tyrosine and alpha-synuclein

tyrosine has been researched along with alpha-synuclein in 94 studies

Research

Studies (94)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's44 (46.81)29.6817
2010's37 (39.36)24.3611
2020's13 (13.83)2.80

Authors

AuthorsStudies
Chen, Q; Giasson, BI; Ischiropoulos, H; Lee, VM; Souza, JM1
Chen, Q; Duda, JE; Giasson, BI; Hurtig, HI; Ischiropoulos, H; Lee, VM; Murray, IV; Souza, JM; Trojanowski, JQ1
Chen, Q; Duda, JE; Giasson, BI; Gollomp, SM; Gur, TL; Hurtig, HI; Ischiropoulos, H; Lee, VM; Stern, MB; Trojanowski, JQ1
Nakamura, S; Nakamura, T; Takahashi, T; Yamashita, H1
Halliwell, B; Hyun, D; Jenner, P; Lee, M1
Chen, Q; Djaldatti, R; Giasson, BI; Ischiropoulos, H; Jackson-Lewis, V; Lee, VM; Przedborski, S; Souza, JM; Vila, M; Vukosavic, S1
Boveris, AD; Cadenas, E; Poderoso, JJ; Riobó, NA; Schöpfer, FJ1
Ahn, BH; Chang, JS; Choi, JY; Chung, KC; Hahn, SJ; Jo, YH; Kim, MS; Kim, SY; Kwon, TK; Lee, MY; Lee, YH; Min, DS; Rhim, H; Sung, YM; Wolozin, B; Yoon, SH1
García Yébenes, J; Gómez-Tortosa, E; Gonzalo, I; Hyman, BT; Newell, K; Vonsattel, P1
Nagano, Y; Nakamura, S; Nakamura, T; Takahashi, T; Yamashita, H1
Avraham, H; Avraham, S; Matsumoto, M; Nagano, Y; Nakamura, S; Nakamura, T; Takahashi, T; Yamashita, H1
Drazba, J; Gaivin, R; Gonzalez-Cabrera, P; McCune, DF; Papay, R; Perez, DM; Ross, SA; Yun, J; Zuscik, MJ1
Biere, AL; Carpenter, JF; Chi, EY; Citron, M; Garzon-Rodriguez, W; Kendrick, BS; Krishnan, S; Li, C; Narhi, LO; Randolph, TW; Wood, SJ; Wypych, J1
Kang, JH; Kim, KS1
Fink, AL; Uversky, VN; Yamin, G1
Giasson, BI; Ischiropoulos, H; Lee, VM; Norris, EH1
Andrekopoulos, C; Joseph, J; Kalivendi, S; Kalyanaraman, B; Zhang, H1
Freed, CR; Zhou, W1
Bennett, JP; Borland, MK; Keeney, PM; Parker, WD; Trimmer, PA1
Fink, AL; Han, S; Kaylor, J; Rajamani, S; Zhou, F; Zhu, M1
Darabie, AA; Fraser, PE; Han, K; Jo, E; McLaurin, J; Tandon, A1
Giasson, BI; Hodara, R; Ischiropoulos, H; Lee, VM; Lynch, DR; Mishizen-Eberz, AJ; Norris, EH1
Olteanu, A; Pielak, GJ1
Doniach, S; Fink, AL; Karymov, MA; Lyubchenko, YL; Millett, IS; Munishkina, LA; Uversky, VN; Yamin, G1
Cribb, AE; Donaldson, MT; Dybdal, N; McFarlane, D; Miller, L1
Giasson, BI; Hodara, R; Ischiropoulos, H; Lee, VM; Norris, EH; Trojanowski, JQ; Xu, S1
Giasson, BI; Hodara, R; Ischiropoulos, H; Lee, VM; Lynch, DR; Mishizen-Eberz, AJ; Norris, EH; Trojanowski, JQ1
Akaike, A; Hayashi, K; Inden, M; Kitamura, Y; Kondo, J; Nishimura, K; Shimohama, S; Sugimoto, H; Takata, K; Taniguchi, T; Tsuchiya, D; Yanagida, T; Yanagisawa, D1
Bodner, N; Edridge, S; Fink, AL; Hong, DP; Kaylor, J; Yamin, G1
Champy, P; Duyckaerts, C; Féger, J; Hirsch, EC; Höglinger, GU; Khondiker, ME; Lannuzel, A; Lombes, A; Medja, F; Michel, PP; Oertel, WH; Prigent, A; Ruberg, M1
Bodner, N; Dusa, A; Edridge, S; Fink, AL; Hong, DP; Kaylor, J1
Dalfó, E; Ferrer, I; Martinez, A; Muntané, G1
Rubbo, H; Trostchansky, A1
Gray, HB; Kozak, JJ; Lai, BT; Lee, JC; Winkler, JR1
Bergantino, E; Bisaglia, M; Bubacco, L; Mammi, S; Samorì, B; Tessari, I; Valle, F1
Rao, KS1
Barry, CH; Fink, AL; Ulrih, NP1
Emmanouilidou, E; Stefanis, L; Vekrellis, K1
Lutz, EA; Pielak, GJ; Ruf, RA; Zigoneanu, IG1
Behr, GA; da Rocha, RF; de Oliveira, MR; Hoff, ML; Moreira, JC; Oliveira, MW1
Da Rocha, RF; De Oliveira, MR; Moreira, JC; Oliveira, MW1
Fink, AL; Meng, X; Munishkina, LA; Uversky, VN1
Li, C; Lutz, EA; Pielak, GJ; Ruf, RA; Slade, KM; Wang, GF1
Andersen, JK; Danielson, SR; Gibson, BW; Held, JM; Oo, M; Schilling, B1
Chen, L; Feany, MB; Hyman, BT; McLean, PJ; Negro, A; Periquet, M; Wang, X1
Bing, G; Cass, WA; Choi, DY; Gash, DM; Hunter, RL; Kim, HC; Liu, M; Pandya, JD; Sullivan, PG1
Graham, DR; Sidhu, A1
He, R; Liu, Y1
Alerte, TN; Daubner, SC; Di Monte, DA; Friedrich, EE; Hong, CS; Lou, H; Mader, SA; Marcus, BS; McCormack, AL; Montoya, SE; Pedersen, CJ; Peng, X; Perez, RG; Wang, J; Wu, J1
Andreoni, S; Begni, B; Brighina, L; Difrancesco, JC; Ferrarese, C; Galbussera, A; Piazza, F; Piolti, R; Prigione, A1
Gabryelak, T; Malachowska, M; Milowska, K1
Fantini, J; Yahi, N1
Dunn, JM; Rhoades, E; Sevcsik, E; Trexler, AJ1
da Rocha, RF; de Oliveira, MR; Moreira, JC; Schnorr, CE1
He, R; Liu, Y; Qiang, M; Wei, Y1
Daian, D; Dodiya, HB; Jaglin, JA; Keshavarzian, A; Kordower, JH; Mutlu, E; Shannon, KM1
Dodiya, HB; Estes, JD; Forsyth, CB; Jaglin, JA; Keshavarzian, A; Kordower, JH; Shaikh, M; Shannon, KM; Voigt, RM1
Butterfield, S; Cui, J; Dikiy, I; Eliezer, D; Fauvet, B; Hejjaoui, M; Lashuel, HA; Olschewski, D; Prudent, M; Vercruysse, F; Zhang, Y1
Cernocká, H; Kurzątkowska, K; Ostatná, V; Paleček, E1
Engelborghs, Y; Kluba, M; Meuvis, J; Schreurs, S1
Borsarelli, CD; Falomir-Lockhart, LJ; Fauerbach, JA; Hsiao, HH; Jares-Erijman, EA; Jovin, TM; Ostatná, V; Paleček, E; Urlaub, H1
Choi, HS; Jang, A; Kim, YM; Lashuel, H; Liew, H; Suh, YH1
Fauvet, B; Girault, HH; Lashuel, HA; Lu, Y; Prudent, M1
Chacón, J; Fernández, E; García-Moreno, JM; Martín de Pablos, A1
Bhat, R; Jain, MK1
Dyrnesli, H; Ferapontova, EE; Lopes, P; Lorenzen, N; Otzen, D1
Cai, Z; Chen, LL; Chua, KK; Li, M; Liu, LF; Luan, H; Meng, N; Mok, VC; Song, JX; Tang, Z; Xie, LX1
Bekei, B; Binolfi, A; Kosten, J; Selenko, P; Stuiver, M; Theillet, FX; van Rossum, M; Verzini, S1
Pirc, K; Pogačnik, L; Poklar-Ulrih, N; Škarabot, M; Žerovnik, E1
Jorge, CD; Maçanita, AL; Santos, H; Saraiva, MA1
Brichtová, E; Niederhafner, P; Šafařík, M; Šebestík, J1
Chen, M; Du, T; Duan, C; Gao, G; Liu, J; Wang, Y; Yang, H1
Braus, GH; Kleinknecht, A; Lázaro, DF; Outeiro, TF; Pinho, R; Popova, B; Valerius, O1
Dempsey, RJ; Kaimal, B; Kim, T; Lyons, K; Mehta, SL; Vemuganti, R1
Abdul-Sada, A; Al-Hilaly, YK; Biasetti, L; Blakeman, BJ; Pollack, SJ; Serpell, LC; Thorpe, JR; Xue, WF; Zibaee, S1
Buell, AK; Gremer, L; Groß, L; Hoyer, W; Shaykhalishahi, H; Stoldt, M; Willbold, D; Wördehoff, MM1
Chiki, A; De Genst, E; Di Trani, J; Dobson, CM; El Turk, F; Fauvet, B; Guilliams, T; Hejjaoui, M; Lashuel, HA; Mittermaier, A; Vendruscolo, M1
Cordaro, M; Crupi, R; Cuzzocrea, S; D'Amico, R; Di Paola, R; Gugliandolo, E; Impellizzeri, D; Peritore, AF; Siracusa, R1
Daiber, A; Delp, J; Gerding, HR; Hammler, D; Karreman, C; Leist, M; Mex, M; Schildknecht, S1
Abou-Zied, OK; Akhtari, K; Aziz, FM; Falahati, M; Mustafa, TA; Salihi, A; Shahpasand, K; Tahaei Gilan, SS; Yahya Rayat, D1
Abeyawardhane, DL; Curry, AM; Forney, AK; Lucas, HR; Roberts, JW1
Abdesselem, H; Attems, J; El-Agnaf, OMA; Erskine, D; Fayyad, M; Ghanem, SS; Lamprokostopoulou, A; Majbour, NK; Morris, CM; Sudhakaran, IP; Vaikath, NN; Vekrellis, K1
Buratti, FA; Carloni, P; Fernandez, CO; Palomino-Hernandez, O; Rossetti, G; Sacco, PS1
Belsom, A; Bieschke, J; Binolfi, A; Rappsilber, J; Selenko, P; Shah, M; Theillet, FX; Verzini, S; Wanker, EE1
Eliezer, D; Pan, B; Park, JH; Petersson, EJ; Ramlall, T; Rhoades, E1
Hegemann, JD; Liu, L; Long, T; Quan, J; Tao, Y; Tian, H; Uesugi, M; Wang, H; Yao, W; Zhang, W; Zheng, J1
Choudhary, S; Hosur, RV; Paithankar, H; Rane, AR1
Bahri, MA; Becker, G; Bezard, E; Caruso, M; Citron, M; De Wolf, C; Deprez, T; Downey, P; Frequin, JM; Freyssin, A; Garraux, G; Gillent, E; Hustadt, F; Jacquin, L; Lemaire, C; Luxen, A; Mairet-Coello, G; Michel, A; Plenevaux, A1
Hosokawa, M; Irie, K; Iwasaki, Y; Mishima, K; Sano, K; Satoh, K; Yamashita, Y1
Medvedeva, MV; Muronetz, VI; Pozdyshev, DV; Sevostyanova, IA1
Amstrup, SK; Bjerrum, MJ; Christiansen, G; Costeira-Paulo, J; Davies, MJ; Grønnemose, AL; Ilag, LL; Jørgensen, TJD; Landreh, M; Marklund, EG; Møller, IM; Nielsen, J; Österlund, N; Otzen, DE; Pedersen, JN; Pedersen, JS; Rao, RSP; Sahin, C; Tiwari, MK; Østerlund, EC1
Al-Hilaly, YK; Biasetti, L; Burra, G; Harrington, CR; Khanom, T; Maina, MB; Marshall, K; Mengham, K; Oakley, S; Serpell, LC; Wischik, CM1
Ayaki, T; Chiba, S; Hirai, H; Hirotsune, S; Ishida, R; Jin, M; Komai, S; Konno, A; Matsumoto, S; Nakajima, H; Taguchi, T; Takahashi, R; Takao, T; Togawa, N; Yamakado, H1
Basso, E; Füchtbauer, A; Füchtbauer, EM; Jensen, PH; Lassen, LB; Moos, T; Outeiro, TF; Thomsen, MS1

