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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.


importin, karyopherin beta1
Nucleocytoplasmic transport, a signal- and energy-dependent process, takes place through nuclear pore complexes embedded in the nuclear envelope. The import of proteins containing a nuclear localization signal (NLS) requires the NLS import receptor, a heterodimer of importin alpha and beta subunits also known as karyopherins. Importin alpha binds the NLS-containing cargo in the cytoplasm and importin beta docks the complex at the cytoplasmic side of the nuclear pore complex. In the presence of nucleoside triphosphates and the small GTP binding protein Ran, the complex moves into the nuclear pore complex and the importin subunits dissociate. Importin alpha enters the nucleoplasm with its passenger protein and importin beta remains at the pore. Interactions between importin beta and the FG repeats of nucleoporins are essential in translocation through the pore complex. The protein encoded by this gene is a member of the importin beta family. [provided by RefSeq, Jul 2008] (from NCBI)
Papers using importin antibodies
Isolation of intact nuclei of high purity from mouse liver.
Bridger Joanna Mary, In PLoS ONE, 2009
... Anti-importin 5 (sc-17802), importin beta (sc-1919) and importin 7 (sc-55235) were purchased from Santa Cruz Biotechnology.
Partial loss of ataxin-1 function contributes to transcriptional dysregulation in spinocerebellar ataxia type 1 pathogenesis
MacKintosh Carol et al., In Biochemical Journal, 2009
... The anti-KPNA3 (importin α4/karyopherin α3) antibody is A301-626A from Bethyl Laboratories, and recognizes an ...
The Nup358-RanGAP complex is required for efficient importin alpha/beta-dependent nuclear import
Kaether Christoph et al., In Cellular and Molecular Life Sciences, 2007
... ], mouse anti-importin β1 (3E9; Dianova), mouse anti-myc (9E10; Santa ...
Predominant intracellular localization of the type I transforming growth factor-β receptor and increased nuclear accumulation after growth arrest
Maher Pamela A. et al., In The Journal of Cell Biology, 1999
... ), using antibodies against the Xpress epitope tag, EGFR, c-Jun, c-Fos, c-Myc, cyclin E, and importin β (Santa Cruz Biotechnology, Inc.), phospho-c-Jun (New England ...
Rac1 and a GTPase-activating protein, MgcRacGAP, are required for nuclear translocation of STAT transcription factors
Kitamura Toshio et al., In The Journal of Cell Biology, 1999
The rabbit polyclonal anti-Rac1, ...
Papers on importin
Nuclear import of exogenous FGF1 requires the ER-protein LRRC59 and the importins Kpnα1 and Kpnβ1.
Wiedlocha et al., Oslo, Norway. In Traffic, 2012
LRRC59 facilitates transport of cytosolic FGF1 through nuclear pores by interaction with Kpns and movement of LRRC59 along the ER and NE membranes
Importin β1 protein-mediated nuclear localization of death receptor 5 (DR5) limits DR5/tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL)-induced cell death of human tumor cells.
Yagita et al., Tokyo, Japan. In J Biol Chem, 2012
Findings suggest that the importin beta1-mediated nuclear localization of DR5 limits the DR5/TRAIL-induced cell death of human tumor cells and thus can be a novel target to improve cancer therapy with recombinant TRAIL and anti-DR5 antibodies.
Nuclear transport of Wilms' tumour protein Wt1 involves importins α and β.
Scholz et al., Lübeck, Germany. In Cell Physiol Biochem, 2011
Nuclear translocation of Wilms' tumour protein involves importins alpha and beta, and a nuclear localisation signal in the third zinc finger
Distinct effects of importin α2 and α4 on Oct3/4 localization and expression in mouse embryonic stem cells.
Jans et al., Australia. In Faseb J, 2011
IMPalpha4 overexpression induced a significant decrease in Oct3/4 protein levels compared to control transfections. IMPalpha4 protein showed a unique and striking shift in subcellular localization from the nucleus to the cytoplasm during differentiation.
Overexpression of Kpnβ1 and Kpnα2 importin proteins in cancer derives from deregulated E2F activity.
Leaner et al., Cape Town, South Africa. In Plos One, 2010
Findings suggest that the deregulated activity of E2F in cancer cells causes increased activation of the Kpnbeta1 and Kpnalpha2 promoters, leading to elevated levels of these proteins, and ultimately impacting the cancer phenotype.
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