catechin and Protein Aggregation, Pathological

catechin has been researched along with Protein Aggregation, Pathological in 20 studies

Research

Studies (20)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's18 (90.00)24.3611
2020's2 (10.00)2.80

Authors

AuthorsStudies
Ding, L; Ding, Y; Teng, Y; Zhao, J; Zhou, P1
Bolakhrif, N; Buell, AK; Haas, R; Peduzzo, A; Sternke-Hoffmann, R1
Cima-Omori, MS; Dominguez-Meijide, A; Griesinger, C; Ibáñez de Opakua, A; König, A; Leonov, A; Outeiro, TF; Ryazanov, S; Vasili, E; Zweckstetter, M1
de Moraes, MC; Fernandes, L; Foguel, D; Grimster, NP; Kelly, JW; Magalhães, AV; Moraes, N; Palhano, FL; Romão, L; Sagrillo, FS1
Gandhi, S; Gour, S; Goyal, P; Harsolia, RS; Kumar, V; Pandey, J; Peter, OS; Yadav, JK1
Chan, S; Deora, GS; Dighe, SN; Kantham, S; Khabbazi, S; McColl, G; Miles, JA; Parat, MO; Ross, BP; Veliyath, SK1
Fleau, C; Guéroux, M; Laguerre, M; Pianet, I; Slozeck, M1
Cox, SJ; Ivanova, M; Kinoshita, M; Lee, YH; Lin, Y; Ramamoorthy, A; Sahoo, BR1
Chen, Z; Jiang, Z; Li, Y; Liu, L; Lu, Z; Qing, H; Yang, Q; Zhang, L; Zhang, X1
Claus, S; Fändrich, M; Puscalau-Girtu, I; Scheller, JS1
Airoldi, C; Bonanomi, M; Colombo, L; Lompo, A; Messa, M; Regonesi, ME; Salmona, M; Sironi, E1
Bieschke, J; Diamond, MI; Sharma, A; Wanker, EE; Wobst, HJ1
Cao, N; Feng, S; Zeng, CM; Zhang, YJ1
Bano, B; Bhat, SA; Bhat, WF1
Bongen, P; Brener, O; Demuth, HU; Dunkelmann, T; Funke, SA; Gremer, L; Hoyer, W; Janssen, A; Jürgens, D; Kadish, I; Kutzsche, J; Langen, KJ; Mirecka, EA; Nagel-Steger, L; Oesterhelt, F; Pietruszka, J; Rudolph, S; Tusche, M; van Groen, T; Willbold, D; Willuweit, A1
Akaji, K; Kashiwada, Y; Kawashima, H; Kobayashi, N; Kuwabara, K; Mikawa, S; Nakajima, H; Nishitsuji, K; Saito, H; Sakashita, N; Uchimura, K1
Kang, H; Li, B; Liu, S; Meng, XY; Zhao, L; Zhou, R1
Abdallah, HM; Alshali, KZ; Banjar, ZM; El-Bassossy, H; El-Halawany, AM; Mohamed, GA1
Ge, ZZ; Li, CM; Nie, RZ; Peng, JM; Zhu, W1
Batra, R; Chowdhury, PK; Gautam, S; Karmakar, S; Kundu, B; Pradhan, P; Sharma, P; Singh, J1

Other Studies

20 other study(ies) available for catechin and Protein Aggregation, Pathological

ArticleYear
Complex of EGCG with Cu(II) Suppresses Amyloid Aggregation and Cu(II)-Induced Cytotoxicity of α-Synuclein.
    Molecules (Basel, Switzerland), 2019, Aug-14, Volume: 24, Issue:16

    Topics: alpha-Synuclein; Amyloidogenic Proteins; Animals; Catechin; Cell Line; Copper; Neuroprotective Agents; Nuclear Magnetic Resonance, Biomolecular; Oxidative Stress; Parkinson Disease; Protein Aggregates; Protein Aggregation, Pathological; Rats; Reactive Oxygen Species

2019
The Aggregation Conditions Define Whether EGCG is an Inhibitor or Enhancer of
    International journal of molecular sciences, 2020, Mar-14, Volume: 21, Issue:6

    Topics: alpha-Synuclein; Amyloid; Catechin; Humans; Parkinson Disease; Protein Aggregates; Protein Aggregation, Pathological

2020
Effects of pharmacological modulators of α-synuclein and tau aggregation and internalization.
    Scientific reports, 2020, 07-30, Volume: 10, Issue:1

