Results 11 to 20 of about 29,648 (219)

Importin-9 wraps around the H2A-H2B core to act as nuclear importer and histone chaperone [PDF]

eLife, 2019
We report the crystal structure of nuclear import receptor Importin-9 bound to its cargo, the histones H2A-H2B. Importin-9 wraps around the core, globular region of H2A-H2B to form an extensive interface.
Abhilash Padavannil, Prithwijit Sarkar, Seung Joong Kim, Tolga Cagatay, Jenny Jiou, Chad A Brautigam, Diana R Tomchick, Andrej Sali, Sheena D'Arcy, Yuh Min Chook   +9 more
doaj   +3 more sources

Xenopus importin beta validates human importin beta as a cell cycle negative regulator [PDF]

BMC Cell Biology, 2008
Background Human importin beta has been used in all Xenopus laevis in vitro nuclear assembly and spindle assembly studies. This disconnect between species raised the question for us as to whether importin beta was an authentic negative regulator of cell ...
Forbes Douglass J, Chan Rene C, Delmar Valerie A   +2 more
doaj   +3 more sources

Structural Insights Into the Nuclear Import of Gallid Alphaherpesvirus 1 Large Tegument Protein. [PDF]

Microbiologyopen
The study identifies and characterizes a bipartite nuclear localization signal within the GaAHV‐1 UL36 large tegument protein, revealing its structural interaction with importin α/β1 and confirming a conserved mechanism of nuclear import through biochemical, crystallographic, and mutational analyses.
Nath BK, Swarbrick CMD, Blades R, Ariawan D, Tietz O, Alvisi G, Forwood JK, Sarker S.   +7 more
europepmc   +2 more sources

The importin-alpha superfamily engages in ethylene signaling by shuttling ETHYLENE INSENSITIVE 2 from the endoplasmic reticulum to the nucleus. [PDF]

FEBS J
The plant hormone ethylene regulates plant growth, ripening, senescence, and stress responses. The hormonal signal transmission, from receptors at the ER membrane to the transcriptional regulators in the nucleus, is still not completely understood.
Wynen F, Maika JE, Eberle RJ, Jahnke N, Wiermer M, Hartmann L, Simon R, Groth G.   +7 more
europepmc   +2 more sources

The Drosophila importin-α3 is required for nuclear import of notch in vivo and it displays synergistic effects with notch receptor on cell proliferation. [PDF]

PLoS ONE, 2013
The Notch signaling pathway controls diverse cell-fate specification events throughout development. The versatility of this pathway to influence different aspects of development comes from its multiple levels of regulation.
Nalani Sachan, Abhinava K Mishra, Mousumi Mutsuddi, Ashim Mukherjee   +3 more
doaj   +1 more source

Importin 7 and Importin α/Importin β Are Nuclear Import Receptors for the Glucocorticoid Receptor [PDF]

Molecular Biology of the Cell, 2004
The vertebrate glucocorticoid receptor (GR) is cytoplasmic without hormone and localizes to the nucleus after hormone binding. GR has two nuclear localization signals (NLS): NL1 is similar in sequence to the SV40 NLS; NL2 is poorly defined, residing in the ligand-binding domain.
Neal D, Freedman, Keith R, Yamamoto
openaire   +2 more sources

Importin α5 Regulates Anxiety through MeCP2 and Sphingosine Kinase 1

Cell Reports, 2018
Summary: Importins mediate transport from synapse to soma and from cytoplasm to nucleus, suggesting that perturbation of importin-dependent pathways should have significant neuronal consequences.
Nicolas Panayotis, Anton Sheinin, Shachar Y. Dagan, Michael M. Tsoory, Franziska Rother, Mayur Vadhvani, Anna Meshcheriakova, Sandip Koley, Letizia Marvaldi, Didi-Andreas Song, Eitan Reuveny, Britta J. Eickholt, Enno Hartmann, Michael Bader, Izhak Michaelevski, Mike Fainzilber   +15 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

Expression Analysis and Nuclear Import Study of Full-length Isoforms Importin α as 6x Histidin-tagged Fusion Protein on the Intracellular Localization of Recombinant HBV Core Protein

Indonesian Journal of Biotechnology, 2005
Isoform importin α molecules play a central role in the classical nuclear import pathway, that occurs through the nuclear pore complex (NPC) and typically requires a specific nuclear localization signal (NLS).
Aris Haryanto
doaj   +1 more source

Crystallographic data of an importin-α3 dimer in which the two protomers are bridged by a bipartite nuclear localization signal

Data in Brief, 2023
53BP1 (TP53-binding protein 1), a key player in DNA double-strand break repair, has a classical bipartite nuclear localization signal (NLS) of sequence 1666-GKRKLITSEEERSPAKRGRKS-1686 that binds to importin-α, a nuclear import adaptor protein ...
Yoshiyuki Matsuura
doaj   +1 more source