Evidence map›Paper›PMID 7787052›Full record

ArticleBiophysical journal1995

Function of the N terminus of the myosin essential light chain of vertebrate striated muscle.

H L Sweeney

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 69 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

1 author at 1 institution in 1 country.

H L SweeneyDepartment of Physiology, University of Pennsylvania School of Medicine, Philadelphia 19104-6085, USA.
University of Pennsylvania · US

Funding

PHYSIOLOGY AND MYOSIN ISOZYMES OF SKELETAL MUSCLE FIBERSR01AR035661 · NIAMS · UNIVERSITY OF TEXAS AUSTIN · PI SWEENEY, H LEE · 1986 to 2010
$3.7M
NIAMS NIH HHS AR-35661
6 · The paper itself

Abstract

All but one (LC3-f; a fast skeletal muscle isoform) of the essential light chain isoforms of myosin (ELC) that are expressed in vertebrate striated muscles have an extended N terminus that is found neither in invertebrate ELCs nor in the majority of vertebrate smooth and nonmuscle myosin ELCs. Studies with permeabilized skeletal muscle fibers and in vitro motility assays have demonstrated that the presence of the ELC isoform lacking the N-terminal extension (LC3-f) is correlated with an increased maximal velocity of filament sliding. To examine further this modulatory role of the ELCs, a procedure was developed for the exchange of ELCs that is based on a technique for the removal of regulatory light chains from permeabilized muscle fibers. Different isoforms of the ELCs and mutant ELCs were exchanged into permeabilized skeletal muscle fibers from rabbit psoas muscle. The role of the ELCs of myosin in altering the shortening Vmax of striated muscle was confirmed. Additionally, experiments with mutant ELCs in which lysines at the extreme N terminus were replaced with alanines, demonstrated an increased shortening Vmax that coincided with removal of the positive charges contributed by the lysines. This suggests that charge interactions (i.e., salt bridges) between the N terminus of the ELC and negatively charged amino acids on the surface of actin cause a slowing of filament sliding. Whether this role in altering shortening velocity is the primary function of the extended N terminus of the ELC or whether it is merely a consequence of providing a tether between the thick and thin filaments is discussed.

Indexed as

Amino Acid SequenceAnimalsBiophysical PhenomenaBiophysicsFemaleIn Vitro TechniquesMolecular Sequence DataMuscle ContractionMutagenesis, Site-DirectedMyosinsPsoas MusclesRabbitsRatsMyosins

Identifiers

PMID7787052
PMCPMC1281889
OpenAlexW1735876679

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.