ArticleBiophysical journal1999
Tropomyosin positions in regulated thin filaments revealed by cryoelectron microscopy.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
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Who cites it
80 citing papers in PubMed, 174 citations in OpenAlex.
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- Calcium's Role and Signaling in Aging Muscle, Cellular Senescence, and Mineral Interactions.International journal of molecular sciences · 2023Review
- Membrane adhesion junctions regulate airway smooth muscle phenotype and function.Physiological reviews · 2023Review
- Sarcomere maturation: function acquisition, molecular mechanism, and interplay with other organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022Review
- Structure and Dynamics of the Flexible Cardiac Troponin T Linker Domain in a Fully Reconstituted Thin Filament.Biochemistry · 2022Article
- Genotype-Phenotype Associations with Restrictive Cardiomyopathy Induced by Pathogenic Genetic Mutations.Reviews in cardiovascular medicine · 2022Review
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Cardiac sarcomere mechanics in health and disease.Biophysical reviews · 2021Review
- Troponin Revealed: Uncovering the Structure of the Thin Filament On-Off Switch in Striated Muscle.Biophysical journal · 2021Review
- Cardiac muscle thin filament structures reveal calcium regulatory mechanism.Nature communications · 2020Article
- Thermal Activation of Thin Filaments in Striated Muscle.Frontiers in physiology · 2020Review
- FRET-based analysis of the cardiac troponin T linker region reveals the structural basis of the hypertrophic cardiomyopathy-causing Δ160E mutation.The Journal of biological chemistry · 2019Article
- High-speed AFM reveals subsecond dynamics of cardiac thin filaments upon CaProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Tropomyosin dynamics during cardiac muscle contraction as governed by a multi-well energy landscape.Progress in biophysics and molecular biology · 2019Article
- After the revolution: how is Cryo-EM contributing to muscle research?Journal of muscle research and cell motility · 2019Review
- The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies.International journal of molecular sciences · 2018Article
- CaBiophysical journal · 2018Article
- Muscle Contraction.Cold Spring Harbor perspectives in biology · 2018Review
- Relaxed and active thin filament structures; a new structural basis for the regulatory mechanism.Journal of structural biology · 2017Article
- Molecular mechanism of anesthetic-induced depression of myocardial contraction.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Past attempts to detect tropomyosin in electron micrograph images of frozen-hydrated troponin-regulated thin filaments under relaxing conditions have not been successful. This raised the possibility that tropomyosin may be disordered on filaments in the off-state, a possibility at odds with the steric blocking model of muscle regulation. By using cryoelectron microscopy and helical image reconstruction we have now resolved the location of tropomyosin in both relaxing and activating conditions. In the off-state, tropomyosin adopts a position on the outer domain of actin with a binding site virtually identical to that determined previously by negative staining, although at a radius of 3.8 nm, slightly higher than found in stained filaments. Molecular fitting to the atomic model of F-actin shows that tropomyosin is localized over sites on actin subdomain 1 required for myosin binding. Restricting access to these sites would inhibit the myosin-cross-bridge cycle, and hence contraction. Under high Ca(2+) activating conditions, tropomyosin moved azimuthally, away from its blocking position to the same site on the inner domain of actin previously determined by negative staining, also at 3.8 nm radius. These results provide strong support for operation of the steric mechanism of muscle regulation under near-native solution conditions and also validate the use of negative staining in investigations of muscle thin filament structure.
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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.