Hsp70/Hsp90 organising protein (hop): beyond interactions with chaperones and prion proteins
- Baindur-Hudson, Swati, Edkins, Adrienne L, Blatch, Gregory L
- Authors: Baindur-Hudson, Swati , Edkins, Adrienne L , Blatch, Gregory L
- Date: 2015
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164852 , vital:41178 , ISBN 978-3-319-11730-0 , DOI: 10.1007/978-3-319-11731-7_3
- Description: The Hsp70/Hsp90 organising protein (Hop), also known as stress-inducible protein 1 (STI1), has received considerable attention for diverse cellular functions in both healthy and diseased states. There is extensive evidence that intracellular Hop is a co-chaperone of the major chaperones Hsp70 and Hsp90, playing an important role in the productive folding of Hsp90 client proteins. Consequently, Hop is implicated in a number of key signalling pathways, including aberrant pathways leading to cancer. However, Hop is also secreted and it is now well established that Hop also serves as a receptor for the prion protein, PrPC.
- Full Text:
- Date Issued: 2015
- Authors: Baindur-Hudson, Swati , Edkins, Adrienne L , Blatch, Gregory L
- Date: 2015
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164852 , vital:41178 , ISBN 978-3-319-11730-0 , DOI: 10.1007/978-3-319-11731-7_3
- Description: The Hsp70/Hsp90 organising protein (Hop), also known as stress-inducible protein 1 (STI1), has received considerable attention for diverse cellular functions in both healthy and diseased states. There is extensive evidence that intracellular Hop is a co-chaperone of the major chaperones Hsp70 and Hsp90, playing an important role in the productive folding of Hsp90 client proteins. Consequently, Hop is implicated in a number of key signalling pathways, including aberrant pathways leading to cancer. However, Hop is also secreted and it is now well established that Hop also serves as a receptor for the prion protein, PrPC.
- Full Text:
- Date Issued: 2015
The networking of chaperones by co-chaperones: control of cellular protein homeostasis
- Edkins, Adrienne L, Blatch, Gregory L
- Authors: Edkins, Adrienne L , Blatch, Gregory L
- Date: 2014
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/165107 , vital:41209 , ISBN 978-3-319-11731-7
- Description: Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.
- Full Text:
- Date Issued: 2014
- Authors: Edkins, Adrienne L , Blatch, Gregory L
- Date: 2014
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/165107 , vital:41209 , ISBN 978-3-319-11731-7
- Description: Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.
- Full Text:
- Date Issued: 2014
Targeting conserved pathways as a strategy for novel drug development: disabling the cellular stress response:
- Edkins, Adrienne L, Blatch, Gregory L
- Authors: Edkins, Adrienne L , Blatch, Gregory L
- Date: 2012
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/165129 , vital:41211 , ISBN 978-3-642-28174-7 , DOI: 10.1007/978-3-642-28175-4_4
- Description: The ability to respond to and cope with stress at a molecular level is essential for cell survival. The stress response is conserved across organisms by the expression of a group of molecular chaperones known as heat shock proteins (HSP). HSP are ubiquitous and highly conserved proteins that regulate cellular protein homeostasis and trafficking under physiological and stressful conditions, including diseases such as cancer and malaria. HSP are good drug targets for the treatment of human diseases, as the significant functional and structural data available suggest that they are essential for cell survival and that, despite conservation across species, there are biophysical and biochemical differences between HSP in normal and disease states that allow HSP to be selectively targeted. In this chapter, we review the international status of this area of research and highlight progress by us and other African researchers towards the characterisation and targeting of HSP from humans and parasites from Plasmodium and Trypanosoma as drug targets.
- Full Text:
- Date Issued: 2012
- Authors: Edkins, Adrienne L , Blatch, Gregory L
- Date: 2012
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/165129 , vital:41211 , ISBN 978-3-642-28174-7 , DOI: 10.1007/978-3-642-28175-4_4
- Description: The ability to respond to and cope with stress at a molecular level is essential for cell survival. The stress response is conserved across organisms by the expression of a group of molecular chaperones known as heat shock proteins (HSP). HSP are ubiquitous and highly conserved proteins that regulate cellular protein homeostasis and trafficking under physiological and stressful conditions, including diseases such as cancer and malaria. HSP are good drug targets for the treatment of human diseases, as the significant functional and structural data available suggest that they are essential for cell survival and that, despite conservation across species, there are biophysical and biochemical differences between HSP in normal and disease states that allow HSP to be selectively targeted. In this chapter, we review the international status of this area of research and highlight progress by us and other African researchers towards the characterisation and targeting of HSP from humans and parasites from Plasmodium and Trypanosoma as drug targets.
- Full Text:
- Date Issued: 2012
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