Results 51 to 60 of about 6,766 (259)

HIV-1 Vpr antagonizes innate immune activation by targeting karyopherin-mediated NF-κB/IRF3 nuclear transport

eLife, 2020
HIV-1 must replicate in cells that are equipped to defend themselves from infection through intracellular innate immune systems. HIV-1 evades innate immune sensing through encapsidated DNA synthesis and encodes accessory genes that antagonize specific ...
Hataf Khan, Rebecca P Sumner, Jane Rasaiyaah, Choon Ping Tan, Maria Teresa Rodriguez-Plata, Chris Van Tulleken, Douglas Fink, Lorena Zuliani-Alvarez, Lucy Thorne, David Stirling, Richard SB Milne, Greg J Towers   +11 more
doaj   +1 more source

Karyopherins: potential biological elements involved in the delayed graft function in renal transplant recipients

BMC Medical Genomics, 2014
BackgroundImmediately after renal transplantation, patients experience rapid and significant improvement of their clinical conditions and undergo considerable systemic and cellular modifications.
G. Zaza, F. Rascio, P. Pontrelli, S. Granata, P. Stifanelli, M. Accetturo, N. Ancona, L. Gesualdo, A. Lupo, G. Grandaliano   +9 more
semanticscholar   +2 more sources

Comparative interactomics provides evidence for functional specialization of the nuclear pore complex [PDF]

, 2017
The core architecture of the eukaryotic cell was established well over one billion years ago, and is largely retained in all extant lineages. However, eukaryotic cells also possess lineage-specific features, frequently keyed to specific functional ...
Field, Mark C., Obado, Samson O., Rout, Michael P.   +2 more
core   +2 more sources

Cloning and characterization of human karyopherin β3 [PDF]

Proceedings of the National Academy of Sciences, 1997
Nuclear import of classical nuclear localization sequence-bearing proteins is mediated by karyopherin α/β1 heterodimers. A second nuclear import pathway, mediated by karyopherin β2 (transportin), recently was described for mRNA-binding proteins. Here we report the cloning and characterization of human karyopherin β3, which may be involved in a third ...
N R, Yaseen, G, Blobel
openaire   +2 more sources

Identification of karyopherins involved in the nuclear import of RNA exosome subunit Rrp6 in Saccharomyces cerevisiae

Journal of Biological Chemistry, 2017
The exosome is a conserved multiprotein complex essential for RNA processing and degradation. The nuclear exosome is a key factor for pre-rRNA processing through the activity of its catalytic subunits, Rrp6 and Rrp44. In Saccharomyces cerevisiae, Rrp6 is
F. Gonzales-Zubiate, E. K. Okuda, J. D. da Cunha, C. Oliveira   +3 more
semanticscholar   +1 more source

The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence. [PDF]

Proceedings of the National Academy of Sciences, 1996
By using proteolysis, recombinant mutant proteins, or synthetic peptides and by testing these reagents in liquid phase binding or nuclear import assays, we have mapped binding regions of karyopherin alpha. We found that the C-terminal region of karyopherin alpha recognizes the nuclear localization sequence (NLS), whereas its N-terminal region binds ...
J, Moroianu, G, Blobel, A, Radu
openaire   +2 more sources

IPO5 promotes the proliferation and tumourigenicity of colorectal cancer cells by mediating RASAL2 nuclear transportation

Journal of Experimental & Clinical Cancer Research, 2019
Background Karyopherin nuclear transport receptors play important roles in tumour development and drug resistance and have been reported as potential biomarkers and therapeutic targets for tumour treatment.
Wenjuan Zhang, Yanxia Lu, Xiaomin Li, Jianming Zhang, Weihao Lin, Wei Zhang, Lin Zheng, Xuenong Li   +7 more
doaj   +1 more source

Sequences within the C terminus of the metabotropic glutamate receptor 5 (mGluR5) are responsible for inner nuclear membrane localization [PDF]

, 2017
Traditionally, G-protein-coupled receptors (GPCR) are thought to be located on the cell surface where they transmit extracellular signals to the cytoplasm.
Harmon, Steven K., Jong, Yuh-Jiin I., Kumar, Vikas, O\u27Malley, Karen L., Sergin, Ismail   +4 more
core   +2 more sources

