serine has been researched along with alpha-synuclein in 99 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 1 (1.01) | 18.2507 |
| 2000's | 36 (36.36) | 29.6817 |
| 2010's | 44 (44.44) | 24.3611 |
| 2020's | 18 (18.18) | 2.80 |
| Authors | Studies |
|---|---|
| Gliemann, J; Hager, H; Hojrup, P; Jakes, R; Jensen, PH; Nielsen, MS | 1 |
| Baba, M; Haass, C; Iwatsubo, T; Kahle, PJ; Koyama, A; Meijer, L; Nakajo, S; Okochi, M; Walter, J | 1 |
| Dohmae, N; Fujiwara, H; Goldberg, MS; Hasegawa, M; Iwatsubo, T; Kawashima, A; Masliah, E; Shen, J; Takio, K | 1 |
| Fujiwara, H; Hasegawa, M; Iwatsubo, T; Kanuka, H; Koyama, A; Miura, M; Takahashi, M | 1 |
| Iwatsubo, T | 1 |
| Junn, E; Kim, YM; Lee, G; Lee, SH; Lee, SS; Mouradian, MM; Park, K; Tanaka, M | 1 |
| Ackerley, S; Anderton, BH; Asuni, AA; Buchman, VL; Davies, AM; Grierson, AJ; Hanger, DP; Hill, J; Miller, CC; Saha, AR; Utton, MA | 1 |
| Chen, L; Feany, MB | 1 |
| Bax, A; Ulmer, TS | 1 |
| Bonini, NM; Covy, JP; Farrer, MJ; Giasson, BI; Hurtig, HI; Trojanowski, JQ; Van Deerlin, VM | 1 |
| Anderson, JP; Banducci, K; Barbour, R; Caccavello, RJ; Chataway, T; Chilcote, TJ; de Laat, R; Diep, L; Gai, WP; Goldstein, JM; Huang, J; Keim, PS; Kling, K; Lee, M; Schenk, D; Schlossmacher, MG; Seubert, P; Shen, X; Sinha, S; Walker, DE | 1 |
| Barrett, JM; Fontaine, D; Shults, CW | 1 |
| Duka, T; Sidhu, A | 1 |
| Chung, KC; Kim, HJ; Kim, J; Lee, CH; Lee, D; Paik, SR | 1 |
| Cobb, SA; Dächsel, JC; Dickson, DW; Farrer, MJ; Lincoln, SJ; Rajput, A; Rajput, ML; Robinson, CA; Ross, OA | 1 |
| Ageyama, N; Hirai, Y; Kitagawa, R; Miyachi, S; Mizuno, Y; Mochizuki, H; Nihira, T; Ren, YR; Shimada, T; Takada, M; Terao, K; Wada, K; Yasuda, T | 1 |
| Hagiwara, A; Hattori, N; Hikawa, R; Ihara, M; Kinoshita, M; Kitano, A; Miyakawa, T; Mori, H; Noda, M; Takanashi, M; Tanigaki, A; Tomimoto, H; Yamasaki, N | 1 |
| Ishii, A; Iwata, S; Iwatsubo, T; Kobayashi, K; Matsumoto, K; Nakamura, A; Ono, M; Sakagami, J; Tada, N; Ukai, Y; Wakamatsu, M; Yoshimoto, M | 1 |
| Hasegawa, M; Hisanaga, S; Iguchi, T; Iwatsubo, T; Kato, K; Kurimoto, E; Masuda, M; Mori, T; Sakata, E; Sasakawa, H; Yamaguchi, Y | 1 |
| Hofmeister, A; Hutter-Paier, B; Windisch, M; Wolf, HJ; Wronski, R | 1 |
| Akiyama, H; Hasegawa, M; Iwatsubo, T; Kondo, H; Mizuno, Y; Mochizuki, H; Obi, K; Shimomura, Y | 1 |
| Chen, W; Gorbatyuk, OS; Kondrikova, G; Li, S; Mandel, RJ; Manfredsson, FP; Muzyczka, N; Sullivan, LF | 1 |
| Dalfó, E; Ferrer, I; Martinez, A; Muntané, G | 1 |
| Eliezer, D; Fernandez, CO; Fredenburg, RA; Kim, HY; Lamberto, GR; Lansbury, PT; Lashuel, HA; Paleologou, KE; Rospigliosi, CC; Schmid, AW; Zweckstetter, M | 1 |
| Ebadi, M; Govitrapong, P; Klongpanichapak, S; Phansuwan-Pujito, P | 1 |
| Giasson, BI; Waxman, EA | 1 |
| Hasegawa, T; Itoyama, Y; Kikuchi, A; Kobayashi, M; Mori, F; Sugeno, N; Takeda, A; Wakabayashi, K | 1 |
| Arawaka, S; Goto, S; Hara, S; Karube, H; Kato, T; Kawanami, T; Koyama, S; Kurita, K; Ren, CH; Sakamoto, M; Sato, H; Wada, M | 1 |
| Arai, T; Hatsuta, H; Ikemura, M; Inoue, K; Kanemaru, K; Mochizuki, H; Murayama, S; Saito, Y; Sakiyama, Y; Sawabe, M; Sengoku, R; Tanaka, N | 1 |
| Anderson, JP; Babcock, M; Bard, F; Basi, GS; Brigham, EF; Caccavello, RJ; Chereau, D; Chian, D; Chilcote, TJ; Chiou, SS; Frigon, NL; Goldstein, JM; Griswold-Prenner, I; Inglis, KJ; McConlogue, L; Motter, R; Nelson, S; Powell, K; Ramos, C; Santiago, P; Schöbel, S; Sham, H; Soriano, F; Wright, S; Yednock, T; Yu, M | 1 |
| El-Agnaf, O; Febbraro, F; Gai, WP; Hansen, HD; Jensen, PH; Kragh, CL; Lund, LB; Richter-Landsberg, C | 1 |
| Hasegawa, T; Kahle, PJ; Neumann, M; Schell, H | 1 |
| Arawaka, S; Cui, C; Hara, S; Kato, T; Kawanami, T; Koyama, S; Kurita, K; Machiya, Y; Sakamoto, M; Sato, H; Wada, M | 1 |
| Fan, Z; Feany, MB; Hyman, BT; McFarland, NR; McLean, PJ; Schwarzschild, MA; Xu, K | 1 |
| McGeer, EG; McGeer, PL; Qing, H; Wong, W | 1 |
| Chen, L; Feany, MB; Hyman, BT; McLean, PJ; Negro, A; Periquet, M; Wang, X | 1 |
| Boyle, JP; Dallas, ML; Hettiarachchi, NT; Hung, CC; Parker, A; Pearson, HA; Peers, C; Pennington, K; Robinson, P | 1 |
| Aebischer, P; Chegini, F; Chiappe, D; Eliezer, D; Fernandez, CO; Gai, WP; Kim, HY; Lamberto, GR; Lashuel, HA; Masliah, E; Moniatte, M; Oueslati, A; Paleologou, KE; Rospigliosi, CC; Schmid, A; Schneider, BL; Shakked, G; Zweckstetter, M | 1 |
| Ferrer, I; Gomez, A | 1 |
| 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, J | 1 |
| Baba, T; Hasegawa, T; Itoyama, Y; Kikuchi, A; Kobayashi, M; Konno, M; Sugeno, N; Takeda, A | 1 |
| Anderson, JP; Broe, M; Gai, WP; Halliday, GM; Howells, D; Huang, Y; Hughes, AJ; Milward, EA; Porritt, M; Wang, X; Zhou, J | 1 |
| Kehm, VM; Lee, EB; Lee, VM; Li, C; Lim, Y; Soper, JH; Trojanowski, JQ | 1 |
| Ferrer, I; Martinez-Vicente, M; Muntané, G | 1 |
| Arawaka, S; Fukushima, S; Hara, S; Kato, T; Koga, K; Koyama, S; Sato, H | 1 |
| Marin, O; Negro, A; Pinna, LA; Salvi, M; Sarno, S; Trashi, E | 1 |
| Aebischer, P; Lashuel, HA; Oueslati, A; Paleologou, KE; Schneider, BL | 1 |
| Braithwaite, SP; Mouradian, MM; Stock, JB | 1 |
| Di Monte, DA; Mak, SK; McCormack, AL | 1 |