    Topics: alpha-Synuclein; Alzheimer Disease; Benzodioxoles; Benzopyrans; Brain; Catechin; Cells, Cultured; Humans; Hydrazones; Lewy Bodies; Molecular Targeted Therapy; Neurofibrillary Tangles; Parkinson Disease; Protein Aggregates; Protein Aggregation, Pathological; Pyrazoles; tau Proteins

2020
An ortho-Iminoquinone Compound Reacts with Lysine Inhibiting Aggregation while Remodeling Mature Amyloid Fibrils.
    ACS chemical neuroscience, 2017, 08-16, Volume: 8, Issue:8

    Topics: alpha-Synuclein; Amyloid beta-Peptides; Animals; Catechin; Cell Survival; Cells, Cultured; Chickens; Dopaminergic Neurons; HEK293 Cells; Humans; Lysine; Methionine; Mice; Micrococcus luteus; Microtubule-Associated Proteins; Muramidase; Neuroprotective Agents; Oxidation-Reduction; Peptide Fragments; Protein Aggregation, Pathological; Quinones; Tyrosine 3-Monooxygenase

2017
Effect of Green Tea Polyphenol Epigallocatechin-3-gallate on the Aggregation of αA(66-80) Peptide, a Major Fragment of αA-crystallin Involved in Cataract Development.
    Current eye research, 2017, Volume: 42, Issue:10

    Topics: alpha-Crystallin A Chain; Amino Acid Sequence; Amyloid; Antioxidants; Cataract; Catechin; Dose-Response Relationship, Drug; Humans; Microscopy, Electron, Transmission; Microscopy, Fluorescence; Molecular Sequence Data; Peptide Fragments; Protein Aggregation, Pathological; Tea

2017
Effect of the Biphenyl Neolignan Honokiol on Aβ
    ACS chemical neuroscience, 2017, 09-20, Volume: 8, Issue:9

    Topics: Amyloid beta-Peptides; Animals; Biphenyl Compounds; Caenorhabditis elegans; Catechin; Chelating Agents; Cholinesterase Inhibitors; Drug Stability; Free Radical Scavengers; Humans; Iron; Lignans; Molecular Docking Simulation; Molecular Structure; Neuroprotective Agents; Paralysis; Peptide Fragments; Picrates; Protein Aggregation, Pathological; Protein Multimerization; Resveratrol; Stilbenes

2017
Epigallocatechin 3-Gallate as an Inhibitor of Tau Phosphorylation and Aggregation: A Molecular and Structural Insight.
    The journal of prevention of Alzheimer's disease, 2017, Volume: 4, Issue:4

    Topics: Catechin; Humans; Models, Molecular; Neuroprotective Agents; Nuclear Magnetic Resonance, Biomolecular; Phosphorylation; Protein Aggregation, Pathological; Protein Conformation; tau Proteins

2017
Zinc boosts EGCG's hIAPP amyloid Inhibition both in solution and membrane.
    Biochimica et biophysica acta. Proteins and proteomics, 2019, Volume: 1867, Issue:5

    Topics: Amyloid; Animals; Catechin; Cell Line, Tumor; Cell Membrane; Cell Survival; Drug Synergism; Humans; Islet Amyloid Polypeptide; Protein Aggregation, Pathological; Rats; Solutions; Zinc

2019
"Cell-addictive" dual-target traceable nanodrug for Parkinson's disease treatment via flotillins pathway.
    Theranostics, 2018, Volume: 8, Issue:19

    Topics: alpha-Synuclein; Animals; Animals, Genetically Modified; Catechin; Cell Line; Disease Models, Animal; Dopaminergic Neurons; Drug Carriers; Humans; Membrane Proteins; Mice; Molecular Targeted Therapy; Nanoparticles; Neuroprotective Agents; Parkinson Disease; Protein Aggregation, Pathological; Treatment Outcome

2018
Cell assay for the identification of amyloid inhibitors in systemic AA amyloidosis.
    Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2019, Volume: 26, Issue:1

    Topics: Amyloidosis; Animals; Biological Assay; Catechin; Cell Line, Tumor; Humans; Mice; Models, Biological; Protein Aggregation, Pathological; Serum Amyloid A Protein

2019
Natural compounds against neurodegenerative diseases: molecular characterization of the interaction of catechins from green tea with Aβ1-42, PrP106-126, and ataxin-3 oligomers.
    Chemistry (Weinheim an der Bergstrasse, Germany), 2014, Oct-13, Volume: 20, Issue:42

