Evidence map›Paper›PMID 8078908›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

cAMP-dependent phosphorylation of Aplysia twitchin may mediate modulation of muscle contractions by neuropeptide cotransmitters.

W C Probst, E C Cropper, J Heierhorst, S L Hooper, H Jaffe, F Vilim, S Beushausen, I Kupfermann, K R Weiss

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Review
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  5. A force-activated kinase in a catch smooth muscle.Journal of muscle research and cell motility · 2011
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  11. Titin/connectin-related proteins in C. elegans: a review and new findings.Journal of muscle research and cell motility · 2005
    Review
  12. Article
  13. 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
  14. Article
  15. Article
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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

9 authors at 1 institution in 1 country.

W C ProbstDepartment of Physiology and Biophysics, Mount Sinai School of Medicine, New York, NY 10029.
E C Cropper
J Heierhorst
S L Hooper
H Jaffe
F Vilim
S Beushausen
I Kupfermann
K R Weiss
Icahn School of Medicine at Mount Sinai · US

Funding

NEURAL BASIS OF BEHAVIORAL PLASTICITY IN A SIMPLE SYSTEMR01MH051393 · NIMH · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI CROPPER, ELIZABETH C · 1993 to 2016
$6.1M
NEURAL BASIS OF BEHAVIORAL AROUSALR01MH036730 · NIMH · NEW YORK STATE PSYCHIATRIC INSTITUTE · PI WEISS, KLAUDIUSZ ROBERT · 1985 to 2007
$3.3M
SYNAPTIC PLASTICITY AT SENSORY SYNAPSESP01GM032099 · NIGMS · NEW YORK STATE PSYCHIATRIC INSTITUTE · PI KUPFERMANN, IRVING · 1985 to 1996
–
NEURAL BASIS OF BEHAVIORAL AROUSALR37MH036730 · NIMH · NEW YORK STATE PSYCHIATRIC INSTITUTE · PI WEISS, KLAUDIUSZ ROBERT · 1988 to 1997
–
NIGMS NIH HHS GM32099NIMH NIH HHS MH36730NIMH NIH HHS MH51393
6 · The paper itself

Abstract

Acting through a cAMP-cAMP-dependent protein kinase (cAPK) cascade, members of two neuropeptide families, the small cardioactive peptides and myomodulins, modulate contraction amplitude and relaxation rate in the accessory radula closer (ARC) muscle of the marine mollusc Aplysia californica. An approximately 750-kDa phosphoprotein was identified in the ARC muscle as the major substrate for cAPK activated either by application of neuropeptides or by peptides released by motorneuron stimulation at physiological frequencies. Immunoblot and immunoelectron microscopy experiments revealed the widespread presence of this protein in Aplysia muscles and its colocalization with contractile filaments in the ARC muscle. Sequence analysis of proteolytic peptide fragments derived from the protein indicated that it is structurally related to the muscle protein twitchin. Finally, the level of neuropeptide-induced phosphorylation of the protein correlated well with peptidergic modulation of the relaxation rate of the muscle. We propose that twitchin in Aplysia, and perhaps in other species, may mediate the modulation of the relaxation rate of muscle contractions.

Indexed as

Calmodulin-Binding ProteinsMuscle ContractionMuscle RelaxationAmino Acid SequenceAnimalsAplysiaBase SequenceCaenorhabditis elegans ProteinsCyclic AMPCyclic AMP-Dependent Protein KinasesHelminth ProteinsMolecular Sequence DataMuscle ProteinsNeuromuscular JunctionNeuropeptidesPhosphorylationCaenorhabditis elegans ProteinsCalmodulin-Binding ProteinsCyclic AMPCyclic AMP-Dependent Protein KinasesHelminth ProteinsMuscle ProteinsNeuropeptidesunc-22 protein, C elegans

Identifiers

PMID8078908
PMCPMC44631
OpenAlexW2061788181

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.