ReviewNature structural & molecular biology2016
Toward the atomic structure of the nuclear pore complex: when top down meets bottom up.
Review in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 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
45 citing papers in PubMed.
- The nuclear envelope protein TMEM209 is an integral component of the nuclear pore complex and interacts with Nup210.Journal of cell science · 2026Article
- Nucleoporin 35: a novel nuclear pore complex protein involved in pathological cardiac remodeling.Cardiovascular research · 2025Article
- Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Charge of karyopherins and nuclear FG-Nups are key ingredients of nucleocytoplasmic transport.Biophysical journal · 2025Article
- Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.Microbiology and molecular biology reviews : MMBR · 2024Review
- Reconstitution of nuclear envelope subdomain formation on mitotic chromosomes in semi-intact cells.Cell structure and function · 2024Article
- CircZCCHC2 decreases pirarubicin sensitivity and promotes triple-negative breast cancer development via the miR-1200/TPR axis.iScience · 2024Article
- Article
- Barrier properties of Nup98 FG phases ruled by FG motif identity and inter-FG spacer length.Nature communications · 2023Article
- Nucleoporin POM121 signals TFEB-mediated autophagy via activation of SIGMAR1/sigma-1 receptor chaperone by pridopidine.Autophagy · 2023Article
- Could artificial intelligence revolutionize the development of nanovectors for gene therapy and mRNA vaccines?Nano today · 2022Article
- Architecture of the linker-scaffold in the nuclear pore.Science (New York, N.Y.) · 2022Article
- Architecture of the cytoplasmic face of the nuclear pore.Science (New York, N.Y.) · 2022Article
- Structure, Maintenance, and Regulation of Nuclear Pore Complexes: The Gatekeepers of the Eukaryotic Genome.Cold Spring Harbor perspectives in biology · 2022Review
- Analysis of Ubiquitylation and SUMOylation of Yeast Nuclear Pore Complex Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Karyopherin abnormalities in neurodegenerative proteinopathies.Brain : a journal of neurology · 2021Review
- Karyopherin-βs play a key role as a phase separation regulator.Journal of biochemistry · 2021Review
- Physics of the Nuclear Pore Complex: Theory, Modeling and Experiment.Physics reports · 2021Article
- Recapitulation of selective nuclear import and export with a perfectly repeated 12mer GLFG peptide.Nature communications · 2021Article
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.
Funding
Abstract
Elucidating the structure of the nuclear pore complex (NPC) is a prerequisite for understanding the molecular mechanism of nucleocytoplasmic transport. However, owing to its sheer size and flexibility, the NPC is unapproachable by classical structure determination techniques and requires a joint effort of complementary methods. Whereas bottom-up approaches rely on biochemical interaction studies and crystal-structure determination of NPC components, top-down approaches attempt to determine the structure of the intact NPC in situ. Recently, both approaches have converged, thereby bridging the resolution gap from the higher-order scaffold structure to near-atomic resolution and opening the door for structure-guided experimental interrogations of NPC function.
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Registered trials
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