Reviews

2 review(s) available for tyrosine and alpha-synuclein

ArticleYear
Lipid nitration and formation of lipid-protein adducts: biological insights.
    Amino acids, 2007, Volume: 32, Issue:4

    Topics: alpha-Synuclein; Humans; Lipid Metabolism; Lipids; Lipoproteins, LDL; Nitrates; Oxidative Stress; Proteins; Reactive Nitrogen Species; Tyrosine

2007
Potential Effect of Post-Transcriptional Substitutions of Tyrosine for Cysteine Residues on Transformation of Amyloidogenic Proteins.
    Biochemistry. Biokhimiia, 2022, Volume: 87, Issue:2

    Topics: alpha-Synuclein; Amyloidogenic Proteins; Codon; Cysteine; Escherichia coli; Humans; Tyrosine

2022

Other Studies

92 other study(ies) available for tyrosine and alpha-synuclein

ArticleYear
Dityrosine cross-linking promotes formation of stable alpha -synuclein polymers. Implication of nitrative and oxidative stress in the pathogenesis of neurodegenerative synucleinopathies.
    The Journal of biological chemistry, 2000, Jun-16, Volume: 275, Issue:24

    Topics: alpha-Synuclein; Electrophoresis, Polyacrylamide Gel; Humans; Nerve Tissue Proteins; Neurodegenerative Diseases; Nitrates; Oxidative Stress; Polymers; Recombinant Proteins; Synucleins; Tyrosine

2000
Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions.
    Science (New York, N.Y.), 2000, Nov-03, Volume: 290, Issue:5493

    Topics: alpha-Synuclein; Alzheimer Disease; Antibodies, Monoclonal; Blotting, Western; Brain; Brain Chemistry; Enzyme-Linked Immunosorbent Assay; Fluorescent Antibody Technique; Humans; Immunohistochemistry; Lewy Bodies; Lewy Body Disease; Microscopy, Immunoelectron; Multiple System Atrophy; Nerve Tissue Proteins; Neurodegenerative Diseases; Neurons; Oxidative Stress; Parkinson Disease; Synucleins; Tyrosine

2000
Widespread nitration of pathological inclusions in neurodegenerative synucleinopathies.
    The American journal of pathology, 2000, Volume: 157, Issue:5

    Topics: Adult; Aged; Aged, 80 and over; alpha-Synuclein; Antibodies; Blotting, Western; Brain Diseases; Female; Humans; Immunohistochemistry; Inclusion Bodies; Lewy Bodies; Male; Middle Aged; Nerve Tissue Proteins; Neurodegenerative Diseases; Neuroglia; Nitrates; Synucleins; Tissue Distribution; Tyrosine

2000
Activated Fyn phosphorylates alpha-synuclein at tyrosine residue 125.
    Biochemical and biophysical research communications, 2001, Feb-02, Volume: 280, Issue:4

