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Wyszukujesz frazę ""Protein aggregation"" wg kryterium: Temat


Tytuł:
A rare natural lipid induces neuroglobin expression to prevent amyloid oligomers toxicity and retinal neurodegeneration.
Autorzy:
Oamen HP; School of Biological and Behavioural Sciences, Queen Mary University of London, London, UK.
Romero Romero N; School of Biological and Behavioural Sciences, Queen Mary University of London, London, UK.
Knuckles P; Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
Saarikangas J; Helsinki Institute of Life Science, HiLIFE, University of Helsinki, Helsinki, Finland.; Research Programme in Molecular and Integrative Biosciences, Faculty of Biological and Environmental Sciences, University of Helsinki, Helsinki, Finland.; Neuroscience Center, University of Helsinki, Helsinki, Finland.
Radman-Livaja M; IGMM, Univ Montpellier, CNRS, Montpellier, France.
Dong Y; SunRegen Healthcare AG, Reinach, Switzerland.
Caudron F; IGMM, Univ Montpellier, CNRS, Montpellier, France.
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Źródło:
Aging cell [Aging Cell] 2022 Jul; Vol. 21 (7), pp. e13645. Date of Electronic Publication: 2022 Jun 03.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Amyloid*/drug effects
Amyloid*/metabolism
Lipids*/pharmacology
Protein Aggregation, Pathological*/genetics
Protein Aggregation, Pathological*/metabolism
Alzheimer Disease ; Amyloid beta-Peptides/drug effects ; Amyloid beta-Peptides/metabolism ; Animals ; Dioxygenases ; Hemeproteins ; Mammals ; Mice ; Neuroglobin/drug effects ; Neuroglobin/metabolism ; Processing Bodies/drug effects ; Processing Bodies/metabolism ; Retinal Ganglion Cells/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins
Czasopismo naukowe
Tytuł:
Mechanistic insights into accelerated α-synuclein aggregation mediated by human microbiome-associated functional amyloids.
Autorzy:
Bhoite SS; Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan, USA.
Han Y; Department of Chemistry, University of Michigan, Ann Arbor, Michigan, USA.
Ruotolo BT; Department of Chemistry, University of Michigan, Ann Arbor, Michigan, USA. Electronic address: .
Chapman MR; Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, Michigan, USA. Electronic address: .
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Źródło:
The Journal of biological chemistry [J Biol Chem] 2022 Jul; Vol. 298 (7), pp. 102088. Date of Electronic Publication: 2022 May 30.
Typ publikacji:
Journal Article
MeSH Terms:
Amyloid*/metabolism
Escherichia coli Proteins*/metabolism
Microbiota*
Protein Aggregation, Pathological*
alpha-Synuclein*/metabolism
Animals ; Escherichia coli ; Humans ; Mice ; Parkinson Disease/pathology
Czasopismo naukowe
Tytuł:
Amyloid polymorphs and pathological diversities.
Autorzy:
Melki R; Institut Francois Jacob (MIRCen), CEA and Laboratory of Neurodegenerative Diseases, CNRS, 18 Route du Panorama, 92265, Fontenay-Aux-Roses cedex, France. Electronic address: .
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Źródło:
Neurochemistry international [Neurochem Int] 2022 Jun; Vol. 156, pp. 105335. Date of Electronic Publication: 2022 Apr 05.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Neurodegenerative Diseases*/metabolism
Protein Aggregation, Pathological*/metabolism
Amyloid/chemistry ; Humans
Czasopismo naukowe
Tytuł:
Acquired Disorder and Asymmetry in a Domain-Swapped Model for γ-Crystallin Aggregation.
Autorzy:
Sagar V; Section on Molecular Structure and Functional Genomics, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Wistow G; Section on Molecular Structure and Functional Genomics, National Eye Institute, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: .
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Źródło:
Journal of molecular biology [J Mol Biol] 2022 May 15; Vol. 434 (9), pp. 167559. Date of Electronic Publication: 2022 Mar 24.
Typ publikacji:
Journal Article; Research Support, N.I.H., Intramural
MeSH Terms:
Protein Aggregation, Pathological*
gamma-Crystallins*/chemistry
Cataract/metabolism ; Disulfides/chemistry ; Humans ; Protein Structure, Secondary
Czasopismo naukowe
Tytuł:
Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation.
