ArticleThe Journal of cell biology1990
Assembly of amino-terminally deleted desmin in vimentin-free cells.
Article in The Journal of cell biology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 88 citations in OpenAlex.
- Impact of N-Terminal Tags on De Novo Vimentin Intermediate Filament Assembly.International journal of molecular sciences · 2022Article
- Dual color photoactivation localization microscopy of cardiomyopathy-associated desmin mutants.The Journal of biological chemistry · 2012Article
- The domain organization of the bacterial intermediate filament-like protein crescentin is important for assembly and function.Cytoskeleton (Hoboken, N.J.) · 2011Article
- Site-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure.The Journal of biological chemistry · 2010Article
- Differentiation of cardiomyocytes requires functional serine residues within the amino-terminal domain of desmin.Differentiation; research in biological diversity · 2007Article
- Desmin aggregate formation by R120G alphaB-crystallin is caused by altered filament interactions and is dependent upon network status in cells.Molecular biology of the cell · 2004Article
- Identification of novel principles of keratin filament network turnover in living cells.Molecular biology of the cell · 2004Article
- A dysfunctional desmin mutation in a patient with severe generalized myopathy.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity.The Journal of clinical investigation · 1994Article
- The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation.The Journal of cell biology · 1993Article
- Neurofilaments are obligate heteropolymers in vivo.The Journal of cell biology · 1993Article
- Dynamics of keratin assembly: exogenous type I keratin rapidly associates with type II keratin in vivo.The Journal of cell biology · 1993Article
- Nuclear A-type lamins are differentially expressed in human lung cancer subtypes.The American journal of pathology · 1993Article
- The roles of K5 and K14 head, tail, and R/K L L E G E domains in keratin filament assembly in vitro.The Journal of cell biology · 1992Article
- Steady state dynamics of intermediate filament networks.The Journal of cell biology · 1992Article
- A synthetic peptide representing the consensus sequence motif at the carboxy-terminal end of the rod domain inhibits intermediate filament assembly and disassembles preformed filaments.The Journal of cell biology · 1992Article
- Intermediate filaments formed de novo from tail-less cytokeratins in the cytoplasm and in the nucleus.The Journal of cell biology · 1991Article
- Desmin/vimentin intermediate filaments are dispensable for many aspects of myogenesis.The Journal of cell biology · 1991Article
- Deletions in epidermal keratins leading to alterations in filament organization in vivo and in intermediate filament assembly in vitro.The Journal of cell biology · 1990Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To study the role of the amino-terminal domain of the desmin subunit in intermediate filament (IF) formation, several deletions in the sequence encoding this domain were made. The deleted hamster desmin genes were fused to the RSV promoter. Expression of such constructs in vimentin-free MCF-7 cells as well as in vimentin-containing HeLa cells, resulted in the synthesis of mutant proteins of the expected size. Single- and double-label immunofluorescence assays of transfected cells showed that in the absence of vimentin, desmin subunits missing amino acids 4-13 are still capable of filament formation, although in addition to filaments large numbers of desmin dots are present. Mutant desmin subunits missing larger portions of their amino terminus cannot form filaments on their own. It may be concluded that the amino-terminal region comprising amino acids 7-17 contains residues indispensable for desmin filament formation in vivo. Furthermore it was shown that the endogenous vimentin IF network in HeLa cells masks the effects of mutant desmin on IF assembly. Intact and mutant desmin colocalized completely with endogenous vimentin in HeLa cells. Surprisingly, in these cells endogenous keratin also seemed to colocalize with endogenous vimentin, even if the endogenous vimentin filaments were disturbed after expression of some of the mutant desmin proteins. In MCF-7 cells some overlap between endogenous keratin and intact exogenous desmin filaments was also observed, but mutant desmin proteins did not affect the keratin IF structures. In the absence of vimentin networks (MCF-7 cells), the initiation of desmin filament formation seems to start on the preexisting keratin filaments. However, in the presence of vimentin (HeLa cells) a gradual integration of desmin in the preexisting vimentin filaments apparently takes place.
Indexed as
Identifiers
What OpenQuestion holds
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.