LRP1 is required for novobiocin-mediated fibronectin turnover:
- Authors: Boel, Natasha M-E , Hunter, Morgan C , Edkins, Adrienne L
- Date: 2018
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164896 , vital:41182 , DOI: 10.1038/s41598-018-29531-2
- Description: Fibronectin (FN) plays a major role in the stability and organization of the extracellular matrix (ECM). We have previously demonstrated that FN interacts directly with Hsp90, as well as showing that the Hsp90 inhibitor novobiocin results in FN turnover via a receptor mediated process. However, the receptor involved has not been previously identified. LRP1 is a ubiquitous receptor responsible for the internalisation of numerous ligands that binds both Hsp90 and FN, and therefore we investigated whether LRP1 was involved in novobiocin-mediated FN turnover.
- Full Text:
- Date Issued: 2018
NMR structural elucidation of channaine, an unusual alkaloid from Sceletium tortuosum:
- Authors: Veale, Clinton G L , Chen, Weiyang , Chaudhary, Sushil , Kituyi, Sarah N , Isaacs, Michelle , Hoppe, Heinrich C , Edkins, Adrienne L , Combrinck, Sandra , Mehari, Bewketu , Viljoen, Alvaro
- Date: 2018
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164345 , vital:41110 , DOI: 10.1016/j.phytol.2017.11.018
- Description: Chemical interrogation of the Sceletium genus and Amaryllidaceae family of plants has yielded a diverse array of aryl-hydroindole containing alkaloids. Included in this class is channaine, which was tentatively identified, without comprehensive structural elucidation from Sceletium tortuosum in 1957. Following its isolation from S. strictum, the structure of channaine was eventually resolved by X-ray crystallographic analysis, which revealed an unusual cage-like ring structure at the interface of two aryl-hydroindole subunits. However, since this report in 1978, channaine has not re-appeared in the literature. In this letter, the full NMR characterisation of channaine, isolated from S. tortuosum collected from St Helena in the Western Cape Province of South Africa, is reported for the first time.
- Full Text:
- Date Issued: 2018
Regulation of the extracellular matrix by heat shock proteins and molecular chaperones:
- Authors: Boel, Natasha M-E , Edkins, Adrienne L
- Date: 2018
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164368 , vital:41112 , ISBN 978-3-319-69040-7 , DOI: 10.1007/978-3-319-69042-1_6
- Description: The extracellular matrix (ECM) serves as a scaffold for cells within tissues and is composed of an intricate network of glycoproteins, growth factors and matricellular proteins which cooperatively function in cell processes such as migration, adhesion and wound healing. ECM morphology is constantly undergoing remodelling (synthesis, assembly and degradation) during normal cell processes and when deregulated may contribute to disease. Heat shock proteins (Hsps) are involved in regulating processes that determine the assembly and degradation of the ECM at multiple levels, in both normal and diseased states. These roles include mediating the activation of ECM-degrading enzymes, maintaining matrix stability and clearing aggregated/misfolded proteins. Hsp may serve as chaperones and receptors or have cytokine-like functions. In this chapter, we review how Hsp90, Hsp70, Hsp40 and a number of ER resident chaperones contribute to ECM regulation. The role of the non-Hsp chaperones, SPARC and clusterin in the ECM is also discussed.
- Full Text:
- Date Issued: 2018
Extracellular Hsp90 and TGFP regulate adhesion, migration and anchorage independent growth in a paired colon cancer cell line model
- Authors: de la Mare, Jo-Anne , Jurgens, Tamarin , Edkins, Adrienne L
- Date: 2017
- Language: English
- Type: article , text
- Identifier: http://hdl.handle.net/10962/59920 , vital:27710 , https://doi.org/10.1186/s12885-017-3190-z
- Description: Tumour metastasis remains the major cause of death in cancer patients and, to date, the mechanism and signalling pathways governing this process are not completely understood. The TGF-ß pathway is the most commonly mutated pathway in cancer, however its role in cancer progression is controversial as it can function as both a promoter and a suppressor of metastasis. Although previous studies have suggested a role for the molecular chaperone Hsp90 in regulating the TGF-ß pathway, the level at which this occurs as well as the consequences in terms of colon cancer metastasis are unknown.