Autorzy:
Okumura H; Exploratory Research Center on Life and Living Systems, National Institutes of Natural Sciences, Okazaki 444-8787, Aichi, Japan.; Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki 444-8787, Aichi, Japan.; Department of Structural Molecular Science, SOKENDAI (The Graduate University for Advanced Studies), Okazaki 444-8787, Aichi, Japan.
Itoh SG; Exploratory Research Center on Life and Living Systems, National Institutes of Natural Sciences, Okazaki 444-8787, Aichi, Japan.; Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki 444-8787, Aichi, Japan.; Department of Structural Molecular Science, SOKENDAI (The Graduate University for Advanced Studies), Okazaki 444-8787, Aichi, Japan.
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Źródło:
Molecules (Basel, Switzerland) [Molecules] 2022 Apr 12; Vol. 27 (8). Date of Electronic Publication: 2022 Apr 12.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Amyloid beta-Peptides*/chemistry
Molecular Dynamics Simulation*
Protein Aggregation, Pathological*/metabolism
Alzheimer Disease ; Amyloid/chemistry ; Humans ; Lasers ; Peptide Fragments ; Ultrasonic Waves ; Water
Czasopismo naukowe
Tytuł:
Targeting α-synuclein aggregation and its role in mitochondrial dysfunction in Parkinson's disease.
Autorzy:
Haque ME; Department of Applied Life Science, Graduate School, BK21 Program, Konkuk University, Chungju, Republic of Korea.
Akther M; Department of Applied Life Science, Graduate School, BK21 Program, Konkuk University, Chungju, Republic of Korea.
Azam S; Department of Applied Life Science, Graduate School, BK21 Program, Konkuk University, Chungju, Republic of Korea.
Kim IS; Department of Biotechnology, College of Biomedical and Health Science, Research Institute of Inflammatory Disease (RID), Konkuk University, Chungju, Republic of Korea.
Lin Y; Research Center for Bioconvergence Analysis, Korea Basic Science Institute, Ochang, Republic of Korea.
Lee YH; Research Center for Bioconvergence Analysis, Korea Basic Science Institute, Ochang, Republic of Korea.; Department of Bio-analytical Science, University of Science and Technology, Daejeon, Republic of Korea.; Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon, Republic of Korea.; Research Headquarters, Korea Brain Research Institute, Daegu, Republic of Korea.
Choi DK; Department of Applied Life Science, Graduate School, BK21 Program, Konkuk University, Chungju, Republic of Korea.; Department of Biotechnology, College of Biomedical and Health Science, Research Institute of Inflammatory Disease (RID), Konkuk University, Chungju, Republic of Korea.
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Źródło:
British journal of pharmacology [Br J Pharmacol] 2022 Jan; Vol. 179 (1), pp. 23-45. Date of Electronic Publication: 2021 Nov 24.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't; Review
MeSH Terms:
Dopaminergic Neurons*/metabolism
Dopaminergic Neurons*/pathology
Mitochondria*/metabolism
Mitochondria*/pathology
Parkinson Disease*/drug therapy
Parkinson Disease*/metabolism
Protein Aggregation, Pathological*/metabolism
Protein Aggregation, Pathological*/pathology
alpha-Synuclein*/metabolism
Apoptosis ; Humans ; Lewy Bodies/metabolism ; Lewy Bodies/pathology ; Mitochondrial Diseases/metabolism ; Mitochondrial Diseases/pathology ; Oxidative Stress
Czasopismo naukowe
Tytuł:
Extracellular Prion Protein Aggregates in Nine Gerstmann-Sträussler-Scheinker Syndrome Subjects with Mutation P102L: A Micromorphological Study and Comparison with Literature Data.
Autorzy:
Jankovska N; Department of Pathology and Molecular Medicine, Third Faculty of Medicine, Charles University and Thomayer University Hospital, 14059 Prague, Czech Republic.
