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English
Academic Press Inc
06 June 2024
The Hidden World of Protein Aggregation, Volume 206 provides a comprehensive exploration of protein aggregation, uncovering the factors behind the formation of amorphous aggregates and ordered structures called amyloid fibrils. It delves into the advantages and disadvantages of protein aggregates, addressing topics such as cytotoxicity and disorders linked to misfolding. Specific chapters in this release include Protein Aggregation: An Overview, Pathways of Amyloid Fibril Formation and Aggregation, Factors Influencing Amyloid Fibril Formation, Morphological Features and Types of Aggregated Structures, Each big journey starts with a first step: Importance of Oligomerization, Liquid-Liquid Phase Separation as Triggering Factor of Fibril Formation, and more.

Additional sections cover Experimental Techniques for Detecting and Evaluating the Amyloid Fibrils, Prediction of Protein Aggregation, Amyloid Fibril Cytotoxicity and Associated Disorders, Inhibitors of Amyloid Fibril Formation, Therapeutic Approaches in Proteinopathies, Functional Amyloids, Biotechnological Applications of Amyloid Fibrils, and The Hidden World of Protein Aggregation.
Series edited by:  
Volume editor:   , , , , , , ,
Imprint:   Academic Press Inc
Country of Publication:   United States
Dimensions:   Height: 229mm,  Width: 152mm, 
Weight:   450g
ISBN:   9780443293405
ISBN 10:   0443293406
Series:   Progress in Molecular Biology and Translational Science
Pages:   528
Publication Date:  
Audience:   Professional and scholarly ,  Undergraduate
Format:   Hardback
Publisher's Status:   Active

David B. Teplow, Ph.D., is a Professor of Neurology, Emeritus, at UCLA and an internationally recognized leader in efforts to understand and treat Alzheimer's disease. Dr. Teplow's group has used a multi-disciplinary approach to determine how neurotoxic peptides, such as the amyloid ß-protein (Alzheimer's disease) and a-synuclein (Parkinson’s disease), form neurotoxic structures that kill neurons and to develop the means to block these processes. Dr. Teplow received undergraduate training at UC Berkeley; a Ph.D. from the University of Washington; and was a postdoctoral scholar at Caltech. Before coming to UCLA, Dr. Teplow was a faculty member in the Department of Neurology, Harvard Medical School. Dr. Teplow has published >250 peer-reviewed articles, books and book chapters, and commentaries, in addition to serving on numerous national and international scientific advisory boards. Dr. Teplow was a founding editor of the Journal of Molecular Neuroscience and Current Chemical Biology, He is Co-Editor-in-Chief of the Elsevier serial Progress in Molecular Biology and Translational Science and is Associate Editor-in-Chief of the American Journal of Neurodegenerative Disease. Bahareh Dabirmanesh received her Ph.D. in Biochemistry from Tarbiat Modares University (Tehran-Iran) in 2013. Following the completion of her doctoral studies, she joined the University as an academic member pursuing both academic and research activities within the Department of Biochemistry, Faculty of Biological Sciences. During this period, she undertook the responsibilities of a supervisor or advisor for a considerable number of master's and PhD theses. Since 2022, she has held the position of associate professor. Her research interests are mainly focused on protein engineering, macromolecular interactions, structure-function relation, amyloidogenic proteins, Biotherapeutics, protein pathways and signaling cascades VLADIMIR N. UVERSKY is a Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida (USF). He obtained his academic degrees from Moscow Institute of Physics and Technology (Ph.D., in 1991) and from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences (D.Sc., in 1998). He spent his early career working mostly on protein folding at the Institute of Protein Research and the Institute for Biological Instrumentation (Russia). In 1998, he moved to the University of California Santa Cruz where for six years he was studying protein folding, misfolding, protein conformation diseases, and protein intrinsic disorder phenomenon. In 2004, he was invited to join the Indiana University School of Medicine as a Senior Research Professor to work on the intrinsically disordered proteins. Since 2010, Professor Uversky is with USF, where he continues to study intrinsically disordered proteins and protein folding and misfolding processes. He has authored over 1150 scientific publications and edited several books and book series on protein structure, function, folding and misfolding. He has been listed as Highly Cited Researchers™ every year from 2014 to 2020. In 2021, he was elected as a Fellow of the Royal Society of Biology and a Fellow of the Royal Society of Chemistry. Professor Uversky collaborated with more than 12,500 colleagues from more than 2,750 research organizations in 89 countries/territories.

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