ReviewCurrent opinion in cell biology2012
A jumbo problem: mapping the structure and functions of the nuclear pore complex.
Review in Current opinion in cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 49 citations in OpenAlex.
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- Karyopherin-βs play a key role as a phase separation regulator.Journal of biochemistry · 2021Review
- Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis.Cell research · 2020Article
- Imaging within single NPCs reveals NXF1's role in mRNA export on the cytoplasmic side of the pore.The Journal of cell biology · 2019Article
- Nuclear pore heterogeneity influences HIV-1 infection and the antiviral activity of MX2.eLife · 2018Article
- Modeling of the mechano-chemical behaviour of the nuclear pore complex: current research and perspectives.Integrative biology : quantitative biosciences from nano to macro · 2016Review
- Revealing Higher Order Protein Structure Using Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
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- Multiple Export Mechanisms for mRNAs.Cells · 2015Review
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- Accurate protein complex retrieval by affinity enrichment mass spectrometry (AE-MS) rather than affinity purification mass spectrometry (AP-MS).Molecular & cellular proteomics : MCP · 2015Article
- Therapeutic potential of mitotic interaction between the nucleoporin Tpr and aurora kinase A.Cell cycle (Georgetown, Tex.) · 2015Article
- Macromolecular transport between the nucleus and the cytoplasm: Advances in mechanism and emerging links to disease.Biochimica et biophysica acta · 2014Review
- The nuclear envelope: an intriguing focal point for neurogenetic disease.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2014Review
- From hypothesis to mechanism: uncovering nuclear pore complex links to gene expression.Molecular and cellular biology · 2014Review
- Cohesiveness tunes assembly and morphology of FG nucleoporin domain meshworks - Implications for nuclear pore permeability.Biophysical journal · 2013Article
- Protein production from the structural genomics perspective: achievements and future needs.Current opinion in structural biology · 2013Review
- Identification of CRM1-dependent Nuclear Export Cargos Using Quantitative Mass Spectrometry.Molecular & cellular proteomics : MCP · 2013Article
- Effect of charge, hydrophobicity, and sequence of nucleoporins on the translocation of model particles through the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Macromolecular assemblies can be intrinsically refractive to classical structural analysis, due to their size, complexity, plasticity and dynamic nature. One such assembly is the nuclear pore complex (NPC). The NPC is formed from ∼450 copies of 30 different proteins, called nucleoporins, and is the sole mediator of exchange between the nucleus and the cytoplasm in eukaryotic cells. Despite significant progress, it has become increasingly clear that new approaches, integrating different sources of structural and functional data, will be needed to understand the functional biology of the NPC. Here, we discuss the latest approaches trying to address this challenge.
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.