Evidence map›Paper›PMID 20801044›Full record

ReviewTrends in biochemical sciences2010

Emerging complex pathways of the actomyosin powerstroke.

András Málnási-Csizmadia, Mihály Kovács

Open access · greenAbstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2010. 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
3.0field-weighted citation impact, top 8% 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, 56 citations in OpenAlex.

  1. Article
  2. Review
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  17. Article
  18. Direct measurements of the coordination of lever arm swing and the catalytic cycle in myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Direct real-time detection of the structural and biochemical events in the myosin power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  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

2 authors at 1 institution in 1 country.

András Málnási-CsizmadiaDepartment of Biochemistry, Eötvös University, Pázmány P. stny. 1/C, H-1117 Budapest, Hungary. malna@elte.hu
Mihály Kovács
Eötvös Loránd University · HU

Funding

Emerging New Types of MotilityR01TW007241 · FIC · EOTVOS LORAND UNIVERSITY · PI KOVACS, MIHALY · 2005 to 2009
$260k
FIC NIH HHS 1 R01TW007241FIC NIH HHS R01 TW007241
6 · The paper itself

Abstract

Actomyosin powers muscle contraction and various cellular activities, including cell division, differentiation, intracellular transport and sensory functions. Despite their crucial roles, key aspects of force generation have remained elusive. To perform efficient force generation, the powerstroke must occur while myosin is bound to actin. Paradoxically, this process must be initiated when myosin is in a very low actin-affinity state. Recent results shed light on a kinetic pathway selection mechanism whereby the actin-induced activation of the swing of myosin's lever enables efficient mechanical functioning. Structural elements and biochemical principles involved in this mechanism are conserved among various NTPase-effector (e.g. kinesin-microtubule, G protein exchange factor and kinase-scaffold protein) systems that perform chemomechanical or signal transduction.

Indexed as

Muscle ContractionActomyosinAnimalsHumansNucleotidesActomyosinNucleotides

Identifiers

PMID20801044
PMCPMC2991434
OpenAlexW2060550088

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.