Evidence map›Paper›PMID 18616971›Full record

ReviewProgress in neurobiology2008

Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.

Scott L Hooper, Kevin H Hobbs, Jeffrey B Thuma

Open access · greenAbstract readReview
In one paragraph

Review in Progress in neurobiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.9field-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

44 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. Review
  3. Two Forms of Thick Filament in the Flight Muscle ofInternational journal of molecular sciences · 2024
    Article
  4. Article
  5. Structure of theInternational journal of molecular sciences · 2023
    Article
  6. Article
  7. Article
  8. Structure of the Flight Muscle Thick Filament from the Bumble Bee,International journal of molecular sciences · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Soft-surface grasping: radular opening inThe Journal of experimental biology · 2019
    Article
  16. Review
  17. Article
  18. Smooth muscle-like CaScientific reports · 2018
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Scott L HooperNeuroscience Program, Department of Biological Sciences, Ohio University, Athens, OH 45701, United States. hooper@ohio.edu
Kevin H Hobbs
Jeffrey B Thuma
Ohio University · US

Funding

PHASE MAINTENANCE, NEURON PROPERTIES TO MUSCLE RESPONSER01MH057832 · NIMH · OHIO UNIVERSITY ATHENS · PI HOOPER, SCOTT L · 1998 to 2007
$1.4M
NIMH NIH HHS R01 MH057832
6 · The paper itself

Abstract

This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vertebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca(++) binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

Indexed as

ActinsActomyosinAnimalsCytoskeletonInvertebratesMuscle ContractionMuscle, SkeletalMyosinsVertebratesActinsActomyosinMyosins

Identifiers

PMID18616971
PMCPMC2650078
OpenAlexW2052781326

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.