ArticleBiochemistry2011
Crystal structure and function of human nucleoplasmin (npm2): a histone chaperone in oocytes and embryos.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 48 citations in OpenAlex.
- Conserved nucleocytoplasmic density homeostasis drives cellular organization across eukaryotes.Nature communications · 2025Article
- Article
- Plant-specific HDT family histone deacetylases are nucleoplasmins.The Plant cell · 2022Article
- Article
- NPM2 in malignant peritoneal mesothelioma: from basic tumor biology to clinical medicine.World journal of surgical oncology · 2022Review
- Histone Chaperones as Cardinal Players in Development.Frontiers in cell and developmental biology · 2022Review
- DPAGT1-Mediated ProteinAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Article
- AtFKBP53: a chimeric histone chaperone with functional nucleoplasmin and PPIase domains.Nucleic acids research · 2020Article
- Structure-function relationship of H2A-H2B specific plant histone chaperones.Cell stress & chaperones · 2020Review
- Nucleoplasmin is a limiting component in the scaling of nuclear size with cytoplasmic volume.The Journal of cell biology · 2019Article
- Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition.Scientific reports · 2019Article
- The histone chaperoning pathway: from ribosome to nucleosome.Essays in biochemistry · 2019Review
- Oligomerization of Drosophila Nucleoplasmin-Like Protein is required for its centromere localization.Nucleic acids research · 2018Article
- Double maternal-effect: duplicated nucleoplasmin 2 genes, npm2a and npm2b, with essential but distinct functions are shared by fish and tetrapods.BMC evolutionary biology · 2018Article
- Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Journal of molecular biology · 2017Review
- Reconstitution of the oocyte nucleolus in mice through a single nucleolar protein, NPM2.Journal of cell science · 2017Article
- Chromosomal passenger complex hydrodynamics suggests chaperoning of the inactive state by nucleoplasmin/nucleophosmin.Molecular biology of the cell · 2017Article
- The NOR1/OSCP1 proteins in cancer: from epigenetic silencing to functional characterization of a novel tumor suppressor.Journal of Cancer · 2017Review
- Nucleophosmin: from structure and function to disease development.BMC molecular biology · 2016Review
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 at 1 institution in 1 country.
Funding
Abstract
Human Npm2 is an ortholog of Xenopus nucleoplasmin (Np), a chaperone that binds histones. We have determined the crystal structure of a truncated Npm2-core at 1.9 Å resolution and show that the N-terminal domains of Npm2 and Np form similar pentamers. This allowed us to model an Npm2 decamer which may be formed by hydrogen bonds between quasi-conserved residues in the interface between two pentamers. Interestingly, the Npm2 pentamer lacks a prototypical A1-acidic tract in each of its subunits. This feature may be responsible for the inability of Npm2-core to bind histones. However, Npm2 with a large acidic tract in its C-terminal tail (Npm2-A2) is able to bind histones and form large complexes. Fluorescence resonance energy transfer experiments and biochemical analysis of loop mutations support the premise that nucleoplasmins form decamers when they bind H2A-H2B dimers and H3-H4 tetramers simultaneously. In the absence of histone tetramers, these chaperones bind H2A-H2B dimers with a single pentamer forming the central hub. When taken together, our data provide insights into the mechanism of histone binding by nucleoplasmins.
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.