ArticleThe Journal of cell biology1991
Desmin/vimentin intermediate filaments are dispensable for many aspects of myogenesis.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 94 citations in OpenAlex.
- Study on the spatiotemporal development of skeletal muscle in embryonic Pekin ducks.Poultry science · 2026Article
- What does desmin do: A bibliometric assessment of the functions of the muscle intermediate filament.Experimental biology and medicine (Maywood, N.J.) · 2022Article
- Cytoskeletal Proteins in Myotendinous Junctions of Human Extraocular Muscles.Investigative ophthalmology & visual science · 2021Article
- Muscle fibre breakdown in venom-induced muscle degeneration.Journal of anatomy · 2003Article
- Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle.The Journal of cell biology · 1997Article
- Disruption of muscle architecture and myocardial degeneration in mice lacking desmin.The Journal of cell biology · 1996Article
- The expression of vimentin in satellite cells of regenerating skeletal muscle in vivo.The Histochemical journal · 1994Article
- Truncated desmin in PtK2 cells induces desmin-vimentin-cytokeratin coprecipitation, involution of intermediate filament networks, and nuclear fragmentation: a model for many degenerative diseases.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Inhibition of desmin expression blocks myoblast fusion and interferes with the myogenic regulators MyoD and myogenin.The Journal of cell biology · 1994Article
- Incorporation of microinjected biotin-labelled actin into nascent myofibrils of cardiac myocytes: an immunoelectron microscopic study.Journal of muscle research and cell motility · 1993Article
- Neurofilament deficiency in quail caused by nonsense mutation in neurofilament-L gene.The Journal of cell biology · 1993Article
- Ectopic synthesis of epidermal cytokeratins in pancreatic islet cells of transgenic mice interferes with cytoskeletal order and insulin production.The Journal of cell biology · 1993Article
- Article
- A sarcomeric alpha-actinin truncated at the carboxyl end induces the breakdown of stress fibers in PtK2 cells and the formation of nemaline-like bodies and breakdown of myofibrils in myotubes.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- The fate of desmin and titin during the degeneration and regeneration of the soleus muscle of the rat.Acta neuropathologica · 1992Article
- RNA protein interactions governing expression of the most abundant protein in human body, type I collagen.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
An expression vector was prepared containing a cDNA coding for a truncated version of the intermediate filament (IF) protein desmin. The encoded truncated desmin protein lacks a portion of the highly conserved alpha-helical rod region as well as the entire nonhelical carboxy-terminal domain. When transiently expressed in primary fibroblasts, or in differentiating postmitotic myoblasts and multinucleated myotubes, the truncated protein induces the complete dismantling of the preexisting vimentin or desmin/vimentin IF networks, respectively. Instead, in both cell types vimentin and desmin are packaged into hybrid spheroid bodies scattered throughout the cytoplasm. Despite the complete lack of intact IFs, myoblasts and myotubes expressing truncated desmin assemble and laterally align normal striated myofibrils and contract spontaneously in a manner indistinguishable from that of control myogenic cells. In older cultures the spheroid bodies shift from a longitudinal to a predominantly transverse orientation and loosely align along the I-Z-I-regions of striated myofibrils (Bennett, G.S., S. Fellini, Y. Toyama, and H. Holtzer. 1979. J. Cell Biol. 82:577-584), analogous to the translocation of intact desmin/vimentin IFs in control muscle. These results suggest the need for a critical reexamination of currently held concepts regarding the functions of desmin IFs during myogenesis.
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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.