Evidence map›Paper›PMID 1378447›Full record

ArticleThe Journal of cell biology1992

Biochemical and immunological characterization of p190-calmodulin complex from vertebrate brain: a novel calmodulin-binding myosin.

F S Espindola, E M Espreafico, M V Coelho, A R Martins, F R Costa, M S Mooseker, R E Larson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1992. 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
7.4field-weighted citation impact, top 2% 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, 112 citations in OpenAlex.

  1. Discovery of the first unconventional myosin:Frontiers in physiology · 2023
    Review
  2. Article
  3. The Role of Calmodulin vs. Synaptotagmin in Exocytosis.Frontiers in molecular neuroscience · 2021
    Review
  4. Myosin Va is developmentally regulated and expressed in the human cerebellum from birth to old age.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2013
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. The kinetic mechanism of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  15. Article
  16. Article
  17. Article
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  19. Article
  20. Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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

7 authors at 1 institution in 1 country.

F S EspindolaDepartment of Biochemistry, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, Brazil.
E M Espreafico
M V Coelho
A R Martins
F R Costa
M S Mooseker
R E Larson
Universidade de Ribeirão Preto · BR

Funding

CYTOSKELETAL STRUCTURE AND CONTRACTILITY IN BRUSH BORDERR01AM025387 · AM · YALE UNIVERSITY · PI MOOSEKER, MARK S · 1985 to 1985
–
NIADDK NIH HHS AM 25387
6 · The paper itself

Abstract

We have recently identified a novel 190-kD calmodulin-binding protein (p190) associated with the actin-based cytoskeleton from mammalian brain (Larson, R. E., D. E. Pitta, and J. A. Ferro. 1988. Braz. J. Med. Biol. Res. 21:213-217; Larson, R. E., F. S. Espindola, and E. M. Espreafico. 1990. J. Neurochem. 54:1288-1294). These studies indicated that p190 is a phosphoprotein substrate for calmodulin-dependent kinase II and has calcium- and calmodulin-stimulated MgATPase activity. We now have biochemical and immunological evidence that this protein is a novel calmodulin-binding myosin whose properties include (a) Ca2+ dependent action activation of its Mg-ATPase activity, which seems to be mediated by Ca2+ binding directly to calmodulin(s) associated with p190 (maximal activation by actin requires the presence of Ca2+ and is further augmented by addition of exogenous calmodulin); (b) ATP-sensitive cross-linking of skeletal muscle F-actin, as demonstrated by the low-speed actin sedimentation assay; and (c) cross-reactivity with mAbs specific for epitopes in the head of brush border myosin I. We also show that p190 has properties distinct from conventional brain myosin II and brush border myosin I, including (a) separation of p190 from brain myosin II by gel filtration on a Sephacryl S-500 column; (b) lack by p190 of K(+)-stimulated EDTA ATPase activity characteristic of most myosins; (c) lack of immunological cross-reactivity of polyclonal antibodies which recognize p190 and brain myosin II, respectively; (d) lack of immunological recognition of p190 by mAbs against an epitope in the tail region of brush border myosin I; and (e) distinctive proteolytic susceptibility to calpain. A survey of rat tissues by immunoblotting indicated that p190 is expressed predominantly in the adult forebrain and cerebellum, and could be detected in embryos 11 d post coitus. Immunocytochemical studies showed p190 to be present in the perikarya and dendritic extensions of Purkinje cells of the cerebellum.

Indexed as

Adenosine TriphosphatasesAnimalsAnimals, NewbornBrainCalmodulinCalmodulin-Binding ProteinsChickensCytoskeletal ProteinsElectrophoresis, Polyacrylamide GelEmbryonic and Fetal DevelopmentEpitopesFemaleImmunohistochemistryMaleMolecular WeightMyosinsAdenosine TriphosphatasesCalmodulinCalmodulin-Binding ProteinsCytoskeletal ProteinsEpitopesMyosinsNerve Tissue Proteins

Identifiers

PMID1378447
PMCPMC2290054
OpenAlexW2160337925

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.