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Wyszukujesz frazę ""Protein Aggregation, Pathological"" wg kryterium: Temat


Tytuł :
Protective effect of Terminalia chebula Retz. extract against Aβ aggregation and Aβ-induced toxicity in Caenorhabditis elegans.
Autorzy :
Zhao L; School of Pharmacy, Lanzhou University, Donggang Road No. 199, Lanzhou, 730000, China.
Duan Z; School of Pharmacy, Lanzhou University, Donggang Road No. 199, Lanzhou, 730000, China.
Wang Y; School of Pharmacy, Lanzhou University, Donggang Road No. 199, Lanzhou, 730000, China.
Wang M; School of Pharmacy, Lanzhou University, Donggang Road No. 199, Lanzhou, 730000, China.
Liu Y; School of Pharmacy, Lanzhou University, Donggang Road No. 199, Lanzhou, 730000, China.
Wang X; School of Pharmacy, Lanzhou University, Donggang Road No. 199, Lanzhou, 730000, China. Electronic address: .
Li H; School of Pharmacy, Lanzhou University, Donggang Road No. 199, Lanzhou, 730000, China; Institute of Microbiology, School of Life Sciences, Lanzhou University, Tianshui Road No. 222, Lanzhou, 730000, China. Electronic address: .
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Źródło :
Journal of ethnopharmacology [J Ethnopharmacol] 2021 Mar 25; Vol. 268, pp. 113640. Date of Electronic Publication: 2020 Dec 08.
Typ publikacji :
Journal Article
MeSH Terms :
Terminalia*
Amyloid beta-Peptides/*toxicity
Peptide Fragments/*toxicity
Plant Extracts/*therapeutic use
Protein Aggregation, Pathological/*chemically induced
Protein Aggregation, Pathological/*prevention & control
Amyloid beta-Peptides/antagonists & inhibitors ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans ; Dose-Response Relationship, Drug ; Humans ; Peptide Fragments/antagonists & inhibitors ; Plant Extracts/isolation & purification ; Plant Extracts/pharmacology ; Protein Aggregation, Pathological/pathology
Czasopismo naukowe
Tytuł :
Biflavonoid-Induced Disruption of Hydrogen Bonds Leads to Amyloid-β Disaggregation.
Autorzy :
Windsor PK; Department of Chemistry, Truman State University, Kirksville, MO 63501, USA.
Plassmeyer SP; Department of Chemistry, Truman State University, Kirksville, MO 63501, USA.
Mattock DS; Department of Chemistry, Truman State University, Kirksville, MO 63501, USA.
Bradfield JC; Department of Chemistry, Truman State University, Kirksville, MO 63501, USA.
Choi EY; Department of Pharmacology, A.T. Still University, Kirksville, MO 63501, USA.
Miller BR 3rd; Department of Chemistry, Truman State University, Kirksville, MO 63501, USA.
Han BH; Department of Pharmacology, A.T. Still University, Kirksville, MO 63501, USA.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Mar 12; Vol. 22 (6). Date of Electronic Publication: 2021 Mar 12.
Typ publikacji :
Journal Article
MeSH Terms :
Alzheimer Disease/*drug therapy
Benzothiazoles/*pharmacology
Biflavonoids/*pharmacology
Protein Aggregation, Pathological/*drug therapy
Alzheimer Disease/pathology ; Amyloid/antagonists & inhibitors ; Amyloid/drug effects ; Amyloid/ultrastructure ; Amyloid beta-Peptides/antagonists & inhibitors ; Amyloid beta-Peptides/ultrastructure ; Biflavonoids/chemistry ; Brain/drug effects ; Brain/pathology ; Humans ; Hydrogen Bonding/drug effects ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/pathology
Czasopismo naukowe
Tytuł :
SARS-CoV-2 spike protein interactions with amyloidogenic proteins: Potential clues to neurodegeneration.
Autorzy :
Idrees D; Faculty of Allied Health Sciences, Shree Guru Gobind Singh Tricentenary University, Gurugram, Haryana, 122505, India. Electronic address: .
Kumar V; Amity Institute of Neuropsychology & Neurosciences, Amity University, Noida, UP, 201303, India. Electronic address: .
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Źródło :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2021 May 21; Vol. 554, pp. 94-98. Date of Electronic Publication: 2021 Mar 24.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Aggregation, Pathological*
Amyloid/*metabolism
COVID-19/*metabolism
Heparin/*metabolism
Neurodegenerative Diseases/*metabolism
SARS-CoV-2/*pathogenicity
Spike Glycoprotein, Coronavirus/*metabolism
Amyloid beta-Peptides/metabolism ; Brain/metabolism ; Brain/pathology ; Brain/virology ; COVID-19/virology ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Humans ; Molecular Docking Simulation ; Neurodegenerative Diseases/virology ; Prions/metabolism ; Protein Binding ; SARS-CoV-2/chemistry ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/chemistry ; alpha-Synuclein/metabolism ; tau Proteins/metabolism
Czasopismo naukowe
Tytuł :
On the Role of Normal Aging Processes in the Onset and Pathogenesis of Diseases Associated with the Abnormal Accumulation of Protein Aggregates.