    Topics: alpha-Synuclein; Animals; Blotting, Northern; Brain; Central Nervous System; COS Cells; Cyclin-Dependent Kinase 5; Cyclin-Dependent Kinases; DNA Mutational Analysis; DNA, Complementary; Enzyme Activation; Focal Adhesion Kinase 1; Focal Adhesion Kinase 2; Focal Adhesion Protein-Tyrosine Kinases; Glutathione Transferase; Humans; Microscopy, Confocal; Microscopy, Fluorescence; Mitogen-Activated Protein Kinase 3; Mitogen-Activated Protein Kinase 9; Mitogen-Activated Protein Kinases; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Neurons; Phosphorylation; Precipitin Tests; Protein Kinase C; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-fyn; Recombinant Fusion Proteins; Signal Transduction; src-Family Kinases; Synucleins; Time Factors; Tissue Distribution; Tyrosine

2001
Effect of the overexpression of wild-type or mutant alpha-synuclein on cell susceptibility to insult.
    Journal of neurochemistry, 2001, Volume: 76, Issue:4

    Topics: 1-Methyl-4-phenylpyridinium; Aldehydes; alpha-Synuclein; Cell Division; Cell Line; Cell Survival; Clone Cells; Culture Media, Serum-Free; Enzyme Inhibitors; Gene Expression; Glutathione; Guanine; Humans; Hydrogen Peroxide; Ketones; Lipid Peroxidation; Mitochondria; Mutation; Nerve Tissue Proteins; Neuroblastoma; Oxidants; Oxidative Stress; Parkinsonian Disorders; Synucleins; Teratocarcinoma; Transfection; Tyrosine

2001
Oxidative post-translational modifications of alpha-synuclein in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease.
    Journal of neurochemistry, 2001, Volume: 76, Issue:2

    Topics: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine; alpha-Synuclein; Animals; beta-Synuclein; Cell Line; Corpus Striatum; Disease Models, Animal; Humans; Kidney; Male; Mice; Mice, Inbred C57BL; Nerve Tissue Proteins; Oxidation-Reduction; Parkinsonian Disorders; Peroxynitrous Acid; Precipitin Tests; Protein Processing, Post-Translational; Synaptophysin; Synucleins; Transfection; Tyrosine

2001
The reaction of nitric oxide with 6-hydroxydopamine: implications for Parkinson's disease.
    Free radical biology & medicine, 2002, Jan-15, Volume: 32, Issue:2

    Topics: alpha-Synuclein; Animals; Cattle; Nerve Tissue Proteins; Nitric Oxide; Oxidation-Reduction; Oxidopamine; Parkinson Disease; Parkinson Disease, Secondary; Peroxynitrous Acid; Serum Albumin, Bovine; Superoxide Dismutase; Synucleins; Tyrosine

2002
alpha-Synuclein interacts with phospholipase D isozymes and inhibits pervanadate-induced phospholipase D activation in human embryonic kidney-293 cells.
    The Journal of biological chemistry, 2002, Apr-05, Volume: 277, Issue:14

    Topics: alpha-Synuclein; Animals; Blood Proteins; Blotting, Western; Brain; Cell Line; Cytoplasm; DNA, Complementary; Enzyme Activation; Enzyme Inhibitors; Eosinophils; Glutathione Transferase; Humans; Microscopy, Fluorescence; Mutation; Nerve Tissue Proteins; Phospholipase D; Phosphoproteins; Phosphorylation; Precipitin Tests; Protein Binding; Protein Isoforms; Protein Structure, Tertiary; Rats; Recombinant Fusion Proteins; Synucleins; Tetradecanoylphorbol Acetate; Time Factors; Transfection; Tyrosine; Vanadates

2002
Patterns of protein nitration in dementia with Lewy bodies and striatonigral degeneration.
    Acta neuropathologica, 2002, Volume: 103, Issue:5

    Topics: Aged; alpha-Synuclein; Brain; Cell Nucleus; Female; Humans; Inclusion Bodies; Lewy Bodies; Lewy Body Disease; Male; Middle Aged; Nerve Tissue Proteins; Neurites; Neuroglia; Neurons; Nitrates; Oxidative Stress; Striatonigral Degeneration; Synucleins; Tyrosine

2002
Tyrosine 125 of alpha-synuclein plays a critical role for dimerization following nitrative stress.
    Brain research, 2002, May-31, Volume: 938, Issue:1-2

    Topics: alpha-Synuclein; Dimerization; DNA, Complementary; Electrophoresis, Polyacrylamide Gel; Humans; Immunoblotting; In Vitro Techniques; Microscopy, Confocal; Nerve Tissue Proteins; Nitrates; Oxidative Stress; Peroxynitrous Acid; Synucleins; Tyrosine

2002
Activation of Pyk2/RAFTK induces tyrosine phosphorylation of alpha-synuclein via Src-family kinases.
    FEBS letters, 2002, Jun-19, Volume: 521, Issue:1-3

    Topics: alpha-Synuclein; Animals; Chlorocebus aethiops; COS Cells; Enzyme Activation; Focal Adhesion Kinase 2; Nerve Tissue Proteins; Phosphoproteins; Phosphorylation; Protein-Tyrosine Kinases; Proto-Oncogene Proteins pp60(c-src); Synucleins; Tyrosine

2002
Mice expressing the alpha(1B)-adrenergic receptor induces a synucleinopathy with excessive tyrosine nitration but decreased phosphorylation.
    Journal of neurochemistry, 2002, Volume: 83, Issue:3

    Topics: Adrenergic alpha-Antagonists; alpha-Synuclein; Animals; Body Weight; Brain; Cerebellum; Disease Models, Animal; Female; Inclusion Bodies; Macromolecular Substances; Male; Mice; Mice, Transgenic; Motor Activity; Multiple System Atrophy; Nerve Tissue Proteins; Neurodegenerative Diseases; Neurons; Nitrates; Oligodendroglia; Phosphorylation; Prazosin; Receptors, Adrenergic, alpha-1; Spinal Cord; Survival Rate; Synucleins; Tyrosine; Ubiquitin

2002
Oxidative dimer formation is the critical rate-limiting step for Parkinson's disease alpha-synuclein fibrillogenesis.
    Biochemistry, 2003, Jan-28, Volume: 42, Issue:3

    Topics: alpha-Synuclein; Amino Acid Substitution; Chromatography, High Pressure Liquid; Cross-Linking Reagents; Dimerization; Humans; Hydrogen-Ion Concentration; Light; Nerve Tissue Proteins; Osmolar Concentration; Osmotic Pressure; Oxidation-Reduction; Oxidative Stress; Parkinson Disease; Protein Isoforms; Scattering, Radiation; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrophotometry, Ultraviolet; Synucleins; Temperature; Tyrosine

2003
Enhanced oligomerization of the alpha-synuclein mutant by the Cu,Zn-superoxide dismutase and hydrogen peroxide system.
    Molecules and cells, 2003, Feb-28, Volume: 15, Issue:1

    Topics: alpha-Synuclein; Amino Acid Substitution; Anserine; Antioxidants; Antiparkinson Agents; Biopolymers; Carnosine; Chelating Agents; Codon; Copper; Edetic Acid; Free Radical Scavengers; Humans; Hydrogen Peroxide; Hydroxyl Radical; Isopropyl Thiogalactoside; Lewy Bodies; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Oxidative Stress; Parkinson Disease; Phenylmethylsulfonyl Fluoride; Point Mutation; Resins, Synthetic; Spin Labels; Superoxide Dismutase; Superoxide Dismutase-1; Synucleins; Tyrosine

2003
Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers.
    FEBS letters, 2003, May-08, Volume: 542, Issue:1-3

    Topics: alpha-Synuclein; Humans; Kinetics; Nerve Tissue Proteins; Parkinson Disease; Solubility; Synucleins; Tetranitromethane; Tyrosine

2003
Effects of oxidative and nitrative challenges on alpha-synuclein fibrillogenesis involve distinct mechanisms of protein modifications.
    The Journal of biological chemistry, 2003, Jul-18, Volume: 278, Issue:29

