Evidence map›Paper›PMID 8906622›Full record

ArticleJournal of muscle research and cell motility1996

Sequence variations in the surface loop near the nucleotide binding site modulate the ATP turnover rates of molluscan myosins.

C L Perreault-Micale, V N Kalabokis, L Nyitray, A G Szent-Györgyi

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

10 citing papers in PubMed, 54 citations in OpenAlex.

  1. Alpha and beta myosin isoforms and human atrial and ventricular contraction.Cellular and molecular life sciences : CMLS · 2021
    Review
  2. Tuning of shortening speed in coleoid cephalopod muscle: no evidence for tissue-specific muscle myosin heavy chain isoforms.Invertebrate biology : a quarterly journal of the American Microscopical Society and the Division of Invertebrate Zoology/ASZ · 2016
    Article
  3. Article
  4. Article
  5. Article
  6. Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  7. Article
  8. Review
  9. An in vitro assay reveals essential protein components for the "catch" state of invertebrate smooth muscle.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  10. Regulation by molluscan myosins.Molecular and cellular biochemistry · 1999
    Review
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

4 authors at 1 institution in 1 country.

C L Perreault-MicaleDepartment of Biology, Brandeis University, Waltham, MA 02254-9110, USA.
V N Kalabokis
L Nyitray
A G Szent-Györgyi
Brandeis University · US

Funding

REGULATION IN STRIATED, SMOOTH, AND CARDIAC MUSCLESR01AR015963 · NIAMS · BRANDEIS UNIVERSITY · PI SZENT-GYORGYI, ANDREW G · 1986 to 1986
–
REGULATORY DOMAIN/S1 CRYSTAL STRUCTURE--SCALLOP MYOSINR01AR041808 · NIAMS · BRANDEIS UNIVERSITY · PI COHEN, CAROLYN · 1995 to 1999
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REGULATION IN STRIATED SMOOTH &CARDIAC MUSCLESR37AR015963 · NIAMS · BRANDEIS UNIVERSITY · PI SZENT-GYORGYI, ANDREW G · 1987 to 1996
–
NIAMS NIH HHS AR15963NIAMS NIH HHS AR41808
6 · The paper itself

Abstract

The muscle and species-specific differences in enzymatic activity between Placopecten and Argopecten striated and catch muscle myosins are attributable to the myosin heavy chain. To identify sequences that may modulate these differences, we cloned and sequenced the cDNA encoding the myosin heavy chains of Placopecten striated and catch muscle. Deduced protein sequences indicate two similar isoforms in catch and striated myosins (97% identical); variations arise by differential RNA splicing of five alternative exons from a single myosin heavy chain gene. The first encodes the phosphate-binding loop; the second, part of the ATP binding site; the third, part of the actin binding site; the fourth, the hinge in the rod; and the fifth, a tailpiece found only in the catch muscle myosin heavy chain. Both Placopecten myosin heavy chains are 96% identical to Argopecten myosin heavy chaina isoforms. Because subfragment-1 ATPase activities reflect the differences observed in the parent myosins, the motor domain is responsible for the variations in ATPase activities. In addition, data show that differences are due to Vmax and not actin affinity. The sequences of all four myosin heavy chain motor domains diverge only in the flexible surface loop near the nucleotide binding pocket. Thus, the different ATPase activities of four molluscan muscle myosins are likely due to myosin heavy chain sequence variations within the flexible surface loop that forms part of the ATP binding pocket of the motor domain.

Indexed as

ActinsAdenosine TriphosphateAmino Acid SequenceAnimalsBase SequenceCa(2+) Mg(2+)-ATPaseElectrophoresis, Polyacrylamide GelMolecular Sequence DataMolluscaMuscle, SkeletalMyosinsActinsAdenosine TriphosphateCa(2+) Mg(2+)-ATPaseMyosins

Identifiers

PMID8906622
OpenAlexW1986070866

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.