Autorzy :
Ilyinsky NS; Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141701, Russia. .
Nesterov SV; Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141701, Russia.; Institute of Cytochemistry and Molecular Pharmacology, Moscow, 115404, Russia.
Shestoperova EI; Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141701, Russia.
Fonin AV; Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141701, Russia.; Institute of Cytology, Russian Academy of Sciences, Saint Petersburg, 194064, Russia.
Uversky VN; Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141701, Russia.; Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.
Gordeliy VI; Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, 141701, Russia.; Forschungszentrum Juelich, Juelich, 52428, Germany.; Institut de Biologie Structurale, Grenoble, 38000, France.
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Źródło :
Biochemistry. Biokhimiia [Biochemistry (Mosc)] 2021 Mar; Vol. 86 (3), pp. 275-289.
Typ publikacji :
Journal Article; Review
MeSH Terms :
Aging*
Protein Aggregation, Pathological*
Proteostasis Deficiencies/*metabolism
Animals ; Humans ; Mitochondria/metabolism ; Mitochondria/pathology ; Neurodegenerative Diseases/etiology ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/physiopathology ; Proteostasis ; Proteostasis Deficiencies/etiology ; Proteostasis Deficiencies/physiopathology
Czasopismo naukowe
Tytuł :
Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing.
Autorzy :
Alberti S; Technische Universität Dresden, Biotechnology Center (BIOTEC) and Center for Molecular and Cellular Engineering (CMCB), Dresden, Germany. .
Hyman AA; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany. .
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Źródło :
Nature reviews. Molecular cell biology [Nat Rev Mol Cell Biol] 2021 Mar; Vol. 22 (3), pp. 196-213. Date of Electronic Publication: 2021 Jan 28.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't; Review
MeSH Terms :
Aging*/metabolism
Aging*/pathology
Macromolecular Substances/*chemistry
Multiprotein Complexes/*physiology
Protein Aggregation, Pathological/*etiology
Stress, Physiological/*physiology
Animals ; Cell Physiological Phenomena ; Humans ; Macromolecular Substances/metabolism ; Protein Aggregates/physiology ; Protein Aggregation, Pathological/metabolism
Czasopismo naukowe
Tytuł :
The Autophagy Pathway: A Critical Route in the Disposal of Alpha 1-Antitrypsin Aggregates That Holds Many Mysteries.
Autorzy :
Leon C; INSERM, CNRS, U1053 BaRITOn, University Bordeaux, F-33000 Bordeaux, France.
Bouchecareilh M; INSERM, CNRS, U1053 BaRITOn, University Bordeaux, F-33000 Bordeaux, France.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Feb 13; Vol. 22 (4). Date of Electronic Publication: 2021 Feb 13.
Typ publikacji :
Journal Article; Review
MeSH Terms :
Autophagy*
Hepatocytes*/metabolism
Hepatocytes*/pathology
Liver*/metabolism
Liver*/pathology
Liver Diseases*/metabolism
Liver Diseases*/pathology
Liver Diseases*/surgery
Liver Transplantation*
Protein Aggregation, Pathological*/genetics
Protein Aggregation, Pathological*/metabolism
Protein Aggregation, Pathological*/pathology
Protein Aggregation, Pathological*/surgery
alpha 1-Antitrypsin*/genetics
alpha 1-Antitrypsin*/metabolism
Humans ; Inclusion Bodies/genetics ; Inclusion Bodies/metabolism ; Inclusion Bodies/pathology ; alpha 1-Antitrypsin Deficiency/genetics ; alpha 1-Antitrypsin Deficiency/metabolism ; alpha 1-Antitrypsin Deficiency/pathology
Czasopismo naukowe
Tytuł :
βB2 W151R mutant is prone to degradation, aggregation and exposes the hydrophobic side chains in the fourth Greek Key motif.
Autorzy :
Xu J; Eye Center of the Second Affiliated Hospital, Medical College of Zhejiang University, 88 Jiefang Road, Hangzhou 310009, China.
Wang H; Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou 310020, China.
Wang A; Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou 310020, China.
Xu J; Eye Center of the Second Affiliated Hospital, Medical College of Zhejiang University, 88 Jiefang Road, Hangzhou 310009, China.