    Topics: alpha-Synuclein; Cell Line; Cross-Linking Reagents; Drug Stability; Humans; In Vitro Techniques; Inclusion Bodies; Microscopy, Electron; Models, Biological; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Nitrates; Oxidation-Reduction; Oxidative Stress; Protein Processing, Post-Translational; Protein Structure, Quaternary; Recombinant Proteins; Synucleins; Tyrosine

2003
Bicarbonate enhances alpha-synuclein oligomerization and nitration: intermediacy of carbonate radical anion and nitrogen dioxide radical.
    The Biochemical journal, 2004, Mar-01, Volume: 378, Issue:Pt 2

    Topics: alpha-Synuclein; Anions; Bicarbonates; Cyclic N-Oxides; Dimerization; Free Radicals; Hydrogen Peroxide; Hydroxylation; Liposomes; Nerve Tissue Proteins; Nitric Oxide Donors; Nitrogen Dioxide; Nitrogen Oxides; Oxidation-Reduction; Peroxidase; Peroxynitrous Acid; Reactive Nitrogen Species; Spin Labels; Superoxide Dismutase; Superoxide Dismutase-1; Synucleins; Tyrosine

2004
Tyrosine-to-cysteine modification of human alpha-synuclein enhances protein aggregation and cellular toxicity.
    The Journal of biological chemistry, 2004, Mar-12, Volume: 279, Issue:11

    Topics: Adenoviridae; alpha-Synuclein; Animals; Apoptosis; beta-Synuclein; Blotting, Western; Cell Line; Cell Survival; Cloning, Molecular; Cysteine; Detergents; Dimerization; Electrophoresis, Polyacrylamide Gel; Humans; Immunohistochemistry; Magnetic Resonance Spectroscopy; Mice; Microscopy, Fluorescence; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Neurons; Nitrogen; Octoxynol; Oxidative Stress; Oxygen; Phenylalanine; Plasmids; Protein Binding; Proteins; Rats; Recombinant Proteins; Synucleins; Time Factors; Transfection; Tyrosine

2004
Parkinson's disease transgenic mitochondrial cybrids generate Lewy inclusion bodies.
    Journal of neurochemistry, 2004, Volume: 88, Issue:4

    Topics: Aged; alpha-Synuclein; Blotting, Western; Carrier Proteins; Case-Control Studies; Cell Line; Cysteine Endopeptidases; Cytochromes c; DNA, Mitochondrial; Electron Transport Complex I; Female; Humans; Immunohistochemistry; Lewy Bodies; Male; Microscopy, Confocal; Microscopy, Electron; Middle Aged; Multienzyme Complexes; Nerve Tissue Proteins; Neuroblastoma; Neurofilament Proteins; Neurons; Parkinson Disease; Precipitin Tests; Proteasome Endopeptidase Complex; Staining and Labeling; Synucleins; Transgenes; Tubulin; Tyrosine; Ubiquitin; Ubiquitin-Protein Ligases

2004
The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils.
    The Journal of biological chemistry, 2004, Jun-25, Volume: 279, Issue:26

    Topics: alpha-Synuclein; Anaerobiosis; Benzothiazoles; Circular Dichroism; Escherichia coli; Flavanones; Flavonoids; Humans; Light; Lysine; Microscopy, Atomic Force; Molecular Weight; Nerve Tissue Proteins; Oxidation-Reduction; Protein Conformation; Quinones; Scattering, Radiation; Solubility; Spectrometry, Fluorescence; Spectrometry, Mass, Electrospray Ionization; Spectrophotometry, Ultraviolet; Synucleins; Thiazoles; Tyrosine

2004
alpha-Synuclein-synaptosomal membrane interactions: implications for fibrillogenesis.
    European journal of biochemistry, 2004, Volume: 271, Issue:15

    Topics: Alanine; alpha-Synuclein; Animals; Circular Dichroism; Dimerization; Fatty Acids; Humans; Microscopy, Electron; Mutation; Nerve Tissue Proteins; Protein Binding; Protein Structure, Quaternary; Rats; Spectrometry, Fluorescence; Surface Properties; Synaptic Membranes; Synaptosomes; Synucleins; Tyrosine

2004
Functional consequences of alpha-synuclein tyrosine nitration: diminished binding to lipid vesicles and increased fibril formation.
    The Journal of biological chemistry, 2004, Nov-12, Volume: 279, Issue:46

    Topics: alpha-Synuclein; Animals; Calpain; Humans; Insulin; Lipid Metabolism; Mice; Molecular Chaperones; Nerve Tissue Proteins; Nitrates; Oxygen; Proteasome Endopeptidase Complex; Protein Binding; Protein Processing, Post-Translational; Protein Structure, Quaternary; Synucleins; Tyrosine

2004
Peroxidative aggregation of alpha-synuclein requires tyrosines.
    Protein science : a publication of the Protein Society, 2004, Volume: 13, Issue:11

    Topics: alpha-Synuclein; Cytochromes c; Dimerization; Humans; Hydrogen Peroxide; Nerve Tissue Proteins; Oxidation-Reduction; Reactive Oxygen Species; Synucleins; Tyrosine

2004
Effects of nitration on the structure and aggregation of alpha-synuclein.
    Brain research. Molecular brain research, 2005, Mar-24, Volume: 134, Issue:1

    Topics: alpha-Synuclein; Animals; Circular Dichroism; Dose-Response Relationship, Drug; Humans; Microscopy, Atomic Force; Microscopy, Electron, Scanning; Models, Molecular; Nerve Tissue Proteins; Oxidants; Recombinant Proteins; Spectrometry, X-Ray Emission; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis; Stress Fibers; Synucleins; Tetranitromethane; Time Factors; Tyrosine

2005
Nitration and increased alpha-synuclein expression associated with dopaminergic neurodegeneration in equine pituitary pars intermedia dysfunction.
    Journal of neuroendocrinology, 2005, Volume: 17, Issue:2

    Topics: alpha-Synuclein; Animals; Blotting, Western; Chronic Disease; Dopamine; Horse Diseases; Horses; Immunohistochemistry; Nerve Degeneration; Nerve Tissue Proteins; Nitrogen; Oxidative Stress; Pituitary ACTH Hypersecretion; Pituitary Gland; Synucleins; Tyrosine; Tyrosine 3-Monooxygenase

2005
Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations.
    The Journal of biological chemistry, 2005, Jun-03, Volume: 280, Issue:22

    Topics: alpha-Synuclein; Amino Acid Motifs; Circular Dichroism; DNA, Complementary; Dopamine; Histidine; Humans; Indolequinones; Methionine; Microscopy, Atomic Force; Microscopy, Electron; Mutagenesis; Mutation; Nerve Tissue Proteins; Oxidative Stress; Oxygen; Parkinson Disease; Peptides; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Synucleins; Time Factors; Tyrosine

2005
Cleavage of alpha-synuclein by calpain: potential role in degradation of fibrillized and nitrated species of alpha-synuclein.
    Biochemistry, 2005, May-31, Volume: 44, Issue:21

    Topics: alpha-Synuclein; Calpain; Chymotrypsin; Humans; Hydrolysis; Microscopy, Immunoelectron; Nerve Degeneration; Nerve Tissue Proteins; Nitrates; Parkinson Disease; Peptide Fragments; Peroxynitrous Acid; Recombinant Proteins; Solubility; Synucleins; Tyrosine

2005
Serofendic acid prevents 6-hydroxydopamine-induced nigral neurodegeneration and drug-induced rotational asymmetry in hemi-parkinsonian rats.
    Journal of neurochemistry, 2005, Volume: 95, Issue:4

    Topics: Adrenergic Agents; Aldehydes; alpha-Synuclein; Animals; Behavior, Animal; Blotting, Western; CD11b Antigen; Cell Count; Cell Line; Disease Models, Animal; Diterpenes; Dose-Response Relationship, Drug; Drug Administration Schedule; Drug Interactions; Functional Laterality; Glial Fibrillary Acidic Protein; Humans; Immunohistochemistry; Male; Neurodegenerative Diseases; Neuroprotective Agents; Oxidopamine; Parkinson Disease, Secondary; Parkinsonian Disorders; Rats; Rats, Wistar; Reactive Oxygen Species; Rotarod Performance Test; Rotation; Substantia Nigra; Synaptophysin; Time Factors; Tyrosine; Tyrosine 3-Monooxygenase

