ReviewInternational journal of molecular sciences2022
Function of the Nuclear Transport Machinery in Maintaining the Distinctive Compositions of the Nucleus and Cytoplasm.
Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
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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.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026Review
- Breaking barriers: Respiratory viral strategies targeting the host's nuclear pore complex and nuclear transport pathways.Molecular biology of the cell · 2026Review
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- From transcription to export: mRNA's winding path to the cytoplasm.Trends in biochemical sciences · 2025Review
- Targeting CRM1 for Progeria Syndrome Therapy.Aging cell · 2025Article
- Role of pore dilation in molecular transport through the nuclear pore complex: Insights from polymer scaling theory.PLoS computational biology · 2025Article
- FrozONE: quick cell nucleus enrichment for comprehensive proteomics analysis of frozen tissues.Life science alliance · 2025Article
- Deciphering the intrinsically disordered characteristics of the FG-Nups through the lens of polymer physics.Nucleus (Austin, Tex.) · 2024Review
- Regulating transport efficiency through the nuclear pore complex: The role of binding affinity with FG-Nups.Molecular biology of the cell · 2024Article
- NUP43 promotes PD-L1/nPD-L1/PD-L1 feedback loop via TM4SF1/JAK/STAT3 pathway in colorectal cancer progression and metastatsis.Cell death discovery · 2024Article
- N2FXm, a method for joint nuclear and cytoplasmic volume measurements, unravels the osmo-mechanical regulation of nuclear volume in mammalian cells.Nature communications · 2024Article
- The role of the FSGS disease gene product and nuclear pore protein NUP205 in regulating nuclear localization and activity of transcriptional regulators YAP and TAZ.Human molecular genetics · 2023Article
- A general method for quantitative fractionation of mammalian cells.The Journal of cell biology · 2023Article
- Improving the hole picture: towards a consensus on the mechanism of nuclear transport.Biochemical Society transactions · 2023Article
- Article
- Self-regulation of the nuclear pore complex enables clogging-free crowded transport.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Review
- Function of Nuclear Pore Complexes in Regulation of Plant Defense Signaling.International journal of molecular sciences · 2022Review
- Non-transport roles of nuclear import receptors: In need of the right balance.Frontiers in cell and developmental biology · 2022Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Although the separation of transcription and translation, mediated by the nuclear envelope, is the defining characteristic of Eukaryotes, the barrier between the nuclear and cytoplasmic compartments needs to be semipermeable to enable material to be moved between them. Moreover, each compartment needs to have a distinctive complement of macromolecules to mediate specific functions and so movement between them needs to be controlled. This is achieved through the selective active transport of macromolecules through the nuclear pores that stud the nuclear envelope, and which serve as a conduit between these compartments. Nuclear pores are huge cylindrical macromolecular assemblies and are constructed from the order of 30 different proteins called nucleoporins. Nuclear pores have a central transport channel that is filled with a dense network of natively unfolded portions of many different nuclear pore proteins (nucleoporins or nups). This network generates a barrier that impedes, but does not entirely prevent, the diffusion of many macromolecules through the pores. The rapid movement of a range of proteins and RNAs through the pores is mediated by a range of transport factors that bind their cargo in one compartment and release it in the other. However, although as their size increases the diffusion of macromolecules through nuclear pores is progressively impaired, additional mechanisms, including the binding of some macromolecules to immobile components of each compartment and also the active removal of macromolecules from the inappropriate compartment, are needed to fully maintain the distinctive compositions of each compartment.
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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.