Fu C; Eye Center of the Second Affiliated Hospital, Medical College of Zhejiang University, 88 Jiefang Road, Hangzhou 310009, China.
Jia Z; Eye Center of the Second Affiliated Hospital, Medical College of Zhejiang University, 88 Jiefang Road, Hangzhou 310009, China.
Yao K; Eye Center of the Second Affiliated Hospital, Medical College of Zhejiang University, 88 Jiefang Road, Hangzhou 310009, China. Electronic address: .
Chen X; Eye Center of the Second Affiliated Hospital, Medical College of Zhejiang University, 88 Jiefang Road, Hangzhou 310009, China; Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou 310020, China. Electronic address: .
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Źródło :
Biochimica et biophysica acta. Molecular basis of disease [Biochim Biophys Acta Mol Basis Dis] 2021 Feb 01; Vol. 1867 (2), pp. 166018. Date of Electronic Publication: 2020 Nov 25.
Typ publikacji :
Case Reports; Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Cataract/*congenital
Lanosterol/*therapeutic use
Lens, Crystalline/*pathology
Protein Aggregation, Pathological/*genetics
beta-Crystallin B Chain/*genetics
Cataract/drug therapy ; Cataract/genetics ; Cataract/pathology ; Child, Preschool ; DNA Mutational Analysis ; Female ; HEK293 Cells ; HeLa Cells ; Humans ; Hydrophobic and Hydrophilic Interactions/drug effects ; Lanosterol/pharmacology ; Lens, Crystalline/drug effects ; Male ; Molecular Dynamics Simulation ; Mutagenesis, Site-Directed ; Mutation ; Pedigree ; Protein Aggregation, Pathological/congenital ; Protein Aggregation, Pathological/drug therapy ; Protein Conformation, beta-Strand/drug effects ; Protein Conformation, beta-Strand/genetics ; Proteolysis/drug effects ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Trypsin/metabolism ; beta-Crystallin B Chain/chemistry ; beta-Crystallin B Chain/isolation & purification ; beta-Crystallin B Chain/metabolism
SCR Disease Name :
Cataract, Progressive Polymorphic Cortical
Czasopismo naukowe
Tytuł :
A protease protection assay for the detection of internalized alpha-synuclein pre-formed fibrils.
Autorzy :
Jarvela TS; Department of Anatomy and Neurobiology, University of Maryland-Baltimore, Baltimore, MD, United States of America.
Chaplot K; Department of Anatomy and Neurobiology, University of Maryland-Baltimore, Baltimore, MD, United States of America.
Lindberg I; Department of Anatomy and Neurobiology, University of Maryland-Baltimore, Baltimore, MD, United States of America.
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Źródło :
PloS one [PLoS One] 2021 Jan 26; Vol. 16 (1), pp. e0241161. Date of Electronic Publication: 2021 Jan 26 (Print Publication: 2021).
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural
MeSH Terms :
Biological Assay*
Neurons/*metabolism
Protein Aggregation, Pathological/*metabolism
alpha-Synuclein/*metabolism
Animals ; Cell Line ; Endopeptidases/genetics ; Endopeptidases/metabolism ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Mice ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/pathology ; alpha-Synuclein/genetics
Czasopismo naukowe
Tytuł :
Loss of TAX1BP1-Directed Autophagy Results in Protein Aggregate Accumulation in the Brain.
Autorzy :
Sarraf SA; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: .
Shah HV; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA; Program in Neuroscience and Cognitive Science, University of Maryland, College Park, MD 20742, USA.
Kanfer G; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
Pickrell AM; School of Neuroscience, College of Science, Virginia Tech, Blacksburg, VA 24061, USA.
Holtzclaw LA; Microscopy and Imaging Core, Office of the Scientific Director, Intramural Research Program, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
Ward ME; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
Youle RJ; Biochemistry Section, Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA; Program in Neuroscience and Cognitive Science, University of Maryland, College Park, MD 20742, USA. Electronic address: .
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Źródło :
Molecular cell [Mol Cell] 2020 Dec 03; Vol. 80 (5), pp. 779-795.e10. Date of Electronic Publication: 2020 Nov 17.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, N.I.H., Intramural
MeSH Terms :
Autophagy*
Apoptosis Regulatory Proteins/*deficiency
Brain/*metabolism
Intracellular Signaling Peptides and Proteins/*deficiency
Neoplasm Proteins/*deficiency
Neurodegenerative Diseases/*metabolism
Protein Aggregation, Pathological/*metabolism
Animals ; Apoptosis Regulatory Proteins/metabolism ; Brain/pathology ; Female ; HEK293 Cells ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins/metabolism ; Lipofuscin/genetics ; Lipofuscin/metabolism ; Male ; Mice ; Mice, Knockout ; Neoplasm Proteins/metabolism ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/pathology ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/pathology ; Rats ; Rats, Sprague-Dawley ; Ubiquitin/genetics ; Ubiquitin/metabolism
Czasopismo naukowe
Tytuł :
Methylselenol Produced In Vivo from Methylseleninic Acid or Dimethyl Diselenide Induces Toxic Protein Aggregation in Saccharomyces cerevisiae .
