.

findingsWe have updated our coiled-coil validation webserver, now called COILCHECK+, where new features were added to efficiently identify the strength of interaction at the interface region and measure the density of charged residues and hydrophobic residues. We have examined charged residues and hydrophobic ladders, using a new algorithm called CHAHO, which is incorporated within COILCHECK + server. CHAHO permits the identification of spatial charged residue patches and the continuity of hydrophobic ladder which stabilizes and destabilizes the coiled-coil structure.

conclusionsThe availability of such computational tools should be useful to understand the importance of spatial clustering of charged residues and the continuity of hydrophobic residues at the interface region of coiled-coil dimers. COILCHECK + is a structure based tool to validate coiled-coil stability; it can be accessed at http://caps.ncbs.res.in/coilcheckplus.

Indexed as

Databases, ProteinStructural Homology, ProteinAlgorithmsAmino Acid MotifsAnimalsHumansHydrogen BondingHydrophobic and Hydrophilic InteractionsInternetModels, MolecularMolecular Motor ProteinsMyosin Heavy ChainsPattern Recognition, AutomatedProtein ConformationProtein StabilityStatic ElectricityMolecular Motor ProteinsMyosin Heavy Chainsmyosin VITropomyosin

Identifiers

PMID23009691
PMCPMC3542152
OpenAlexW2153538021

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.