Results 51 to 60 of about 73,362 (284)

Analysis and prediction of leucine-rich nuclear export signals [PDF]

Protein Engineering, Design and Selection, 2004
We present a thorough analysis of nuclear export signals and a prediction server, which we have made publicly available. The machine learning prediction method is a significant improvement over the generally used consensus patterns. Nuclear export signals (NESs) are extremely important regulators of the subcellular location of proteins. This regulation
la Cour, Tanja, Kiemer, Lars, Mølgaard, Anne, Gupta, Ramneek, Skriver, Karen, Brunak, Søren   +5 more
openaire   +3 more sources

A non-canonical mechanism for Crm1-export cargo complex assembly

eLife, 2015
The transport receptor Crm1 mediates the export of diverse cargos containing leucine-rich nuclear export signals (NESs) through complex formation with RanGTP.
Ute Fischer, Nico Schäuble, Sabina Schütz, Martin Altvater, Yiming Chang, Marius Boulos Faza, Vikram Govind Panse   +6 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

Nuclear export of cutaneous HPV8 E7 oncoprotein is mediated by a leucine-rich nuclear export signal via a CRM1 pathway [PDF]

, 2015
We recently determined that the nuclear import of cutaneous beta genus HPV8 E7 oncoprotein it is mediated by its zinc-binding domain via direct hydrophobic interactions with the FG nucleoporins Nup62 and Nup153 (Onder and Moroianu, 2014).
Chang, Vivian, Onder, Zeynep, Moroianu, Junona   +2 more
core   +1 more source

Molecular Characterizations of Subcellular Localization Signals in the Nucleocapsid Protein of Porcine Epidemic Diarrhea Virus

Viruses, 2014
The nucleolus is a dynamic subnuclear structure, which is crucial to the normal operation of the eukaryotic cell. The porcine epidemic diarrhea virus (PEDV), coronavirus nucleocapsid (N) protein, plays important roles in the process of virus replication ...
Da Shi, Maojie Lv, Jianfei Chen, Hongyan Shi, Sha Zhang, Xin Zhang, Li Feng   +6 more
doaj   +1 more source

Active nuclear import and passive nuclear export are the primary determinants of TDP-43 localization

Scientific Reports, 2018
ALS (Amyotrophic Lateral Sclerosis) is a neurodegenerative disease characterized by the redistribution of the RNA binding protein TDP-43 in affected neurons: from predominantly nuclear to aggregated in the cytosol.
Emile S. Pinarbasi, Tolga Cağatay, Ho Yee Joyce Fung, Ying C. Li, Yuh Min Chook, Philip J. Thomas   +5 more
doaj   +1 more source

NESbase version 1.0: a database of nuclear export signals [PDF]

Nucleic Acids Research, 2003
Protein export from the nucleus is often mediated by a Leucine-rich Nuclear Export Signal (NES). NESbase is a database of experimentally validated Leucine-rich NESs curated from literature. These signals are not annotated in databases such as SWISS-PROT, PIR or PROSITE.
Tanja la Cour, Ramneek Gupta, Kristoffer Rapacki, Karen Skriver, Flemming M. Poulsen, Søren Brunak   +5 more
openaire   +2 more sources

Nuclear phosphoinositide signaling regulates messenger RNA export [PDF]

RNA Biology, 2009
Messenger RNA export from the nucleus to the cytoplasm plays an essential role in linking transcription to translation and consequently regulation of protein expression. mRNA export requires a series of events: pre-mRNA processing, ribonucleoprotein targeting to the NPC (nuclear pore complexes), and translocation through nuclear pores to the cytoplasm.
Masashi, Okada, Keqiang, Ye
openaire   +2 more sources

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

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

FEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source