Autorzy :
Dauplais M; Laboratoire de Biologie Structurale de la Cellule, BIOC, École Polytechnique, CNRS-UMR7654, IP Paris, 91128 Palaiseau CEDEX, France.
Bierla K; IPREM UMR5254, E2S UPPA, Institut des Sciences Analytiques et de Physico-Chimie Pour l'Environnement et les Matériaux, CNRS, Université de Pau et des Pays de l'Adour, Hélioparc, 64053 Pau, France.
Maizeray C; Laboratoire de Biologie Structurale de la Cellule, BIOC, École Polytechnique, CNRS-UMR7654, IP Paris, 91128 Palaiseau CEDEX, France.
Lestini R; Laboratoire d'Optique et Biosciences, École Polytechnique, CNRS UMR7645-INSERM U1182, IP Paris, 91128 Palaiseau CEDEX, France.
Lobinski R; IPREM UMR5254, E2S UPPA, Institut des Sciences Analytiques et de Physico-Chimie Pour l'Environnement et les Matériaux, CNRS, Université de Pau et des Pays de l'Adour, Hélioparc, 64053 Pau, France.; Laboratory of Molecular Dietetics, I.M. Sechenov First Moscow State Medical University, 19048 Moscow, Russia.; Chair of Analytical Chemistry, Faculty of Chemistry, Warsaw University of Technology, Noakowskiego 3, 00-664 Warszawa, Poland.
Plateau P; Laboratoire de Biologie Structurale de la Cellule, BIOC, École Polytechnique, CNRS-UMR7654, IP Paris, 91128 Palaiseau CEDEX, France.
Szpunar J; IPREM UMR5254, E2S UPPA, Institut des Sciences Analytiques et de Physico-Chimie Pour l'Environnement et les Matériaux, CNRS, Université de Pau et des Pays de l'Adour, Hélioparc, 64053 Pau, France.
Lazard M; Laboratoire de Biologie Structurale de la Cellule, BIOC, École Polytechnique, CNRS-UMR7654, IP Paris, 91128 Palaiseau CEDEX, France.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2021 Feb 24; Vol. 22 (5). Date of Electronic Publication: 2021 Feb 24.
Typ publikacji :
Journal Article
MeSH Terms :
Protein Aggregation, Pathological*
Methanol/*analogs & derivatives
Organoselenium Compounds/*metabolism
Saccharomyces cerevisiae/*metabolism
Saccharomyces cerevisiae Proteins/*metabolism
Methanol/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae Proteins/genetics
Czasopismo naukowe
Tytuł :
Fast green FCF inhibits Aβ fibrillogenesis, disintegrates mature fibrils, reduces the cytotoxicity, and attenuates Aβ-induced cognitive impairment in mice.
Autorzy :
Liu F; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China. Electronic address: .
Wang W; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Xuan Z; Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University, Ningbo 315211, China.
Jiang L; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Chen B; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Dong Q; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Zhao F; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China.
Cui W; Ningbo Key Laboratory of Behavioral Neuroscience, Zhejiang Provincial Key Laboratory of Pathophysiology, School of Medicine, Ningbo University, Ningbo 315211, China.
Li L; College of Marine and Environmental Science, Tianjin University of Science & Technology, Tianjin 300457, China. Electronic address: .
Lu F; State Key Laboratory of Food Nutrition and Safety, Key Laboratory of Industrial Fermentation Microbiology of Ministry of Education, Tianjin Key Laboratory of Industrial Microbiology, College of Biotechnology, Tianjin University of Science & Technology, Tianjin 300457, China. Electronic address: .
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Źródło :
International journal of biological macromolecules [Int J Biol Macromol] 2021 Feb 15; Vol. 170, pp. 33-41. Date of Electronic Publication: 2020 Dec 19.
