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Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.
Nguyen, Phuong H; Ramamoorthy, Ayyalusamy; Sahoo, Bikash R; Zheng, Jie; Faller, Peter; Straub, John E; Dominguez, Laura; Shea, Joan-Emma; Dokholyan, Nikolay V; De Simone, Alfonso; Ma, Buyong; Nussinov, Ruth; Najafi, Saeed; Ngo, Son Tung; Loquet, Antoine; Chiricotto, Mara; Ganguly, Pritam; McCarty, James; Li, Mai Suan; Hall, Carol; Wang, Yiming; Miller, Yifat; Melchionna, Simone; Habenstein, Birgit; Timr, Stepan; Chen, Jiaxing; Hnath, Brianna; Strodel, Birgit; Kayed, Rakez; Lesné, Sylvain; Wei, Guanghong; Sterpone, Fabio; Doig, Andrew J; Derreumaux, Philippe.
Afiliação
  • Nguyen PH; CNRS, UPR9080, Université de Paris, Laboratory of Theoretical Biochemistry, IBPC, Fondation Edmond de Rothschild, PSL Research University, Paris 75005, France.
  • Ramamoorthy A; Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, United States.
  • Sahoo BR; Biophysics and Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, United States.
  • Zheng J; Department of Chemical & Biomolecular Engineering, The University of Akron, Akron, Ohio 44325, United States.
  • Faller P; Institut de Chimie, UMR 7177, CNRS-Université de Strasbourg, 4 rue Blaise Pascal, 67000 Strasbourg, France.
  • Straub JE; Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, Massachusetts 02215, United States.
  • Dominguez L; Facultad de Química, Departamento de Fisicoquímica, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico.
  • Shea JE; Department of Chemistry and Biochemistry, and Department of Physics, University of California, Santa Barbara, California 93106, United States.
  • Dokholyan NV; Department of Pharmacology and Biochemistry & Molecular Biology, Penn State University College of Medicine, Hershey, Pennsylvania 17033, United States.
  • De Simone A; Department of Chemistry, and Biomedical Engineering, Pennsylvania State University, University Park, Pennsylvania 16802, United States.
  • Ma B; Department of Life Sciences, Imperial College London, London SW7 2AZ, U.K.
  • Nussinov R; Molecular Biology, University of Naples Federico II, Naples 80138, Italy.
  • Najafi S; Basic Science Program, Leidos Biomedical Research, Inc., Cancer and Inflammation Program, National Cancer Institute, Frederick, Maryland 21702, United States.
  • Ngo ST; School of Pharmacy, Shanghai Jiao Tong University, Shanghai, China.
  • Loquet A; Basic Science Program, Leidos Biomedical Research, Inc., Cancer and Inflammation Program, National Cancer Institute, Frederick, Maryland 21702, United States.
  • Chiricotto M; Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel.
  • Ganguly P; Department of Chemistry and Biochemistry, and Department of Physics, University of California, Santa Barbara, California 93106, United States.
  • McCarty J; Laboratory of Theoretical and Computational Biophysics & Faculty of Applied Sciences, Ton Duc Thang University, 33000 Ho Chi Minh City, Vietnam.
  • Li MS; Institute of Chemistry & Biology of Membranes & Nanoobjects, (UMR5248 CBMN), CNRS, Université Bordeaux, Institut Européen de Chimie et Biologie, 33600 Pessac, France.
  • Hall C; Department of Chemical Engineering and Analytical Science, University of Manchester, Manchester M13 9PL, U.K.
  • Wang Y; Department of Chemistry and Biochemistry, and Department of Physics, University of California, Santa Barbara, California 93106, United States.
  • Miller Y; Chemistry Department, Western Washington University, Bellingham, Washington 98225, United States.
  • Melchionna S; Institute for Computational Science and Technology, SBI Building, Quang Trung Software City, Tan Chanh Hiep Ward, District 12, Ho Chi Minh City 700000, Vietnam.
  • Habenstein B; Institute of Physics, Polish Academy of Sciences, Al. Lotnikow 32/46, 02-668 Warsaw, Poland.
  • Timr S; Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695-7905, United States.
  • Chen J; Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, North Carolina 27695-7905, United States.
  • Hnath B; Department of Chemistry and The Ilse Katz Institute for Nanoscale Science & Technology, Ben-Gurion University of the Negev, Be'er Sheva 84105, Israel.
  • Strodel B; ISC-CNR, via dei Taurini, 00185 Rome, Italy.
  • Kayed R; Institute of Chemistry & Biology of Membranes & Nanoobjects, (UMR5248 CBMN), CNRS, Université Bordeaux, Institut Européen de Chimie et Biologie, 33600 Pessac, France.
  • Lesné S; CNRS, UPR9080, Université de Paris, Laboratory of Theoretical Biochemistry, IBPC, Fondation Edmond de Rothschild, PSL Research University, Paris 75005, France.
  • Wei G; Department of Pharmacology and Biochemistry & Molecular Biology, Penn State University College of Medicine, Hershey, Pennsylvania 17033, United States.
  • Sterpone F; Department of Pharmacology and Biochemistry & Molecular Biology, Penn State University College of Medicine, Hershey, Pennsylvania 17033, United States.
  • Doig AJ; Institute of Complex Systems: Structural Biochemistry (ICS-6), Forschungszentrum Jülich, 52425 Jülich, Germany.
  • Derreumaux P; Mitchell Center for Neurodegenerative Diseases, and Departments of Neurology, Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, Texas 77555, United States.
Chem Rev ; 121(4): 2545-2647, 2021 02 24.
Article em En | MEDLINE | ID: mdl-33543942
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting either the central nervous system or a variety of peripheral tissues. Structural and dynamic characterization of all species along the pathways from monomers to fibrils is challenging by experimental and computational means because they involve intrinsically disordered proteins in most diseases. Yet understanding how amyloid species become toxic is the challenge in developing a treatment for these diseases. Here we review what computer, in vitro, in vivo, and pharmacological experiments tell us about the accumulation and deposition of the oligomers of the (Aß, tau), α-synuclein, IAPP, and superoxide dismutase 1 proteins, which have been the mainstream concept underlying Alzheimer's disease (AD), Parkinson's disease (PD), type II diabetes (T2D), and amyotrophic lateral sclerosis (ALS) research, respectively, for many years.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doenças Neurodegenerativas / Amiloide Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Doenças Neurodegenerativas / Amiloide Idioma: En Ano de publicação: 2021 Tipo de documento: Article