Evidence map›Paper›PMID 2480352›Full record

ArticleThe Journal of cell biology1989

Monoclonal antibodies detect and stabilize conformational states of smooth muscle myosin.

K M Trybus, L Henry

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

15 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  9. Article
  10. Article
  11. Distribution of developmental myosin isoforms in isolated A-segments.Journal of muscle research and cell motility · 1992
    Article
  12. Probing myosin light chain 1 structure with monoclonal antibodies.Journal of muscle research and cell motility · 1992
    Article
  13. Article
  14. Article
  15. 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

2 authors at 1 institution in 1 country.

K M TrybusRosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254-9110.
L Henry
Brandeis University · US

Funding

SMOOTH MUSCLE MYOSIN--CONFORMATION AND ACTIVITYR01HL038113 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1993 to 2011
$3.9M
CHEMISTRY OF MUSCLE PROTEINSR01AR017350 · NIAMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI LOWEY, SUSAN · 1996 to 2000
$438k
VASCULAR SMOOTH MUSCLE MYOSIN--CONFORMATION &ACTIVITYR29HL038113 · NHLBI · BRANDEIS UNIVERSITY · PI TRYBUS, KATHLEEN M · 1987 to 1991
–
CHEMISTRY OF MUSCLE PROTEINSR37AR017350 · NIAMS · BRANDEIS UNIVERSITY · PI LOWEY, SUSAN · 1986 to 1995
–
NHLBI NIH HHS HL38113NIAMS NIH HHS AR17350
6 · The paper itself

Abstract

Antibodies with epitopes near the heavy meromyosin/light meromyosin junction distinguish the folded from the extended conformational states of smooth muscle myosin. Antibody 10S.1 has 100-fold higher avidity for folded than for extended myosin, while antibody S2.2 binds preferentially to the extended state. The properties of these antibodies provide direct evidence that the conformation of the rod is different in the folded than the extended monomeric state, and suggest that this perturbation may extend into the subfragment 2 region of the rod. Two antihead antibodies with epitopes on the heavy chain map at or near the head/rod junction. Magnesium greatly enhances the binding of these antibodies to myosin, showing that the conformation of the heavy chain in the neck region changes upon divalent cation binding to the regulatory light chain. Myosin assembly is also altered by antibody binding. Antibodies that bind to the central region of the rod block disassembly of filaments upon MgATP addition. Antibodies with epitopes near the COOH terminus of the rod, in contrast, promote filament depolymerization, suggesting that this region of the tail is important for assembly. The monoclonal antibodies described here are therefore useful both for detecting and altering conformational states of smooth muscle myosin.

Indexed as

Antibodies, MonoclonalAnimalsAntigen-Antibody ComplexEnzyme-Linked Immunosorbent AssayEpitopesGizzard, AvianImmunoblottingKineticsMiceMice, Inbred StrainsMicroscopy, ElectronMuscle, SmoothMyosinsProtein ConformationTurkeysAntibodies, MonoclonalAntigen-Antibody ComplexEpitopesMyosins

Identifiers

PMID2480352
PMCPMC2115922
OpenAlexW2021719716

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.