Typ publikacji :
Journal Article
MeSH Terms :
Amyloid/*antagonists & inhibitors
Amyloid beta-Peptides/*drug effects
Cognitive Dysfunction/*prevention & control
Food Additives/*therapeutic use
Lissamine Green Dyes/*therapeutic use
Neuroprotective Agents/*therapeutic use
Protein Aggregation, Pathological/*prevention & control
Alzheimer Disease/metabolism ; Alzheimer Disease/prevention & control ; Amyloid/drug effects ; Amyloid/toxicity ; Amyloid/ultrastructure ; Amyloid beta-Peptides/chemistry ; Animals ; Cognitive Dysfunction/etiology ; Cognitive Dysfunction/metabolism ; Exploratory Behavior/drug effects ; Food Additives/pharmacology ; Humans ; Hydrogen Bonding ; Lissamine Green Dyes/pharmacology ; Mice ; Microscopy, Atomic Force ; Models, Molecular ; Molecular Dynamics Simulation ; Morris Water Maze Test/drug effects ; Neuroprotective Agents/pharmacology ; Peptide Fragments/chemistry ; Peptide Fragments/drug effects ; Protein Aggregation, Pathological/drug therapy ; Protein Structure, Secondary/drug effects ; Random Allocation ; Static Electricity
Czasopismo naukowe
Tytuł :
TDP-43 aggregation induced by oxidative stress causes global mitochondrial imbalance in ALS.
Autorzy :
Zuo X; State Key Laboratory of Virology, Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, China.; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Zhou J; State Key Laboratory of Virology, Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, China.
Li Y; State Key Laboratory of Virology, Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, China.; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Wu K; State Key Laboratory of Virology, Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, China.; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Chen Z; State Key Laboratory of Virology, Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, China.
Luo Z; Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, China.
Zhang X; Key Laboratory for Nucleic Acid Research, Institute of Biophysics, Chinese Academy of Science, Beijing, China.
Liang Y; State Key Laboratory of Virology, Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, China.
Esteban MA; Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou, China.
Zhou Y; State Key Laboratory of Virology, Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences, Wuhan University, Wuhan, China. .; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China. .
Fu XD; Department of Cellular and Molecular Medicine, Institute of Genomic Medicine, University of California, San Diego, USA. .
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Źródło :
Nature structural & molecular biology [Nat Struct Mol Biol] 2021 Feb; Vol. 28 (2), pp. 132-142. Date of Electronic Publication: 2021 Jan 04.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Protein Aggregation, Pathological*
Amyotrophic Lateral Sclerosis/*metabolism
DNA-Binding Proteins/*metabolism
Mitochondria/*metabolism
Mitochondrial Proteins/*metabolism
Animals ; Cell Line ; Embryo, Mammalian ; Humans ; Mice ; Mice, Inbred C57BL ; Neurons/metabolism ; Oxidative Stress ; Protein Aggregates ; Reactive Oxygen Species/metabolism
SCR Disease Name :
Amyotrophic lateral sclerosis 1
Czasopismo naukowe
Tytuł :
Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers.
Autorzy :
Ruggeri FS; Department of Chemistry, Center for Misfolding Diseases, University of Cambridge, Cambridge, UK. .; Laboratory of Organic Chemistry & Laboratory of Physical Chemistry, Wageningen University, Wageningen, The Netherlands. .
Habchi J; Department of Chemistry, Center for Misfolding Diseases, University of Cambridge, Cambridge, UK.
Chia S; Department of Chemistry, Center for Misfolding Diseases, University of Cambridge, Cambridge, UK.
Horne RI; Department of Chemistry, Center for Misfolding Diseases, University of Cambridge, Cambridge, UK.
Vendruscolo M; Department of Chemistry, Center for Misfolding Diseases, University of Cambridge, Cambridge, UK. .
Knowles TPJ; Department of Chemistry, Center for Misfolding Diseases, University of Cambridge, Cambridge, UK. .; Cavendish Laboratory, University of Cambridge, Cambridge, UK. .
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Źródło :
Nature communications [Nat Commun] 2021 Jan 29; Vol. 12 (1), pp. 688. Date of Electronic Publication: 2021 Jan 29.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease/*drug therapy
Amyloid beta-Peptides/*antagonists & inhibitors
Bexarotene/*pharmacology
Peptide Fragments/*antagonists & inhibitors
Protein Aggregation, Pathological/*drug therapy
Spectrophotometry, Infrared/*methods
Alzheimer Disease/pathology ; Amyloid beta-Peptides/chemistry ; Amyloid beta-Peptides/metabolism ; Bexarotene/chemistry ; Bexarotene/therapeutic use ; Drug Discovery/methods ; Feasibility Studies ; Humans ; Hydrogen Bonding ; Kinetics ; Microscopy, Atomic Force ; Peptide Fragments/chemistry ; Peptide Fragments/metabolism ; Protein Aggregates/drug effects ; Protein Aggregation, Pathological/pathology ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Single Molecule Imaging ; Structure-Activity Relationship ; Vibration
Czasopismo naukowe
Tytuł :
Regulatory mechanisms of tau protein fibrillation under the conditions of liquid-liquid phase separation.