2005
Characterization of oligomeric intermediates in alpha-synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F alpha-synuclein.
    Journal of molecular biology, 2005, Oct-21, Volume: 353, Issue:2

    Topics: alpha-Synuclein; Anilino Naphthalenesulfonates; Benzothiazoles; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Humans; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Parkinson Disease; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Synucleins; Thiazoles; Tryptophan; Tyrosine

2005
The mitochondrial complex I inhibitor rotenone triggers a cerebral tauopathy.
    Journal of neurochemistry, 2005, Volume: 95, Issue:4

    Topics: alpha-Synuclein; Amyloid beta-Peptides; Analysis of Variance; Animals; Antineoplastic Combined Chemotherapy Protocols; Behavior, Animal; Benzothiazoles; Body Weight; Caspase 3; Caspases; Cell Death; Cerebral Cortex; Cytarabine; Diagnostic Imaging; Dopamine and cAMP-Regulated Phosphoprotein 32; Doxorubicin; Dystonia; Electron Transport Complex III; Enzyme Activation; Glial Fibrillary Acidic Protein; Immunohistochemistry; Locomotion; Male; Microscopy, Electron, Transmission; Mitochondria; Neurons; Phosphopyruvate Hydratase; Phosphorylation; Posture; Psychomotor Performance; Rats; Rats, Inbred Lew; Rotenone; tau Proteins; Tauopathies; Thiazoles; Time Factors; Tyrosine; Tyrosine 3-Monooxygenase; Ubiquitin; Uncoupling Agents

2005
Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence.
    Biochemistry, 2006, Feb-28, Volume: 45, Issue:8

    Topics: Acrylamide; alpha-Synuclein; Amino Acid Substitution; Amyloid; Anilino Naphthalenesulfonates; Fluorescence; Fluorescence Polarization; Fluorescence Resonance Energy Transfer; Protein Structure, Secondary; Solvents; Time Factors; Tryptophan; Tyrosine

2006
Abnormal alpha-synuclein solubility, aggregation and nitration in the frontal cortex in Pick's disease.
    Neuroscience letters, 2006, May-29, Volume: 400, Issue:1-2

    Topics: Aged; alpha-Synuclein; Blotting, Western; Case-Control Studies; Female; Frontal Lobe; Humans; Immunohistochemistry; Male; Molecular Weight; Parkinson Disease; Pick Disease of the Brain; Postmortem Changes; Tyrosine

2006
Alpha-synuclein tertiary contact dynamics.
    The journal of physical chemistry. B, 2007, Mar-01, Volume: 111, Issue:8

    Topics: alpha-Synuclein; Amino Acid Sequence; Electron Transport; Molecular Sequence Data; Protein Conformation; Tryptophan; Tyrosine

2007
The reaction of alpha-synuclein with tyrosinase: possible implications for Parkinson disease.
    The Journal of biological chemistry, 2008, Jun-13, Volume: 283, Issue:24

    Topics: alpha-Synuclein; Circular Dichroism; Cytosol; Dopamine; Humans; Models, Biological; Monophenol Monooxygenase; Mutation; Oxygen; Parkinson Disease; Quinones; Reactive Oxygen Species; Spectrophotometry, Ultraviolet; Time Factors; Tyrosine

2008
Molecular understanding of copper and iron interaction with alpha-synuclein by fluorescence analysis.
    Journal of molecular neuroscience : MN, 2008, Volume: 35, Issue:3

    Topics: alpha-Synuclein; Anilino Naphthalenesulfonates; Benzothiazoles; Binding Sites; Copper; Fluorescence; Fluorescent Dyes; Humans; Iron; Protein Binding; Thiazoles; Tyrosine

2008
Impact of Tyr to Ala mutations on alpha-synuclein fibrillation and structural properties.
    Biochimica et biophysica acta, 2008, Volume: 1782, Issue:10

    Topics: Alanine; alpha-Synuclein; Amino Acid Substitution; Amyloid; Circular Dichroism; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Mutation, Missense; Parkinson Disease; Protein Folding; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Tyrosine

2008
Cell-produced alpha-synuclein oligomers are targeted to, and impair, the 26S proteasome.
    Neurobiology of aging, 2010, Volume: 31, Issue:6

    Topics: Alanine; alpha-Synuclein; Ammonium Chloride; Animals; Benzoquinones; Cerebral Cortex; Chromatography, Gel; Coloring Agents; Congo Red; Enzyme Inhibitors; Gene Expression Regulation, Enzymologic; Green Fluorescent Proteins; Humans; Immunoprecipitation; Lactams, Macrocyclic; Mice; Mice, Inbred C57BL; Mice, Transgenic; Mutation; PC12 Cells; Proteasome Endopeptidase Complex; Protein Folding; Rats; Transfection; Tyrosine

2010
Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation.
    Biochemistry, 2008, Dec-23, Volume: 47, Issue:51

    Topics: alpha-Synuclein; Cytochromes c; Humans; Hydrogen Peroxide; Molecular Conformation; Mutation; Oxidative Stress; Oxygen; Parkinson Disease; Protein Binding; Protein Denaturation; Protein Structure, Tertiary; Recombinant Proteins; Tyrosine

2008
Evaluation of the effects of vitamin A supplementation on adult rat substantia nigra and striatum redox and bioenergetic states: mitochondrial impairment, increased 3-nitrotyrosine and alpha-synuclein, but decreased D2 receptor contents.
    Progress in neuro-psychopharmacology & biological psychiatry, 2009, Mar-17, Volume: 33, Issue:2

    Topics: alpha-Synuclein; Animals; Caspase 3; Dietary Supplements; Electron Transport; Electron Transport Complex I; Electron Transport Complex II; Electron Transport Complex III; Electron Transport Complex IV; Energy Metabolism; Free Radical Scavengers; Glutathione Transferase; Indicators and Reagents; Mitochondria; Neostriatum; Oxidation-Reduction; Rats; Receptors, Dopamine D2; Substantia Nigra; Tumor Necrosis Factor-alpha; Tyrosine; Vitamin A; Vitamins

2009
Vitamin A supplementation at pharmacological doses induces nitrosative stress on the hypothalamus of adult Wistar rats.
    Chemico-biological interactions, 2009, Aug-14, Volume: 180, Issue:3

    Topics: Administration, Oral; alpha-Synuclein; Animals; Brain; Caspase 3; Electron Transport Chain Complex Proteins; Hypothalamus; Oxidation-Reduction; Oxidative Stress; Rats; Rats, Wistar; Receptors, Dopamine D2; Superoxides; Tumor Necrosis Factor-alpha; Tyrosine; Vitamin A

2009
Molecular mechanisms underlying the flavonoid-induced inhibition of alpha-synuclein fibrillation.
    Biochemistry, 2009, Sep-01, Volume: 48, Issue:34

    Topics: alpha-Synuclein; Animals; Binding Sites; Catalase; Cattle; Cyclic N-Oxides; Flavanones; Flavonoids; Free Radicals; Humans; Hydrogen Peroxide; Isoelectric Focusing; Mass Spectrometry; Mutation; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Stability; Time Factors; Tyrosine

2009
19F NMR studies of alpha-synuclein conformation and fibrillation.
    Biochemistry, 2009, Sep-15, Volume: 48, Issue:36

    Topics: alpha-Synuclein; Buffers; Drug Combinations; Fluorine Radioisotopes; Fluorometry; Humans; Magnetic Resonance Spectroscopy; Molecular Weight; Mutagenesis, Site-Directed; Protein Binding; Protein Conformation; Sodium Dodecyl Sulfate; Spectrometry, Mass, Electrospray Ionization; Spermine; Tyrosine

2009
Preferentially increased nitration of alpha-synuclein at tyrosine-39 in a cellular oxidative model of Parkinson's disease.
    Analytical chemistry, 2009, Sep-15, Volume: 81, Issue:18

