Molecular chaperone network11/10/2023 ![]() Ltd, USA) “CHAMPS (Chaperone-mediated Protein Degradation/Degrader)”Ģ:00pm Jason Gestwicki, (UCSF, USA), “Leveraging New Insights into the Structure-Function of Heat Shock Protein 60 (Hsp60) to Design High Throughput Chemical Screens”Ģ:15pm Anushka Wickramaratne, (National Institutes of Health) " An intermediate Hsp90-J-protein complex in the pathway of protein remodeling"Ģ:45pm Ahmed Chadli, (Augusta University, USA) "EnnA inhibits the chaperone Hsp90 and unleashes the immune system against triple-negative breast cancer "ģ:00pm Fortunate Mokoena (North-West University, South Africa) "A pharmacophore model based virtual screening workflow for discovery of inhibitors targeting Plasmodium falciparum Hsp90"ģ:15pm Tawanda Zininga, (Stellenbosch University, South Africa) "Screening and characterization of peptide based inhibitors targeting the ER localised Plasmodium falciparum Hsp90"Ĥ:00pm Ferruccio Ritossa Early Career Award, Alfred Tissières Young Investigator Award Session 2: HSP INHIBITORS AND CANCER THERAPYġ:30pm Christine Heske, (National Cancer Institute, USA) "Hsp90 inhibitor drug conjugates: Increased tumor retention and decreased systemic toxicity of the active topoisomerase inhibitor SN-38"ġ:45pm Kevin Foley, (Ranok Therapeutics Co. “Regulation of the heat shock response by the Hsp70 network."Ĭhair: Lea Sistonen and Stuart Calderwoodġ0:00am Nahid Mivechi, (University of Georgia, USA) “Role of Heat Shock Factor 2 (HSF2) in Tumorigenesis”ġ0:15am Takanori Eguchi, (Okayama University, Japan) “Role of Zinc finger transcription factors in regulating molecular chaperone expression”ġ0:30am Adrienne Edkins, (Rhodes University, South Africa)ġ0:45am Valerie Lallemand Mezger, (CNRS, Paris, France)ġ1:15am Lea Sistonen, (Åbo Akademi University, Finland) ”Novel Targets of HSFs in Cell Stress and Differentiation Programsġ1:30am Anniina Vihervaara, (KTH Royal Institute of Technology) "Priming and timing: The genetic basis for ordered synthesis of chaperone machineries"ġ1:45am Jenny Joutsen, () "Comprehensive analysis of human tissues reveals novel expression and localization patterns of HSF1 and HSF2" This opens the way to the chaperone-regulated modular evolution of cellular networks, and helps us to design novel therapeutic and anti-ageing strategies.Center for Molecular Biology of Heidelberg University (ZMBH) DKFZ-ZMBH alliance Heidelberg, Germany Moreover, chaperones are essential to rebuild inter-modular contacts after stress by their low affinity, 'quasi-random' sampling of the potential interaction partners in different cellular modules. Importantly, chaperones may uncouple or even quarantine modules of protein-protein interaction networks, signalling networks, genetic regulatory networks and membrane organelle networks during stress, which gives an additional chaperone-mediated protection for the cell at the network-level. act as 'masterminds' of the cell being close to several centre proteins with a lot of neighbours and (3) are in the overlaps of network modules, which confers upon them a special regulatory role. low affinity, transient interactions with most of their partners (2) connect hubs, i.e. ![]() Why are chaperones special in the context of cellular networks? Chaperones: (1) have weak links, i.e. As a notable example for the network-related roles of chaperones they may act as genetic buffers stabilizing the phenotype of various cells and organisms, and may serve as potential regulators of evolvability. These functions can be understood only by considering the emergent properties of cellular networks-and that of chaperones as special network constituents. Molecular chaperones are not only fascinating molecular machines that help the folding, refolding, activation or assembly of other proteins, but also have a number of functions.
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