Compounds > thioflavin t
Page last updated: 2024-08-22

thioflavin t and alpha-synuclein

thioflavin t has been researched along with alpha-synuclein in 125 studies

Research

Studies (125)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (1.60)18.2507
2000's37 (29.60)29.6817
2010's62 (49.60)24.3611
2020's24 (19.20)2.80

Authors

AuthorsStudies
Curran, MD; El-Agnaf, OM; Jakes, R; Wallace, A1
Bianchi, E; Curran, MD; El-Agnaf, OM; Ingenito, R; Jakes, R; Middleton, D; Neill, D; Pessi, A; Wallace, A1
Conway, KA; Ding, TT; Lansbury, PT; Lee, SJ; Rochet, JC; Williamson, RE1
Conway, KA; Harper, JD; Lansbury, PT1
Farer, M; Hardy, J; Lee, JM; Ostrerova-Golts, N; Petrucelli, L; Wolozin, B1
Chung, KC; Kim, J; Kim, YS; Lee, D; Lee, EK; Paik, SR; Sung, JY1
Duda, JE; Giasson, BI; Golbe, LI; Lee, VM; Mabon, ME; Miller, DC; Trojanowski, JQ1
Antony, T; Cherny, D; Heim, G; Hoyer, W; Jovin, TM; Subramaniam, V1
Choi, SY; Kang, JH; Kang, TC; Kim, KS; Kwon, HY; Won, MH1
Fink, AL; Munishkina, LA; Phelan, C; Uversky, VN1
Du, HN; Hu, HY; Hu, J; Li, HT; Luo, XY; Tang, L; Zhou, JW1
Emadi, S; Liu, R; Lyubchenko, Y; McAllister, C; Messer, A; Schulz, P; Sierks, MR; Yuan, B1
Fink, AL; Han, S; Kaylor, J; Rajamani, S; Zhou, F; Zhu, M1
Fernández, CO; Griesinger, C; Hoyer, W; Jares-Erijman, EA; Jovin, TM; Subramaniam, V; Zweckstetter, M1
Dauer, WT; Dietrich, P; Rideout, HJ; Stefanis, L; Wang, Q1
Christodoulou, J; Dedmon, MM; Dobson, CM; Wilson, MR1
Ali, FE; Barnham, KJ; Bottomley, SP; Cappai, R; Cherny, RA; Culvenor, JG; Curtain, CC; Galatis, D; Hill, AF; Leck, SL; Masters, CL; Sharples, RA; Smith, DP; Tew, DJ; Williamson, NA1
Minichiello, L; Unsicker, K; von Bohlen und Halbach, O1
Hongo, K; Kawata, Y; Kusaka, E; Mizobata, T; Yagi, H1
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
Alfonso, A; Burnam, L; Hoener, M; Liu, L; Perier, C; Przedborski, S; Rodrigues, CM; Saha, S; Sluder, A; Steer, C; Ved, R; Westlund, B; Wolozin, B1
Lev, N; Melamed, E; Offen, D1
Naiki, H; Noguchi-Shinohara, M; Ono, K; Yamada, M; Yoshita, M1
Ono, K; Yamada, M1
Hirohata, M; Ono, K; Yamada, M1
Ahn, JS; Kim, JH; Lee, JH; Paik, SR1
Austin, CP; Honson, NS; Huang, W; Inglese, J; Johnson, RL; Kuret, J1
Crowther, RA; Fraser, G; Goedert, M; Jakes, R; Serpell, LC; Zibaee, S1
Cappai, R; Carver, JA; Jankova, L; Rekas, A; Thorn, DC1
Danzer, KM; Duan, W; Finger, S; Garidel, P; Giese, A; Glabe, CG; Habeck, M; Heinzelmann, U; Högen, T; Kostka, M; Kretzschmar, H; Levin, J; Ross, CA; Wagner, R; Wirth, A1
Battistin, L; Bellucci, A; Collo, G; Missale, C; Sarnico, I; Spano, P1
Rao, KS1
Ko, HH; Ko, LW; Kulathingal, JG; Lin, WL; Yen, SH1
Choe, YJ; Gai, WP; Hahn, JS; Kang, S; Kim, HY; Lee, IH; Lee, JH; Paik, SR1
Fink, AL; Hong, DP; Uversky, VN1
Chiappe, D; Grimminger, V; Hang, I; Lashuel, HA; Moniatte, M; Pignat, V; Schmid, AW1
Hirohata, M; Ikeda, T; Morinaga, A; Ono, K; Yamada, M1
Cheng, H; Wang, CC; Wang, L1
Ahmad, A1
Giasson, BI; Waxman, EA1
Giehm, L; Otzen, DE1
Carver, JA; Christodoulou, J; Devlin, GL; Dobson, CM; Ecroyd, H; Knowles, TP; Meehan, S; Skepper, JN; Waudby, CA; Welland, ME1
Björklund, A; Brundin, P; Englund, E; Li, JY; Lindvall, O; Rehncrona, S; Widner, H1