    Topics: alpha-Synuclein; Animals; Lewy Bodies; Mass Spectrometry; Models, Biological; Monoamine Oxidase; Nitrates; Oxidative Stress; Parkinson Disease; PC12 Cells; Rats; Tyrosine

2009
Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation.
    The Journal of clinical investigation, 2009, Volume: 119, Issue:11

    Topics: Aging; alpha-Synuclein; Animals; Animals, Genetically Modified; Disease Models, Animal; Drosophila melanogaster; Humans; Neurons; Parkinson Disease; Phosphorylation; Serine; Tyrosine

2009
Trichloroethylene induces dopaminergic neurodegeneration in Fisher 344 rats.
    Journal of neurochemistry, 2010, Volume: 112, Issue:3

    Topics: alpha-Synuclein; Animals; Caspase 3; CD11b Antigen; Choline O-Acetyltransferase; Chromatography, High Pressure Liquid; Disease Models, Animal; Dopamine; Dopamine and cAMP-Regulated Phosphoprotein 32; Dose-Response Relationship, Drug; Electrochemistry; Encephalitis; Gene Expression Regulation; Male; Mitochondria; Neurodegenerative Diseases; Oxidative Stress; Rats; Rats, Inbred F344; Rotarod Performance Test; Solvents; Substantia Nigra; Trichloroethylene; Tyrosine; Tyrosine 3-Monooxygenase

2010
Mice expressing the A53T mutant form of human alpha-synuclein exhibit hyperactivity and reduced anxiety-like behavior.
    Journal of neuroscience research, 2010, Volume: 88, Issue:8

    Topics: Age Factors; Alanine; alpha-Synuclein; Analysis of Variance; Animals; Anxiety; Disease Models, Animal; Dopamine Plasma Membrane Transport Proteins; Exploratory Behavior; Gene Expression Regulation; Humans; Hyperkinesis; Maze Learning; Mice; Mice, Transgenic; Motor Activity; Mutation; Norepinephrine; Serotonin Plasma Membrane Transport Proteins; Tyrosine

2010
Fasting induces a high level of 3-nitrotyrosine in the brain of rats.
    Neuroscience letters, 2010, Mar-26, Volume: 472, Issue:3

    Topics: alpha-Synuclein; Animals; Brain; Diabetes Mellitus, Experimental; Fasting; Male; Mitochondrial Proteins; Nitric Oxide; Nitric Oxide Synthase Type II; Rats; Rats, Sprague-Dawley; Tyrosine

2010
Serine 129 phosphorylation reduces the ability of alpha-synuclein to regulate tyrosine hydroxylase and protein phosphatase 2A in vitro and in vivo.
    The Journal of biological chemistry, 2010, Jun-04, Volume: 285, Issue:23

    Topics: alpha-Synuclein; Animals; Dopamine; Humans; In Vitro Techniques; Lentivirus; Mice; Mice, Transgenic; Mutagenesis; Neurotransmitter Agents; Parkinson Disease; Phosphorylation; Protein Phosphatase 2; Serine; Tyrosine; Tyrosine 3-Monooxygenase

2010
Alpha-synuclein nitration and autophagy response are induced in peripheral blood cells from patients with Parkinson disease.
    Neuroscience letters, 2010, Jun-14, Volume: 477, Issue:1

    Topics: Aged; alpha-Synuclein; Antiparkinson Agents; Autophagy; Female; Gene Frequency; Genotype; Humans; Levodopa; Male; Middle Aged; Parkinson Disease; Polymorphism, Genetic; Promoter Regions, Genetic; Reactive Oxygen Species; Sex Distribution; Tyrosine

2010
PAMAM G4 dendrimers affect the aggregation of α-synuclein.
    International journal of biological macromolecules, 2011, Jun-01, Volume: 48, Issue:5

    Topics: alpha-Synuclein; Dendrimers; Humans; Protein Binding; Protein Structure, Secondary; Tyrosine

2011
Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: key role of tyrosine 39 in membrane insertion.
    Journal of molecular biology, 2011, May-13, Volume: 408, Issue:4

    Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid beta-Peptides; Cell Membrane; Gangliosides; Glycosphingolipids; Humans; Membrane Microdomains; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Phosphatidylcholines; Protein Binding; Protein Conformation; Sphingomyelins; Tyrosine

2011
Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding.
    Journal of the American Chemical Society, 2011, May-11, Volume: 133, Issue:18

    Topics: Allosteric Regulation; alpha-Synuclein; Humans; Hydrodynamics; Lipid Bilayers; Membrane Lipids; Mutation; Nitrates; Oxidation-Reduction; Oxidative Stress; Parkinson Disease; Protein Binding; Protein Structure, Secondary; Tyrosine

2011
L-NAME cotreatment did prevent neither mitochondrial impairment nor behavioral abnormalities in adult Wistar rats treated with vitamin A supplementation.
    Fundamental & clinical pharmacology, 2012, Volume: 26, Issue:4

    Topics: alpha-Synuclein; Animals; Anxiety Disorders; Behavior, Animal; Central Nervous System; Dietary Supplements; Diterpenes; Electron Transport; Glutathione Transferase; Heat-Shock Proteins; Illness Behavior; Locomotion; Male; Manganese; Mitochondria; Monoamine Oxidase; Neurodegenerative Diseases; NG-Nitroarginine Methyl Ester; Nitric Oxide; Oxidation-Reduction; Rats; Rats, Wistar; Receptor for Advanced Glycation End Products; Receptors, Dopamine; Receptors, Immunologic; Retinyl Esters; Superoxide Dismutase; Superoxides; Tyrosine; Vitamin A

2012
A novel molecular mechanism for nitrated {alpha}-synuclein-induced cell death.
    Journal of molecular cell biology, 2011, Volume: 3, Issue:4

    Topics: alpha-Synuclein; Antibodies; Apoptosis; Calcium; Caspase 3; Cell Line, Tumor; Focal Adhesion Protein-Tyrosine Kinases; Humans; Immunoprecipitation; Integrin alpha5beta1; Nitric Oxide; Nitric Oxide Synthase Type II; Nitrites; Polymerization; Recombinant Proteins; Signal Transduction; Tyrosine

2011
Alpha-synuclein in colonic submucosa in early untreated Parkinson's disease.
    Movement disorders : official journal of the Movement Disorder Society, 2012, Volume: 27, Issue:6

    Topics: Aged; alpha-Synuclein; Biomarkers; Colon; Enteric Nervous System; Female; Humans; Male; Middle Aged; Neurons; Oxidative Stress; Parkinson Disease; Substantia Nigra; Tyrosine

2012
Increased intestinal permeability correlates with sigmoid mucosa alpha-synuclein staining and endotoxin exposure markers in early Parkinson's disease.
    PloS one, 2011, Volume: 6, Issue:12

    Topics: Acute-Phase Proteins; Aged; alpha-Synuclein; Biomarkers; Carrier Proteins; Endotoxins; Escherichia coli; Escherichia coli Infections; Female; Humans; Immunoenzyme Techniques; Intestinal Mucosa; Intestines; Male; Membrane Glycoproteins; Middle Aged; Neurons; Oxidative Stress; Parkinson Disease; Permeability; Sucrose; Tyrosine

2011
Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: α-synuclein phosphorylation at tyrosine 125.
    Journal of the American Chemical Society, 2012, Mar-21, Volume: 134, Issue:11

    Topics: alpha-Synuclein; Amino Acid Sequence; Cells, Cultured; HEK293 Cells; HeLa Cells; Humans; Phosphorylation; Protein Processing, Post-Translational; Sequence Alignment; Tyrosine

2012
Native and denatured forms of proteins can be discriminated at edge plane carbon electrodes.
    Analytica chimica acta, 2012, Jul-20, Volume: 735

    Topics: alpha-Synuclein; Animals; Cattle; Chickens; Electrochemical Techniques; Electrodes; Fructose-Bisphosphate Aldolase; Graphite; Humans; Protein Denaturation; Proteins; Serum Albumin; Tryptophan; Tyrosine; Urea