Matej R; Department of Pathology and Molecular Medicine, Third Faculty of Medicine, Charles University and Thomayer University Hospital, 14059 Prague, Czech Republic.; Department of Pathology, First Faculty of Medicine, Charles University and General University Hospital, 12800 Prague, Czech Republic.; Department of Pathology, Third Faculty of Medicine, Charles University and University Hospital Kralovske Vinohrady, 10034 Prague, Czech Republic.
Olejar T; Department of Pathology and Molecular Medicine, Third Faculty of Medicine, Charles University and Thomayer University Hospital, 14059 Prague, Czech Republic.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Dec 10; Vol. 22 (24). Date of Electronic Publication: 2021 Dec 10.
Typ publikacji:
Comparative Study; Journal Article
MeSH Terms:
Gerstmann-Straussler-Scheinker Disease*/genetics
Gerstmann-Straussler-Scheinker Disease*/metabolism
Gerstmann-Straussler-Scheinker Disease*/pathology
Mutation, Missense*
Prion Proteins*/genetics
Prion Proteins*/metabolism
Protein Aggregation, Pathological*/genetics
Protein Aggregation, Pathological*/metabolism
Protein Aggregation, Pathological*/pathology
Adult ; Aged ; Female ; Humans ; Male ; Middle Aged
Czasopismo naukowe
Tytuł:
Thioridazine reverts the phenotype in cellular and Drosophila models of amyotrophic lateral sclerosis by enhancing TDP-43 aggregate clearance.
Autorzy:
Cragnaz L; International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34149 Trieste, Italy.
Spinelli G; International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34149 Trieste, Italy.
De Conti L; International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34149 Trieste, Italy.
Bureau EA; LifeArc, Accelerator Building, Open Innovation Campus, Stevenage SG1 2FX, United Kingdom.
Brownlees J; LifeArc, Accelerator Building, Open Innovation Campus, Stevenage SG1 2FX, United Kingdom.
Feiguin F; International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34149 Trieste, Italy; Department of Life and Environmental Sciences, University of Cagliari, 09042 Monserrato, Cagliari, Italy.
Romano V; International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34149 Trieste, Italy.
Skoko N; International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34149 Trieste, Italy.
Klima R; International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34149 Trieste, Italy.
Kettleborough CA; LifeArc, Accelerator Building, Open Innovation Campus, Stevenage SG1 2FX, United Kingdom.
Baralle FE; Fondazione Italiana Fegato-Onlus, Bldg. Q, AREA Science Park, ss14, Km 163.5, Basovizza, 34149 Trieste, Italy.
Baralle M; International Centre for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34149 Trieste, Italy. Electronic address: .
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Źródło:
Neurobiology of disease [Neurobiol Dis] 2021 Dec; Vol. 160, pp. 105515. Date of Electronic Publication: 2021 Sep 24.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Amyotrophic Lateral Sclerosis/*drug therapy
DNA-Binding Proteins/*metabolism
Dopamine Antagonists/*therapeutic use
Drosophila Proteins/*metabolism
Protein Aggregation, Pathological/*drug therapy
Thioridazine/*therapeutic use
Amyotrophic Lateral Sclerosis/metabolism ; Amyotrophic Lateral Sclerosis/pathology ; Animals ; Autophagy/drug effects ; Cell Line ; Disease Models, Animal ; Dopamine Antagonists/pharmacology ; Drosophila ; Humans ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/pathology ; Thioridazine/pharmacology
Czasopismo naukowe
Tytuł:
The translocator protein ligands as mitochondrial functional modulators for the potential anti-Alzheimer agents.
Autorzy:
Kim T; Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology, Seoul, Republic of Korea.; Division of Bio-Medical Science and Technology, KIST School, Korea University of Science and Technology, Seoul, Republic of Korea.
Morshed MN; Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology, Seoul, Republic of Korea.; Division of Bio-Medical Science and Technology, KIST School, Korea University of Science and Technology, Seoul, Republic of Korea.; Center for Advanced Research in Sciences (CARS), University of Dhaka, Dhaka, Bangladesh.
Londhe AM; Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology, Seoul, Republic of Korea.; Division of Bio-Medical Science and Technology, KIST School, Korea University of Science and Technology, Seoul, Republic of Korea.
