"alpha Karyopherins" 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.
Nucleocytoplasmic transport molecules that bind to the NUCLEAR LOCALIZATION SIGNALS of cytoplasmic molecules destined to be imported into the CELL NUCLEUS. Once attached to their cargo they bind to BETA KARYOPHERINS and are transported through the NUCLEAR PORE COMPLEX. Inside the CELL NUCLEUS alpha karyopherins dissociate from beta karypherins and their cargo. They then form a complex with CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN and RAN GTP-BINDING PROTEIN which is exported to the CYTOPLASM.
| Descriptor ID |
D028901
|
| MeSH Number(s) |
D12.776.157.530.750.500.100 D12.776.543.585.750.500.100 D12.776.660.502.100
|
| Concept/Terms |
alpha Karyopherins- alpha Karyopherins
- Karyopherins, alpha
- Karyopherin alpha
- Nuclear Localization Signal-Binding Protein
- NLS-Binding Protein
- NLSBP
- Nuclear Localization Sequence Receptor
- Importin-alpha
- NLS Receptor
- receptor, NLS
|
Below are MeSH descriptors whose meaning is more general than "alpha Karyopherins".
Below are MeSH descriptors whose meaning is more specific than "alpha Karyopherins".
This graph shows the total number of publications written about "alpha Karyopherins" by people in this website by year, and whether "alpha Karyopherins" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2004 | 1 | 0 | 1 |
| 2010 | 3 | 1 | 4 |
| 2011 | 2 | 0 | 2 |
| 2014 | 0 | 1 | 1 |
| 2015 | 2 | 0 | 2 |
| 2017 | 2 | 0 | 2 |
| 2022 | 0 | 2 | 2 |
| 2024 | 1 | 0 | 1 |
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Below are the most recent publications written about "alpha Karyopherins" by people in Profiles.
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Ko YH, Lokareddy RK, Doll SG, Yeggoni DP, Girdhar A, Mawn I, Klim JR, Rizvi NF, Meyers R, Gillilan RE, Guo L, Cingolani G. Single Acetylation-mimetic Mutation in TDP-43 Nuclear Localization Signal Disrupts Importin a1/? Signaling. J Mol Biol. 2024 10 15; 436(20):168751.
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Doll SG, Cingolani G. Importin a/? and the tug of war to keep TDP-43 in solution: quo vadis? Bioessays. 2022 12; 44(12):e2200181.
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Doll SG, Meshkin H, Bryer AJ, Li F, Ko YH, Lokareddy RK, Gillilan RE, Gupta K, Perilla JR, Cingolani G. Recognition of the TDP-43 nuclear localization signal by importin a1/?. Cell Rep. 2022 06 28; 39(13):111007.
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Sankhala RS, Lokareddy RK, Begum S, Pumroy RA, Gillilan RE, Cingolani G. Three-dimensional context rather than NLS amino acid sequence determines importin a subtype specificity for RCC1. Nat Commun. 2017 10 17; 8(1):979.
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Wu W, Sankhala RS, Florio TJ, Zhou L, Nguyen NLT, Lokareddy RK, Cingolani G, Pant? N. Synergy of two low-affinity NLSs determines the high avidity of influenza A virus nucleoprotein NP for human importin a isoforms. Sci Rep. 2017 09 12; 7(1):11381.
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Pumroy RA, Cingolani G. Diversification of importin-a isoforms in cellular trafficking and disease states. Biochem J. 2015 Feb 15; 466(1):13-28.
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Pumroy RA, Ke S, Hart DJ, Zachariae U, Cingolani G. Molecular determinants for nuclear import of influenza A PB2 by importin a isoforms 3 and 7. Structure. 2015 Feb 03; 23(2):374-84.
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Lieu KG, Shim EH, Wang J, Lokareddy RK, Tao T, Cingolani G, Zambetti GP, Jans DA. The p53-induced factor Ei24 inhibits nuclear import through an importin ?-binding-like domain. J Cell Biol. 2014 May 12; 205(3):301-12.
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Pumroy RA, Nardozzi JD, Hart DJ, Root MJ, Cingolani G. Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin a5. J Biol Chem. 2012 Jan 13; 287(3):2022-31.
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Lott K, Bhardwaj A, Sims PJ, Cingolani G. A minimal nuclear localization signal (NLS) in human phospholipid scramblase 4 that binds only the minor NLS-binding site of importin alpha1. J Biol Chem. 2011 Aug 12; 286(32):28160-9.