ArticleThe EMBO journal1995
Epitope mapping and direct visualization of the parallel, in-register arrangement of the double-stranded coiled-coil in the NuMA protein.
Article in The EMBO journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 62 citations in OpenAlex.
- Activation and regulation of the dynein-dynactin-NuMA complex.Nature chemical biology · 2026Article
- NuMA mechanically reinforces the spindle independently of its partner dynein.Current biology : CB · 2025Article
- NuMA is a mitotic adaptor protein that activates dynein and connects it to microtubule minus ends.The Journal of cell biology · 2025Article
- NuMA mechanically reinforces the spindle independently of its partner dynein.bioRxiv : the preprint server for biology · 2024Article
- Relaxation and Noise-Driven Oscillations in a Model of Mitotic Spindle Dynamics.Bulletin of mathematical biology · 2024Article
- Role of NuMA1 in breast cancer stem cells with implications for combination therapy of PIM1 and autophagy inhibition in triple negative breast cancer.Research square · 2024Article
- 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
- Num1 versus NuMA: insights from two functionally homologous proteins.Biophysical reviews · 2018Review
- Cortical dynein is critical for proper spindle positioning in human cells.The Journal of cell biology · 2012Article
- Multicoil2: predicting coiled coils and their oligomerization states from sequence in the twilight zone.PloS one · 2011Article
- NuMA after 30 years: the matrix revisited.Trends in cell biology · 2010Review
- Requirements for NuMA in maintenance and establishment of mammalian spindle poles.The Journal of cell biology · 2009Article
- Comprehensive analysis of NuMA variation in breast cancer.BMC cancer · 2008Article
- NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis.The Biochemical journal · 2005Article
- Spindle pole organization in Drosophila S2 cells by dynein, abnormal spindle protein (Asp), and KLP10A.Molecular biology of the cell · 2005Article
- The C terminus of the nuclear protein NuMA: phylogenetic distribution and structure.Protein science : a publication of the Protein Society · 2004Article
- An Enterococcus faecium secreted antigen, SagA, exhibits broad-spectrum binding to extracellular matrix proteins and appears essential for E. faecium growth.Infection and immunity · 2003Article
- Review
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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
NuMA, a 238 kDa protein present in the nucleus during interphase, translocates to the spindle poles in mitosis. NuMA plays an essential role in mitosis, since microinjection of the NuMA SPN-3 monoclonal antibody causes mitotic arrest and micronuclei formation. We have mapped the approximate position of the epitopes of six monoclonal NuMA antibodies using recombinant NuMA fragments. The SPN-3 epitope has been located to residues 255-267 at the C-terminus of the first helical subdomain of the central rod domain and several residues crucial for antibody binding have been identified. To gain insight into the ultrastructure of NuMA, several defined fragments, as well as the full-length recombinant protein, were expressed in Escherichia coli and purified to homogeneity. They were then characterized by chemical cross-linking, circular dichroism spectra and electron microscopy. The results directly reveal the tripartate structure of NuMA. A long central rod domain is flanked by globular end domains. The rod is 207 nm long and is at least 90% alpha-helical. It reflects a double-stranded coiled-coil with the alpha-helices arranged parallel and in register. The NuMA protein thus forms the longest coiled-coil currently known. Our analyses reveal no indication that recombinant NuMA assembles into filaments or other higher order structures.
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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.