Lim JW; Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology, Seoul, Republic of Korea.; KHU-KIST Department of Converging Science and Technology, Kyung Hee University, Seoul, Republic of Korea.
Lee HE; Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology, Seoul, Republic of Korea.; Division of Bio-Medical Science and Technology, KIST School, Korea University of Science and Technology, Seoul, Republic of Korea.
Cho S; Department of Food Science and Technology, Pukyong National University, Pusan, Republic of Korea.
Cho SJ; New Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation (DGMIF), Daegu, Republic of Korea.
Hwang H; New Drug Development Center, Daegu-Gyeongbuk Medical Innovation Foundation (DGMIF), Daegu, Republic of Korea.
Lim SM; Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology, Seoul, Republic of Korea.; Division of Bio-Medical Science and Technology, KIST School, Korea University of Science and Technology, Seoul, Republic of Korea.
Lee JY; Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology, Seoul, Republic of Korea.; KHU-KIST Department of Converging Science and Technology, Kyung Hee University, Seoul, Republic of Korea.
Lee J; Department of Global Medical Science, Sungshin University, Seoul, Republic of Korea.
Pae AN; Convergence Research Center for Diagnosis, Treatment and Care System of Dementia, Korea Institute of Science and Technology, Seoul, Republic of Korea.; Division of Bio-Medical Science and Technology, KIST School, Korea University of Science and Technology, Seoul, Republic of Korea.; KHU-KIST Department of Converging Science and Technology, Kyung Hee University, Seoul, Republic of Korea.
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Źródło:
Journal of enzyme inhibition and medicinal chemistry [J Enzyme Inhib Med Chem] 2021 Dec; Vol. 36 (1), pp. 831-846.
Typ publikacji:
Journal Article
MeSH Terms:
Alzheimer Disease/*drug therapy
Mitochondria/*drug effects
Neuroprotective Agents/*pharmacology
Protein Aggregation, Pathological/*drug therapy
Small Molecule Libraries/*pharmacology
Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloid beta-Peptides/antagonists & inhibitors ; Amyloid beta-Peptides/metabolism ; Animals ; Cell Survival/drug effects ; Cells, Cultured ; Disease Models, Animal ; Drug Evaluation, Preclinical ; Humans ; Ligands ; Mice ; Mitochondria/metabolism ; Molecular Structure ; Neuroprotective Agents/chemical synthesis ; Neuroprotective Agents/chemistry ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/pathology ; Small Molecule Libraries/chemical synthesis ; Small Molecule Libraries/chemistry ; Transcriptional Regulator ERG/antagonists & inhibitors ; Transcriptional Regulator ERG/metabolism
Czasopismo naukowe
Tytuł:
Proximity proteomics of C9orf72 dipeptide repeat proteins identifies molecular chaperones as modifiers of poly-GA aggregation.
Autorzy:
Liu F; Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.; Department of Ophthalmology, The Second Hospital of Jilin University, Changchun, China.
Morderer D; Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Wren MC; Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Vettleson-Trutza SA; Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Wang Y; Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.; Department of Neurology, The First Affiliated Hospital of China Medical University, Shenyang, Liaoning, China.
Rabichow BE; Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Salemi MR; Proteomics Core, University of California Davis, Davis, CA, USA.
Phinney BS; Proteomics Core, University of California Davis, Davis, CA, USA.
Oskarsson B; Department of Neurology, Mayo Clinic, Jacksonville, FL, USA.
Dickson DW; Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA.
Rossoll W; Department of Neuroscience, Mayo Clinic, Jacksonville, FL, USA. .
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Źródło:
Acta neuropathologica communications [Acta Neuropathol Commun] 2022 Feb 14; Vol. 10 (1), pp. 22. Date of Electronic Publication: 2022 Feb 14.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
MeSH Terms:
Amyotrophic Lateral Sclerosis*
C9orf72 Protein*
Frontotemporal Dementia*
Protein Aggregation, Pathological*
Repetitive Sequences, Nucleic Acid*
Dipeptides ; HEK293 Cells ; Humans ; Molecular Chaperones ; Proteomics ; RNA
Czasopismo naukowe
Tytuł:
Neurotoxic or neuroprotective: Post-translational modifications of α-synuclein at the cross-roads of functions.