| Adler, CH; Akiyama, H; Beach, TG; Caviness, JN; Lue, LF; Sabbagh, MN; Serrano, GE; Shill, HA; Sue, LI; Walker, DG | 1 |
| Cashikar, AG; Kamitani, T; Lee, BR; Matsuo, Y | 1 |
| Arawaka, S; Kato, T; Sato, H | 1 |
| Farran, A; Febbraro, F; Jensen, PH; Kirik, D; Romero-Ramos, M; Sahin, G; Soares, S | 1 |
| Arawaka, S; Cui, C; Hara, S; Kato, T; Koyama, S; Machiya, Y; Sasaki, A; Sato, H | 1 |
| Chau, KY; Cooper, JM; Schapira, AH | 1 |
| Bandopadhyay, R; Dihanich, S; Lees, A; Lewis, PA; Mamais, A; Manzoni, C; Moore, D; Raja, M | 1 |
| Anderson, JP; Babcock, M; Bergeron, M; Chiou, SS; Fauss, D; Motter, R; Nelson, S; San Pablo, F; Tanaka, P | 1 |
| Ciociaro, A; Di Monte, DA; Hettich, MM; Kahle, PJ; Krauss, S; Pérez-Revuelta, BI; Rotermund, C | 1 |
| Bader, B; Giese, A; Hillmer, A; Högen, T; Kamp, F; Levin, J; Lorenzl, S; Nübling, GS | 1 |
| Arnold, SE; Arvanitakis, Z; Han, LY; Kazi, H; Kim, SF; Lee, EB; Lee, VM; Louneva, N; Toledo, JB; Trojanowski, JQ; Yarchoan, M | 1 |
| Bekei, B; Binolfi, A; Kosten, J; Selenko, P; Stuiver, M; Theillet, FX; van Rossum, M; Verzini, S | 1 |
| Love, S; Miners, JS; Renfrew, R; Swirski, M | 1 |
| Al Dakheel, A; Gao, A; Hazrati, LN; Kern, DS; Lang, AE; Liu, LW; Marras, C; Visanji, NP | 1 |
| Fares, MB; Lashuel, HA; Masliah, E; Mbefo, MK; Oueslati, A; Outeiro, T; Paleologou, K; Pinto, M; Tenreiro, S; Yin, G; Zweckstetter, M | 1 |
| Colin, P; Dusonchet, J; Moore, DJ; Nguyen, AP; Schneider, BL; Tsika, E | 1 |
| Buck, K; El-Agnaf, OM; Kirik, D; Landeck, N; Majbour, NK; Ulusoy, A | 1 |
| Arawaka, S; Kato, T; Sasaki, A; Sato, H | 1 |
| Campbell, EM; Flavin, WP; Fraser, PE; Iqbal, S; Pacelli, C; Samuel, F; Sri Renganathan, SD; Tandon, A; Trudeau, LE | 1 |
| Bekei, B; Binolfi, A; Kosten, J; Limatola, A; Rose, HM; Selenko, P; Stuiver, M; Theillet, FX; van Rossum, M; Verzini, S | 1 |
| Braus, GH; Kleinknecht, A; Lázaro, DF; Outeiro, TF; Pinho, R; Popova, B; Valerius, O | 1 |
| Brooks, M; Giasson, BI; Rutherford, NJ | 1 |
| Feuerstein, S; Gremer, L; Hoyer, W; Mirecka, EA; Schröder, GF; Stoldt, M; Willbold, D | 1 |
| Blanco-Prieto, MJ; Garbayo, E; Luquin, MR; Martínez-Valbuena, I; Rodríguez-Nogales, C; Sebastián, V | 1 |
| Bérard, M; Dahmene, M; Oueslati, A | 1 |
| Brennan, CK; De Leon, CA; Galesic, A; Lamiri, N; Levine, PM; Lewis, YE; Pratt, MR | 1 |
| Craven, TW; De Leon, CA; Levine, PM; Pratt, MR | 1 |
| Chiki, A; De Genst, E; Di Trani, J; Dobson, CM; El Turk, F; Fauvet, B; Guilliams, T; Hejjaoui, M; Lashuel, HA; Mittermaier, A; Vendruscolo, M | 1 |
| Deng, Y; Jiang, B; Maupin-Furlow, JA; Moskovitz, J; Rankin, CL; Richter, ML; Toyo-Oka, K | 1 |
| Chao, D; Chen, T; Ding, G; Li, ZR; Sheng, S; Wang, Q; Wen, GQ; Xia, TC; Xia, Y; Zhao, JN | 1 |
| Goswami, A; Hans, F; Kahle, PJ; Katona, I; Outeiro, TF; Prasad, V; Schulz, JB; Voigt, A; Wasser, Y | 1 |
| Buell, AK; Dobson, CM; Galvagnion, C; Linse, S; Makasewicz, K; Sparr, E; Topgaard, D | 1 |
| Chen, J; Gui, C; Li, H; Li, W; Mao, K; Ren, Y; Wu, X; Yu, H; Zou, F | 1 |
| Abdesselem, H; El-Agnaf, OMA; El-Tarawneh, H; Erskine, D; Fayyad, M; Majbour, NK; Sudhakaran, IP; Vaikath, NN | 1 |
| Abdesselem, H; Attems, J; El-Agnaf, OMA; Erskine, D; Fayyad, M; Ghanem, SS; Lamprokostopoulou, A; Majbour, NK; Morris, CM; Sudhakaran, IP; Vaikath, NN; Vekrellis, K | 1 |
| Chung, KKK; Li, J; Sung, CC; Wu, W; Yu, P | 1 |
| Ding, J; He, Y; Huang, J; Li, C; Lian, Y; Meng, Y; Qiu, P; Wang, Y | 1 |
| Cao, X; Chen, C; Peng, Q; Tan, Y; Wang, J; Wu, Y; Xu, Y; Yang, X; Zeng, W | 1 |
| Gabrielyan, L; Hatami, A; John, V; Liang, H; Minalyan, A; Wang, L | 1 |
| Brockway, NL; Cook, ZT; Glover, G; Osterberg, VR; Pizano, S; Sal, MK; Schultz, BI; Stackhouse, TL; Tobias, ZJC; Unni, VK; Weissman, TA; Weston, LJ | 1 |
| Avenali, M; Blandini, F; Cerri, S; Croce, S; Di Monte, DA; Ghezzi, C; Ongari, G; Valente, EM; Zangaglia, R | 1 |
| Elfarrash, S; Ferreira, N; Gregersen, E; Jensen, NM; Jensen, PH; Meyer, M; Nabavi, S; Schmidt, SI; Vestergaard, MV | 1 |
| Hosokawa, M; Irie, K; Iwasaki, Y; Mishima, K; Sano, K; Satoh, K; Yamashita, Y | 1 |
| Adams, EK; Dent, SE; King, DP; Mackiewicz, MR; Osterberg, VR; Unni, VK; Weissman, TA | 1 |
| Abdi, IY; Ardah, MT; Attems, J; Carloni, P; Dorn, A; El-Agnaf, OMA; Erskine, D; Fayyad, M; Ghanem, SS; Jensen, NM; Jensen, PH; Majbour, NK; McKeith, I; Melachroinou, K; Outeiro, TF; Poggiolini, I; Santos, P; Sudhakaran, IP; Vaikath, NN; Vasili, E; Vekrellis, K | 1 |
| Brino, L; Brüstle, O; Cousin, L; Hanifehlou, Z; Haupt, S; Kwon, YJ; Lee, J; Ogier, A; Peitz, M; Segschneider, M; Sommer, P; Vuidel, A; Weykopf, B; Wiest-Daesslé, N; Wilbertz, JH | 1 |
| Basso, E; Füchtbauer, A; Füchtbauer, EM; Jensen, PH; Lassen, LB; Moos, T; Outeiro, TF; Thomsen, MS | 1 |
| Duan, Q; Gao, Y; He, P; Huang, H; Huang, Y; Liu, Q; Nie, K; Wang, L; Wu, A; Zhang, Q | 1 |
| Chaturvedi, M; Devi, S; Dharmadana, D; Kumar, D; Priya, S; Raj, R; Sharma, SK; Srivastava, T; Valéry, C; Yadav, SK | 1 |
| Brontesi, L; Dettmer, U; Jin, SX; Ramalingam, N; Selkoe, DJ | 1 |
3 review(s) available for serine and alpha-synuclein
| Article | Year |
|---|---|
Is alpha-synuclein pathology a target for treatment of neurodegenerative disorders?
