ArticleProceedings of the National Academy of Sciences of the United States of America1997
Evolutionary specialization of the nuclear targeting apparatus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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.
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
49 citing papers in PubMed, 121 citations in OpenAlex.
- Histone Nuclear Import and Beyond: Multifunctional Roles of Importins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Identification of the Karyopherin Superfamily in Maize and Its Functional Cues in Plant Development.International journal of molecular sciences · 2022Review
- Article
- The vacuolar morphology protein VAC14 plays an important role in sexual development in the filamentous ascomycete Sordaria macrospora.Current genetics · 2022Article
- Nuclear transport genes recurrently duplicate by means of RNA intermediates in Drosophila but not in other insects.BMC genomics · 2021Article
- A Novel Proteomic Method Reveals NLS Tagging of T-DM1 Contravenes Classical Nuclear Transport in a Model of HER2-Positive Breast Cancer.Molecular therapy. Methods & clinical development · 2020Article
- Thiosemicarbazone scaffold for the design of antifungal and antiaflatoxigenic agents: evaluation of ligands and related copper complexes.Scientific reports · 2017Article
- Condensin HEAT subunits required for DNA repair, kinetochore/centromere function and ploidy maintenance in fission yeast.PloS one · 2015Article
- Expansion and Function of Repeat Domain Proteins During Stress and Development in Plants.Frontiers in plant science · 2015Review
- Recombinant adeno-associated virus utilizes host cell nuclear import machinery to enter the nucleus.Journal of virology · 2014Article
- Nuclear localization signals of varicella zoster virus ORF4.Virus genes · 2014Article
- Enriching the pore: splendid complexity from humble origins.Traffic (Copenhagen, Denmark) · 2014Review
- The way Wnt works: components and mechanism.Growth factors (Chur, Switzerland) · 2013Review
- Birth, death, and replacement of karyopherins in Drosophila.Molecular biology and evolution · 2012Article
- Specific Cooperation Between Imp-α2 and Imp-β/Ketel in Spindle Assembly During Drosophila Early Nuclear Divisions.G3 (Bethesda, Md.) · 2012Article
- The importin β binding domain as a master regulator of nucleocytoplasmic transport.Biochimica et biophysica acta · 2011Review
- Probing the specificity of binding to the major nuclear localization sequence-binding site of importin-alpha using oriented peptide library screening.The Journal of biological chemistry · 2010Article
- Article
- Article
- Evolution of the metazoan-specific importin alpha gene family.Journal of molecular evolution · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The alpha- and beta-karyopherins (Kaps), also called importins, mediate the nuclear transport of proteins. All alpha-Kaps contain a central domain composed of eight approximately 40 amino acid, tandemly arranged, armadillo-like (Arm) repeats. The number and order of these repeats have not changed since the common origin of fungi, plants, and mammals. Phylogenetic analysis suggests that the various alpha-Kaps fall into two groups, alpha1 and alpha2. Whereas animals encode both types, the yeast genome encodes only an alpha1-Kap. The beta-Kaps are characterized by 14-15 tandemly arranged HEAT motifs. We show that the Arm repeats of alpha-Kaps and the HEAT motifs of beta-Kaps are similar, suggesting that the alpha-Kaps and beta-Kaps (and for that matter, all Arm and HEAT repeat-containing proteins) are members of the same protein superfamily. Phylogenetic analysis indicates that there are at least three major groups of beta-Kaps, consistent with their proposed cargo specificities. We present a model in which an alpha-independent beta-Kap progenitor gave rise to the alpha-dependent beta-Kaps and the alpha-Kaps.
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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.