Autorzy:
Gadhavi J; Biological Engineering Discipline, Indian Institute of Technology Gandhinagar, Palaj, 382355, Gujarat, India.
Patel M; Biological Engineering Discipline, Indian Institute of Technology Gandhinagar, Palaj, 382355, Gujarat, India.
Bhatia D; Biological Engineering Discipline, Indian Institute of Technology Gandhinagar, Palaj, 382355, Gujarat, India; Center for Biomedical Engineering Discipline, Indian Institute of Technology Gandhinagar, Palaj, 382355, Gujarat, India.
Gupta S; Biological Engineering Discipline, Indian Institute of Technology Gandhinagar, Palaj, 382355, Gujarat, India; Center for Biomedical Engineering Discipline, Indian Institute of Technology Gandhinagar, Palaj, 382355, Gujarat, India. Electronic address: .
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Źródło:
Biochimie [Biochimie] 2022 Jan; Vol. 192, pp. 38-50. Date of Electronic Publication: 2021 Sep 25.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Protein Processing, Post-Translational*
Brain/*metabolism
Neuroprotective Agents/*metabolism
Neurotoxins/*metabolism
Parkinson Disease/*metabolism
Protein Aggregation, Pathological/*metabolism
alpha-Synuclein/*metabolism
Dopaminergic Neurons/metabolism ; Humans ; Lewy Bodies/genetics ; Lewy Bodies/metabolism ; Neurotoxins/genetics ; Parkinson Disease/genetics ; Protein Aggregation, Pathological/genetics ; alpha-Synuclein/genetics
Czasopismo naukowe
Tytuł:
The curious cases of nanoparticle induced amyloidosis during protein corona formation and anti-amyloidogenic nanomaterials: Paradox or prejudice?
Autorzy:
Randhawa S; Biotechnology Division, CSIR-Institute of Himalayan Bioresource Technology, Palampur (H.P.) 176061, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.
Abidi SMS; Biotechnology Division, CSIR-Institute of Himalayan Bioresource Technology, Palampur (H.P.) 176061, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.
Dar AI; Biotechnology Division, CSIR-Institute of Himalayan Bioresource Technology, Palampur (H.P.) 176061, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India.
Acharya A; Biotechnology Division, CSIR-Institute of Himalayan Bioresource Technology, Palampur (H.P.) 176061, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India. Electronic address: .
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Źródło:
International journal of biological macromolecules [Int J Biol Macromol] 2021 Dec 15; Vol. 193 (Pt A), pp. 1009-1020. Date of Electronic Publication: 2021 Oct 30.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Protein Aggregation, Pathological*
Protein Corona*/chemistry
Protein Corona*/metabolism
Alzheimer Disease/*metabolism
Amyloidosis/*metabolism
Nanoparticles/*chemistry
Nanostructures/*chemistry
Humans ; Particle Size ; Protein Binding
Czasopismo naukowe
Tytuł:
Diplazium esculentum (Retz.) Sw. reduces BACE-1 activities and amyloid peptides accumulation in Drosophila models of Alzheimer's disease.
Autorzy:
Kunkeaw T; Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.
Suttisansanee U; Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.
Trachootham D; Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.
Karinchai J; Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Meung, Chiang Mai, 50200, Thailand.
Chantong B; Department of Preclinical Science and Applied Animal Science, Faculty of Veterinary Science, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.
Potikanond S; Department of Pharmacology, Faculty of Medicine, Chiang Mai University, Meung, Chiang Mai, 50200, Thailand.
Inthachat W; Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand.
Pitchakarn P; Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Meung, Chiang Mai, 50200, Thailand.
Temviriyanukul P; Institute of Nutrition, Mahidol University, Salaya, Phuttamonthon, 73170, Nakhon Pathom, Thailand. .