Topics: alpha-Synuclein; Animals; Enzyme Inhibitors; Humans; Neurodegenerative Diseases; Serine | 2007 |
α-Synuclein phosphorylation as a therapeutic target in Parkinson's disease.
Topics: alpha-Synuclein; Animals; Casein Kinase I; Casein Kinase II; Cell Cycle Proteins; Drosophila; G-Protein-Coupled Receptor Kinases; Humans; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Lewy Bodies; Mice; Mice, Transgenic; Molecular Targeted Therapy; Neurons; Parkinson Disease; Phosphoprotein Phosphatases; Phosphorylation; Polo-Like Kinase 1; Protein Kinase Inhibitors; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins; Rats; Serine | 2012 |
The role of Ser129 phosphorylation of α-synuclein in neurodegeneration of Parkinson's disease: a review of in vivo models.
Topics: alpha-Synuclein; Animals; Disease Models, Animal; Humans; Nerve Degeneration; Parkinson Disease; Phosphorylation; Serine | 2013 |
96 other study(ies) available for serine and alpha-synuclein
| Article | Year |
|---|---|
alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356.
Topics: alpha-Synuclein; Axons; Cyclic AMP-Dependent Protein Kinases; Escherichia coli; Humans; Nerve Tissue Proteins; Neurons; Phosphoproteins; Phosphorylation; Serine; Signal Transduction; Synucleins; tau Proteins | 1999 |
Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein.
Topics: alpha-Synuclein; Amino Acid Sequence; Animals; Antibody Specificity; Brain Chemistry; Casein Kinase II; Casein Kinases; Humans; Molecular Sequence Data; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Parkinson Disease; PC12 Cells; Phosphoproteins; Phosphorylation; Protein Kinase Inhibitors; Protein Kinases; Protein Serine-Threonine Kinases; Rats; Serine; Synucleins | 2000 |
alpha-Synuclein is phosphorylated in synucleinopathy lesions.
Topics: Aged; alpha-Synuclein; Amino Acid Sequence; Brain Chemistry; Cerebral Cortex; Humans; Lewy Bodies; Mass Spectrometry; Molecular Sequence Data; Nerve Tissue Proteins; Neurodegenerative Diseases; Phosphoproteins; Recombinant Proteins; Serine; Synucleins | 2002 |
Phosphorylation of alpha-synuclein characteristic of synucleinopathy lesions is recapitulated in alpha-synuclein transgenic Drosophila.
Topics: alpha-Synuclein; Animals; Drosophila; Immunohistochemistry; Mutation; Nerve Tissue Proteins; Neurodegenerative Diseases; Neurons; Phosphorylation; Serine; Synucleins; Time Factors | 2003 |
Aggregation of alpha-synuclein in the pathogenesis of Parkinson's disease.
Topics: alpha-Synuclein; Antibodies, Monoclonal; Blotting, Western; Brain; Chromatography, High Pressure Liquid; Humans; Immunohistochemistry; Lewy Bodies; Nerve Tissue Proteins; Parkinson Disease; Phosphorylation; Serine; Synucleins | 2003 |
Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation.
Topics: alpha-Synuclein; Animals; Binding Sites; Blotting, Western; Carrier Proteins; Casein Kinase II; Cell Line; Cytoplasm; Dichlororibofuranosylbenzimidazole; Humans; Immunohistochemistry; Microscopy, Fluorescence; Mutation; Nerve Tissue Proteins; PC12 Cells; Phosphorylation; Protein Binding; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Rats; Serine; Synucleins; Transfection | 2004 |
Parkinson's disease alpha-synuclein mutations exhibit defective axonal transport in cultured neurons.
Topics: alpha-Synuclein; Animals; Axonal Transport; Base Sequence; Cells, Cultured; DNA, Complementary; Humans; Mutagenesis, Site-Directed; Nerve Tissue Proteins; Neurons; Parkinson Disease; Phosphorylation; Point Mutation; Rats; Recombinant Proteins; Serine; Synucleins; Transfection | 2004 |
Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease.
Topics: alpha-Synuclein; Amino Acid Substitution; Animals; Animals, Genetically Modified; Aspartic Acid; beta-Adrenergic Receptor Kinases; Brain; Central Nervous System; Cyclic AMP-Dependent Protein Kinases; Disease Models, Animal; Dopamine; Drosophila; Drosophila Proteins; G-Protein-Coupled Receptor Kinase 2; Inclusion Bodies; Nerve Degeneration; Nerve Tissue Proteins; Neurons; Parkinson Disease; Phosphorylation; Point Mutation; Retina; Serine; Synucleins | 2005 |
Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants.
Topics: Alanine; alpha-Synuclein; Amino Acid Sequence; Humans; Kinetics; Magnetic Resonance Spectroscopy; Micelles; Models, Molecular; Molecular Conformation; Molecular Sequence Data; Mutation; Parkinson Disease; Point Mutation; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Serine; Sodium Dodecyl Sulfate; Valine | 2005 |
Biochemical and pathological characterization of Lrrk2.
Topics: Adult; Aged; Aged, 80 and over; alpha-Synuclein; Amino Acid Sequence; Animals; Blotting, Western; Brain; Cell Line; DNA Mutational Analysis; Female; Genetic Predisposition to Disease; Glycine; Humans; Immunohistochemistry; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Male; Mice; Middle Aged; Molecular Weight; Mutation; Parkinson Disease; Protein Serine-Threonine Kinases; Serine; Time Factors; Transfection | 2006 |
Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease.
