ArticleProceedings of the National Academy of Sciences of the United States of America1994
Enhanced force generation by smooth muscle myosin in vitro.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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.
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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.
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Who cites it
27 citing papers in PubMed, 62 citations in OpenAlex.
- Force Measurements From Myofibril to Filament.Frontiers in physiology · 2021Review
- Positional Isomers of a Non-Nucleoside Substrate Differentially Affect Myosin Function.Biophysical journal · 2020Article
- Biomaterials to Mimic and Heal Connective Tissues.Advanced materials (Deerfield Beach, Fla.) · 2019Review
- The (dys)functional extracellular matrix.Biochimica et biophysica acta · 2015Review
- The role of caldesmon and its phosphorylation by ERK on the binding force of unphosphorylated myosin to actin.Biochimica et biophysica acta · 2014Article
- Ca++-sensitizing mutations in troponin, P(i), and 2-deoxyATP alter the depressive effect of acidosis on regulated thin-filament velocity.Journal of applied physiology (Bethesda, Md. : 1985) · 2014Article
- Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin.Biochimica et biophysica acta · 2013Article
- Push and pull of tropomyosin's opposite effects on myosin attachment to actin. A chimeric tropomyosin host-guest study.Biochemistry · 2010Article
- Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit.Cell motility and the cytoskeleton · 2009Article
- Affinity for MgADP and force of unbinding from actin of myosin purified from tonic and phasic smooth muscle.American journal of physiology. Cell physiology · 2008Article
- Coiled-coil unwinding at the smooth muscle myosin head-rod junction is required for optimal mechanical performance.Biophysical journal · 2001Article
- Aging-related changes in skeletal muscle. Mechanisms and interventions.Drugs & aging · 2000Review
- A simple method for measuring the relative force exerted by myosin on actin filaments in the in vitro motility assay: evidence that tropomyosin and troponin increase force in single thin filaments.The Biochemical journal · 2000Article
- Measurement of the force produced by an intact bull sperm flagellum in isometric arrest and estimation of the dynein stall force.Biophysical journal · 2000Article
- Regulation of force and unloaded sliding speed in single thin filaments: effects of regulatory proteins and calcium.The Journal of physiology · 2000Article
- Tropomyosin directly modulates actomyosin mechanical performance at the level of a single actin filament.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms.The Journal of physiology · 1999Article
- Unphosphorylated crossbridges and latch: smooth muscle regulation revisited.Journal of muscle research and cell motility · 1999Article
- A 7-amino-acid insert in the heavy chain nucleotide binding loop alters the kinetics of smooth muscle myosin in the laser trap.Journal of muscle research and cell motility · 1998Article
- Two-dimensional tracking of ncd motility by back focal plane interferometry.Biophysical journal · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
To determine whether the apparent enhanced force-generating capabilities of smooth muscle relative to skeletal muscle are inherent to the myosin cross-bridge, the isometric steady-state force produced by myosin in the in vitro motility assay was measured. In this assay, myosin adhered to a glass surface pulls on an actin filament that is attached to an ultracompliant (50-200 nm/pN) glass microneedle. The number of myosin cross-bridge heads able to interact with a length of actin filament was estimated by measuring the density of biochemically active myosin adhered to the surface; with this estimate, the average force per cross-bridge head of smooth and skeletal muscle myosins is 0.6 pN and 0.2 pN, respectively. Surprisingly, smooth muscle myosin generates approximately three times greater average force per cross-bridge head than does skeletal muscle myosin.
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Registered trials
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.