- Full Text:
- Date Issued: 2017
Fibronectin is a stress responsive gene regulated by HSF1 in response to geldanamycin
- Authors: Dhanani, Karim C H , Samson, William J , Edkins, Adrienne L
- Date: 2017
- Language: English
- Type: article , text
- Identifier: http://hdl.handle.net/10962/59931 , vital:27711 , https://doi:10.1038/s41598-017-18061-y
- Description: Fibronectin is an extracellular matrix glycoprotein with key roles in cell adhesion and migration. Hsp90 binds directly to fibronectin and Hsp90 depletion regulates fibronectin matrix stability. Where inhibition of Hsp90 with a C-terminal inhibitor, novobiocin, reduced the fibronectin matrix, treatment with an N-terminal inhibitor, geldanamycin, increased fibronectin levels. Geldanamycin treatment induced a stress response and a strong dose and time dependent increase in fibronectin mRNA via activation of the fibronectin promoter. Three putative heat shock elements (HSEs) were identified in the fibronectin promoter. Loss of two of these HSEs reduced both basal and geldanamycin-induced promoter activity, as did inhibition of the stress-responsive transcription factor HSF1. Binding of HSF1 to one of the putative HSE was confirmed by ChIP under basal conditions, and occupancy shown to increase with geldanamycin treatment. These data support the hypothesis that fibronectin is stress-responsive and a functional HSF1 target gene. COLA42 and LAMB3 mRNA levels were also increased with geldanamycin indicating that regulation of extracellular matrix (ECM) genes by HSF1 may be a wider phenomenon. Taken together, these data have implications for our understanding of ECM dynamics in stress-related diseases in which HSF1 is activated, and where the clinical application of N-terminal Hsp90 inhibitors is intended.
- Full Text:
- Date Issued: 2017
Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective
- 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’).
- Full Text:
- Date Issued: 2017
Isolation, characterization and antiproliferative activity of new metabolites from the South African endemic red algal species Laurencia alfredensis
- Authors: Dziwornu, Godwin A , Caira, Mino R , de la Mare, Jo-Anne , Edkins, Adrienne L , Bolton, John J , Beukes, Denzil R , Sunassee, Suthananda N
- Date: 2017
- Language: English
- Type: article , text
- Identifier: http://hdl.handle.net/10962/59963 , vital:27715 , https://doi:10.3390/molecules22040513
- Description: The marine red algae of the genus Laurencia have been widely studied for their structurally diverse and biologically active secondary metabolites. We report here the natural product investigation of the organic extract of a newly identified South African endemic species, Laurencia alfredensis. A sequence of column chromatography, preparative TLC and normal phase HPLC resulted in the isolation of eleven compounds comprising three labdane-type diterpenes (1-3), four polyether triterpenes (4-7), three cholestane-type ecdysteroids (8-10) and a glycolipid (11). Compounds 1-3, 5-8 and 10 have not previously been reported, while compound 9 is reported here for the first time from a natural source and the known compound 11 isolated for the first time from the genus Laurencia. The structural elucidation and the relative configuration assignments of the compounds were accomplished by extensive use of ID- and 2D-NMR, HR-ESI-MS, UV and IR spectroscopic techniques, while the absolute configuration of compound 1 was determined by single-crystal X-ray diffraction analysis. All compounds were evaluated against the MDA-MB-231 breast and HeLa cervical cancer cell lines. Compound 2 exhibited low micromolar antiproliferative activity (IC50 = 9.3 gM) against the triple negative breast carcinoma and compound 7 was similarly active (IC50 = 8.8 gM) against the cervical cancer cell line.
