Evidence map›Paper›PMID 12668734›Full record

ArticleThe Journal of general physiology2003

Nonmuscle Myosin motor of smooth muscle.

Mia Löfgren, Eva Ekblad, Ingo Morano, Anders Arner

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of general physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Visceral myopathy: clinical syndromes, genetics, pathophysiology, and fall of the cytoskeleton.American journal of physiology. Gastrointestinal and liver physiology · 2021
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Signaling and metabolic properties of fast and slow smooth muscle types from mice.Pflugers Archiv : European journal of physiology · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Smooth muscle-protein translocation and tissue function.Anatomical record (Hoboken, N.J. : 2007) · 2014
    Review
  20. 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

4 authors at 2 institutions in 2 countries.

Mia LöfgrenDepartment of Physiological Sciences, Medical Faculty, Lund University, SE-221 84 Lund, Sweden.
Eva Ekblad
Ingo Morano
Anders Arner
Lund University · SEMax Delbrück Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonmuscle myosin can generate force and shortening in smooth muscle, as revealed by studies of the urinary bladder from mice lacking smooth muscle myosin heavy chain (SM-MHC) but expressing the nonmuscle myosin heavy chains A and B (NM-MHC A and B; Morano, I., G.X. Chai, L.G. Baltas, V. Lamounier-Zepter, G. Lutsch, M. Kott, H. Haase, and M. Bader. 2000. Nat. Cell Biol. 2:371-375). Intracellular calcium was measured in urinary bladders from SM-MHC-deficient and SM-MHC-expressing mice in relaxed and contracted states. Similar intracellular [Ca2+] transients were observed in the two types of preparations, although the contraction of SM-MHC-deficient bladders was slow and lacked an initial peak in force. The difference in contraction kinetics thus do not reflect differences in calcium handling. Thick filaments were identified with electron microscopy in smooth muscle cells of SM-MHC-deficient bladders, showing that NM-MHC can form filaments in smooth muscle cells. Maximal shortening velocity of maximally activated, skinned smooth muscle preparations from SM-MHC-deficient mice was significantly lower and more sensitive to increased MgADP compared with velocity of SM-MHC-expressing preparations. Active force was significantly lower and less inhibited by increased inorganic phosphate. In conclusion, large differences in nucleotide and phosphate binding exist between smooth and nonmuscle myosins. High ADP binding and low phosphate dependence of nonmuscle myosin would influence both velocity of actin translocation and force generation to promote slow motility and economical force maintenance of the cell.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateAnimalsCalciumIsometric ContractionMiceMice, TransgenicMolecular Motor ProteinsMuscle ContractionMuscle, SmoothMyosin Heavy ChainsNonmuscle Myosin Type IIBPhosphatesSmooth Muscle MyosinsUrinary BladderAdenosine DiphosphateAdenosine TriphosphateCalciumMolecular Motor ProteinsMyosin Heavy ChainsNonmuscle Myosin Type IIBnonmuscle myosin type IIB heavy chainPhosphatesSmooth Muscle Myosins

Identifiers

PMID12668734
PMCPMC2217371
OpenAlexW2165186349

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.