ArticleThe Journal of cell biology1987
Biosynthesis and interconversion of Drosophila nuclear lamin isoforms during normal growth and in response to heat shock.
Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 104 citations in OpenAlex.
- Review
- Lamin A/C phosphorylation at serine 22 is a conserved heat shock response to regulate nuclear adaptation during stress.Journal of cell science · 2023Article
- Drosophila p38 MAPK interacts with BAG-3/starvin to regulate age-dependent protein homeostasis.Aging cell · 2021Article
- Silencing of Euchromatic Transposable Elements as a Consequence of Nuclear Lamina Dysfunction.Cells · 2020Article
- Mechanotransduction via the LINC complex regulates DNA replication in myonuclei.The Journal of cell biology · 2018Article
- Laminopathies: what can humans learn from fruit flies.Cellular & molecular biology letters · 2018Review
- Why Quantification Matters: Characterization of Phenotypes at the Drosophila Larval Neuromuscular Junction.Journal of visualized experiments : JoVE · 2016Article
- Review
- The different function of single phosphorylation sites of Drosophila melanogaster lamin Dm and lamin C.PloS one · 2012Article
- The genome and the nucleus: a marriage made by evolution. Genome organisation and nuclear architecture.Chromosoma · 2005Review
- Drosophila ORC specifically binds to ACE3, an origin of DNA replication control element.Genes & development · 1999Article
- Interactions among Drosophila nuclear envelope proteins lamin, otefin, and YA.Molecular and cellular biology · 1998Article
- Functional dissection of YA, an essential, developmentally regulated nuclear lamina protein in Drosophila melanogaster.Molecular and cellular biology · 1998Article
- Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae.The Journal of cell biology · 1997Article
- Monoclonal antibody raised against murine IL-1 alpha peptide cross-reacts with a 60-kDa antigen in early Drosophila melanogaster embryo.Cell and tissue research · 1995Article
- Glucocorticoids down-regulate beta 1-adrenergic-receptor expression by suppressing transcription of the receptor gene.The Biochemical journal · 1994Article
- Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract.The Journal of cell biology · 1992Article
- Localization of a myosin heavy chain-like polypeptide to Drosophila nuclear pore complexes.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Indirect immunofluorescence localization of beta-adrenergic receptors and G-proteins in human A431 cells.The Biochemical journal · 1989Article
- Identification of the gene for fly non-muscle myosin heavy chain: Drosophila myosin heavy chains are encoded by a gene family.The EMBO journal · 1989Article
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.
Funding
Abstract
Two major immunocross-reactive polypeptides of the Drosophila nuclear envelope, distinguishable in interphase cells on the basis of one-dimensional SDS-PAGE mobility, have been localized to the nuclear lamina by immunoelectron microscopy. These have been designated lamins Dm1 and Dm2. Both lamins are apparently derived posttranslationally from a single, primary translation product, lamin Dm0. A pathway has been established whereby lamin Dm0 is processed almost immediately upon synthesis in the cytoplasm to lamin Dm1. Processing occurs posttranslationally, is apparently proteolytic, and has been reconstituted from cell-free extracts in vitro. Processing in vitro is ATP dependent. Once assembled into the nuclear envelope, a portion of lamin Dm1 is converted into lamin Dm2 by differential phosphorylation. Throughout most stages of development and in Schneider 2 tissue culture cells, both lamin isoforms are present in approximately equal abundance. However, during heat shock, lamin Dm2 is converted nearly quantitatively into lamin Dm1. Implications for understanding the regulation of nuclear lamina plasticity through normal growth and in response to heat shock are discussed.
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.