ArticleBiophysical journal2005
Hierarchical extensibility in the PEVK domain of skeletal-muscle titin.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 55 citations in OpenAlex.
- Titin's Intrinsically Disordered PEVK Domain Modulates Actin Polymerization.International journal of molecular sciences · 2025Article
- Structure of the ISW1a complex bound to the dinucleosome.Nature structural & molecular biology · 2024Article
- Contributions of Titin and Collagen to Passive Stress in Muscles fromInternational journal of molecular sciences · 2022Article
- Regulation of Poly-E Motif Flexibility by pH, CaInternational journal of molecular sciences · 2022Article
- CARs-DB: A Database of Cryptic Amyloidogenic Regions in Intrinsically Disordered Proteins.Frontiers in molecular biosciences · 2022Article
- Protein Unfolding: Denaturant vs. Force.Biomedicines · 2021Article
- The Poly-E motif in Titin's PEVK region undergoes pH dependent conformational changes.Biochemistry and biophysics reports · 2020Article
- Genetics of Muscle Stiffness, Muscle Elasticity and Explosive Strength.Journal of human kinetics · 2020Article
- Differences in stability and calcium sensitivity of the Ig domains in titin's N2A region.Protein science : a publication of the Protein Society · 2020Article
- Deleting Titin's C-Terminal PEVK Exons Increases Passive Stiffness, Alters Splicing, and Induces Cross-Sectional and Longitudinal Hypertrophy in Skeletal Muscle.Frontiers in physiology · 2020Article
- Crystal structure of Zen4 in the apo state reveals a missing conformation of kinesin.Nature communications · 2017Article
- The increase in non-cross-bridge forces after stretch of activated striated muscle is related to titin isoforms.American journal of physiology. Cell physiology · 2016Article
- Non-crossbridge forces in activated striated muscles: a titin dependent mechanism of regulation?Journal of muscle research and cell motility · 2015Review
- Structure of giant muscle proteins.Frontiers in physiology · 2013Review
- Cross-species mechanical fingerprinting of cardiac myosin binding protein-C.Biophysical journal · 2013Article
- Conformational dynamics of titin PEVK explored with FRET spectroscopy.Biophysical journal · 2012Article
- Modular structure of smooth muscle Myosin light chain kinase: hydrodynamic modeling and functional implications.Biochemistry · 2010Article
- Dynamic strength of titin's Z-disk end.Journal of biomedicine & biotechnology · 2010Article
- Comparative biomechanics of thick filaments and thin filaments with functional consequences for muscle contraction.Journal of biomedicine & biotechnology · 2010Review
- Tuning passive mechanics through differential splicing of titin during skeletal muscle development.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Titin is the main determinant of passive muscle force. Physiological extension of titin derives largely from its PEVK (Pro-Glu-Val-Lys) domain, which has a different length in different muscle types. Here we characterized the elasticity of the full-length, human soleus PEVK domain by mechanically manipulating its contiguous, recombinant subdomain segments: an N-terminal (PEVKI), a middle (PEVKII), and a C-terminal (PEVKIII) one third. Measurement of the apparent persistence lengths revealed a hierarchical arrangement according to local flexibility: the N-terminal PEVKI is the most rigid and the C-terminal PEVKIII is the most flexible segment within the domain. Immunoelectron microscopy supported the hierarchical extensibility within the PEVK domain. The effective persistence lengths decreased as a function of ionic strength, as predicted by the Odijk-Skolnick-Fixman model of polyelectrolyte chains. The ionic strength dependence of persistence length was similar in all segments, indicating that the residual differences in the elasticity of the segments derive from nonelectrostatic mechanisms.
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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.