Topics: alpha-Synuclein; Amino Acid Sequence; Female; Humans; Lewy Body Disease; Middle Aged; Molecular Sequence Data; Phosphorylation; Serine | 2006 |
alpha-synuclein from platelets is not phosphorylated at serine 129 in Parkinson's disease and multiple system atrophy.
Topics: Adult; Aged; alpha-Synuclein; Animals; Arabidopsis Proteins; Blood Platelets; Blotting, Western; Carrier Proteins; Female; Humans; Male; Mice; Mice, Transgenic; Middle Aged; Multiple System Atrophy; Parkinson Disease; Serine | 2006 |
The neurotoxin, MPP+, induces hyperphosphorylation of Tau, in the presence of alpha-Synuclein, in SH-SY5Y neuroblastoma cells.
Topics: 1-Methyl-4-phenylpyridinium; alpha-Synuclein; Blotting, Western; Cell Fractionation; Cell Line, Tumor; Cell Survival; Dopamine Plasma Membrane Transport Proteins; Dose-Response Relationship, Drug; Gene Expression; Humans; Neuroblastoma; Neurotoxins; Phosphorylation; Serine; tau Proteins; Tetrazolium Salts; Thiazoles; Transfection | 2006 |
Calpain-resistant fragment(s) of alpha-synuclein regulates the synuclein-cleaving activity of 20S proteasome.
Topics: alpha-Synuclein; Amino Acid Sequence; Amino Acid Substitution; Amino Acids; Animals; Calpain; Electrophoresis, Polyacrylamide Gel; Glutamates; Hydrolysis; Models, Biological; Molecular Sequence Data; Mutation; Proline; Proteasome Endopeptidase Complex; Serine; Substrate Specificity; Swine; Threonine | 2006 |
Parkinsonism, Lrrk2 G2019S, and tau neuropathology.
Topics: Aged; alpha-Synuclein; Brain; Cell Line; Disability Evaluation; Disease Progression; Female; Glycine; Humans; Immunohistochemistry; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Male; Middle Aged; Mutation; Neurofibrillary Tangles; Parkinsonian Disorders; Pedigree; Protein Serine-Threonine Kinases; Serine; tau Proteins | 2006 |
Neuronal specificity of alpha-synuclein toxicity and effect of Parkin co-expression in primates.
Topics: alpha-Synuclein; Animals; Brain; Cell Count; Dependovirus; Fluorescent Antibody Technique; Gene Expression; Genetic Vectors; Green Fluorescent Proteins; Macaca mulatta; Male; Nerve Tissue Proteins; Neurons; Rats; Rats, Sprague-Dawley; Serine; Ubiquitin-Protein Ligases | 2007 |
Sept4, a component of presynaptic scaffold and Lewy bodies, is required for the suppression of alpha-synuclein neurotoxicity.
Topics: Acoustic Stimulation; Aged; Aged, 80 and over; alpha-Synuclein; Animals; Brain; Cytoskeletal Proteins; Disease Models, Animal; Dopamine; Dopamine Plasma Membrane Transport Proteins; Female; GTP Phosphohydrolases; Humans; Male; Mice; Mice, Transgenic; Middle Aged; Mutation; Neural Inhibition; Neurons; Parkinson Disease; Presynaptic Terminals; Reflex, Startle; Septins; Serine; Synaptophysin | 2007 |
Accumulation of phosphorylated alpha-synuclein in dopaminergic neurons of transgenic mice that express human alpha-synuclein.
Topics: alpha-Synuclein; Animals; Brain; Casein Kinase II; Cell Nucleus; Dopamine; Humans; Immunohistochemistry; Mice; Mice, Transgenic; Neurons; Phosphorylation; Point Mutation; Promoter Regions, Genetic; Rats; Serine; Tyrosine 3-Monooxygenase | 2007 |
Ultra-high field NMR studies of antibody binding and site-specific phosphorylation of alpha-synuclein.
Topics: alpha-Synuclein; Antibodies, Monoclonal; Binding Sites; Epitope Mapping; Epitopes; Humans; Magnetic Resonance Spectroscopy; Mutation; Phosphorylation; Serine | 2007 |
Relationship of phosphorylated alpha-synuclein and tau accumulation to Abeta deposition in the cerebral cortex of dementia with Lewy bodies.
Topics: Aged; Aged, 80 and over; alpha-Synuclein; Amyloid beta-Peptides; Analysis of Variance; Cerebral Cortex; Female; Humans; Lewy Bodies; Lewy Body Disease; Male; Microscopy, Immunoelectron; Middle Aged; Phosphorylation; Plaque, Amyloid; Serine; Statistics, Nonparametric; tau Proteins | 2008 |
The phosphorylation state of Ser-129 in human alpha-synuclein determines neurodegeneration in a rat model of Parkinson disease.
Topics: alpha-Synuclein; Animals; Brain; Dependovirus; Disease Models, Animal; Dopamine; Humans; Lewy Bodies; Microscopy, Fluorescence; Neurodegenerative Diseases; Parkinson Disease; Phosphorylation; Rats; Recombinant Proteins; Serine; Tyrosine 3-Monooxygenase | 2008 |
Phosphorylation of tau and alpha-synuclein in synaptic-enriched fractions of the frontal cortex in Alzheimer's disease, and in Parkinson's disease and related alpha-synucleinopathies.
Topics: Aged; Aged, 80 and over; alpha-Synuclein; Alzheimer Disease; Biopsy; Case-Control Studies; Cyclin-Dependent Kinase 5; Female; Frontal Bone; Glycogen Synthase Kinase 3; Glycogen Synthase Kinase 3 beta; Humans; Male; Microscopy, Electron, Transmission; Middle Aged; Parkinson Disease; Phosphorylation; Serine; Synapses; Synaptophysin; tau Proteins | 2008 |
Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein.
Topics: alpha-Synuclein; Chromatography, Gel; Circular Dichroism; Humans; Liposomes; Magnetic Resonance Spectroscopy; Micelles; Models, Biological; Models, Molecular; Molecular Conformation; Phosphorylation; Protein Conformation; Recombinant Proteins; Serine; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | 2008 |
Melatonin inhibits amphetamine-induced increase in alpha-synuclein and decrease in phosphorylated tyrosine hydroxylase in SK-N-SH cells.
Topics: alpha-Synuclein; Amphetamine; Antioxidants; Cell Line, Tumor; Central Nervous System Stimulants; Dose-Response Relationship, Drug; Drug Interactions; Electron Transport Complex I; Gene Expression Regulation, Neoplastic; Humans; Melatonin; Neuroblastoma; Phosphorylation; Serine; Tyrosine 3-Monooxygenase | 2008 |
Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein.
Topics: Adult; Aged; Aged, 80 and over; alpha-Synuclein; Animals; Binding Sites; Casein Kinase II; Cell Line, Tumor; Disease Models, Animal; Female; Humans; Immunohistochemistry; Inclusion Bodies; Male; Mice; Mice, Transgenic; Middle Aged; Neurons; Parkinson Disease; Phosphorylation; Proteasome Endopeptidase Complex; Serine; Substantia Nigra; Substrate Specificity; Up-Regulation | 2008 |
Serine 129 phosphorylation of alpha-synuclein induces unfolded protein response-mediated cell death.
Topics: alpha-Synuclein; Apoptosis; Caspase 3; Cell Death; Cell Line, Tumor; Endoplasmic Reticulum; Enzyme Activation; Golgi Apparatus; Humans; Lewy Bodies; Mutation; Phosphorylation; Protein Denaturation; Rotenone; Serine | 2008 |
N-terminal region of alpha-synuclein is essential for the fatty acid-induced oligomerization of the molecules.
