Results 81 to 90 of about 709,714 (368)

Raver2, a new member of the hnRNP family [PDF]

, 2005
Raver2 was identified as a novel member of the hnRNP family based on sequence homology within three RNA recognition motifs and its general domain organization reminiscent of the previously described raver1 protein.
Arnold, Hans Henning, Fabienke, Manuela, Illenberger, Susanne, Jockusch, Brigitte M., Kirsch, Joachim, Kleinhenz, Berenike, Swiniarski, Sascha, Wittenmayer, Nina   +7 more
core   +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

Novel localization of formin mDia2: importin β-mediated delivery to and retention at the cytoplasmic side of the nuclear envelope

Biology Open, 2015
The formin family proteins are important regulators of actin polymerization that are involved in many cellular processes. However, little is known about their specific cellular localizations.
Xiaowei Shao, Keiko Kawauchi, G. V. Shivashankar, Alexander D. Bershadsky   +3 more
doaj   +1 more source

posterior end mark 2 (pem-2),pem-4,pem-5, andpem-6: Maternal Genes with Localized mRNA in the Ascidian Embryo [PDF]

, 1997
The posterior–vegetal cytoplasm of an ascidian egg contains maternal factors required for pattern formation and cell specification of the embryo. We report here the isolation and characterization of cDNA clones for novel maternal genes,posterior end mark
Satoh, Noriyuki, Satou, Yutaka
core   +1 more source

Probing the Specificity of Binding to the Major Nuclear Localization Sequence-binding Site of Importin-α Using Oriented Peptide Library Screening*

Journal of Biological Chemistry, 2010
Importin-α is the nuclear import receptor that recognizes the classic monopartite and bipartite nuclear localization sequences (cNLSs), which contain one or two clusters of basic amino acids, respectively.
Sundy N. Y. Yang, A. Takeda, M. Fontes, Jonathan M. Harris, D. Jans, B. Kobe   +5 more
semanticscholar   +1 more source

Phylogenetic analysis of the SAP30 family of transcriptional regulators reveals functional divergence in the domain that binds the nuclear matrix [PDF]

, 2009
Background: Deacetylation of histones plays a fundamental role in gene silencing, and this is mediated by a corepressor complex containing Sin3 as an essential scaffold protein. In this report we examine the evolution of two proteins in this complex, the
Heinonen, TYK, Lohi, O, Maki, M, Viiri, KM   +3 more
core   +3 more sources

Sequences enriched in Alu repeats drive nuclear localization of long RNAs in human cells

Nature, 2017
Long noncoding RNAs (lncRNAs) are emerging as key parts of multiple cellular pathways, but their modes of action and how these are dictated by sequence remain unclear.
Yoav Lubelsky, I. Ulitsky
semanticscholar   +1 more source

Insights into PI3K/AKT signaling in B cell development and chronic lymphocytic leukemia

FEBS Letters, EarlyView.
This Review explores how the phosphoinositide 3‐kinase and protein kinase B pathway shapes B cell development and drives chronic lymphocytic leukemia, a common blood cancer. It examines how signaling levels affect disease progression, addresses treatment challenges, and introduces novel experimental strategies to improve therapies and patient outcomes.
Maike Buchner
wiley   +1 more source

Plastid proteome prediction for diatoms and other algae with secondary plastids of the red lineage [PDF]

, 2014
The plastids of ecologically and economically important algae from phyla such as stramenopiles, dinoflagellates and cryptophytes were acquired via a secondary endosymbiosis and are surrounded by three or four membranes.
Allen, Allen, Altschul, Apt, Armbrust, Ast, Baldi, Bendtsen, Blum, Bowler, Brown, Bruckner, Bullmann, Cavalier-Smith, Cock, Crooks, Curtis, Domergue, Emanuelsson, Emanuelsson, Fawcett, Felsner, Gould, Gould, Grigoriev, Grouneva, Gruber, Gruber, Gruber, Gschloessl, Hall, Hempel, Hempel, Horton, Huesgen, Joshi-Deo, Kilian, Kilian, Kitao, Kitao, Kroth, Kroth, Kroth, Lepetit, Liaud, Mernberger, Moog, Nielsen, Nielsen, Patron, Patron, Petersen, Schneider, Siaut, Sommer, Sturm, Tachibana, Tanaka, Terashima, Timmis, Vugrinec, Weber, Yandell   +62 more
core   +2 more sources

Nuclear accumulation of Saccharomyces cerevisiae Mcm3 is dependent on its nuclear localization sequence [PDF]

Genes to Cells, 1997
Background:The proteins of the Mcm2‐7 family are required for the initiation of DNA replication. In Saccharomyces cerevisiae the nuclear envelope does not break down during the mitotic phase of the cell cycle. Large nuclear proteins, such as the Mcm proteins, which accumulate in the nucleus during specific portions of the cell cycle, must have ...
Young, Michael R., Suzuki, Katsunori, Yan, Hong, Gibson, Susan, Tye, Bik Kwoon   +4 more
openaire   +4 more sources