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Źródło:
Scientific reports [Sci Rep] 2021 Dec 10; Vol. 11 (1), pp. 23796. Date of Electronic Publication: 2021 Dec 10.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Alzheimer Disease/*metabolism
Amyloid Precursor Protein Secretases/*metabolism
Amyloid beta-Peptides/*metabolism
Ferns/*chemistry
Plant Extracts/*pharmacology
Protein Aggregation, Pathological/*metabolism
Alzheimer Disease/drug therapy ; Alzheimer Disease/etiology ; Alzheimer Disease/pathology ; Animals ; Antioxidants/chemistry ; Antioxidants/pharmacology ; Behavior, Animal ; Biological Products ; Biomarkers ; Disease Models, Animal ; Drosophila ; Gene Expression ; Humans ; Peptide Fragments/metabolism ; Phytochemicals/chemistry ; Phytochemicals/pharmacology ; Plant Extracts/chemistry ; Protein Aggregates/drug effects ; Protein Aggregation, Pathological/drug therapy
Czasopismo naukowe
Tytuł:
Modulating α-Synuclein Liquid-Liquid Phase Separation.
Autorzy:
Sawner AS; Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.
Ray S; Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.
Yadav P; Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.
Mukherjee S; Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.
Panigrahi R; Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.
Poudyal M; Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.
Patel K; Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.
Ghosh D; Department of Chemistry and Applied Biosciences, ETH Zurich, Vladimir-Prelog-Weg 1-5/10, 8093 Zürich, Switzerland.
Kummerant E; Department of Chemistry and Applied Biosciences, ETH Zurich, Vladimir-Prelog-Weg 1-5/10, 8093 Zürich, Switzerland.
Kumar A; Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.
Riek R; Department of Chemistry and Applied Biosciences, ETH Zurich, Vladimir-Prelog-Weg 1-5/10, 8093 Zürich, Switzerland.
Maji SK; Department of Biosciences and Bioengineering, IIT Bombay, Powai, Mumbai 400076, India.
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Źródło:
Biochemistry [Biochemistry] 2021 Dec 07; Vol. 60 (48), pp. 3676-3696. Date of Electronic Publication: 2021 Aug 25.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Amyloid/*chemistry
Protein Aggregation, Pathological/*genetics
alpha-Synuclein/*chemistry
Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Amyloid/genetics ; Amyloid/ultrastructure ; Amyotrophic Lateral Sclerosis/genetics ; Amyotrophic Lateral Sclerosis/pathology ; Humans ; Hydrophobic and Hydrophilic Interactions ; Kinetics ; Parkinson Disease/genetics ; Parkinson Disease/pathology ; Phase Transition ; Protein Aggregation, Pathological/pathology ; alpha-Synuclein/genetics ; alpha-Synuclein/ultrastructure
Czasopismo naukowe
Tytuł:
(De)stabilization of Alpha-Synuclein Fibrillary Aggregation by Charged and Uncharged Surfactants.
Autorzy:
Loureiro JA; LEPABE, Department of Chemical Engineering, Faculty of Engineering of the University of Porto, 4200-465 Porto, Portugal.
Andrade S; LEPABE, Department of Chemical Engineering, Faculty of Engineering of the University of Porto, 4200-465 Porto, Portugal.
Goderis L; Faculty of Pharmaceutical Sciences, Ghent University, Sint-Pietersnieuwstraat 25, B-9000 Ghent, Belgium.
Gomez-Gutierrez R; Department of Neurology, The University of Texas Health Science Centre at Houston, Houston, TX 77030, USA.; Department of Cell Biology, University of Malaga, 29071 Malaga, Spain.
Soto C; Department of Neurology, The University of Texas Health Science Centre at Houston, Houston, TX 77030, USA.
Morales R; Department of Neurology, The University of Texas Health Science Centre at Houston, Houston, TX 77030, USA.; CIBQA, Universidad Bernardo O'Higgins, Santiago 1497, Chile.
Pereira MC; LEPABE, Department of Chemical Engineering, Faculty of Engineering of the University of Porto, 4200-465 Porto, Portugal.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Nov 19; Vol. 22 (22). Date of Electronic Publication: 2021 Nov 19.
