ArticleThe Journal of cell biology1992
NuMA: an unusually long coiled-coil related protein in the mammalian nucleus.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
What it found
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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
75 citing papers in PubMed, 230 citations in OpenAlex.
- Activation and regulation of the dynein-dynactin-NuMA complex.Nature chemical biology · 2026Article
- Article
- The nuclear structural protein NuMA is required for efficient DNA replication by ensuring association of core replication factors to replication forks.bioRxiv : the preprint server for biology · 2026Article
- NuMA mechanically reinforces the spindle independently of its partner dynein.Current biology : CB · 2025Article
- NuMA mechanically reinforces the spindle independently of its partner dynein.bioRxiv : the preprint server for biology · 2024Article
- CDK5-cyclin B1 regulates mitotic fidelity.Nature · 2024Article
- Article
- NuMA regulates mitotic spindle assembly, structural dynamics and function via phase separation.Nature communications · 2021Article
- The Nuclear Mitotic Apparatus (NuMA) Protein: A Key Player for Nuclear Formation, Spindle Assembly, and Spindle Positioning.Frontiers in cell and developmental biology · 2021Review
- The mitotic protein NuMA plays a spindle-independent role in nuclear formation and mechanics.The Journal of cell biology · 2020Article
- NuMA interaction with chromatin is vital for proper chromosome decondensation at the mitotic exit.Molecular biology of the cell · 2020Article
- PP2A--B55γ counteracts Cdk1 and regulates proper spindle orientation through the cortical dynein adaptor NuMA.Journal of cell science · 2020Article
- The nuclear mitotic apparatus protein NuMA controls rDNA transcription and mediates the nucleolar stress response in a p53-independent manner.Nucleic acids research · 2017Article
- Spindle pole cohesion requires glycosylation-mediated localization of NuMA.Scientific reports · 2017Article
- Organization of nuclear architecture during adipocyte differentiation.Nucleus (Austin, Tex.) · 2016Review
- Sensitive Electrochemical Immunosensor for Detection of Nuclear Matrix Protein-22 based on NH2-SAPO-34 Supported Pd/Co Nanoparticles.Scientific reports · 2016Article
- Warts phosphorylates mud to promote pins-mediated mitotic spindle orientation in Drosophila, independent of Yorkie.Current biology : CB · 2015Article
- NuMA interacts with phosphoinositides and links the mitotic spindle with the plasma membrane.The EMBO journal · 2014Article
- NuMA promotes homologous recombination repair by regulating the accumulation of the ISWI ATPase SNF2h at DNA breaks.Nucleic acids research · 2014Article
- Cell cycle-regulated membrane binding of NuMA contributes to efficient anaphase chromosome separation.Molecular biology of the cell · 2014Article
15 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A bank of 892 autoimmune sera was screened by indirect immunofluorescence on mammalian cells. Six sera were identified that recognize an antigen(s) with a cell cycle-dependent localization pattern. In interphase cells, the antibodies stained the nucleus and in mitotic cells the spindle apparatus was recognized. Immunological criteria indicate that the antigen recognized by at least one of these sera corresponds to a previously identified protein called the nuclear mitotic apparatus protein (NuMA). A cDNA which partially encodes NuMA was cloned from a lambda gt11 human placental cDNA expression library, and overlapping cDNA clones that encode the entire gene were isolated. DNA sequence analysis of the clones has identified a long open reading frame capable of encoding a protein of 238 kD. Analysis of the predicted protein sequence suggests that NuMA contains an unusually large central alpha-helical domain of 1,485 amino acids flanked by nonhelical terminal domains. The central domain is similar to coiled-coil regions in structural proteins such as myosin heavy chains, cytokeratins, and nuclear lamins which are capable of forming filaments. Double immunofluorescence experiments performed with anti-NuMA and antilamin antibodies indicate that NuMA dissociates from condensing chromosomes during early prophase, before the complete disintegration of the nuclear lamina. As mitosis progresses, NuMA reassociates with telophase chromosomes very early during nuclear reformation, before substantial accumulation of lamins on chromosomal surfaces is evident. These results indicate that the NuMA proteins may be a structural component of the nucleus and may be involved in the early steps of nuclear reformation during telophase.
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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.