2012
Fluorescence lifetime measurements of intrinsically unstructured proteins: application to α-synuclein.
    Methods in molecular biology (Clifton, N.J.), 2012, Volume: 895

    Topics: Algorithms; alpha-Synuclein; Amino Acid Substitution; Anisotropy; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Naphthalenesulfonates; Protein Conformation; Spectrometry, Fluorescence; Staining and Labeling; Tryptophan; Tyrosine

2012
Biophysical properties and cellular toxicity of covalent crosslinked oligomers of α-synuclein formed by photoinduced side-chain tyrosyl radicals.
    Free radical biology & medicine, 2012, Aug-15, Volume: 53, Issue:4

    Topics: alpha-Synuclein; Ammonium Sulfate; Amyloid; Cell Line; Cell Survival; Cross-Linking Reagents; Free Radicals; Humans; Kinetics; Organometallic Compounds; Oxidative Stress; Photochemical Processes; Photosensitizing Agents; Protein Stability; Tyrosine

2012
Phosphorylation of α-synuclein is crucial in compensating for proteasomal dysfunction.
    Biochemical and biophysical research communications, 2012, Aug-03, Volume: 424, Issue:3

    Topics: alpha-Synuclein; Animals; Cell Line; Disease Models, Animal; Dopaminergic Neurons; Focal Adhesion Protein-Tyrosine Kinases; HSC70 Heat-Shock Proteins; Male; Mice; Mice, Inbred C57BL; Neuroprotective Agents; Parkinson Disease; Phosphorylation; Proteasome Endopeptidase Complex; Protein Tyrosine Phosphatase, Non-Receptor Type 1; Tyrosine

2012
Phosphorylation of α-Synuclein at Y125 and S129 alters its metal binding properties: implications for understanding the role of α-Synuclein in the pathogenesis of Parkinson's Disease and related disorders.
    ACS chemical neuroscience, 2011, Nov-16, Volume: 2, Issue:11

    Topics: alpha-Synuclein; Amino Acid Sequence; Binding Sites; Copper; Cross-Linking Reagents; Fluorescence; Humans; Iron; Lead; Metals; Models, Molecular; Molecular Sequence Data; Neuropeptides; Parkinson Disease; Phosphorylation; Spectrometry, Mass, Electrospray Ionization; Tandem Mass Spectrometry; Tyrosine

2011
May the evaluation of nitrosative stress through selective increase of 3-nitrotyrosine proteins other than nitroalbumin and dominant tyrosine-125/136 nitrosylation of serum α-synuclein serve for diagnosis of sporadic Parkinson's disease?
    Antioxidants & redox signaling, 2013, Sep-20, Volume: 19, Issue:9

    Topics: Albumins; alpha-Synuclein; Biomarkers; Humans; Mass Spectrometry; Oxidation-Reduction; Oxidative Stress; Parkinson Disease; Tyrosine

2013
Modulation of human α-synuclein aggregation by a combined effect of calcium and dopamine.
    Neurobiology of disease, 2014, Volume: 63

    Topics: alpha-Synuclein; Calcium; Calorimetry; Cell Line, Tumor; Circular Dichroism; Dopamine; Humans; Microscopy, Confocal; Microscopy, Electron, Transmission; Mutation; Neuroblastoma; Protein Binding; Protein Transport; Thermodynamics; Transfection; Tyrosine

2014
Electrochemical analysis of the fibrillation of Parkinson's disease α-synuclein.
    The Analyst, 2014, Feb-21, Volume: 139, Issue:4

    Topics: alpha-Synuclein; Amyloid; Electrochemical Techniques; Electrodes; Graphite; Humans; Oxidation-Reduction; Parkinson Disease; Protein Folding; Proteostasis Deficiencies; Tyrosine

2014
LC-MS-based urinary metabolite signatures in idiopathic Parkinson's disease.
    Journal of proteome research, 2015, Jan-02, Volume: 14, Issue:1

    Topics: alpha-Synuclein; Animals; Biomarkers; Chromatography, Liquid; Drosophila melanogaster; Fatty Acids; Histidine; Humans; Kynurenine; Mass Spectrometry; Metabolomics; Nucleotides; Parkinson Disease; Phenotype; Phenylalanine; Steroids; Tryptophan; Tyrosine

2015
Efficient modification of alpha-synuclein serine 129 by protein kinase CK1 requires phosphorylation of tyrosine 125 as a priming event.
    ACS chemical neuroscience, 2014, Dec-17, Volume: 5, Issue:12

    Topics: alpha-Synuclein; Casein Kinase I; Cell Line, Transformed; Green Fluorescent Proteins; Humans; Magnetic Resonance Spectroscopy; Phosphorylation; Serine; Transfection; Tyrosine

2014
The effect of tyrosine residues on α-synuclein fibrillation.
    Acta chimica Slovenica, 2015, Volume: 62, Issue:1

    Topics: alpha-Synuclein; Humans; Mutation; Tyrosine

2015
Earliest events in α-synuclein fibrillation probed with the fluorescence of intrinsic tyrosines.
    Journal of photochemistry and photobiology. B, Biology, 2016, Volume: 154

    Topics: alpha-Synuclein; Fluorescent Dyes; Humans; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Protein Multimerization; Protons; Recombinant Proteins; Spectrophotometry, Ultraviolet; Tyrosine

2016
Rapid acidolysis of benzyl group as a suitable approach for syntheses of peptides naturally produced by oxidative stress and containing 3-nitrotyrosine.
    Amino acids, 2016, Volume: 48, Issue:4

    Topics: alpha-Synuclein; Amino Acid Sequence; Fluorenes; Hydrolysis; Oxidative Stress; Peptides; Prions; Trifluoroacetic Acid; Tyrosine

2016
The novel mechanism of rotenone-induced α-synuclein phosphorylation via reduced protein phosphatase 2A activity.
    The international journal of biochemistry & cell biology, 2016, Volume: 75

    Topics: alpha-Synuclein; Animals; Calmodulin; Cerebral Cortex; Down-Regulation; Humans; Mesencephalon; Neurons; Parkinson Disease; Phosphorylation; Protein Aggregates; Protein Phosphatase 2; Rats; Rotenone; src-Family Kinases; Tyrosine

2016
C-Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α-Synuclein in a Yeast Model of Parkinson's Disease.
    PLoS genetics, 2016, Volume: 12, Issue:6

    Topics: alpha-Synuclein; Animals; Autophagy; Globins; Humans; Lewy Bodies; Nerve Tissue Proteins; Neuroglobin; Oxidation-Reduction; Parkinson Disease; Phosphorylation; Proteasome Endopeptidase Complex; Saccharomyces cerevisiae; Serine; Tyrosine

2016
Poststroke Induction of α-Synuclein Mediates Ischemic Brain Damage.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2016, 06-29, Volume: 36, Issue:26

    Topics: alpha-Synuclein; Animals; Brain Infarction; Brain Ischemia; Caspase 3; Death-Associated Protein Kinases; Disease Models, Animal; Gene Expression Regulation; Male; Mice; Mice, Transgenic; Microtubule-Associated Proteins; Motor Activity; PC12 Cells; Protein Serine-Threonine Kinases; Rats; Rats, Inbred SHR; RNA, Small Interfering; Stroke; Tyrosine

2016
The involvement of dityrosine crosslinking in α-synuclein assembly and deposition in Lewy Bodies in Parkinson's disease.
    Scientific reports, 2016, 12-16, Volume: 6

    Topics: Aged; Aged, 80 and over; alpha-Synuclein; Amino Acid Sequence; Brain; Copper; Dimerization; Electrophoresis, Polyacrylamide Gel; Humans; Lewy Bodies; Male; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Oxidation-Reduction; Oxidative Stress; Parkinson Disease; Recombinant Proteins; Tandem Mass Spectrometry; Tyrosine

2016
Opposed Effects of Dityrosine Formation in Soluble and Aggregated α-Synuclein on Fibril Growth.
    Journal of molecular biology, 2017, 10-13, Volume: 429, Issue:20