Typ publikacji:
Journal Article
MeSH Terms:
Neurodegenerative Diseases/*drug therapy
Parkinson Disease/*drug therapy
Protein Aggregation, Pathological/*drug therapy
alpha-Synuclein/*genetics
Amyloid/antagonists & inhibitors ; Amyloid/genetics ; Cetrimonium/pharmacology ; Circular Dichroism ; Galactosides/pharmacology ; Humans ; Lewy Bodies/drug effects ; Lewy Bodies/ultrastructure ; Neurodegenerative Diseases/pathology ; Parkinson Disease/genetics ; Parkinson Disease/pathology ; Protein Aggregation, Pathological/genetics ; Protein Aggregation, Pathological/pathology ; Protein Conformation ; Protein Conformation, beta-Strand/genetics ; Protein Folding/drug effects ; Protein Structure, Secondary/drug effects ; Sodium Dodecyl Sulfate/pharmacology ; Spectroscopy, Fourier Transform Infrared ; alpha-Synuclein/antagonists & inhibitors
Czasopismo naukowe
Tytuł:
Mechanisms of amyloid proteins aggregation and their inhibition by antibodies, small molecule inhibitors, nano-particles and nano-bodies.
Autorzy:
Salahuddin P; DISC, Interdisciplinary Biotechnology Unit, A.M.U., Aligarh 202002, India.
Khan RH; Interdisciplinary Biotechnology Unit, A.M.U., Aligarh 202002, India. Electronic address: .
Furkan M; Interdisciplinary Biotechnology Unit, A.M.U., Aligarh 202002, India.
Uversky VN; Protein Research Group, Institute for Biological Instrumentation of the Russian Academy of Sciences, Institutskaya Str., 7, Pushchino, Moscow region 142290, Russia; Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA.
Islam Z; Qatar Biomedical Research Institute, Hamad Bin Khalifa University, Qatar Foundation, P.O Box 5825, Doha, Qatar.
Fatima MT; Department of Pharmaceutical Sciences, College of Pharmacy, QU Health, Qatar University, P.O. Box 2713, Doha, Qatar.
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Źródło:
International journal of biological macromolecules [Int J Biol Macromol] 2021 Sep 01; Vol. 186, pp. 580-590. Date of Electronic Publication: 2021 Jul 14.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Nanoparticles*
Protein Aggregates*
Protein Aggregation, Pathological*
Alzheimer Disease/*drug therapy
Amyloidogenic Proteins/*metabolism
Amyloidosis/*drug therapy
Single-Domain Antibodies/*pharmacology
Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Amyloidogenic Proteins/antagonists & inhibitors ; Amyloidosis/metabolism ; Amyloidosis/pathology ; Animals ; Humans ; Protein Conformation ; Protein Folding
Czasopismo naukowe
Tytuł:
Neurotoxicity of oligomers of phosphorylated Tau protein carrying tauopathy-associated mutation is inhibited by prion protein.
Autorzy:
Nieznanska H; Nencki Institute of Experimental Biology of Polish Academy of Sciences, 3 Pasteur Str., 02-093 Warsaw, Poland.
Boyko S; Nencki Institute of Experimental Biology of Polish Academy of Sciences, 3 Pasteur Str., 02-093 Warsaw, Poland.
Dec R; Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, 1 Pasteur Str., 02-093 Warsaw, Poland.
Redowicz MJ; Nencki Institute of Experimental Biology of Polish Academy of Sciences, 3 Pasteur Str., 02-093 Warsaw, Poland.
Dzwolak W; Faculty of Chemistry, Biological and Chemical Research Centre, University of Warsaw, 1 Pasteur Str., 02-093 Warsaw, Poland.
Nieznanski K; Nencki Institute of Experimental Biology of Polish Academy of Sciences, 3 Pasteur Str., 02-093 Warsaw, Poland. Electronic address: .
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Źródło:
Biochimica et biophysica acta. Molecular basis of disease [Biochim Biophys Acta Mol Basis Dis] 2021 Nov 01; Vol. 1867 (11), pp. 166209. Date of Electronic Publication: 2021 Jul 08.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Neurons/*pathology
Prion Proteins/*metabolism
Protein Aggregation, Pathological/*pathology
Tauopathies/*pathology
tau Proteins/*metabolism
Animals ; Cells, Cultured ; Hippocampus/cytology ; Hippocampus/pathology ; Humans ; Phosphorylation ; Primary Cell Culture ; Prion Proteins/genetics ; Prion Proteins/isolation & purification ; Protein Aggregation, Pathological/genetics ; Protein Binding ; Rats ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Tauopathies/genetics ; tau Proteins/genetics ; tau Proteins/isolation & purification
Czasopismo naukowe
Tytuł:
Protein Aggregation and Disaggregation in Cells and Development.
