Evidence map›Paper›PMID 22930330›Full record

ArticleJournal of muscle research and cell motility2012

Temperature dependent measurements reveal similarities between muscle and non-muscle myosin motility.

Christopher M Yengo, Yasuharu Takagi, James R Sellers

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of muscle research and cell motility, 2012. 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
1.9field-weighted citation impact, top 13% 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, 39 citations in OpenAlex.

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  12. CaATP prolongs strong actomyosin binding and promotes futile myosin stroke.Journal of muscle research and cell motility · 2019
    Article
  13. Article
  14. Microscopic heat pulses activate cardiac thin filaments.The Journal of general physiology · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Tension, contraction and tissue morphogenesis.Development (Cambridge, England) · 2017
    Review
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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

3 authors at 2 institutions in 1 country.

Christopher M YengoDepartment of Cellular and Molecular Physiology, College of Medicine, Pennsylvania State University, 500 University Drive, Hershey, PA 17033, USA. cmy11@psu.edu
Yasuharu Takagi
James R Sellers
National Heart Lung and Blood Institute · USPennsylvania State University · US

Funding

Regulation Of Smooth and Nonmuscle MyosinZIAHL001786 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$17.4M
Enzymatic and Motor Properties of Myosin IIIR01EY018141 · NEI · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI YENGO, CHRISTOPHER M · 2008 to 2012
$1.3M
Energy Transduction in MyosinR21HL093531 · NHLBI · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI YENGO, CHRISTOPHER M · 2009 to 2010
$390k
NEI NIH HHS R01 EY018141NHLBI NIH HHS HL093531NHLBI NIH HHS R21 HL093531PHS HHS EYE018141
6 · The paper itself

Abstract

We examined the temperature dependence of muscle and non-muscle myosin (heavy meromyosin, HMM) with in vitro motility and actin-activated ATPase assays. Our results indicate that myosin V (MV) has a temperature dependence that is similar in both ATPase and motility assays. We demonstrate that skeletal muscle myosin (SK), smooth muscle myosin (SM), and non-muscle myosin IIA (NM) have different temperature dependence in ATPase compared to in vitro motility assays. In the class II myosins we examined (SK, SM, and NM) the rate-limiting step in ATPase assays is thought to be attachment to actin or phosphate release, while for in vitro motility assays it is controversial. In MV the rate-limiting step for both in vitro motility and ATPase assays is known to be ADP release. Consequently, in MV the temperature dependence of the ADP release rate constant is similar to the temperature dependence of in vitro motility. Interestingly, the temperature dependence of the ADP release rate constant of SM and NM was shifted toward the in vitro motility temperature dependence. Our results suggest that the rate-limiting step in SK, SM, and NM may shift from attachment-limited in solution to detachment limited in the in vitro motility assay. Internal strain within the myosin molecule or by neighboring myosin motors may slow ADP release which becomes rate-limiting in the in vitro motility assay. Within this small subset of myosins examined, the in vitro sliding velocity correlates reasonably well with actin-activated ATPase activity, which was suggested by the original study by Barany (J Gen Physiol 50:197-218, 1967).

Indexed as

MovementTemperatureAdenosine DiphosphateAdenosine TriphosphatasesAnimalsChickensKineticsMiceMyosinsNonmuscle Myosin Type IIARabbitsSkeletal Muscle MyosinsSmooth Muscle MyosinsAdenosine DiphosphateAdenosine TriphosphatasesMyosinsNonmuscle Myosin Type IIASkeletal Muscle MyosinsSmooth Muscle Myosins

Identifiers

PMID22930330
PMCPMC3666341
OpenAlexW2084801581

What OpenQuestion holds

Textmetadata
LicenceTDM
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.