    Topics: Amino Acid Sequence; Amyloid beta-Peptides; Ataxin-3; Biological Products; Catechin; Flavonoids; Humans; Molecular Sequence Data; Nerve Tissue Proteins; Neurodegenerative Diseases; Nuclear Magnetic Resonance, Biomolecular; Nuclear Proteins; Peptide Fragments; Prions; Protein Aggregation, Pathological; Repressor Proteins; Tea

2014
The green tea polyphenol (-)-epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios.
    FEBS letters, 2015, Jan-02, Volume: 589, Issue:1

    Topics: Animals; Catechin; Humans; PC12 Cells; Protein Aggregation, Pathological; Rats; tau Proteins; Tea

2015
Quinopeptide formation associated with the disruptive effect of epigallocatechin-gallate on lysozyme fibrils.
    International journal of biological macromolecules, 2015, Volume: 78

    Topics: Amyloid; Animals; Catechin; Molecular Structure; Muramidase; Peptides; Polyphenols; Protein Aggregation, Pathological

2015
Evaluation of polyphenols as possible therapeutics for amyloidoses: Comparative analysis of Kaempferol and Catechin.
    International journal of biological macromolecules, 2015, Volume: 81

    Topics: Amyloid; Amyloidosis; Animals; Brain; Catechin; Circular Dichroism; Cystatins; Goats; Hydrogen-Ion Concentration; Kaempferols; Polyphenols; Protein Aggregation, Pathological; Protein Structure, Secondary; Spectrometry, Fluorescence

2015
QIAD assay for quantitating a compound's efficacy in elimination of toxic Aβ oligomers.
    Scientific reports, 2015, Sep-23, Volume: 5

    Topics: Alzheimer Disease; Amyloid beta-Peptides; Animals; Carrier Proteins; Catechin; Disease Models, Animal; Ferredoxin-NADP Reductase; Humans; Inositol; Mice; Mice, Inbred C57BL; Mice, Inbred DBA; Mice, Transgenic; Oligopeptides; Protein Aggregation, Pathological; Taurine

2015
The polyphenol (-)-epigallocatechin-3-gallate prevents apoA-IIowa amyloidosis in vitro and protects human embryonic kidney 293 cells against amyloid cytotoxicity.
    Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2016, Volume: 23, Issue:1

    Topics: Amyloid; Amyloidosis; Apolipoprotein A-I; Catechin; Cell Survival; Drug Evaluation, Preclinical; HEK293 Cells; Humans; Protein Aggregation, Pathological; Protein Structure, Secondary; Reactive Oxygen Species

2016
EGCG in Green Tea Induces Aggregation of HMGB1 Protein through Large Conformational Changes with Polarized Charge Redistribution.
    Scientific reports, 2016, Feb-22, Volume: 6

    Topics: Binding Sites; Catechin; Cysteine; HMGB1 Protein; Humans; Molecular Conformation; Molecular Dynamics Simulation; Molecular Structure; Protein Aggregates; Protein Aggregation, Pathological; Protein Binding; Protein Domains; Protein Multimerization; Static Electricity; Tea

2016
Phenolics from Garcinia mangostana Inhibit Advanced Glycation Endproducts Formation: Effect on Amadori Products, Cross-Linked Structures and Protein Thiols.
    Molecules (Basel, Switzerland), 2016, Feb-22, Volume: 21, Issue:2

    Topics: Animals; Benzophenones; Catechin; Cattle; Flavonoids; Garcinia mangostana; Glucose; Glucosides; Glycation End Products, Advanced; Plant Extracts; Protein Aggregation, Pathological; Serum Albumin, Bovine; Sulfhydryl Compounds

2016
A-type dimeric epigallocatechin-3-gallate (EGCG) is a more potent inhibitor against the formation of insulin amyloid fibril than EGCG monomer.
    Biochimie, 2016, Volume: 125

    Topics: Amyloid; Animals; Catechin; Cattle; Insulin; Protein Aggregation, Pathological

2016
Polyphenols in combination with β-cyclodextrin can inhibit and disaggregate α-synuclein amyloids under cell mimicking conditions: A promising therapeutic alternative.
    Biochimica et biophysica acta. Proteins and proteomics, 2017, Volume: 1865, Issue:5

    Topics: alpha-Synuclein; Amyloid; Amyloidogenic Proteins; Animals; beta-Cyclodextrins; Catechin; Cell Line; Cell Survival; Circular Dichroism; Curcumin; Humans; Mice; Parkinson Disease; Polyphenols; Protein Aggregation, Pathological

2017