    Topics: alpha-Synuclein; Humans; Oxidative Stress; Protein Aggregation, Pathological; Protein Multimerization; Tyrosine; Ultraviolet Rays

2017
Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding.
    Protein science : a publication of the Protein Society, 2018, Volume: 27, Issue:7

    Topics: alpha-Synuclein; Autopsy; Binding Sites; Brain; Humans; Parkinson Disease; Phosphorylation; Protein Binding; Protein Processing, Post-Translational; Serine; Single-Domain Antibodies; Tyrosine

2018
2-Pentadecyl-2-Oxazoline Reduces Neuroinflammatory Environment in the MPTP Model of Parkinson Disease.
    Molecular neurobiology, 2018, Volume: 55, Issue:12

    Topics: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine; alpha-Synuclein; Animals; Astrocytes; Behavior, Animal; Cyclooxygenase 2; Cytokines; Disease Models, Animal; DNA Damage; Dopamine Plasma Membrane Transport Proteins; Inflammation; Mice, Inbred C57BL; Microglia; NF-E2-Related Factor 2; Nitric Oxide Synthase Type II; Nitrosative Stress; Oxazoles; Oxidative Stress; Parkinson Disease; Poly Adenosine Diphosphate Ribose; Transcription Factor RelA; Tyrosine; Tyrosine 3-Monooxygenase

2018
Reductive modification of genetically encoded 3-nitrotyrosine sites in alpha synuclein expressed in E.coli.
    Redox biology, 2019, Volume: 26

    Topics: alpha-Synuclein; Cloning, Molecular; Escherichia coli; Escherichia coli Proteins; Gene Expression; Genetic Vectors; Green Fluorescent Proteins; Humans; Metabolic Networks and Pathways; Oxidation-Reduction; Protein Engineering; Recombinant Proteins; Tyrosine

2019
α-synuclein interaction with zero-valent iron nanoparticles accelerates structural rearrangement into amyloid-susceptible structure with increased cytotoxic tendency.
    International journal of nanomedicine, 2019, Volume: 14

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Cell Death; Cell Line, Tumor; Congo Red; Humans; Iron; Kinetics; L-Lactate Dehydrogenase; Metal Nanoparticles; Molecular Docking Simulation; Molecular Dynamics Simulation; Oxazines; Protein Aggregates; Protein Structure, Secondary; Spectrometry, Fluorescence; Tyrosine

2019
Biometals as conformational modulators of α-synuclein photochemical crosslinking.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2019, Volume: 24, Issue:8

    Topics: alpha-Synuclein; Ammonium Sulfate; Coordination Complexes; Copper; Cross-Linking Reagents; Fluorescence; Iron; Light; Organometallic Compounds; Oxidation-Reduction; Photochemical Processes; Photosensitizing Agents; Protein Binding; Protein Conformation; Tyrosine

2019
Investigating the presence of doubly phosphorylated α-synuclein at tyrosine 125 and serine 129 in idiopathic Lewy body diseases.
    Brain pathology (Zurich, Switzerland), 2020, Volume: 30, Issue:4

    Topics: Aged; Aged, 80 and over; alpha-Synuclein; Animals; Female; Humans; Lewy Body Disease; Male; Mice; Phosphorylation; Protein Processing, Post-Translational; Serine; Tyrosine

2020
Role of Tyr-39 for the Structural Features of α-Synuclein and for the Interaction with a Strong Modulator of Its Amyloid Assembly.
    International journal of molecular sciences, 2020, Jul-17, Volume: 21, Issue:14

    Topics: alpha-Synuclein; Amyloid; Humans; Intrinsically Disordered Proteins; Parkinson Disease; Point Mutation; Protein Conformation; Tyrosine

2020
Megadalton-sized Dityrosine Aggregates of α-Synuclein Retain High Degrees of Structural Disorder and Internal Dynamics.
    Journal of molecular biology, 2020, 12-04, Volume: 432, Issue:24

    Topics: alpha-Synuclein; Amyloid; Amyloid beta-Peptides; Cytochromes c; Humans; Magnetic Resonance Spectroscopy; Mitochondria; Neurons; Oxidative Stress; Parkinson Disease; Protein Aggregates; Protein Conformation; Reactive Oxygen Species; Tyrosine

2020
Chemoenzymatic Semi-synthesis Enables Efficient Production of Isotopically Labeled α-Synuclein with Site-Specific Tyrosine Phosphorylation.
    Chembiochem : a European journal of chemical biology, 2021, 04-16, Volume: 22, Issue:8

    Topics: alpha-Synuclein; Molecular Structure; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Phosphorylation; Tyrosine

2021
Light-Controlled Tyrosine Nitration of Proteins.
    Angewandte Chemie (International ed. in English), 2021, 06-07, Volume: 60, Issue:24

    Topics: alpha-Synuclein; Animals; Light; Mice; Nitrates; Oxidation-Reduction; Tumor Necrosis Factor-alpha; Tyrosine

2021
Modulation of α-synuclein fibrillation by plant metabolites, daidzein, fisetin and scopoletin under physiological conditions.
    International journal of biological macromolecules, 2021, Jul-01, Volume: 182

    Topics: alpha-Synuclein; Biological Products; Cell Line; Flavonols; Fluorescence; Humans; Hydrophobic and Hydrophilic Interactions; Isoflavones; Kinetics; Metabolome; Molecular Docking Simulation; Molecular Dynamics Simulation; Protein Aggregates; Protein Conformation; Scopoletin; Tyrosine

2021
Monitoring of a progressive functional dopaminergic deficit in the A53T-AAV synuclein rats by combining 6-[
    Neurobiology of aging, 2021, Volume: 107

    Topics: alpha-Synuclein; Animals; Dependovirus; Disease Models, Animal; Disease Progression; Dopaminergic Neurons; Fluorine Radioisotopes; Male; Motor Activity; Parkinson Disease; Phosphorylation; Positron-Emission Tomography; Protein Aggregates; Rats, Sprague-Dawley; Synucleinopathies; Tyrosine

2021
Tyrosine 136 phosphorylation of α-synuclein aggregates in the Lewy body dementia brain: involvement of serine 129 phosphorylation by casein kinase 2.
    Acta neuropathologica communications, 2021, 11-12, Volume: 9, Issue:1

    Topics: Aged; Aged, 80 and over; alpha-Synuclein; Amino Acid Substitution; Autopsy; Brain; Casein Kinase II; Cells, Cultured; Female; Humans; Lewy Body Disease; Male; Mutation; Phosphorylation; Serine; Tyrosine

2021
Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization.
    Journal of the American Chemical Society, 2022, 07-13, Volume: 144, Issue:27

    Topics: alpha-Synuclein; Amyloid; Humans; Parkinson Disease; Tyrosine

2022
Dityrosine Cross-links are Present in Alzheimer's Disease-derived Tau Oligomers and Paired Helical Filaments (PHF) which Promotes the Stability of the PHF-core Tau (297-391) In Vitro.
    Journal of molecular biology, 2022, 10-15, Volume: 434, Issue:19

    Topics: alpha-Synuclein; Alzheimer Disease; Humans; Neurofibrillary Tangles; Protein Conformation, alpha-Helical; tau Proteins; Tyrosine

2022
DOPAnization of tyrosine in α-synuclein by tyrosine hydroxylase leads to the formation of oligomers.
    Nature communications, 2022, 11-12, Volume: 13, Issue:1

    Topics: alpha-Synuclein; Animals; Dopaminergic Neurons; Humans; Mice; Parkinson Disease; Substantia Nigra; Tyrosine; Tyrosine 3-Monooxygenase

2022
Mutation of Tyrosine Sites in the Human Alpha-Synuclein Gene Induces Neurotoxicity in Transgenic Mice with Soluble Alpha-Synuclein Oligomer Formation.
    Cells, 2022, 11-18, Volume: 11, Issue:22

    Topics: alpha-Synuclein; Animals; Humans; Mice; Mice, Transgenic; Mutation; Neurotoxicity Syndromes; Phenylalanine; Serine; Tyrosine

2022