Karyopherin α 3 and Karyopherin α 4 Proteins Mediate the Nuclear Import of Methyl-CpG Binding Protein 2 [PDF]

Journal of Biological Chemistry, 2015
Methyl-CpG binding protein 2 (MeCP2) is a nuclear protein with important roles in regulating chromatin structure and gene expression, and mutations in MECP2 cause Rett syndrome (RTT). Within the MeCP2 protein sequence, the nuclear localization signal (NLS) is reported to reside between amino acids 255-271, and certain RTT-causing mutations overlap with
Steven Andrew, Baker, Laura Marie, Lombardi, Huda Yahya, Zoghbi   +2 more
openaire   +2 more sources

Diversification of importin-α isoforms in cellular trafficking and disease states. [PDF]

, 2015
The human genome encodes seven isoforms of importin α which are grouped into three subfamilies known as α1, α2 and α3. All isoforms share a fundamentally conserved architecture that consists of an N-terminal, autoinhibitory, importin-β-binding (IBB ...
Ahluwalia, Andrade, Ao, Aratani, Arjomand, Banninger, Bannister, Bao, Bednenko, Ben-Yaakov, Bian, Bian, Boivin, Chang, Chen, Chen, Chen, Cingolani, Conti, Conti, Cook, Cortes, Cuomo, Dahl, de Barros, Depping, Dissanayake, Dolinsky, Donaldson, Du, Fagerlund, Fagerlund, Fagerlund, Fahrenkrog, Fanara, Fischer, Fontes, Fontes, Forwood, Friedrich, Frieman, Gabriel, Ghosh, Giesecke, Gino Cingolani, Glinsky, Goldfarb, Gorlich, Gorlich, Gousias, Gousias, Grundt, Guillemain, Haenni, Han, Hanz, Harreman, Harreman, Hatayama, Hearps, Henikoff, Hogarth, Holt, Hosokawa, Hu, Huang, Huang, Hudjetz, Huenniger, Hugel, Ilmarinen, Isegawa, Jans, Jenkins, Jensen, Jin, Kamata, Kelley, Kim, Kitamura, Kobe, Kohler, Kohler, Kohler, Koksal, Koksal, Kosugi, Kumar, Lai, Lange, Larkin, Laurila, Lee, Levin, Li, Li, Li, Liang, Lin, Liu, Liu, Lott, Lott, Lufei, Ma, Maas, Macara, Mahalakshmi, Marchenko, Marfori, Marshall, Mason, Matsuura, Matsuura, McConville, Mehmood, Melen, Melzer, Meyer, Misheva, Miyamoto, Miyamoto, Miyamoto, Montgomery, Moriyama, Morris, Mortezavi, Nachury, Nadler, Najarro, Nakamura, Nardozzi, Nardozzi, Nishinaka, Nitahara-Kasahara, O'Neill, O'Neill, Okada, Paciorkowski, Page, Papadopoulos, Paterson, Perez-Villar, Perry, Pettersen, Poon, Pujol, Pumroy, Pumroy, Qu, Reid, Reid, Resa-Infante, Resa-Infante, Rivera, Roman, Rona, Rother, Roussos, Ruth A. Pumroy, Sakai, Seki, Sekimoto, Sekimoto, Shabman, Shaw, Shin, Shmidt, Simkus, Sims, Snow, Song, Spanopoulou, Stewart, Sun, Sun, Sun, Tachibana, Takeda, Takeda, Takeda, Talcott, Tarendeau, Tay, Taylor, Tejomurtula, Theiss, Thomas, Torgerson, Tseng, Tsuji, Umegaki, Ushijima, van der Watt, van der Watt, Wagstaff, Wang, Wang, Wang, Wang, Weis, Weis, Welch, Wente, Winnepenninckx, Xu, Yang, Yang, Yano, Yasuhara, Yasuhara, Ye, Yeung, Yeung, Yoshitake, Zachariae, Zhang, Zhen, Zheng, Zhong, Zhou, Zienkiewicz   +221 more
core   +2 more sources