Topics: alpha-Synuclein; Amino Acid Sequence; Cell Line; DNA Mutational Analysis; Fatty Acids, Unsaturated; Humans; Parkinson Disease; Phosphorylation; Recombinant Proteins; Sequence Deletion; Serine | 2008 |
Incidence and extent of Lewy body-related alpha-synucleinopathy in aging human olfactory bulb.
Topics: Aged; Aged, 80 and over; Aging; alpha-Synuclein; Amyloid beta-Peptides; Brain; Female; Humans; Incidence; Lewy Bodies; Male; Mental Status Schedule; Olfactory Bulb; Serine; Spinal Cord; Statistics as Topic; tau Proteins; Tyrosine 3-Monooxygenase; Ubiquitin | 2008 |
Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system.
Topics: alpha-Synuclein; Animals; Base Sequence; Cell Line; Central Nervous System; DNA Primers; Enzyme-Linked Immunosorbent Assay; Humans; Mice; Mice, Inbred C57BL; Mice, Knockout; Phosphorylation; Protein Kinases; Protein Serine-Threonine Kinases; RNA Interference; Serine | 2009 |
Alpha-synuclein aggregation and Ser-129 phosphorylation-dependent cell death in oligodendroglial cells.
Topics: alpha-Synuclein; Animals; Apoptosis; Caspase 3; Cell Death; Cell Line; Congo Red; Flavanones; Microscopy, Fluorescence; Microtubules; Models, Biological; Oligodendroglia; Phosphorylation; Rats; Serine | 2009 |
Nuclear and neuritic distribution of serine-129 phosphorylated alpha-synuclein in transgenic mice.
Topics: Aging; alpha-Synuclein; Amygdala; Animals; Brain; Cell Nucleus; Cells, Cultured; Cerebral Cortex; Conditioning, Psychological; Disease Models, Animal; Fear; Hippocampus; Hypothalamic Area, Lateral; Immunohistochemistry; Lewy Body Disease; Mice; Mice, Inbred C57BL; Mice, Transgenic; Neurons; Parkinson Disease; Phosphorylation; Presynaptic Terminals; Serine | 2009 |
Contribution of endogenous G-protein-coupled receptor kinases to Ser129 phosphorylation of alpha-synuclein in HEK293 cells.
Topics: alpha-Synuclein; Animals; G-Protein-Coupled Receptor Kinases; Humans; Lewy Bodies; Parkinson Disease; Phosphorylation; Serine | 2009 |
Alpha-synuclein S129 phosphorylation mutants do not alter nigrostriatal toxicity in a rat model of Parkinson disease.
Topics: Alanine; alpha-Synuclein; Animals; Aspartic Acid; Basal Ganglia; Cell Count; Dependovirus; Disease Models, Animal; Dopamine; Green Fluorescent Proteins; Humans; Mutation; Nerve Tissue Proteins; Parkinson Disease; Phosphorylation; Rats; Rats, Sprague-Dawley; Serine; Substantia Nigra; Tyrosine 3-Monooxygenase | 2009 |
Lrrk2 phosphorylates alpha synuclein at serine 129: Parkinson disease implications.
Topics: alpha-Synuclein; Cell Line; Humans; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Mutation; Parkinson Disease; Phosphorylation; Protein Serine-Threonine Kinases; Protein Structure, Tertiary; Serine | 2009 |
Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation.
Topics: Aging; alpha-Synuclein; Animals; Animals, Genetically Modified; Disease Models, Animal; Drosophila melanogaster; Humans; Neurons; Parkinson Disease; Phosphorylation; Serine; Tyrosine | 2009 |
alpha-Synuclein modulation of Ca2+ signaling in human neuroblastoma (SH-SY5Y) cells.
Topics: alpha-Synuclein; Amino Acids; Analysis of Variance; Calcium; Calcium Channel Blockers; Calcium Channels, L-Type; Calcium Signaling; Cell Line, Tumor; Cell Survival; Enzyme Inhibitors; Fura-2; Gene Expression Regulation; Humans; Indoles; Mutation; Neuroblastoma; Nifedipine; Oligomycins; omega-Conotoxin GVIA; Potassium Chloride; Serine; Transfection | 2009 |
Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions.
Topics: alpha-Synuclein; Alzheimer Disease; Amino Acid Sequence; Animals; Brain; Cell Membrane; Creatine Kinase; Disease Models, Animal; Humans; Lewy Bodies; Lewy Body Disease; Male; Mice; Mice, Transgenic; Multiple System Atrophy; Neurodegenerative Diseases; Neurons; Parkinson Disease; Phosphorylation; Polymers; Protein Isoforms; Rats; Rats, Wistar; Serine | 2010 |
Involvement of the cerebral cortex in Parkinson disease linked with G2019S LRRK2 mutation without cognitive impairment.
Topics: Aged; Aged, 80 and over; alpha-Synuclein; Cerebral Cortex; Cognition Disorders; Electrophoresis, Gel, Two-Dimensional; Female; Glial Fibrillary Acidic Protein; Glycine; Humans; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Malondialdehyde; Mass Spectrometry; Mutation; Parkinson Disease; Protein Serine-Threonine Kinases; Receptor for Advanced Glycation End Products; Receptors, Immunologic; Serine; Statistics, Nonparametric | 2010 |
Serine 129 phosphorylation reduces the ability of alpha-synuclein to regulate tyrosine hydroxylase and protein phosphatase 2A in vitro and in vivo.
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 |
Role of TPPP/p25 on α-synuclein-mediated oligodendroglial degeneration and the protective effect of SIRT2 inhibition in a cellular model of multiple system atrophy.
Topics: alpha-Synuclein; Apoptosis; Gene Expression Regulation, Enzymologic; Glycogen Synthase Kinase 3; HEK293 Cells; Humans; Multiple System Atrophy; Nerve Tissue Proteins; Oligodendroglia; Phosphorylation; Serine; Sirtuin 2 | 2010 |
Changes in the solubility and phosphorylation of α-synuclein over the course of Parkinson's disease.
Topics: Aged; Aged, 80 and over; alpha-Synuclein; Analysis of Variance; Disease Progression; Female; Frontal Lobe; Humans; Male; Parkinson Disease; Phosphorylation; Putamen; Serine; Statistics, Nonparametric | 2011 |
α-Syn suppression reverses synaptic and memory defects in a mouse model of dementia with Lewy bodies.
Topics: Acoustic Stimulation; Age Factors; alpha-Synuclein; Analysis of Variance; Animals; Animals, Newborn; Brain; Calcium-Calmodulin-Dependent Protein Kinase Type 2; Conditioning, Classical; Cues; Disease Models, Animal; Disease Progression; Embryo, Mammalian; Fear; Female; Gene Expression Regulation; Glial Fibrillary Acidic Protein; Gliosis; Humans; In Vitro Techniques; Indoles; Lewy Body Disease; Male; Memory Disorders; Mice; Mice, Inbred C57BL; Mice, Transgenic; Mutation; Nerve Degeneration; Nerve Tissue Proteins; Serine; Synapses | 2011 |
α-synuclein phosphorylation and truncation are normal events in the adult human brain.