Autorzy :
Boyko S; Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106.
Surewicz K; Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106.
Surewicz WK; Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH 44106 .
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Źródło :
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2020 Dec 15; Vol. 117 (50), pp. 31882-31890. Date of Electronic Publication: 2020 Dec 01.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease/*pathology
Protein Aggregation, Pathological/*pathology
tau Proteins/*metabolism
Alternative Splicing/genetics ; Alzheimer Disease/genetics ; Brain/pathology ; Humans ; Microscopy, Atomic Force ; Mutation ; Protein Aggregation, Pathological/genetics ; Protein Isoforms/chemistry ; Protein Isoforms/genetics ; Protein Isoforms/isolation & purification ; Protein Isoforms/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; tau Proteins/chemistry ; tau Proteins/genetics ; tau Proteins/isolation & purification
Czasopismo naukowe
Tytuł :
Attenuation of subcutaneous insulin induced amyloid mass in vivo using Lumbrokinase and Serratiopeptidase.
Autorzy :
Metkar SK; Medical Bionanotechnology, Faculty of Allied Health Sciences, Chettinad Hospital and Research Institute (CHRI), Chettinad Academy of Research and Education (CARE), Chettinad Health City, Kelambakkam, Chennai 603103, India.
Girigoswami A; Medical Bionanotechnology, Faculty of Allied Health Sciences, Chettinad Hospital and Research Institute (CHRI), Chettinad Academy of Research and Education (CARE), Chettinad Health City, Kelambakkam, Chennai 603103, India.
Vijayashree R; Department of Pathology, Chettinad Hospital and Research Institute (CHRI), Chettinad Academy of Research and Education (CARE), Chettinad Health City, Kelambakkam, Chennai 603103, India.
Girigoswami K; Medical Bionanotechnology, Faculty of Allied Health Sciences, Chettinad Hospital and Research Institute (CHRI), Chettinad Academy of Research and Education (CARE), Chettinad Health City, Kelambakkam, Chennai 603103, India. Electronic address: .
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Źródło :
International journal of biological macromolecules [Int J Biol Macromol] 2020 Nov 15; Vol. 163, pp. 128-134. Date of Electronic Publication: 2020 Jun 29.
Typ publikacji :
Journal Article
MeSH Terms :
Endopeptidases/*pharmacology
Insulin/*adverse effects
Peptide Hydrolases/*pharmacology
Plaque, Amyloid/*metabolism
Plaque, Amyloid/*prevention & control
Protein Aggregation, Pathological/*metabolism
Protein Aggregation, Pathological/*prevention & control
Animals ; Benzothiazoles/chemistry ; Congo Red/chemistry ; Disease Models, Animal ; Injection Site Reaction/pathology ; Injection Site Reaction/prevention & control ; Injections, Subcutaneous ; Insulin/administration & dosage ; Male ; Microscopy, Fluorescence ; Microscopy, Polarization ; Plaque, Amyloid/chemically induced ; Plaque, Amyloid/pathology ; Protein Aggregation, Pathological/chemically induced ; Protein Aggregation, Pathological/pathology ; Rats ; Rats, Wistar ; Subcutaneous Tissue/drug effects ; Subcutaneous Tissue/pathology
Czasopismo naukowe
Tytuł :
Disease-related Huntingtin seeding activities in cerebrospinal fluids of Huntington's disease patients.
Autorzy :
Lee CYD; Center for Neurobehavioral Genetics, The Jane and Terry Semel Institute for Neuroscience & Human Behavior, University of California, Los Angeles, Los Angeles, USA.; Department of Psychiatry and Biobehavioral Sciences, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA.
Wang N; Center for Neurobehavioral Genetics, The Jane and Terry Semel Institute for Neuroscience & Human Behavior, University of California, Los Angeles, Los Angeles, USA.; Department of Psychiatry and Biobehavioral Sciences, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA.
Shen K; Department of Biology and BioX Program, Stanford University, Stanford, CA, USA.; Department of Molecular and Cell Biology, UC Berkeley, Berkeley, CA, USA.
Stricos M; Center for Neurobehavioral Genetics, The Jane and Terry Semel Institute for Neuroscience & Human Behavior, University of California, Los Angeles, Los Angeles, USA.; Department of Psychiatry and Biobehavioral Sciences, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA.
Langfelder P; Center for Neurobehavioral Genetics, The Jane and Terry Semel Institute for Neuroscience & Human Behavior, University of California, Los Angeles, Los Angeles, USA.; Department of Psychiatry and Biobehavioral Sciences, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA.
