Evidence map›Paper›PMID 35563177›Full record

ArticleInternational journal of molecular sciences2022

Regulation of Poly-E Motif Flexibility by pH, Ca

Sudarshi Premawardhana Dassanayake Mudiyanselage, Matthew J Gage

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 52% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Sudarshi Premawardhana Dassanayake MudiyanselageDepartment of Chemistry, University of Massachusetts Lowell, Lowell, MA 01854, USA.
Matthew J GageDepartment of Chemistry, University of Massachusetts Lowell, Lowell, MA 01854, USA.ORCID 0000-0003-2304-6960
University of Massachusetts Lowell · US

Funding

Exploring the role of pH in protein conformational change and muscle elasticityR15GM132840 · NIGMS · UNIVERSITY OF MASSACHUSETTS LOWELL · PI GAGE, MATTHEW J · 2019 to 2019
$457k
NIGMS NIH HHS R15 GM132840NIH HHS R15GM132840-01
6 · The paper itself

Abstract

The disordered PEVK region of titin contains two main structural motifs: PPAK and poly-E. The distribution of these motifs in the PEVK region contributes to the elastic properties of this region, but the specific mechanism of how these motifs work together remains unclear. Previous work from our lab has demonstrated that 28-amino acid peptides of the poly-E motif are sensitive to shifts in pH, becoming more flexible as the pH decreases. We extend this work to longer poly-E constructs, including constructs containing PPAK motifs. Our results demonstrate that longer poly-E motifs have a much larger range of pH sensitivity and that the inclusion of the PPAK motif reduces this sensitivity. We also demonstrate that binding calcium can increase the conformational flexibility of the poly-E motif, though the PPAK motif can block this calcium-dependent change. The data presented here suggest a model where PPAK and calcium can alter the stiffness of the poly-E motif by modulating the degree of charge repulsion in the glutamate clusters.

Indexed as

CalciumMuscle ProteinsAmino Acid SequenceConnectinHydrogen-Ion ConcentrationPeptidesCalciumConnectinMuscle ProteinsPeptidesintrinsically disordered proteinPEVKpHpoly-Etitin

Identifiers

PMID35563177
PMCPMC9100103
OpenAlexW4224986471

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.