Topics: Adult; Aged; Aged, 80 and over; alpha-Synuclein; Animals; Brain; Cell Line, Tumor; Female; Humans; Lewy Bodies; Lewy Body Disease; Male; Mass Spectrometry; Mice; Mice, Transgenic; Microscopy, Confocal; Middle Aged; Mutation; Nerve Tissue Proteins; Neuroblastoma; Neurons; Phosphorylation; Postmortem Changes; Protein Structure, Tertiary; Serine; Subcellular Fractions; Time Factors; Transfection | 2012 |
Authentically phosphorylated α-synuclein at Ser129 accelerates neurodegeneration in a rat model of familial Parkinson's disease.
Topics: alpha-Synuclein; Animals; Cell Count; Cell Line, Transformed; Disease Models, Animal; Dopamine Plasma Membrane Transport Proteins; ELAV Proteins; G-Protein-Coupled Receptor Kinases; Gene Expression Regulation; Genetic Vectors; Green Fluorescent Proteins; Humans; Mutation; Neurodegenerative Diseases; Neurons; Parkinson Disease; Phosphorylation; Rats; Rats, Sprague-Dawley; Rats, Transgenic; Serine; Substantia Nigra; Transduction, Genetic; Transfection; Tyrosine 3-Monooxygenase | 2011 |
Superiority of PLK-2 as α-synuclein phosphorylating agent relies on unique specificity determinants.
Topics: alpha-Synuclein; Casein Kinase II; Catalysis; Humans; Peptides; Phosphorylation; Protein Serine-Threonine Kinases; Serine; Tumor Suppressor Proteins | 2012 |
Mimicking phosphorylation at serine 87 inhibits the aggregation of human α-synuclein and protects against its toxicity in a rat model of Parkinson's disease.
Topics: alpha-Synuclein; Animals; Corpus Striatum; Disease Models, Animal; Gene Transfer Techniques; Humans; Male; Mutation; Parkinson Disease; Phosphorylation; Rats; Rats, Wistar; Serine | 2012 |
Increased α-synuclein phosphorylation and nitration in the aging primate substantia nigra.
Topics: Aging; alpha-Synuclein; Animals; Humans; Neurons; Nitro Compounds; Phosphorylation; Protein Processing, Post-Translational; Saimiri; Serine; Substantia Nigra | 2012 |
Changes in properties of serine 129 phosphorylated α-synuclein with progression of Lewy-type histopathology in human brains.
Topics: Aged; Aged, 80 and over; alpha-Synuclein; Female; Gyrus Cinguli; Humans; Lewy Body Disease; Male; Parkinson Disease; Phosphorylation; Serine; Solubility; Temporal Lobe | 2013 |
Role of Ser129 phosphorylation of α-synuclein in melanoma cells.
Topics: alpha-Synuclein; Amino Acid Sequence; Antibodies, Monoclonal; Cell Line, Tumor; Epitope Mapping; Humans; Melanoma; Molecular Sequence Data; Phosphorylation; Serine; Skin Neoplasms | 2013 |
Ser129D mutant alpha-synuclein induces earlier motor dysfunction while S129A results in distinctive pathology in a rat model of Parkinson's disease.
Topics: alpha-Synuclein; Animals; Behavior, Animal; Blotting, Western; Corpus Striatum; Densitometry; Dependovirus; Dopamine; Female; Genetic Vectors; Immunohistochemistry; Movement Disorders; Mutation; Parkinson Disease; Phosphorylation; Rats; Rats, Sprague-Dawley; Serine; Transgenes | 2013 |
Serine 129 phosphorylation of membrane-associated α-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner.
Topics: alpha-Synuclein; Biological Transport; Casein Kinase II; Cell Line; Cell Membrane; Dopamine; G-Protein-Coupled Receptor Kinase 3; G-Protein-Coupled Receptor Kinase 5; G-Protein-Coupled Receptor Kinases; Gene Expression Regulation; HEK293 Cells; Humans; Neurons; Phosphorylation; RNA, Small Interfering; Serine; Signal Transduction | 2013 |
Pramipexole reduces phosphorylation of α-synuclein at serine-129.
Topics: alpha-Synuclein; Antiparkinson Agents; Benzothiazoles; Casein Kinase II; Cell Line, Tumor; Humans; Phosphorylation; Pramipexole; Serine | 2013 |
Divergent α-synuclein solubility and aggregation properties in G2019S LRRK2 Parkinson's disease brains with Lewy Body pathology compared to idiopathic cases.
Topics: Aged; Aged, 80 and over; alpha-Synuclein; Brain; Female; Gene Expression Regulation; Glycine; Humans; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Lewy Bodies; Male; Parkinson Disease; Postmortem Changes; Protein Serine-Threonine Kinases; Serine | 2013 |
In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 α-synuclein phosphorylation in mouse brain.
Topics: alpha-Synuclein; Analysis of Variance; Animals; Brain; Enzyme Inhibitors; Enzyme-Linked Immunosorbent Assay; G-Protein-Coupled Receptor Kinase 5; G-Protein-Coupled Receptor Kinases; Gene Expression Regulation; Mice; Mice, Knockout; Phosphorylation; Protein Serine-Threonine Kinases; Pteridines; RNA, Messenger; Serine | 2014 |
Metformin lowers Ser-129 phosphorylated α-synuclein levels via mTOR-dependent protein phosphatase 2A activation.
Topics: alpha-Synuclein; AMP-Activated Protein Kinases; Animals; Dose-Response Relationship, Drug; Down-Regulation; Enzyme Activation; Gestational Age; HeLa Cells; Hippocampus; Humans; Hypoglycemic Agents; Metformin; Mice; Mice, Inbred C57BL; Neurons; Phosphorylation; Primary Cell Culture; Protein Kinase Inhibitors; Protein Phosphatase 2; Serine; Signal Transduction; Time Factors; TOR Serine-Threonine Kinases; Transfection | 2014 |
Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers.
Topics: 1,2-Dipalmitoylphosphatidylcholine; alpha-Synuclein; Cell Membrane; Humans; Mutation; Phosphatidylcholines; Phosphorylation; Porosity; Protein Binding; Protein Multimerization; Protein Structure, Quaternary; Serine; Temperature; Unilamellar Liposomes | 2014 |
Abnormal serine phosphorylation of insulin receptor substrate 1 is associated with tau pathology in Alzheimer's disease and tauopathies.
Topics: Age Factors; Aged; Aged, 80 and over; alpha-Synuclein; Alzheimer Disease; Analysis of Variance; Animals; Brain; Diet, High-Fat; DNA-Binding Proteins; Female; Humans; Insulin Receptor Substrate Proteins; Male; Mice; Mice, Inbred C57BL; Mice, Transgenic; Middle Aged; Phosphorylation; Serine; tau Proteins; Tauopathies; TDP-43 Proteinopathies | 2014 |
Efficient modification of alpha-synuclein serine 129 by protein kinase CK1 requires phosphorylation of tyrosine 125 as a priming event.
Topics: alpha-Synuclein; Casein Kinase I; Cell Line, Transformed; Green Fluorescent Proteins; Humans; Magnetic Resonance Spectroscopy; Phosphorylation; Serine; Transfection; Tyrosine | 2014 |
Accumulation of α-synuclein in dementia with Lewy bodies is associated with decline in the α-synuclein-degrading enzymes kallikrein-6 and calpain-1.
Topics: alpha-Synuclein; Alzheimer Disease; Brain; Calpain; Case-Control Studies; Cell Line, Tumor; Child; Child, Preschool; Enzyme-Linked Immunosorbent Assay; Female; Gene Expression Regulation; Humans; Kallikreins; Lewy Body Disease; Male; Neuroblastoma; Phosphorylation; RNA, Small Interfering; Serine | 2014 |
Colonic mucosal a-synuclein lacks specificity as a biomarker for Parkinson disease.
