Functional interaction between cellular p100 and the dengue virus 3' UTR
نویسندگان
چکیده
منابع مشابه
p100 increases AT1R expression through interaction with AT1R 3′-UTR
p100 protein (SND1, Tudor-SN) is a multifunctional protein that functions as a co-activator for several transcription factors, has a role in mRNA processing and participates in RNAi-induced silencing complex (RISC) with yet unknown function. In this study we identified a novel function for p100 as a regulator of angiotensin II type 1 receptor (AT1R) expression. The binding of p100 to AT1R 3'-un...
متن کاملLSm1 binds to the Dengue virus RNA 3' UTR and is a positive regulator of Dengue virus replication.
Dengue virus (DENV) is a mosquito-transmitted flavivirus that can cause severe disease in humans. The DENV positive strand RNA genome contains 5' and 3' untranslated regions (UTRs) that have been shown to be required for virus replication and interaction with host cell proteins. In the present study LSm1 was identified as a host cellular protein involved in DENV RNA replication. By using two in...
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Type II collagen is the major component of articular cartilage and is mainly synthesized by chondrocytes. Repeated sub-culturing of primary chondrocytes leads to reduction of type II collagen gene (Col2a1) expression, which mimics the process of chondrocyte dedifferentiation. Although the functional importance of Col2a1 expression has been extensively investigated, mechanism of transcriptional ...
متن کاملDengue virus type-3 envelope protein domain III; expression and immunogenicity
Objective(s): Production of a recombinant and immunogenic antigen using dengue virus type-3 envelope protein is a key point in dengue vaccine development and diagnostic researches. The goals of this study were providing a recombinant protein from dengue virus type-3 envelope protein and evaluation of its immunogenicity in mice. Materials and Methods: Multiple amino acid sequences of different i...
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ژورنال
عنوان ژورنال: Journal of General Virology
سال: 2010
ISSN: 0022-1317,1465-2099
DOI: 10.1099/vir.0.028597-0