Literature DB >> 29521101

Functional role of Hsp60 as a positive regulator of human viral infection progression.

Z Wyżewski, K P Gregorczyk, J Szczepanowska, L Szulc-Dąbrowska.   

Abstract

Heat shock proteins (Hsps) are a family of proteins highly conserved in evolution. Members of the Hsp family are mainly responsible for proper protein folding, however they perform many other functions in living organisms. Hsp60 is a molecular chaperone that is present in mitochondria and cytosol of eukaryotic cells, as well as on their surface. It is also found in the extracellular space and in the peripheral blood. Apart from its role in assisting protein folding in cooperation with Hsp10, Hsp60 contributes to regulation of apoptosis, as well as participates in modulation of the immune system activity. Hsp60 may favor oncogenesis by promoting survival or growth of some tumor cell types. Hsp60 is a subject of medical research due to its role in pathogenesis of certain tumors and infectious diseases. In this review we discuss mechanisms by which Hsp60 promotes development and progression of infections caused by three human viruses: hepatitis B virus (HBV), human immunodeficiency virus (HIV) and influenza A virus.

Entities:  

Keywords:  heat shock protein 60; Hsp60; viral infection; hepatitis B virus human immunodeficiency virus; influenza A virus.

Mesh:

Substances:

Year:  2018        PMID: 29521101     DOI: 10.4149/av_2018_104

Source DB:  PubMed          Journal:  Acta Virol        ISSN: 0001-723X            Impact factor:   1.162


  8 in total

Review 1.  Role of the heat shock protein family in bone metabolism.

Authors:  Kai Hang; Chenyi Ye; Erman Chen; Wei Zhang; Deting Xue; Zhijun Pan
Journal:  Cell Stress Chaperones       Date:  2018-09-05       Impact factor: 3.667

Review 2.  Heat shock proteins and the calcineurin-crz1 signaling regulate stress responses in fungi.

Authors:  Avishek Roy; Ranjan Tamuli
Journal:  Arch Microbiol       Date:  2022-04-04       Impact factor: 2.552

3.  Host HSPD1 Translocation from Mitochondria to the Cytoplasm Induced by Streptococcus suis Serovar 2 Enolase Mediates Apoptosis and Loss of Blood-Brain Barrier Integrity.

Authors:  Tong Wu; Li Jia; Siyu Lei; Hexiang Jiang; Jianan Liu; Na Li; Paul R Langford; Hongtao Liu; Liancheng Lei
Journal:  Cells       Date:  2022-06-29       Impact factor: 7.666

4.  Quercetin May Improve Fat Graft Survival by Promoting Fat Browning Peripherally.

Authors:  Panxi Yu; Zhenyu Yang; Haibin Lu; Xiaolei Jin; Xiaonan Yang; Zuoliang Qi
Journal:  Aesthetic Plast Surg       Date:  2022-03-24       Impact factor: 2.326

5.  Anti-Influenza Activity of the Ribonuclease Binase: Cellular Targets Detected by Quantitative Proteomics.

Authors:  Vera Ulyanova; Raihan Shah Mahmud; Alexander Laikov; Elena Dudkina; Maria Markelova; Ahmed Mostafa; Stephan Pleschka; Olga Ilinskaya
Journal:  Int J Mol Sci       Date:  2020-11-05       Impact factor: 5.923

6.  PARP1 Might Substitute HSF1 to Reactivate Latent HIV-1 by Binding to Heat Shock Element.

Authors:  Xinfeng Xu; Yingtong Lin; Xiaoyun Zeng; Chan Yang; Siqin Duan; Liqiong Ding; Wanzhen Lu; Jian Lin; Xiaoyan Pan; Xiancai Ma; Shuwen Liu
Journal:  Cells       Date:  2022-07-29       Impact factor: 7.666

7.  Mitochondrial Heat Shock Response Induced by Ectromelia Virus is Accompanied by Reduced Apoptotic Potential in Murine L929 Fibroblasts.

Authors:  Zbigniew Wyżewski; Karolina P Gregorczyk-Zboroch; Matylda B Mielcarska; Magdalena Bossowska-Nowicka; Justyna Struzik; Joanna Szczepanowska; Felix N Toka; Marek G Niemiałtowski; Lidia Szulc-Dąbrowska
Journal:  Arch Immunol Ther Exp (Warsz)       Date:  2019-07-19       Impact factor: 4.291

8.  HSPA4 Knockdown Retarded Progression and Development of Colorectal Cancer.

Authors:  Mingliang Zhang; Weigang Dai; Zhanyu Li; Liang Tang; Jianhui Chen; Chuangqi Chen
Journal:  Cancer Manag Res       Date:  2021-06-14       Impact factor: 3.989

  8 in total

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