Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective
- Edkins, Adrienne L, Price, John T, Pockley, A Graham, Blatch, Gregory L
- Authors: Edkins, Adrienne L , Price, John T , Pockley, A Graham , Blatch, Gregory L
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164332 , vital:41109 , DOI: 10.1098/rstb.2016.0521
- Description: Many heat shock proteins (HSPs) are essential to survival as a consequence of their role as molecular chaperones, and play a critical role in maintaining cellular proteostasis by integrating the fundamental processes of protein folding and degradation. HSPs are arguably among the most prominent classes of proteins that have been broadly linked to many human disorders, with changes in their expression profile and/or intracellular/extracellular location now being described as contributing to the pathogenesis of a number of different diseases. Although the concept was initially controversial, it is now widely accepted that HSPs have additional biological functions over and above their role in proteostasis (so-called ‘protein moonlighting’).
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- Authors: Edkins, Adrienne L , Price, John T , Pockley, A Graham , Blatch, Gregory L
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164332 , vital:41109 , DOI: 10.1098/rstb.2016.0521
- Description: Many heat shock proteins (HSPs) are essential to survival as a consequence of their role as molecular chaperones, and play a critical role in maintaining cellular proteostasis by integrating the fundamental processes of protein folding and degradation. HSPs are arguably among the most prominent classes of proteins that have been broadly linked to many human disorders, with changes in their expression profile and/or intracellular/extracellular location now being described as contributing to the pathogenesis of a number of different diseases. Although the concept was initially controversial, it is now widely accepted that HSPs have additional biological functions over and above their role in proteostasis (so-called ‘protein moonlighting’).
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STAT3 interacts directly with Hsp90:
- Prinsloo, Earl, Kramer, Adam H, Edkins, Adrienne L, Blatch, Gregory L
- Authors: Prinsloo, Earl , Kramer, Adam H , Edkins, Adrienne L , Blatch, Gregory L
- Date: 2012
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/165142 , vital:41212 , DOI: 10.1002/iub.607
- Description: Heat shock protein 90 (Hsp90) functionally modulates signal transduction. The signal transducer and activator of transcription 3 (STAT3) mediates interleukin‐6 family cytokine signaling. Aberrant activation and mutation of STAT3 is associated with oncogenesis and immune disorders, respectively. Hsp90 and STAT3 have previously been shown to colocalize and coimmunoprecipitate in common complexes.
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- Authors: Prinsloo, Earl , Kramer, Adam H , Edkins, Adrienne L , Blatch, Gregory L
- Date: 2012
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/165142 , vital:41212 , DOI: 10.1002/iub.607
- Description: Heat shock protein 90 (Hsp90) functionally modulates signal transduction. The signal transducer and activator of transcription 3 (STAT3) mediates interleukin‐6 family cytokine signaling. Aberrant activation and mutation of STAT3 is associated with oncogenesis and immune disorders, respectively. Hsp90 and STAT3 have previously been shown to colocalize and coimmunoprecipitate in common complexes.
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Localisation of Theiler's murine encephalomyelitis virus protein 2C to the golgi apparatus using antibodies generated against a peptide region:
- Jauka, Tembisa, Mutsvunguma, Lorraine Z, Boshoff, Aileen, Edkins, Adrienne L, Knox, Caroline M
- Authors: Jauka, Tembisa , Mutsvunguma, Lorraine Z , Boshoff, Aileen , Edkins, Adrienne L , Knox, Caroline M
- Date: 2010
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/165074 , vital:41206 , DOI: 10.1016/j.jviromet.2010.05.009
- Description: The picornavirus 2C protein is highly conserved and indispensible for virus replication. Polyclonal antibodies against Theiler's murine encephalomyelitis virus (TMEV) 2C protein were generated by immunisation of rabbits with a peptide comprising amino acids 31–210 of the protein. Antibodies were used to investigate the localisation of 2C in infected cells by indirect immunofluorescence and confocal microscopy. Analysis of infected cells revealed that the distribution of 2C changed during infection.
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- Authors: Jauka, Tembisa , Mutsvunguma, Lorraine Z , Boshoff, Aileen , Edkins, Adrienne L , Knox, Caroline M
- Date: 2010
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/165074 , vital:41206 , DOI: 10.1016/j.jviromet.2010.05.009
- Description: The picornavirus 2C protein is highly conserved and indispensible for virus replication. Polyclonal antibodies against Theiler's murine encephalomyelitis virus (TMEV) 2C protein were generated by immunisation of rabbits with a peptide comprising amino acids 31–210 of the protein. Antibodies were used to investigate the localisation of 2C in infected cells by indirect immunofluorescence and confocal microscopy. Analysis of infected cells revealed that the distribution of 2C changed during infection.
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