Topics: Aged; alpha-Synuclein; Biomarkers; Biopsy; Colon; Female; Humans; Immunohistochemistry; Intestinal Mucosa; Male; Middle Aged; Paraffin Embedding; Parkinson Disease; Predictive Value of Tests; Sensitivity and Specificity; Serine | 2015 |
Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo.
Topics: alpha-Synuclein; Animals; Blotting, Western; Brain; Casein Kinase I; Cell Nucleus; Endoplasmic Reticulum; HEK293 Cells; HeLa Cells; Hippocampus; Humans; Kinetics; Male; Mice, Inbred C57BL; Microscopy, Confocal; Mutation; Parkinson Disease; Phosphorylation; Proteasome Endopeptidase Complex; Protein Serine-Threonine Kinases; Saccharomyces cerevisiae; Serine; Substrate Specificity | 2015 |
Adenoviral-mediated expression of G2019S LRRK2 induces striatal pathology in a kinase-dependent manner in a rat model of Parkinson's disease.
Topics: Adenoviridae; alpha-Synuclein; Animals; Corpus Striatum; Disease Models, Animal; Female; Forelimb; Gene Expression Regulation; Glycine; HEK293 Cells; Humans; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Mutation; Parkinson Disease; Phosphopyruvate Hydratase; Protein Serine-Threonine Kinases; Rats; Rats, Wistar; Serine; Time Factors; Transduction, Genetic; Tubulin | 2015 |
Ser129 phosphorylation of endogenous α-synuclein induced by overexpression of polo-like kinases 2 and 3 in nigral dopamine neurons is not detrimental to their survival and function.
Topics: alpha-Synuclein; Animals; Brain; Cell Cycle Proteins; Cell Survival; Dependovirus; Dopamine; Dopaminergic Neurons; Female; Genetic Vectors; Phosphorylation; Protein Serine-Threonine Kinases; Rats; Rats, Sprague-Dawley; Serine; Substantia Nigra | 2015 |
Sensitive western blotting for detection of endogenous Ser129-phosphorylated α-synuclein in intracellular and extracellular spaces.
Topics: alpha-Synuclein; Animals; Blotting, Western; Brain; Cell Line, Tumor; Codon; Extracellular Space; Humans; Intracellular Space; Phosphorylation; Rats; Sensitivity and Specificity; Serine | 2015 |
Effects of Serine 129 Phosphorylation on α-Synuclein Aggregation, Membrane Association, and Internalization.
Topics: alpha-Synuclein; Amino Acid Substitution; Animals; Animals, Newborn; Cell Line; Cells, Cultured; Dopaminergic Neurons; Endocytosis; Humans; Mesencephalon; Mice; Mutation; Parkinson Disease; Phosphorylation; Protein Aggregation, Pathological; Protein Folding; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Recombinant Fusion Proteins; Recombinant Proteins; Serine; Synaptosomes | 2016 |
Intracellular repair of oxidation-damaged α-synuclein fails to target C-terminal modification sites.
Topics: alpha-Synuclein; Amino Acid Motifs; Humans; Magnetic Resonance Spectroscopy; Methionine; Oxidation-Reduction; Oxidative Stress; Parkinson Disease; Phosphorylation; Serine | 2016 |
C-Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α-Synuclein in a Yeast Model of Parkinson's Disease.
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 |
Novel antibodies to phosphorylated α-synuclein serine 129 and NFL serine 473 demonstrate the close molecular homology of these epitopes.
Topics: alpha-Synuclein; Animals; Antibodies; Brain; Casein Kinase II; Cells, Cultured; Epitopes; Escherichia coli; Female; Humans; Hybridomas; Mice, Inbred BALB C; Mice, Inbred C57BL; Mice, Transgenic; Neurofilament Proteins; Phosphorylation; Protein Serine-Threonine Kinases; Recombinant Proteins; Sequence Homology, Amino Acid; Serine; Spinal Cord | 2016 |
β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor.
Topics: alpha-Synuclein; Amino Acid Motifs; Amino Acid Sequence; Amyloid; Amyloid beta-Peptides; Humans; Islet Amyloid Polypeptide; Models, Molecular; Protein Aggregates; Protein Binding; Protein Structure, Secondary; Recombinant Proteins; Serine | 2016 |
Development and characterization of polo-like kinase 2 loaded nanoparticles-A novel strategy for (serine-129) phosphorylation of alpha-synuclein.
Topics: alpha-Synuclein; Cell Line; Dopaminergic Neurons; Drug Delivery Systems; Humans; Nanoparticles; Parkinson Disease; Phosphorylation; Protein Serine-Threonine Kinases; Serine | 2016 |
Dissecting the Molecular Pathway Involved in PLK2 Kinase-mediated α-Synuclein-selective Autophagic Degradation.
Topics: alpha-Synuclein; Autophagy; Catalysis; HEK293 Cells; Humans; Mutation; Phosphorylation; Plasmids; Protein Interaction Mapping; Protein Processing, Post-Translational; Protein Serine-Threonine Kinases; Proteolysis; Serine; Tumor Suppressor Proteins; Ubiquitin | 2017 |
O-GlcNAcylation of α-Synuclein at Serine 87 Reduces Aggregation without Affecting Membrane Binding.
Topics: Acetylglucosamine; Acylation; alpha-Synuclein; Cell Membrane; Escherichia coli; Protein Binding; Serine | 2017 |
The Sulfur-Linked Analogue of O-GlcNAc (S-GlcNAc) Is an Enzymatically Stable and Reasonable Structural Surrogate for O-GlcNAc at the Peptide and Protein Levels.
Topics: Acetylglucosamine; alpha-Synuclein; Animals; beta-N-Acetylhexosaminidases; Circular Dichroism; Computational Biology; Humans; Models, Molecular; Nuclear Magnetic Resonance, Biomolecular; Peptide Fragments; Protein Folding; Protein Processing, Post-Translational; Protein Stability; Recombinant Proteins; Serine; Substrate Specificity; Threonine | 2017 |
Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding.
Topics: alpha-Synuclein; Autopsy; Binding Sites; Brain; Humans; Parkinson Disease; Phosphorylation; Protein Binding; Protein Processing, Post-Translational; Serine; Single-Domain Antibodies; Tyrosine | 2018 |
Methionine sulfoxide reductase A (MsrA) mediates the ubiquitination of 14-3-3 protein isotypes in brain.
Topics: 14-3-3 Proteins; alpha-Synuclein; Amino Acid Sequence; Animals; Archaeal Proteins; Binding, Competitive; Brain; Brain Chemistry; Dopamine; Lysine; Methionine; Methionine Sulfoxide Reductases; Mice; Mice, Knockout; Phosphorylation; Protein Binding; Protein Isoforms; Protein Processing, Post-Translational; Serine; Ubiquitin; Ubiquitin-Protein Ligases; Ubiquitination | 2018 |
δ-Opioid Receptor Activation Attenuates the Oligomer Formation Induced by Hypoxia and/or α-Synuclein Overexpression/Mutation Through Dual Signaling Pathways.
Topics: alpha-Synuclein; Animals; Benzimidazoles; Cell Hypoxia; Cell Survival; Cyclic AMP Response Element-Binding Protein; HEK293 Cells; Humans; Models, Biological; Mutant Proteins; Mutation; Oligopeptides; PC12 Cells; Phosphorylation; Protein Deglycase DJ-1; Protein Multimerization; Protein Serine-Threonine Kinases; Rats; Receptors, Opioid, delta; Serine; Signal Transduction | 2019 |
Monitoring α-synuclein multimerization in vivo.