Cheon KH; Center for Neurobehavioral Genetics, The Jane and Terry Semel Institute for Neuroscience & Human Behavior, University of California, Los Angeles, Los Angeles, USA.; Department of Psychiatry and Biobehavioral Sciences, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA.
Cortés EP; Division of Aging and Dementia, Department of Neurology, Columbia University Medical Center, New York, NY, USA.
Vinters HV; Department of Pathology and Laboratory Medicine, Neurology, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA.
Vonsattel JP; Division of Aging and Dementia, Department of Neurology, Columbia University Medical Center, New York, NY, USA.
Wexler NS; Departments of Neurology and Psychiatry, College of Physicians and Surgeons, Columbia University, New York, NY, USA.; Hereditary Disease Foundation, New York, NY, USA.
Damoiseaux R; California NanoSystems Institute, University of California, Los Angeles, CA, USA.; Department of Molecular and Medical Pharmacology, University of California, Los Angeles, CA, USA.
Frydman J; Department of Biology and BioX Program, Stanford University, Stanford, CA, USA.
Yang XW; Center for Neurobehavioral Genetics, The Jane and Terry Semel Institute for Neuroscience & Human Behavior, University of California, Los Angeles, Los Angeles, USA. .; Department of Psychiatry and Biobehavioral Sciences, David Geffen School of Medicine at UCLA, Los Angeles, CA, USA. .
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Źródło :
Scientific reports [Sci Rep] 2020 Nov 20; Vol. 10 (1), pp. 20295. Date of Electronic Publication: 2020 Nov 20.
Typ publikacji :
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
MeSH Terms :
Cerebrospinal Fluid/*metabolism
HSP40 Heat-Shock Proteins/*metabolism
Huntingtin Protein/*metabolism
Huntington Disease/*pathology
Molecular Chaperones/*metabolism
Nerve Tissue Proteins/*metabolism
Protein Aggregation, Pathological/*pathology
Adult ; Aged ; Aged, 80 and over ; Brain/pathology ; Cell Line ; Exons/genetics ; Female ; Genes, Reporter/genetics ; HSP40 Heat-Shock Proteins/genetics ; Humans ; Huntingtin Protein/cerebrospinal fluid ; Huntingtin Protein/genetics ; Huntington Disease/cerebrospinal fluid ; Huntington Disease/genetics ; Intravital Microscopy ; Male ; Middle Aged ; Molecular Chaperones/genetics ; Mutation ; Nerve Tissue Proteins/genetics ; Protein Aggregation, Pathological/cerebrospinal fluid ; Protein Aggregation, Pathological/genetics ; Protein Domains/genetics ; Protein Engineering ; Protein Folding
Czasopismo naukowe
Tytuł :
Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers.
Autorzy :
Kreiser RP; Department of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
Wright AK; Department of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
Block NR; Department of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
Hollows JE; Department of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
Nguyen LT; Department of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
LeForte K; Department of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
Mannini B; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Vendruscolo M; Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.
Limbocker R; Department of Chemistry and Life Science, United States Military Academy, West Point, NY 10996, USA.
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Źródło :
International journal of molecular sciences [Int J Mol Sci] 2020 Nov 17; Vol. 21 (22). Date of Electronic Publication: 2020 Nov 17.
Typ publikacji :
Journal Article; Review
MeSH Terms :
Protein Multimerization*
Protein Aggregation, Pathological/*therapy
Proteostasis Deficiencies/*therapy
Animals ; Humans ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/pathology ; Proteostasis Deficiencies/metabolism ; Proteostasis Deficiencies/pathology
Czasopismo naukowe
Tytuł :
The inhibition of cellular toxicity of amyloid-β by dissociated transthyretin.
Autorzy :
Cao Q; Department of Biological Chemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA.; Department of Chemistry and Biochemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA.
Anderson DH; Department of Biological Chemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA.; Department of Chemistry and Biochemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA.
Liang WY; Department of Biological Chemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA.; Department of Chemistry and Biochemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA.
Chou J; Department of Biological Chemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA.; Department of Chemistry and Biochemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA.
Saelices L; Department of Biological Chemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA .; Department of Chemistry and Biochemistry, Molecular Biology Institute, University of California, Los Angeles, Los Angeles, California, USA.; Center for Alzheimer's and Neurodegenerative Diseases, Department of Biophysics, O'Donnell Brain Institute, University of Texas Southwestern Medical Center, Dallas, Texas, USA.
