نتایج جستجو برای: core protein

تعداد نتایج: 1424777  

2011
Jiao Liu Xiong Ding Jia Tang Youde Cao Peng Hu Fan Zhou Xiaoliang Shan Xuefei Cai Qingmei Chen Ning Ling Bingqiang Zhang Yang Bi Ke Chen Hong Ren Ailong Huang Tong-Chuan He Ni Tang

BACKGROUND The Hepatitis C virus (HCV) core protein has been implicated as a potential oncogene or a cofactor in HCV-related hepatocellular carcinoma (HCC), but the underlying mechanisms are unknown. Overactivation of the Wnt/β-catenin signaling is a major factor in oncogenesis of HCC. However, the pathogenesis of HCV core-associated Wnt/β-catenin activation remains to be further characterized....

2011
Andrea Cerutti Patrick Maillard Rosalba Minisini Pierre-Olivier Vidalain Farzin Roohvand Eve-Isabelle Pecheur Mario Pirisi Agata Budkowska

Hepatitis C virus (HCV) infection is a major cause of chronic liver disease worldwide. HCV core protein is involved in nucleocapsid formation, but it also interacts with multiple cytoplasmic and nuclear molecules and plays a crucial role in the development of liver disease and hepatocarcinogenesis. The core protein is found mostly in the cytoplasm during HCV infection, but also in the nucleus i...

Journal: :The Journal of clinical investigation 2000
D J Kittlesen K A Chianese-Bullock Z Q Yao T J Braciale Y S Hahn

Hepatitis C virus (HCV) is an important human pathogen that is remarkably efficient at establishing persistent infection. The HCV core protein is the first protein expressed during the early phase of HCV infection. Our previous work demonstrated that the HCV core protein suppresses host immune responses, including anti-viral cytotoxic T-lymphocyte responses in a murine model. To investigate the...

2017
Cecilia Fernández-Ponce Maria C. Durán-Ruiz Isaac Narbona-Sánchez Juan P. Muñoz-Miranda Mikel M. Arbulo-Echevarria Antonio Serna-Sanz Christian Baumann Rocío Litrán Enrique Aguado Wilhelm Bloch Francisco García-Cozar

Hepatitis C virus core protein is a highly basic viral protein that multimerizes with itself to form the viral capsid. When expressed in CD4+ T lymphocytes, it can induce modifications in several essential cellular and biological networks. To shed light on the mechanisms underlying the alterations caused by the viral protein, we have analyzed HCV-core subcellular localization and its associatio...

P. Chakrabarti, S. K. Ghosh

  The distribution and localization of acid and neutral mucins in various cells lining the olfactory epithelium of Cyprinus carpio have been studied histochemically by employing the PAS-AB technique. Variations in the localization of protein in different cells lining the olfactory epithelium have been correlated with the functional significance of the region concerned. Intense localization of t...

Objectives: The study of core-shell magnetic nanoparticles has a wide range of applications because of the unique combination of the nanoscale magnetic core and the functional shell. Characterization and application of one important class of core-shell magnetic nanoparticles (MNPs), i.e., iron oxide core (Fe3O4/γ-Fe2O3) with a silica shell and outer of gold (Fe3O4-SiO2@Gold (FSG)) in Boron Neut...

Journal: :The Journal of biological chemistry 1989
B Clément B Segui-Real J R Hassell G R Martin Y Yamada

We have identified a protein(s) on the surface of hepatocytes that binds to the core protein of the heparan sulfate proteoglycan of basement membranes. These cells attached and spread on substrates prepared from the basement membrane heparan sulfate proteoglycan (HSPG) and its core protein (HSPG-core). Three proteins (Mr = 38,000, 36,000, and 26,000) were found to bind to a HSPG-core affinity c...

2010
Chaomin Sun Cara T. Pager Guangxiang Luo Peter Sarnow Jamie H. D. Cate

The protein DDX3X is a DEAD-box RNA helicase that is essential for the hepatitis C virus (HCV) life cycle. The HCV core protein has been shown to bind to DDX3X both in vitro and in vivo. However, the specific interactions between these two proteins and the functional importance of these interactions for the HCV viral life cycle remain unclear. We show that amino acids 16-36 near the N-terminus ...

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