Autorzy:
Fassler JS; Department of Biology, University of Iowa, Iowa City, IA 52242, United States. Electronic address: .
Skuodas S; Department of Biology, University of Iowa, Iowa City, IA 52242, United States. Electronic address: https:.
Weeks DL; Department of Biochemistry, University of Iowa, Iowa City, IA 52242, United States.
Phillips BT; Department of Biology, University of Iowa, Iowa City, IA 52242, United States. Electronic address: https:.
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Źródło:
Journal of molecular biology [J Mol Biol] 2021 Oct 15; Vol. 433 (21), pp. 167215. Date of Electronic Publication: 2021 Aug 24.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Review
MeSH Terms:
Protein Processing, Post-Translational*
Embryonic Development/*genetics
Gametogenesis/*genetics
Neurodegenerative Diseases/*genetics
Protein Aggregates/*genetics
Protein Aggregation, Pathological/*genetics
ATP-Binding Cassette Transporters/genetics ; ATP-Binding Cassette Transporters/metabolism ; Animals ; Cell Differentiation ; Cell Proliferation ; Eukaryotic Cells/cytology ; Eukaryotic Cells/metabolism ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Humans ; Memory/physiology ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Nuclear Pore Complex Proteins/genetics ; Nuclear Pore Complex Proteins/metabolism ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/pathology ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Signal Transduction
Czasopismo naukowe
Tytuł:
Viral Induced Protein Aggregation: A Mechanism of Immune Evasion.
Autorzy:
Muscolino E; Leibniz Institute for Experimental Virology (HPI), 20251 Hamburg, Germany.; Molecular Virology Group, Department of Experimental and Health Sciences, Universitat Pompeu Fabra, 08003 Barcelona, Spain.
Luoto LM; Leibniz Institute for Experimental Virology (HPI), 20251 Hamburg, Germany.
Brune W; Leibniz Institute for Experimental Virology (HPI), 20251 Hamburg, Germany.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Sep 06; Vol. 22 (17). Date of Electronic Publication: 2021 Sep 06.
Typ publikacji:
Journal Article; Review
MeSH Terms:
Protein Aggregates*
Immune Evasion/*immunology
Protein Aggregation, Pathological/*immunology
Virus Diseases/*immunology
Viruses/*immunology
Herpesviridae/immunology ; Herpesviridae/physiology ; Herpesviridae Infections/immunology ; Herpesviridae Infections/metabolism ; Herpesviridae Infections/virology ; Host-Pathogen Interactions/immunology ; Humans ; Protein Aggregation, Pathological/metabolism ; Protein Aggregation, Pathological/virology ; Ribonucleotide Reductases/immunology ; Ribonucleotide Reductases/metabolism ; Virus Diseases/metabolism ; Virus Diseases/virology
Czasopismo naukowe
Tytuł:
Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration.
Autorzy:
Ziaunys M; Institute of Biotechnology, Life Sciences Centre, Vilnius University, 10257 Vilnius, Lithuania.
Sakalauskas A; Institute of Biotechnology, Life Sciences Centre, Vilnius University, 10257 Vilnius, Lithuania.
Mikalauskaite K; Institute of Biotechnology, Life Sciences Centre, Vilnius University, 10257 Vilnius, Lithuania.
Smirnovas V; Institute of Biotechnology, Life Sciences Centre, Vilnius University, 10257 Vilnius, Lithuania.
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Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Nov 17; Vol. 22 (22). Date of Electronic Publication: 2021 Nov 17.
Typ publikacji:
Journal Article
MeSH Terms:
Protein Aggregates*
Protein Aggregation, Pathological*
Amyloid/*chemistry
alpha-Synuclein/*chemistry
Amyloid/metabolism ; In Vitro Techniques/methods ; Kinetics ; Osmolar Concentration ; Parkinson Disease/metabolism ; Protein Binding ; Protein Structure, Secondary ; alpha-Synuclein/metabolism
Czasopismo naukowe

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