Nucleocytoplasmic Transport Proteins
"Nucleocytoplasmic Transport Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Proteins involved in the process of transporting molecules in and out the cell nucleus. Included here are: NUCLEOPORINS, which are membrane proteins that form the NUCLEAR PORE COMPLEX; KARYOPHERINS, which carry molecules through the nuclear pore complex; and proteins that play a direct role in the transport of karyopherin complexes through the nuclear pore complex.
| Descriptor ID |
D029543
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| MeSH Number(s) |
D12.776.157.530.750 D12.776.543.585.750
|
| Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Nucleocytoplasmic Transport Proteins".
Below are MeSH descriptors whose meaning is more specific than "Nucleocytoplasmic Transport Proteins".
This graph shows the total number of publications written about "Nucleocytoplasmic Transport Proteins" by people in this website by year, and whether "Nucleocytoplasmic Transport Proteins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2004 | 1 | 0 | 1 |
| 2019 | 0 | 1 | 1 |
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Below are the most recent publications written about "Nucleocytoplasmic Transport Proteins" by people in Profiles.
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Improved clinical outcome following liver transplant in patients with ethylmalonic encephalopathy. Am J Med Genet A. 2019 06; 179(6):1015-1019.
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Nuclear Export of Smads by RanBP3L Regulates Bone Morphogenetic Protein Signaling and Mesenchymal Stem Cell Differentiation. Mol Cell Biol. 2015 May; 35(10):1700-11.
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IL-30 (IL27p28) attenuates liver fibrosis through inducing NKG2D-rae1 interaction between NKT and activated hepatic stellate cells in mice. Hepatology. 2014 Dec; 60(6):2027-39.
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Nuclear export of Smad2 and Smad3 by RanBP3 facilitates termination of TGF-beta signaling. Dev Cell. 2009 Mar; 16(3):345-57.
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Computational and biochemical identification of a nuclear pore complex binding site on the nuclear transport carrier NTF2. J Mol Biol. 2004 Nov 19; 344(2):303-10.
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Androgen-induced NH2- and COOH-terminal Interaction Inhibits p160 coactivator recruitment by activation function 2. J Biol Chem. 2001 Nov 09; 276(45):42293-301.