Results 31 to 40 of about 177,922 (281)

Arabidopsis NMD3 is required for nuclear export of 60S ribosomal subunits and affects secondary cell wall thickening. [PDF]

PLoS ONE, 2012
NMD3 is required for nuclear export of the 60S ribosomal subunit in yeast and vertebrate cells, but no corresponding function of NMD3 has been reported in plants.
Mei-Qin Chen, Ai-Hong Zhang, Quan Zhang, Bao-Cai Zhang, Jie Nan, Xia Li, Na Liu, Hong Qu, Cong-Ming Lu, Sudmorgen, Yi-Hua Zhou, Zhi-Hong Xu, Shu-Nong Bai   +12 more
doaj   +1 more source

Model system to study classical nuclear export signals [PDF]

AAPS PharmSci, 2002
Signal-mediated protein transport through the nuclear pore complex is of considerable interest in the field of molecular pharmaceutics. Nuclear localization signals can be used to target genes/antisense delivery systems to the nucleus. Studying nuclear export is useful in enhancing the expression and the efficiency of action of these therapeutic agents.
Charu, Kanwal, Henan, Li, Carol S, Lim
openaire   +2 more sources

Antileukemic Activity of Nuclear Export Inhibitors that Spare Normal Hematopoietic Cells [PDF]

, 2012
Drugs that target the chief mediator of nuclear export, chromosome region maintenance 1 protein (CRM1) have potential as therapeutics for leukemia, but existing CRM1 inhibitors show variable potencies and a broad range of cytotoxic effects.
Barcelo, C, Chook, Y M, Christie, A L, Etchin, Julia, Farmer, A, Kauffman, M, Kentsis, Alex, Kung, A L, Look, A. Thomas, Mansour, M R, McCauley, D, Rodig, Scott J., Sanda, Takaomi, Shacham, S, Sun, Q, Zhang, Z C   +15 more
core   +1 more source

Identification of Nuclear Export Signals in Antizyme-1 [PDF]

Journal of Biological Chemistry, 2003
Antizyme-1 (AZ1) is a protein that negatively regulates polyamine synthesis by inhibiting the key synthetic enzyme ornithine decarboxylase and targeting it for degradation by the 26 S proteasome. Recent work shows that antizyme protein translocates to the nucleus during mouse development (Gritli-Linde, A., Nilssom, J., Bohlooly, Y.
Noriyuki, Murai, Yasuko, Murakami, Senya, Matsufuji   +2 more
openaire   +2 more sources

Mechanisms of Progesterone Receptor Export from Nuclei: Role of Nuclear Localization Signal, Nuclear Export Signal, and Ran Guanosine Triphosphate [PDF]

Molecular Endocrinology, 1998
Steroid hormone receptors are, in most cases, mainly nuclear proteins that undergo a continuous nucleocytoplasmic shuttling. The mechanism of the nuclear export of these proteins remains largely unknown. To approach this problem experimentally in vivo, we have prepared cell lines permanently coexpressing the wild-type nuclear progesterone receptor (PR)
R K, Tyagi, L, Amazit, P, Lescop, E, Milgrom, A, Guiochon-Mantel   +4 more
openaire   +3 more sources

Nuclear export of the influenza virus ribonucleoprotein complex: Interaction of Hsc70 with viral proteins M1 and NS2

FEBS Open Bio, 2014
The influenza virus replicates in the host cell nucleus, and the progeny viral ribonucleoprotein complex (vRNP) is exported to the cytoplasm prior to maturation.
Ken Watanabe, Teppei Shimizu, Saiko Noda, Fujiko Tsukahara, Yoshiro Maru, Nobuyuki Kobayashi   +5 more
doaj   +1 more source

Huntingtin contains a highly conserved nuclear export signal [PDF]

Human Molecular Genetics, 2003
Huntington's disease (HD), is a genetic neurodegenerative disease characterized by a DNA CAG triplet repeat expansion in the first exon of the disease gene, HD. CAG DNA expansion results in a polyglutamine tract expansion in mutant huntingtin protein. Wild-type and mutant full-length huntingtin have been detected in the nucleus, but elevated levels of ...
Jianrun, Xia, Denise H, Lee, Jillian, Taylor, Mark, Vandelft, Ray, Truant   +4 more
openaire   +2 more sources

Specific inhibition of the Survivin–CRM1 interaction by peptide-modified molecular tweezers

Nature Communications, 2021
Survivin’s dual function as apoptosis inhibitor and regulator of cell proliferation is mediated via its interaction with the export receptor CRM1. Here authors report a strategy addressing its dimer interface overlapping with the nuclear export signal ...
Annika Meiners, Sandra Bäcker, Inesa Hadrović, Christian Heid, Christine Beuck, Yasser B. Ruiz-Blanco, Joel Mieres-Perez, Marius Pörschke, Jean-Noël Grad, Cecilia Vallet, Daniel Hoffmann, Peter Bayer, Elsa Sánchez-García, Thomas Schrader, Shirley K. Knauer   +14 more
doaj   +1 more source

Inhibition of cellular protein secretion by norwalk virus nonstructural protein p22 requires a mimic of an endoplasmic reticulum export signal. [PDF]

, 2013
Protein trafficking between the endoplasmic reticulum (ER) and Golgi apparatus is central to cellular homeostasis. ER export signals are utilized by a subset of proteins to rapidly exit the ER by direct uptake into COPII vesicles for transport to the ...
Crawford, Sue E., Estes, M. K., Guix Arnau, Susana, Katayama, K., Sharp, T. M.   +4 more
core   +2 more sources

The Human Tap Nuclear RNA Export Factor Contains a Novel Transportin-dependent Nuclear Localization Signal That Lacks Nuclear Export Signal Function [PDF]

Journal of Biological Chemistry, 1999
The human Tap protein mediates the sequence-specific nuclear export of RNAs containing the constitutive transport element and is likely also critical for general mRNA export. Here, we demonstrate that a previously defined arginine-rich nuclear localization signal (NLS) present in Tap acts exclusively via the transportin import factor.
R, Truant, Y, Kang, B R, Cullen
openaire   +2 more sources