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Źródło :
The Journal of biological chemistry [J Biol Chem] 2020 Oct 09; Vol. 295 (41), pp. 14015-14024. Date of Electronic Publication: 2020 Aug 07.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease*/genetics
Alzheimer Disease*/metabolism
Alzheimer Disease*/pathology
Amyloid beta-Peptides*/chemistry
Amyloid beta-Peptides*/genetics
Amyloid beta-Peptides*/metabolism
Molecular Docking Simulation*
Prealbumin*/chemistry
Prealbumin*/genetics
Prealbumin*/metabolism
Protein Aggregation, Pathological*/genetics
Protein Aggregation, Pathological*/metabolism
Protein Aggregation, Pathological*/pathology
Aged, 80 and over ; Binding Sites ; Cell Line ; Female ; Humans
Czasopismo naukowe
Tytuł :
Asparagine residue 368 is involved in Alzheimer's disease tau strain-specific aggregation.
Autorzy :
Shimonaka S; Research Institute for Diseases of Old Age, Juntendo University Graduate School of Medicine, Tokyo, Japan.; Department of Diagnosis, Prevention, and Treatment of Dementia, Juntendo University School of Medicine, Tokyo, Japan.
Matsumoto SE; Department of Immunology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima, Japan.
Elahi M; Department of Diagnosis, Prevention, and Treatment of Dementia, Juntendo University School of Medicine, Tokyo, Japan.; Department of Neurology, Juntendo University School of Medicine, Tokyo, Japan.
Ishiguro K; Department of Neurology, Juntendo University School of Medicine, Tokyo, Japan.
Hasegawa M; Dementia Research Project, Tokyo Metropolitan Institute of Medical Science, Tokyo, Japan.
Hattori N; Research Institute for Diseases of Old Age, Juntendo University Graduate School of Medicine, Tokyo, Japan.; Department of Neurology, Juntendo University School of Medicine, Tokyo, Japan.
Motoi Y; Department of Diagnosis, Prevention, and Treatment of Dementia, Juntendo University School of Medicine, Tokyo, Japan .; Department of Neurology, Juntendo University School of Medicine, Tokyo, Japan.
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Źródło :
The Journal of biological chemistry [J Biol Chem] 2020 Oct 09; Vol. 295 (41), pp. 13996-14014. Date of Electronic Publication: 2020 Aug 05.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Alzheimer Disease*/genetics
Alzheimer Disease*/metabolism
Amino Acid Sequence*
Protein Aggregation, Pathological*/genetics
Protein Aggregation, Pathological*/metabolism
Sequence Deletion*
tau Proteins*/chemistry
tau Proteins*/genetics
tau Proteins*/metabolism
Asparagine/chemistry ; Asparagine/genetics ; Asparagine/metabolism ; Cell Line, Tumor ; Humans
Czasopismo naukowe
Tytuł :
A seven-residue deletion in PrP leads to generation of a spontaneous prion formed from C-terminal C1 fragment of PrP.
Autorzy :
Munoz-Montesino C; Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université de Versailles Saint-Quentin-en-Yvelines, Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.
Larkem D; Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université de Versailles Saint-Quentin-en-Yvelines, Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.
Barbereau C; Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université de Versailles Saint-Quentin-en-Yvelines, Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.
Igel-Egalon A; Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université de Versailles Saint-Quentin-en-Yvelines, Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.
Truchet S; Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université de Versailles Saint-Quentin-en-Yvelines, Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.
Jacquet E; Institut de Chimie des Substances Naturelles, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
Nhiri N; Institut de Chimie des Substances Naturelles, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
Moudjou M; Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université de Versailles Saint-Quentin-en-Yvelines, Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.
Sizun C; Institut de Chimie des Substances Naturelles, CNRS, Université Paris-Saclay, Gif-sur-Yvette, France.
Rezaei H; Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université de Versailles Saint-Quentin-en-Yvelines, Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.
Béringue V; Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université de Versailles Saint-Quentin-en-Yvelines, Virologie et Immunologie Moléculaires, Jouy-en-Josas, France.
Dron M; Université Paris-Saclay, Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement, Université de Versailles Saint-Quentin-en-Yvelines, Virologie et Immunologie Moléculaires, Jouy-en-Josas, France .
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Źródło :
The Journal of biological chemistry [J Biol Chem] 2020 Oct 09; Vol. 295 (41), pp. 14025-14039. Date of Electronic Publication: 2020 Aug 11.
Typ publikacji :
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms :
Amino Acid Sequence*
PrPSc Proteins*/chemistry
PrPSc Proteins*/genetics
PrPSc Proteins*/metabolism
Prion Diseases*/genetics
Prion Diseases*/metabolism
Prion Diseases*/pathology
Protein Aggregation, Pathological*/genetics
Protein Aggregation, Pathological*/metabolism
Protein Aggregation, Pathological*/pathology
Sequence Deletion*
Animals ; Cell Line ; Humans ; Protein Conformation, alpha-Helical ; Protein Domains ; Rabbits ; Sheep ; Solubility
Czasopismo naukowe

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