Topics: alpha-Synuclein; Amyloid; Animals; Disease Models, Animal; Drosophila melanogaster; Male; Phosphorylation; Protein Multimerization; Reactive Oxygen Species; Serine | 2019 |
Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils.
Topics: alpha-Synuclein; Amyloid; Kinetics; Lipid Bilayers; Molecular Structure; Phase Transition; Protein Binding; Serine; Structure-Activity Relationship; Thermodynamics; Transition Temperature | 2019 |
p38 MAPK-DRP1 signaling is involved in mitochondrial dysfunction and cell death in mutant A53T α-synuclein model of Parkinson's disease.
Topics: alpha-Synuclein; Animals; Apoptosis; Cell Line, Tumor; Dynamins; Humans; Imidazoles; MAP Kinase Signaling System; Mice; Mitochondria; Mitochondrial Dynamics; Mutation; Neurons; Oxidative Stress; p38 Mitogen-Activated Protein Kinases; Parkinson Disease; Phosphorylation; Pyridines; Reactive Oxygen Species; Serine | 2020 |
Generation of monoclonal antibodies against phosphorylated α-Synuclein at serine 129: Research tools for synucleinopathies.
Topics: alpha-Synuclein; Animals; Antibodies, Monoclonal; Cells, Cultured; Dose-Response Relationship, Drug; Female; Humans; Mice; Mice, Inbred BALB C; Phosphorylation; Serine; Synucleinopathies | 2020 |
Investigating the presence of doubly phosphorylated α-synuclein at tyrosine 125 and serine 129 in idiopathic Lewy body diseases.
Topics: Aged; Aged, 80 and over; alpha-Synuclein; Animals; Female; Humans; Lewy Body Disease; Male; Mice; Phosphorylation; Protein Processing, Post-Translational; Serine; Tyrosine | 2020 |
S-Nitrosylation of G protein-coupled receptor kinase 6 and Casein kinase 2 alpha modulates their kinase activity toward alpha-synuclein phosphorylation in an animal model of Parkinson's disease.
Topics: Age Factors; alpha-Synuclein; Animals; Casein Kinase II; Disease Models, Animal; G-Protein-Coupled Receptor Kinases; Gene Deletion; HEK293 Cells; Humans; Mice; Mice, Transgenic; Mutation; Nitric Oxide; Nitric Oxide Synthase Type I; Nitroarginine; Nitrosative Stress; Parkinson Disease; Phosphorylation; Serine | 2020 |
Role of alpha-synuclein phosphorylation at Serine 129 in methamphetamine-induced neurotoxicity in vitro and in vivo.
Topics: alpha-Synuclein; Animals; Cell Line; Central Nervous System Stimulants; Humans; Male; Methamphetamine; Mice; Mice, Inbred C57BL; Neurons; Neurotoxicity Syndromes; Phosphorylation; Protein Aggregation, Pathological; Serine | 2020 |
Structural brain changes in Ser129-phosphorylated alpha-synuclein rats based on voxel-based morphometry.
Topics: alpha-Synuclein; Animals; Brain; Disease Models, Animal; Male; Medial Forebrain Bundle; Parkinson Disease; Phosphorylation; Protein Aggregation, Pathological; Rats, Sprague-Dawley; Serine | 2020 |
Behavioral Deficits and Brain α-Synuclein and Phosphorylated Serine-129 α-Synuclein in Male and Female Mice Overexpressing Human α-Synuclein.
Topics: alpha-Synuclein; Animals; Behavior, Animal; Brain; Brain Chemistry; Enzyme-Linked Immunosorbent Assay; Female; Humans; Male; Mice; Mice, Inbred C57BL; Mice, Transgenic; Phosphorylation; Serine; Sex Factors | 2021 |
In vivo aggregation of presynaptic alpha-synuclein is not influenced by its phosphorylation at serine-129.
Topics: alpha-Synuclein; Animals; Animals, Genetically Modified; Disease Models, Animal; Humans; Parkinson Disease; Phosphorylation; Presynaptic Terminals; Protein Aggregation, Pathological; Serine; Zebrafish | 2021 |
GBA Mutations Influence the Release and Pathological Effects of Small Extracellular Vesicles from Fibroblasts of Patients with Parkinson's Disease.
Topics: alpha-Synuclein; Cells, Cultured; Extracellular Vesicles; Fibroblasts; Glucosylceramidase; Humans; Mutation; Parkinson Disease; Serine | 2021 |
Polo-like kinase 2 inhibition reduces serine-129 phosphorylation of physiological nuclear alpha-synuclein but not of the aggregated alpha-synuclein.
Topics: alpha-Synuclein; Animals; Brain; Dopamine; Lewy Bodies; Mice; Mice, Inbred C57BL; Neurons; Parkinson Disease; Phosphorylation; Protein Aggregates; Protein Serine-Threonine Kinases; Serine | 2021 |
Tyrosine 136 phosphorylation of α-synuclein aggregates in the Lewy body dementia brain: involvement of serine 129 phosphorylation by casein kinase 2.
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 |
Phosphorylation of the aggregate-forming protein alpha-synuclein on serine-129 inhibits its DNA-bending properties.
Topics: alpha-Synuclein; DNA; Neurodegenerative Diseases; Phosphorylation; Serine; Structure-Activity Relationship | 2022 |
α-Synuclein phosphorylation at serine 129 occurs after initial protein deposition and inhibits seeded fibril formation and toxicity.
Topics: alpha-Synuclein; Amyloid; Humans; Lewy Body Disease; Parkinson Disease; Phosphorylation; Protein Aggregates; Protein Aggregation, Pathological; Serine | 2022 |
High-content phenotyping of Parkinson's disease patient stem cell-derived midbrain dopaminergic neurons using machine learning classification.
Topics: alpha-Synuclein; Dopaminergic Neurons; Humans; Induced Pluripotent Stem Cells; Inducible T-Cell Co-Stimulator Protein; Leucine-Rich Repeat Serine-Threonine Protein Kinase-2; Machine Learning; Mesencephalon; Mutation; Parkinson Disease; Serine | 2022 |
Mutation of Tyrosine Sites in the Human Alpha-Synuclein Gene Induces Neurotoxicity in Transgenic Mice with Soluble Alpha-Synuclein Oligomer Formation.
Topics: alpha-Synuclein; Animals; Humans; Mice; Mice, Transgenic; Mutation; Neurotoxicity Syndromes; Phenylalanine; Serine; Tyrosine | 2022 |
Calcium/calmodulin-dependent serine protein kinase exacerbates mitochondrial calcium uniporter-related mitochondrial calcium overload by phosphorylating α-synuclein in Parkinson's disease.
Topics: alpha-Synuclein; Calcium; Calmodulin; Humans; Parkinson Disease; Protein Kinases; Serine | 2023 |
Implications of In Vitro Multi-Serine Phosphorylation of Alpha-Synuclein in Aggregation and Cytotoxicity.
Topics: alpha-Synuclein; Humans; Neuroblastoma; Parkinson Disease; Phosphorylation; Serine | 2023 |
Dynamic reversibility of α-synuclein serine-129 phosphorylation is impaired in synucleinopathy models.
Topics: alpha-Synuclein; Animals; Parkinson Disease; Phosphorylation; Rats; Serine; Synucleinopathies | 2023 |