Results 31 to 40 of about 519,246 (298)

The Ebola Virus Interferon Antagonist VP24 Undergoes Active Nucleocytoplasmic Trafficking

Viruses, 2021
Viral interferon (IFN) antagonist proteins mediate evasion of IFN-mediated innate immunity and are often multifunctional, with distinct roles in viral replication.
Angela R. Harrison, Cassandra T. David, Stephen M. Rawlinson, Gregory W. Moseley   +3 more
doaj   +1 more source

Dimerization and nuclear entry of mPER proteins in mammalian cells [PDF]

, 2000
Nuclear entry of circadian oscillatory gene products is a key step for the generation of a 24-hr cycle of the biological clock. We have examined nuclear import of clock proteins of the mammalian period gene family and the effect of ...
Yagita, K. (Kazuhiro), Yamaguchi, S., Tamanini, F. (Filippo), Yasui, A. (Akira), Loros, J.J., Dunlap, J.C., Okamura, H. (Hitoshi), Hoeijmakers, J.H.J. (Jan), Horst, G.T.J. (Gijsbertus) van der   +8 more
core   +4 more sources

Adenovirus type 5 E4 Orf3 protein targets promyelocytic leukaemia (PML) protein nuclear domains for disruption via a sequence in PML isoform II that is predicted as a protein interaction site by bioinformatic analysis [PDF]

, 2009
Human adenovirus type 5 infection causes the disruption of structures in the cell nucleus termed promyelocytic leukaemia (PML) protein nuclear domains or ND10, which contain the PML protein as a critical component. This disruption is achieved through the
Araujo, Beech, Bernardi, Bernardi, Borden, Bourhis, Callaghan, Carvalho, Condemine, Condemine, Dalessio, Doucas, E. Emmott, Evans, Everett, Everett, Everett, Fagioli, Fagioli, Hoppe, Ishov, Janderova-Rossmeislova, Jensen, K. N. Leppard, Kalderon, Kelly, Liu, M. S. Cortese, Mohan, Nevels, Peng, Romero, Salomoni, Scaglioni, Shen, Sternsdorf, Stracker, T. Rich   +37 more
core   +1 more source

Neofunctionalization of ciliary BBS proteins to nuclear roles is likely a frequent innovation across eukaryotes

iScience, 2023
Summary: The eukaryotic BBSome is a transport complex within cilia and assembled by chaperonin-like BBS proteins. Recent work indicates nuclear functions for BBS proteins in mammals, but it is unclear how common these are in extant proteins or when they ...
Alexander Ewerling, Vanessa Maissl, Bill Wickstead, Helen Louise May-Simera   +3 more
doaj   +1 more source

Targeting a ruthenium complex to the nucleus with short peptides [PDF]

, 2010
In an effort to develop octahedral metal complexes as chemotherapeutic and diagnostic agents targeted to DNA, it is critical to optimize the properties of their cellular uptake.
Barton, Jacqueline K., Puckett, Cindy A.
core   +1 more source

Identification of Nuclear Localization Signals in the ORF2 Protein of Porcine Circovirus Type 3

Viruses, 2019
Porcine circovirus type 3 (PCV3) contains two major open reading frames (ORFs) and the ORF2 gene encodes the major structural capsid protein. In this study, nuclear localization of ORF2 was demonstrated by fluorescence observation and subcellular ...
Chunxiao Mou, Minmin Wang, Shuonan Pan, Zhenhai Chen   +3 more
doaj   +1 more source

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

Mad2, Bub3, and Mps1 regulate chromosome segregation and mitotic synchrony in Giardia intestinalis, a binucleate protist lacking an anaphase-promoting complex. [PDF]

, 2014
The binucleate pathogen Giardia intestinalis is a highly divergent eukaryote with a semiopen mitosis, lacking an anaphase-promoting complex/cyclosome (APC/C) and many of the mitotic checkpoint complex (MCC) proteins.
Cande, W Zacheus, Vicente, Juan-Jesus
core   +2 more sources

Enhancing the cellular uptake of Py–Im polyamides through next-generation aryl turns [PDF]

, 2012
Pyrrole–imidazole (Py–Im) hairpin polyamides are a class of programmable, sequence-specific DNA binding oligomers capable of disrupting protein–DNA interactions and modulating gene expression in living cells.
Baird, Belitsky, Best, Bijsterbosch, Bradford, Chenoweth, Chenoweth, Chenoweth, Cleutjens, Cohen, Crowley, David C. Montgomery, Dervan, Dervan, Dickinson, Dose, D’Adamio, Edelson, Edwards, Gissot, Herman, Hesselberth, Hsu, Hsu, Jacobs, Johnson, Jordan L. Meier, Krutzik, Kwon, Magee, Mapp, Matsuda, Meijsing, Mrksich, Muzikar, Nickols, Nickols, Nickols, Nishijima, Ohtsukia, Olenyuk, Peter B. Dervan, Poulin-Kerstien, Reddy, Riegman, Rucker, Schmidt, Schultz, So, Swalley, Tsai, Van Dyke, Vaquerizas, Vichai, Yao   +54 more
core   +2 more sources

Interaction with LC8 is required for Pak1 nuclear import and is indispensable for zebrafish development. [PDF]

PLoS ONE, 2009
Pak1 (p21 activated kinase 1) is a serine/threonine kinase implicated in regulation of cell motility and survival and in malignant transformation of mammary epithelial cells.
Christine M Lightcap, Gabor Kari, Luis E Arias-Romero, Jonathan Chernoff, Ulrich Rodeck, John C Williams   +5 more
doaj   +1 more source