Results 41 to 50 of about 15,999 (168)

δ-Catenin promotes prostate cancer cell growth and progression by altering cell cycle and survival gene profiles

Molecular Cancer, 2009
Background δ-Catenin is a unique member of β-catenin/armadillo domain superfamily proteins and its primary expression is restricted to the brain. However, δ-catenin is upregulated in human prostatic adenocarcinomas, although the effects of δ-catenin ...
Chen Yan-Hua, Wang Tao, Lu Jian-Ping, Abdallah Agustin, Zeng Yan, Terrian David M, Kim Kwonseop, Lu Qun   +7 more
doaj   +1 more source

Architecture of the chromatin remodeler RSC and insights into its nucleosome engagement. [PDF]

, 2019
Eukaryotic DNA is packaged into nucleosome arrays, which are repositioned by chromatin remodeling complexes to control DNA accessibility. The Saccharomyces cerevisiae RSC (Remodeling the Structure of Chromatin) complex, a member of the SWI/SNF chromatin ...
Afonine, Afonine, Allen, Angus-Hill, Ashkenazy, Ashkenazy, Asturias, Badis, Buchan, Buchan, Cairns, Cairns, Campsteijn, Chaban, Chambers, Chatterjee, Clapier, Clapier, Côté, Da, Dechassa, Duan, Dutta, Dürr, El-Gebali, Emsley, Erkina, Filippakopoulos, Goddard, Han, Jones, Jones, Kadoch, Kasten, Klein-Brill, Krietenstein, Kuryan, Leschziner, Leschziner, Li, Liu, Lopéz-Blanco, Mashtalir, Morin, Nagai, Nakane, Ng, Patel, Pettersen, Puig, Saha, Sammak, Schorb, Schubert, Sen, Shim, Sievers, Skiniotis, Smith, Suloway, Söding, Tan, Tsunaka, Ungar, Valencia, Wagner, Wang, Wilson, Xia, Yan, Yang, Ye, Yen, Zhang, Zhang, Zhang, Zheng, Zivanov, Zivanov, Zukin   +79 more
core   +3 more sources

Unveiling the Binding between the Armadillo-Repeat Domain of Plakophilin 1 and the Intrinsically Disordered Transcriptional Repressor RYBP

Biomolecules
Plakophilin 1 (PKP1), a member of the p120ctn subfamily of the armadillo (ARM)-repeat-containing proteins, is an important structural component of cell–cell adhesion scaffolds although it can also be ubiquitously found in the cytoplasm and the nucleus ...
Salome Araujo-Abad, Bruno Rizzuti, Miguel Vidal, Olga Abian, María Esther Fárez-Vidal, Adrian Velazquez-Campoy, Camino de Juan Romero, José L. Neira   +7 more
doaj   +1 more source

Structural characterization of human importin alpha 7 in its cargo-free form at 2.5 Å resolution

Scientific Reports, 2022
Shuttling of macromolecules between nucleus and cytoplasm is a tightly regulated process mediated through specific interactions between cargo and nuclear transport proteins.
S. Tsimbalyuk, C. M. Donnelly, J. K. Forwood   +2 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

A motif within the armadillo repeat of Parkinson’s-linked LRRK2 interacts with FADD to hijack the extrinsic death pathway

Scientific Reports, 2018
In experimental models, both in vivo and cellular, over-expression of Parkinson’s linked mutant leucine-rich repeat kinase 2 (LRRK2) is sufficient to induce neuronal death. While several cell death associated proteins have been linked to LRRK2, either as
Nasia Antoniou, Dimitrios Vlachakis, Anna Memou, Emmanouela Leandrou, Polytimi-Eleni Valkimadi, Katerina Melachroinou, Diane B. Re, Serge Przedborski, William T. Dauer, Leonidas Stefanis, Hardy J. Rideout   +10 more
doaj   +1 more source

FAK acts as a suppressor of RTK-MAP kinase signalling in Drosophila melanogaster epithelia and human cancer cells [PDF]

, 2014
Receptor Tyrosine Kinases (RTKs) and Focal Adhesion Kinase (FAK) regulate multiple signalling pathways, including mitogen-activated protein (MAP) kinase pathway. FAK interacts with several RTKs but little is known about how FAK regulates their downstream
A Bergmann, A Boulay, A Ueda, AC Dar, B Corkery, B Gabriel, BA Edgar, BA Hay, BJ Dickson, C Grabbe, CJ Marshall, D Tenenbaum, DD Schlaepfer, DJ Sieg, E Macia, E Rainero, E Rainero, E Sandilands, E Sandilands, Emma Sandilands, FD Karim, FJ Diaz-Benjumea, G Adam, GL Fox, I Bongarzone, I Plaza-Menacho, I Rebay, Iain MacPherson, IH Gelman, J Cordero, J Fujimoto, J Verdu, J Zhao, Jesica Diaz Vera, Jim C. Norman, JR Infante, JT Parsons, JT Price, Juan Pablo Macagno, K Blochlinger, K Halfar, K Mesaki, K Sawamoto, L Henriksen, L Sadowski, LV Owens, M Agochiya, M Ayaki, M Freeman, M Grieco, M Miaczynska, M Roberts, M Santoro, M Therrien, M Vidal, M Vidal, Marcos Vidal, Margaret Frame, Marshall S. Horwitz, MC Frame, ME Grether, ME Irwin, MM Bradford, P Kurada, P-I Tsai, PM Siesser, R Gleichauf, R Ohta, RD Read, RH Palmer, Ruth Palmer, S Leboulleux, S Murakami, S Rizzolio, S Sigismund, SA Speicher, SM Jhiang, SY Chen, T Das, T Matsuo, T-H Chen, W Long, WG Cance, X Zhao, Y Zheng, Yachuan Yu, Z Lu   +86 more
core   +4 more sources

EFR3A, an Intriguing Gene, and Protein with a Scaffolding Function

Cells
The EFR3 (Eighty-Five Requiring 3) protein and its homologs are rather poorly understood eukaryotic plasma membrane peripheral proteins. They belong to the armadillo-like family of superhelical proteins.
Magdalena Trybus, Anita Hryniewicz-Jankowska, Aleksander Czogalla, Aleksander F. Sikorski   +3 more
doaj   +1 more source

Novel Flavivirus Antiviral That Targets the Host Nuclear Transport Importin α/β1 Heterodimer

Cells, 2019
Dengue virus (DENV) threatens almost 70% of the world’s population, with no effective vaccine or therapeutic currently available. A key contributor to infection is nuclear localisation in the infected cell of DENV nonstructural protein 5 (NS5 ...
Sundy N. Y. Yang, Sarah C. Atkinson, Johanna E. Fraser, Chunxiao Wang, Belinda Maher, Noelia Roman, Jade K. Forwood, Kylie M. Wagstaff, Natalie A. Borg, David A. Jans   +9 more
doaj   +1 more source

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

FEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes, Guilherme M. Azevedo, Amanda P. Barcellos, Diana Bahia   +3 more
wiley   +1 more source