- Full Text:
- Date Issued: 2017
Cytotoxic activity of marine sponge extracts from the sub-Antarctic Islands and the Southern Ocean
- Authors: Olsen, Elisabeth , De Cerf, Christopher , Dziwornu, Godwin A , Puccinelli, Eleonora , Parker-Nance, Shirley , Ansorge, Isabelle J , Samaai, Toufiek , Dingle, Laura M K , Edkins, Adrienne L , Sunassee, Suthananda N
- Date: 2016
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/66300 , vital:28931 , https://doi.org/10.17159/sajs.2016/20160202
- Description: publisher version , Over the past 50 years, marine invertebrates, especially sponges, have proven to be a valuable source of new and/or bioactive natural products that have the potential to be further developed as lead compounds for pharmaceutical applications. Although marine benthic invertebrate communities occurring off the coast of South Africa have been explored for their biomedicinal potential, the natural product investigation of marine sponges from the sub-Antarctic Islands in the Southern Ocean for the presence of bioactive secondary metabolites has been relatively unexplored thus far. We report here the results for the biological screening of both aqueous and organic extracts prepared from nine specimens of eight species of marine sponges, collected from around Marion Island and the Prince Edward Islands in the Southern Ocean, for their cytotoxic activity against three cancer cell lines. The results obtained through this multidisciplinary collaborative research effort by exclusively South African institutions has provided an exciting opportunity to discover cytotoxic compounds from sub-Antarctic sponges, whilst contributing to our understanding of the biodiversity and geographic distributions of these cold-water invertebrates. Therefore, we acknowledge here the various contributions of the diverse scientific disciplines that played a pivotal role in providing the necessary platform for the future natural products chemistry investigation of these marine sponges from the sub- Antarctic Islands and the Southern Ocean. Significance: This study will contribute to understanding the biodiversity and geographic distributions of sponges in the Southern Ocean. This multidisciplinary project has enabled the investigation of marine sponges for the presence of cytotoxic compounds. Further investigation will lead to the isolation and identification of cytotoxic compounds present in the active sponge extracts. , University of Cape Town; South African Medical Research Council; National Research Foundation (South Africa); CANSA; Rhodes University; Department of Science and Technology; Department of Environmental Affairs; SANAP
- Full Text:
- Date Issued: 2016
CHIP: a co-chaperone for degradation by the proteasome
- Authors: Edkins, Adrienne L
- Date: 2015
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164863 , vital:41179 , ISBN 978-3-319-11730-0 , DOI: 10.1007/978-3-319-11731-7_11
- Description: Protein homeostasis relies on a balance between protein folding and protein degradation. Molecular chaperones like Hsp70 and Hsp90 fulfil well-defined roles in protein folding and conformational stability via ATP dependent reaction cycles. These folding cycles are controlled by associations with a cohort of non-client protein co-chaperones, such as Hop, p23 and Aha1. Pro-folding co-chaperones facilitate the transit of the client protein through the chaperone mediated folding process. However, chaperones are also involved in ubiquitin-mediated proteasomal degradation of client proteins. Similar to folding complexes, the ability of chaperones to mediate protein degradation is regulated by co-chaperones, such as the C terminal Hsp70 binding protein (CHIP).
- Full Text:
- Date Issued: 2015
Dynamic mitochondrial localisation of STAT3 in the cellular adipogenesis model 3T3-L1:
- Authors: Kramer, Adam H , Edkins, Adrienne L , Hoppe, Heinrich C , Prinsloo, Earl
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164885 , vital:41181 , DOI: 10.1002/jcb.25076
- Description: A mechanistic relationship exists between protein localisation, activity and cellular differentiation. Understanding the contribution of these molecular mechanisms is required for elucidation of conditions that drive development. Literature suggests non‐canonical translocation of the Signal Transducer and Activator of Transcription 3 (STAT3) to the mitochondria contributes to the regulation of the electron transport chain, cellular respiration and reactive oxygen species production. Based on this we investigated the role of mitochondrial STAT3, specifically the serine 727 phosphorylated form, in cellular differentiation using the well‐defined mouse adipogenic model 3T3-L1.
- Full Text:
- Date Issued: 2015
Hsp70/Hsp90 organising protein (hop): beyond interactions with chaperones and prion proteins
- 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 palladacycle, AJ-5, exhibits anti-tumour and anti-cancer stem cell activity in breast cancer cells:
- Authors: Aliwaini, Saeb , Peres, Jade , Kröger, Wendy L , Blanckenberg, Angelique , de la Mare, Jo-Anne , Edkins, Adrienne L , Mapolie, Selwyn , Prince, Sharon
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164874 , vital:41180 , DOI: 10.1016/j.canlet.2014.11.027
- Description: Breast cancer is the most common malignancy amongst women worldwide but despite enormous efforts to address this problem, there is still limited success with most of the current therapeutic strategies. The current study describes the anti-cancer activity of a binuclear palladacycle complex (AJ-5) in oestrogen receptor positive (MCF7) and oestrogen receptor negative (MDA-MB-231) breast cancer cells as well as human breast cancer stem cells. AJ-5 is shown to induce DNA double strand breaks leading to intrinsic and extrinsic apoptosis and autophagy cell death pathways which are mediated by the p38 MAP kinase. This study provides evidence that AJ-5 is potentially an effective compound in the treatment of breast cancer.
