Evidence map›Paper›PMID 11032348›Full record

ArticleJournal of muscle research and cell motility2000

Functional diversity between orthologous myosins with minimal sequence diversity.

M Canepari, R Rossi, M A Pellegrino, R Bottinelli, S Schiaffino, C Reggiani

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
  2. Actomyosin interaction at low ATP concentrations.European biophysics journal : EBJ · 2017
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Myosin as a potential redox-sensor: an in vitro study.Journal of muscle research and cell motility · 2008
    Article
  10. Article
  11. Two independent mechanical events in the interaction cycle of skeletal muscle myosin with actin.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  12. Article
  13. 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

6 authors at 2 institutions in 1 country.

M CanepariInstitute of Human Physiology, University of Pavia, Italy.
R Rossi
M A Pellegrino
R Bottinelli
S Schiaffino
C Reggiani
University of Pavia · ITUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To define the structural differences that are responsible for the functional diversity between orthologous sarcomeric myosins, we compared the rat and human beta/slow myosins. Functional comparison showed that rat beta/slow myosin has higher ATPase activity and moves actin filaments at higher speed in in vitro motility assay than human beta/slow myosin. Sequence analysis shows that the loop regions at the junctions of the 25 and 50 kDa domains (loop 1) and the 50 and 20 kDa domains (loop 2), which have been implicated in determining functional diversity of myosin heavy chains, are essentially identical in the two orthologs. There are only 14 non-conservative substitutions in the two myosin heavy chains, three of which are located in the secondary actin-binding loop and flanking regions and others correspond to residues so far not assigned a functional role, including two residues in the proximal S2 domain. Interestingly, in some of these positions the rat beta/slow myosin heavy chain has the same residues found in human cardiac alpha myosin, a fast-type myosin, and fast skeletal myosins. These observations indicate that functional and structural analysis of myosin orthologs with limited sequence diversity can provide useful clues to identify amino acid residues involved in modulating myosin function.

Indexed as

ActinsAdenosine TriphosphatasesAmino Acid SequenceAnimalsGenetic VariationHumansMolecular Sequence DataMyosin Heavy ChainsRatsRats, WistarSarcomeresSequence AlignmentActinsAdenosine TriphosphatasesMyosin Heavy Chains

Identifiers

PMID11032348
OpenAlexW135427814

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.