ArticleThe Journal of cell biology1996
Three-dimensional structure of the Z band in a normal mammalian skeletal muscle.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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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Who cites it
11 citing papers in PubMed, 40 citations in OpenAlex.
- Cryo-electron tomography of cardiac myofibrils reveals a 3D lattice spring within the Z-discs.Communications biology · 2020Article
- Three-Dimensional Structure of Vertebrate Muscle Z-Band: The Small-Square Lattice Z-Band in Rat Cardiac Muscle.Journal of molecular biology · 2015Article
- The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling.Journal of muscle research and cell motility · 2009Review
- Effects of physical training and detraining, immobilisation, growth and aging on human fascicle geometry.Sports medicine (Auckland, N.Z.) · 2006Review
- Nebulin regulates the assembly and lengths of the thin filaments in striated muscle.The Journal of cell biology · 2005Article
- Distinct families of Z-line targeting modules in the COOH-terminal region of nebulin.The Journal of cell biology · 2000Article
- Architecture of the thin filament-Z-line junction: lessons from nebulette and nebulin homologies.Journal of muscle research and cell motility · 2000Article
- Exchange of alpha-actinin in isolated rigor myofibrils.Journal of muscle research and cell motility · 1999Article
- Alpha actinin-CapZ, an anchoring complex for thin filaments in Z-line.Journal of muscle research and cell motility · 1999Article
- The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity.The Journal of cell biology · 1998Article
- Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin.The EMBO 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
4 authors at 1 institution in 1 country.
Funding
Abstract
The three-dimensional structure of the vertebrate skeletal muscle Z band reflects its function as the muscle component essential for tension transmission between successive sarcomeres. We have investigated this structure as well as that of the nearby I band in a normal, unstimulated mammalian skeletal muscle by tomographic three-dimensional reconstruction from electron micrograph tilt series of sectioned tissue. The three-dimensional Z band structure consists of interdigitating axial filaments from opposite sarcomeres connected every 18 +/- 12 nm (mean +/- SD) to one to four cross-connecting Z-filaments are observed to meet the axial filaments in a fourfold symmetric arrangement. The substantial variation in the spacing between cross-connecting Z-filament to axial filament connection points suggests that the structure of the Z band is not determined solely by the arrangement of alpha-actinin to actin-binding sites along the axial filament. The cross-connecting filaments bind to or form a "relaxed interconnecting body" halfway between the axial filaments. This filamentous body is parallel to the Z band axial filaments and is observed to play an essential role in generating the small square lattice pattern seen in electron micrographs of unstimulated muscle cross sections. This structure is absent in cross section of the Z band from muscles fixed in rigor or in tetanus, suggesting that the Z band lattice must undergo dynamic rearrangement concomitant with crossbridge binding in the A band.
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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.