Evidence map›Paper›PMID 2045132›Full record

ReviewHypertension (Dallas, Tex. : 1979)1991

Vascular smooth muscle contractile elements. Cellular regulation.

J T Stull, P J Gallagher, B P Herring, K E Kamm

Open access · bronzeAbstract readReview
In one paragraph

Review in Hypertension (Dallas, Tex. : 1979), 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
8.4field-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

24 citing papers in PubMed, 94 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Potential Benefits of Peroxynitrite.The open pharmacology journal · 2008
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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
  16. Article
  17. Article
  18. Article
  19. Calcium and smooth muscle contraction.Molecular and cellular biochemistry · 1994
    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 1 institution in 1 country.

J T StullDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas 75235-9040.
P J Gallagher
B P Herring
K E Kamm
The University of Texas Southwestern Medical Center · US

Funding

MYOSIN LIGHT CHAIN KINASE FUNCTION IN SMOOTH MUSCLER01HL026043 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI STULL, JAMES T · 1985 to 2009
$3.4M
BIOCHEMICAL MECHANISMS OF SMOOTH MUSCLE CONTRACTIONR37HL026043 · NHLBI · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI STULL, JAMES T · 1991 to 1999
–
NHLBI NIH HHS R01 HL026043NHLBI NIH HHS R37 HL026043
6 · The paper itself

Abstract

For many years the simple view was held that contractile force in smooth muscle was proportional to cytosolic Ca2+ concentrations ([Ca2+]i). With the discovery that phosphorylation of myosin light chain by Ca2+/calmodulin-dependent myosin light chain kinase initiated contraction, regulation of the contractile elements developed more complex properties. Molecular and biochemical investigations have identified important domains of myosin light chain kinase: light chain binding sites, catalytic core, pseudosubstrate prototope, and calmodulin-binding domain. New protein phosphatase inhibitors such as okadaic acid and calyculin A should help in the identification of the physiologically important phosphatase and potential modes of regulation. The proposal of an attached, dephosphorylated myosin cross bridge (latch bridge) that can maintain force has evoked considerable controversy about the detailed functions of the myosin phosphorylation system. The latch bridge has been defined by a model based on physiological properties but has not been identified biochemically. Thin-filament proteins have been proposed as secondary sites of regulation of contractile elements, but additional studies are needed to establish physiological roles. Changes in the Ca2+ sensitivity of smooth muscle contractile elements with different modes of cellular stimulation may be related to inactivation of myosin light chain kinase or activation of protein phosphatase activities. Thus, contractile elements in smooth muscle cells are not dependent solely on [Ca2+]i but use additional regulatory mechanisms. The immediate challenge is to define their relative importance and to describe molecular-biochemical properties that provide insights into proposed physiological functions.

Indexed as

Muscle ContractionAmino Acid SequenceAnimalsHumansMolecular Sequence DataMuscle ProteinsMuscle, Smooth, VascularMuscle Proteins

Identifiers

PMID2045132
PMCPMC2836766
OpenAlexW2151180509

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.