نتایج جستجو برای: nuclear localization

تعداد نتایج: 363249  

Journal: :The Journal of biological chemistry 2001
J Qiu X Li G Frank B Shen

Flap endonuclease-1 (FEN-1), a 43-kDa protein, is a structure-specific and multifunctional nuclease. It plays important roles in RNA primer removal of Okazaki fragments during DNA replication, DNA base excision repair, and maintenance of genome stability. Three functional motifs of the enzyme were proposed to be responsible for its nuclease activities, interaction with proliferating cell nuclea...

Journal: :Journal of virology 2009
Kimberly A Fryrear Sarah S Durkin Saurabh K Gupta Jessica B Tiedebohl O John Semmes

The human T-cell leukemia virus type 1 oncoprotein Tax has pleiotropic activities, a subset of which likely leads to immortalization of T cells. Tax is expressed and known to function in both the cell nucleus and the cytoplasm. Tax has defined nuclear localization (NLS) and nuclear export signals that enable shuttling between the two compartments. In this study, we identified a novel region in ...

Journal: :The EMBO journal 1998
C R Wilkinson M Wallace M Morphew P Perry R Allshire J P Javerzat J R McIntosh C Gordon

The 26S proteasome is a large multisubunit complex involved in degrading both cytoplasmic and nuclear proteins. We have investigated the localization of this complex in the fission yeast, Schizosaccharomyces pombe. Immunofluorescence microscopy shows a striking localization pattern whereby the proteasome is found predominantly at the nuclear periphery, both in interphase and throughout mitosis....

Journal: :Journal of Biological Chemistry 2001

2005
Muluye E. Liku Van Q. Nguyen Audrey W. Rosales Kaoru Irie Joachim J. Li

Cyclin-dependent kinases (CDKs) use multiple mechanisms to block reassembly of prereplicative complexes (pre-RCs) at replication origin to prevent inappropriate re-replication. In Saccharomyces cerevisiae, one of these mechanisms promotes the net nuclear export of a pre-RC component, the Mcm2-7 complex, during S, G2 and M phases. Here we identify two partial nuclear localization signals (NLSs) ...

Journal: :Nucleic acids research 2015
Kenji Nishi Tomoko Takahashi Masataka Suzawa Takuya Miyakawa Tatsuya Nagasawa Yvelt Ming Masaru Tanokura Kumiko Ui-Tei

GW182 family proteins play important roles in microRNA (miRNA)-mediated RNA silencing. They directly interact with Argonaute (Ago) proteins in processing bodies (P bodies), cytoplasmic foci involved in mRNA degradation and storage. Recently, we revealed that a human GW182 family protein, TNRC6A, is a nuclear-cytoplasmic shuttling protein, and its subcellular localization is regulated by its own...

2016
Antoine Larrieu Antony Champion Jonathan Legrand Julien Lavenus David Mast Géraldine Brunoud Jaesung Oh Soazig Guyomarc′h Maxime Pizot Edward E. Farmer Colin Turnbull Teva Vernoux Malcolm J. Bennett Laurent Laplaze

It has come to our attention that the control version of the Jas9-VENUS reporter construct reported in this Article, mJas9-VENUS, which consists of a mutated version of Jas9 fused to VENUS, does not contain a nuclear localization signal as described in Fig. 1a. The conclusion that degradation of the Jas9-VENUS reporter is dependent on jasmonate signalling in the nucleus remains unaffected by th...

2016
Ryosuke Yamagishi Hiroki Kaneko

This article describes data related to a research article titled "Comprehensive analysis of the dynamic structure of nuclear localization signals" by Yamagishi et al. [1]. In this article, we provide the data covering wider range of the mammalian NLSs in UniProt (Universal Protein Resource) [2] regardless of their conformations. To be more specific as follows: We have extracted all NLSs which a...

2014
Ravindra Kumar Sohni Jain Bandana Kumari Manish Kumar

The nucleus is the largest and the highly organized organelle of eukaryotic cells. Within nucleus exist a number of pseudo-compartments, which are not separated by any membrane, yet each of them contains only a specific set of proteins. Understanding protein sub-nuclear localization can hence be an important step towards understanding biological functions of the nucleus. Here we have described ...

Journal: :The Journal of biological chemistry 2005
Hisanori Kurooka Yoshifumi Yokota

Id proteins function as negative regulators for basic helix-loop-helix transcriptional factors that play important roles in cell fate determination. They preferentially associate with ubiquitously expressed E proteins of the basic helix-loop-helix family and prevent them from binding to DNA and activating transcription. Although their small size suggests that Id proteins enter and exit the nucl...

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