- Full Text:
- Date Issued: 2015
Breast cancer: current developments in molecular approaches to diagnosis and treatment
- Authors: de la Mare, Jo-Anne , Contu, Lara , Hunter, Morgan C , Moyo, Buhle , Sterrenberg, Jason N , Dhanani, Karim C H , Mutsvunguma, Lorraine Z , Edkins, Adrienne L
- Date: 2014
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164819 , vital:41175 , DOI: 10.2174/15748928113086660046
- Description: Due to the high heterogeneity of breast cancers, numerous recent patents describe improved methods of detection and classification which promise better patient prognosis and treatment. In particular, there has been a shift towards more effective genetic screening to identify specific mutations associated with breast tumours, which may lead to “personalised medicine” with improved outcomes. Two challenging areas of breast cancer research involve the development of treatments for the highly aggressive triple negative breast cancer subtype as well as the chemotherapy-resistant cancer stem cell subpopulation. In addition, despite numerous recent advances in breast cancer treatment in woman, male breast cancer remains poorly understood and there are limited therapies available which are developed specifically for men. This review serves to report on important developments in the treatment of breast malignancies patented in the past two years as well as to highlight the current gaps in the field of breast cancer therapeutics and areas which require further study.
- Full Text:
- Date Issued: 2014
General structural and functional features of molecular chaperones:
- Authors: Edkins, Adrienne L , Boshoff, Aileen
- Date: 2014
- Language: English
- Type: text , book
- Identifier: http://hdl.handle.net/10962/164808 , vital:41174 , ISBN 978-94-007-7437-7 , DOI: 10.1007/978-94-007-7438-4_2
- Description: Molecular chaperones are a group of structurally diverse and highly conserved ubiquitous proteins. They play crucial roles in facilitating the correct folding of proteins in vivo by preventing protein aggregation or facilitating the appropriate folding and assembly of proteins. Heat shock proteins form the major class of molecular chaperones that are responsible for protein folding events in the cell. This is achieved by ATP-dependent (folding machines) or ATP-independent mechanisms (holders). Heat shock proteins are induced by a variety of stresses, besides heat shock. The large and varied heat shock protein class is categorised into several subfamilies based on their sizes in kDa namely, small Hsps (HSPB), Hsp40 (DNAJ), Hsp60 (HSPD/E; Chaperonins), Hsp70 (HSPA), Hsp90 (HSPC), and Hsp100.
- Full Text:
- Date Issued: 2014
Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells
- Authors: Hunter, Morgan C , O’Hagan, Kyle L , Kenyon, Amy , Dhanani, Karim C H , Prinsloo, Earl , Edkins, Adrienne L
- Date: 2014
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/431143 , vital:72748 , xlink:href="https://doi.org/10.1371/journal.pone.0086842"
- Description: Heat shock protein 90 (Hsp90) has been identified in the extracellular space and has been shown to chaperone a finite number of extracellular proteins involved in cell migration and invasion. We used chemical cross-linking and immunoprecipitation followed by tandem mass spectrometry (MS/MS) to isolate a complex containing Hsp90 and the matrix protein fibronectin (FN) from breast cancer cells. Further analysis showed direct binding of Hsp90 to FN using an in vitro co-immunoprecipitation assay, a solid phase binding assay and surface plasmon resonance (SPR) spectroscopy. Confocal microscopy showed regions of co-localisation of Hsp90 and FN in breast cancer cell lines. Exogenous Hsp90β was shown to increase the formation of extracellular FN matrix in the Hs578T cell line, whilst knockdown or inhibition of Hsp90 led to a reduction in the levels of both soluble and insoluble FN and could be partially rescued by addition of exogenous Hsp90β. Treatment of cells with novobiocin led to internalization of FN into vesicles that were positive for the presence of the lysosomal marker, LAMP-1. Taken together, the direct interaction between FN and Hsp90, as well as the decreased levels of both soluble and insoluble FN upon Hsp90 inhibition or knockdown, suggested that FN may be a new client protein for Hsp90 and that Hsp90 was involved in FN matrix assembly and/or stability. The identification of FN as a putative client protein of Hsp90 suggests a role for Hsp90 in FN matrix stability, which is important for a number of fundamental cellular processes including embryogenesis, wound healing, cell migration and metastasis.
