ArticleGenetics2006
Long-term evolution and functional diversification in the members of the nucleophosmin/nucleoplasmin family of nuclear chaperones.
Article in Genetics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 66 citations in OpenAlex.
- Proteomic and phosphoproteomic signatures of disease progression in unmutated IGHV chronic lymphocytic leukemia.Clinical proteomics · 2026Article
- AML Disparities Across Racial Ancestry Groups: A Spotlight on the NPM1 Mutations.International journal of molecular sciences · 2026Review
- Review
- Pan-cancer analysis of the prognostic and immunological role of nucleophosmin/nucleoplasmin 3 (Cancer pathogenesis and therapy · 2023Article
- Nucleophosmin3 carried by small extracellular vesicles contribute to white adipose tissue browning.Journal of nanobiotechnology · 2022Article
- Two Functionally Redundant FK506-Binding Proteins Regulate Multidrug Resistance Gene Expression and Govern Azole Antifungal Resistance.Antimicrobial agents and chemotherapy · 2021Article
- Nucleophosmin in Its Interaction with Ligands.International journal of molecular sciences · 2020Review
- Landscape of Tumor Suppressor Mutations in Acute Myeloid Leukemia.Journal of clinical medicine · 2020Review
- Proteomic Analysis of Histones H2A/H2B and Variant Hv1 in Tetrahymena thermophila Reveals an Ancient Network of Chaperones.Molecular biology and evolution · 2019Article
- 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
- A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility.Scientific reports · 2016Article
- Nucleophosmin: from structure and function to disease development.BMC molecular biology · 2016Review
- Molecules that target nucleophosmin for cancer treatment: an update.Oncotarget · 2016Review
- Altered machinery of protein synthesis is region- and stage-dependent and is associated with α-synuclein oligomers in Parkinson's disease.Acta neuropathologica communications · 2015Article
- Molecular evolution of NASP and conserved histone H3/H4 transport pathway.BMC evolutionary biology · 2014Article
- Structural polymorphism in the N-terminal oligomerization domain of NPM1.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones.Nucleic acids research · 2014Article
- Identification of two novel NPM1 mutations in patients with acute myeloid leukemia.Annals of laboratory medicine · 2013Article
- Elucidation of motifs in ribosomal protein S9 that mediate its nucleolar localization and binding to NPM1/nucleophosmin.PloS one · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proper assembly of basic proteins with nucleic acids is a reaction that must be facilitated to prevent protein aggregation and formation of nonspecific nucleoprotein complexes. The proteins that mediate this orderly protein assembly are generally termed molecular (or nuclear) chaperones. The nucleophosmin/nucleoplasmin (NPM) family of molecular chaperones encompasses members ubiquitously expressed in many somatic tissues (NPM1 and -3) or specific to oocytes and eggs (NPM2). The study of this family of molecular chaperones has experienced a renewed interest in the past few years. However, there is a lack of information regarding the molecular evolution of these proteins. This work represents the first attempt to characterize the long-term evolution followed by the members of this family. Our analysis shows that there is extensive silent divergence at the nucleotide level suggesting that this family has been subject to strong purifying selection at the protein level. In contrast to NPM1 and NPM-like proteins in invertebrates, NPM2 and NPM3 have a polyphyletic origin. Furthermore, the presence of selection for high frequencies of acidic residues as well as the existence of higher levels of codon bias was detected at the C-terminal ends, which can be ascribed to the critical role played by these residues in constituting the acidic tracts and to the preferred codon usage for phosphorylatable amino acids at these regions.
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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.