ReviewBiochimica et biophysica acta2009
Functionalization of a nanopore: the nuclear pore complex paradigm.
Review in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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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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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Multicolor Super-resolution Fluorescence Imaging of Cells by Expansion Microscopy.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Potential of Nuclear Pore Complexes in Cancer Therapy.Molecules (Basel, Switzerland) · 2024Review
- Crowding-induced phase separation of nuclear transport receptors in FG nucleoporin assemblies.eLife · 2022Article
- Entropic Trapping of DNA with a Nanofiltered Nanopore.ACS applied nano materials · 2019Article
- A coarse-grained computational model of the nuclear pore complex predicts Phe-Gly nucleoporin dynamics.The Journal of general physiology · 2017Article
- Slide-and-exchange mechanism for rapid and selective transport through the nuclear pore complex.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Disordered proteinaceous machines.Chemical reviews · 2014Review
- Enriching the pore: splendid complexity from humble origins.Traffic (Copenhagen, Denmark) · 2014Review
- Article
- Nucleocytoplasmic transport: a role for nonspecific competition in karyopherin-nucleoporin interactions.Molecular & cellular proteomics : MCP · 2012Article
- The yeast nuclear pore complex and transport through it.Genetics · 2012Article
- Nucleocytoplasmic shuttling of cytoskeletal proteins: molecular mechanism and biological significance.International journal of cell biology · 2012Article
- Single molecule studies of nucleocytoplasmic transport.Biochimica et biophysica acta · 2011Review
- Regaining eukaryotic identity after cell division: relax, young cell.Biophysical journal · 2009Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Biological cells maintain a myriad of nanopores which, although relying on the same basic small-hole principle, serve a large variety of functions. Here we consider how the nuclear pore complex (NPC), a large nanopore mediating the traffic between genetic material and protein synthesizing apparatus, is functionalized to carry out a set of transport functions. A major parameter of NPC functionalization is a lining of it external and internal surfaces with so-called phenylalanine glycine (FG) proteins. FG proteins integrate a multitude of transport factor binding sites into intrinsically disordered domains. This surprising finding has given rise to a number of transport models assigning direct gating functions to FG proteins. However, recent data suggest that the properties of FG proteins cannot be properly assessed by considering only the purified, transport-factor-stripped NPC. At physiological conditions transport factors may shape FG proteins in a way allotting an essential role to surface diffusion, reconciling tight binding with efficient transport. Thus, NPC studies are revealing both general traits and novel aspects of nanopore functionalization. In addition, they inspire artificial molecule sorters for proteomic and pharmaceutical applications.
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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.