- Full Text:
- Date Issued: 2014
Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells:
- Authors: Hunter, Morgan C , O’Hagan, Kyle L , Kenyon, Amy , Dhanani, Karim C H , Prinsloo, Earl , Edkins, Adrienne L
- Date: 2014
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164841 , vital:41177 , DOI: 10.1371/journal.pone.0086842
- Description: Heat shock protein 90 (Hsp90) has been identified in the extracellular space and has been shown to chaperone a finite number of extracellular proteins involved in cell migration and invasion. We used chemical cross-linking and immunoprecipitation followed by tandem mass spectrometry (MS/MS) to isolate a complex containing Hsp90 and the matrix protein fibronectin (FN) from breast cancer cells.
- Full Text:
- Date Issued: 2014
Real-time monitoring of 3T3-L1 preadipocyte differentiation using a commercially available electric cell-substrate impedance sensor system
- Authors: Kramer, Adam H , Joos-Vandewalle, Julia , Edkins, Adrienne L , Frost, Carminita L , Prinsloo, Earl
- Date: 2014
- Subjects: To be catalogued
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/431171 , vital:72751 , xlink:href="https://doi.org/10.1016/j.bbrc.2013.12.123"
- Description: Real-time analysis offers multiple benefits over traditional end point assays. Here, we present a method of monitoring the optimisation of the growth and differentiation of murine 3T3-L1 preadipocytes to adipocytes using the commercially available ACEA xCELLigence Real-Time Cell Analyser Single Plate (RTCA SP) system. Our findings indicate that the ACEA xCELLigence RTCA SP can reproducibly monitor the primary morphological changes in pre- and post-confluent 3T3-L1 fibroblasts induced to differentiate using insulin, dexamethasone, 3-isobutyl-1-methylxanthine and rosiglitazone; and may be a viable primary method of screening compounds for adipogenic factors.
- Full Text:
- Date Issued: 2014
Real-time monitoring of 3T3-L1 preadipocyte differentiation using a commercially available electric cell-substrate impedance sensor system:
- Authors: Kramer, Adam H , Joos-Vandewalle, Julia , Edkins, Adrienne L , Frost, Carminita L , Prinsloo, Earl
- Date: 2014
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/164830 , vital:41176 , DOI: 10.1016/j.bbrc.2013.12.123
- Description: Real-time analysis offers multiple benefits over traditional end point assays. Here, we present a method of monitoring the optimisation of the growth and differentiation of murine 3T3-L1 preadipocytes to adipocytes using the commercially available ACEA xCELLigence Real-Time Cell Analyser Single Plate (RTCA SP) system. Our findings indicate that the ACEA xCELLigence RTCA SP can reproducibly monitor the primary morphological changes in pre- and post-confluent 3T3-L1 fibroblasts induced to differentiate using insulin, dexamethasone, 3-isobutyl-1-methylxanthine and rosiglitazone; and may be a viable primary method of screening compounds for adipogenic factors.
- Full Text:
- Date Issued: 2014
Sequence and domain conservation of the coelacanth Hsp40 and Hsp90 chaperones suggests conservation of function
- Authors: Tastan Bishop, Özlem , Edkins, Adrienne L , Blatch, Gregory L
- Date: 2014
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/126932 , vital:35936 , https://doi.10.1002/jez.b.22541
- Description: Molecular chaperones and their associated co‐chaperones play an important role in preserving and regulating the active conformational state of cellular proteins. The chaperone complement of the Indonesian Coelacanth, Latimeria menadoensis, was elucidated using transcriptomic sequences. Heat shock protein 90 (Hsp90) and heat shock protein 40 (Hsp40) chaperones, and associated cochaperones were focused on, and homologous human sequences were used to search the sequence databases. Coelacanth homologs of the cytosolic, mitochondrial and endoplasmic reticulum (ER) homologs of human Hsp90 were identified, as well as all of the major co‐chaperones of the cytosolic isoform. Most of the human Hsp40s were found to have coelacanth homologs, and the data suggested that all of the chaperone machinery for protein folding at the ribosome, protein translocation to cellular compartments such as the ER and protein degradation were conserved. Some interesting similarities and differences were identified when interrogating human, mouse, and zebrafish homologs. For example, DnaJB13 is predicted to be a non‐functional Hsp40 in humans, mouse, and zebrafish due to a corrupted histidine‐proline‐aspartic acid (HPD) motif, while the coelacanth homolog has an intact HPD. These and other comparisons enabled important functional and evolutionary questions to be posed for future experimental studies.
- Full Text:
- Date Issued: 2014
The networking of chaperones by co-chaperones: control of cellular protein homeostasis
- 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