Haddix, T; Lee, VM; Nakashima-Yasuda, H; Robinson, J; Trojanowski, JQ; Uryu, K1
Jiang, H; Li, WJ; Song, N; Xie, JX1
Goto, Y; Hongo, K; Ito, N; Kawata, Y; Mizobata, T; Ogawa, S; Sakane, I; Takeuchi, H; Yagi, H1
Abedini, A; Meng, F; Plesner, A; Raleigh, DP; Verchere, CB1
Bae, SY; Hwang, H; Kim, HK; Kim, JH; Kim, S; Kim, TD; Lee, S; Yoon, HC1
Fink, AL; Han, S; Hong, DP; Uversky, VN1
Chang, JY; Hong, DP; Jiang, C; Xiong, W1
Jethva, PN; Makwana, PK; Roy, I1
C Serpell, L; Cherny, I; Crockett, R; Gazit, E; Kearn, G; P Jarvis, S; S Mostaert, A1
Andersen, NH; Bisaglia, M; Bubacco, L; Huggins, KN; Kapurniotu, A; Tatarek-Nossol, M1
Ikeda, T; Mochizuki, H; Nihira, T; Ono, K; Takasaki, J; Teplow, DB; Yamada, M1
Bannach, O; Birkmann, E; Funke, SA; Hübinger, S; Willbold, D1
Dikiy, I; Eliezer, D; Fares, MB; Fauvet, B; Lashuel, HA; Samuel, F; Tandon, A1
Ikeda, T; Ono, K; Takahashi, R; Yamada, M1
Coffey, MP; Dang, L; Klaver, AC; Loeffler, DA; Smith, LM1
Abedini, A; Bhattacharya, M; Cao, P; Ladiwala, AR; Langen, R; Perchiacca, JM; Raleigh, DP; Schmidt, AM; Tessier, PM; Varkey, J1
Brucale, M; Bubacco, L; Codolo, G; de Bernard, M; Plotegher, N; Pozzobon, T; Tessari, I1
Egoz-Matia, N; Frenkel-Pinter, M; Gazit, E; Levy-Sakin, M; Masliah, E; Patrick, C; Rockenstein, E; Schiller, A; Segal, D; Shaltiel-Karyo, R1
Christiansen, G; Giehm, L; Kyrsting, A; Langkilde, AE; Macchi, F; Manno, M; Nielsen, NC; Nielsen, SB; Oddershede, L; Otzen, DE; Raccosta, S; Svane, AS; Vestergaard, B1
Casadei, N; De Heer, R; Kahle, PJ; Klucken, J; Krüger, R; Lucas, JJ; Noldus, LP; Nuber, S; Pöhler, AM; Riess, O; Schwedhelm, I; Spruijt, B; Tomás-Zapico, C; Torres-Peraza, J; Witz, A; Zamolo, I1
Berrocal, R; Indi, SS; Rao, KS; Sambasiva Rao, KR; Vasudevaraju, P1
Bongarzone, ER; Cantuti-Castelvetri, L; Celej, MS; Claycomb, KI; Crocker, SJ; Gallea, JI; Givogri, MI; Li, G; Lopez-Rosas, A; Marshall, MS; Santos, MB; Smith, BR; van Breemen, R1
Anoop, A; Chakraborty, C; Das, S; Dutta, P; Ghosh, D; Jacob, RS; Jha, NN; Maji, SK; Malik, S; Mankar, S; Mondal, M; Singh, PK1
Calabrese, AN; Carver, JA; Liu, Y; Pukala, TL1
Coelho-Cerqueira, E; Follmer, C; Pinheiro, AS1
Bose, A; Chowdhury, PK; Gautam, S; Karmakar, S1
Claessens, MM; Iyer, A; Petersen, NO; Subramaniam, V1
Bartels, T; Kristal, BS; Luth, ES; Selkoe, DJ; Stavrovskaya, IG1
Basak, S; Chattopadhyay, K; Prasad, GV; Varkey, J1
Breydo, L; Morgan, D; Uversky, VN1
Rochet, JC; Stanciu, LA; Zhang, H1
Chorell, E; Edlund, H; Sharma, SK; Steneberg, P; Vernersson-Lindahl, E; Wittung-Stafshede, P1
Cremades, N; Dalla Serra, M; Dear, AJ; Dobson, CM; Horrocks, MH; Klenerman, D; Knowles, TP; Tosatto, L1
Baekelandt, V; Debyser, Z; Deleersnijder, A; Gerard, M; Macchi, F; Michiels, A; Munck, S; Pottel, H; Van den Haute, C1
Segers-Nolten, I; Sidhu, A; Subramaniam, V1
Decossas-Mendoza, M; Krisa, S; Lambert, O; Mérillon, JM; Richard, T; Temsamani, H1
Breydo, L; Jäger, AK; Jorgensen, L; Lobbens, ES; Skamris, T; Uversky, V; van de Weert, M; Vestergaard, B1
Bickle, L; Hopwood, JJ; Karageorgos, L1
Hasegawa, M; Higuchi, M; Hisanaga, SI; Imura, S; Masuda-Suzukake, M; Ono, M; Shimozawa, A; Takahara, D; Tarutani, A; Yanai, K1
Claessens, MM; Raussens, V; Segers-Nolten, I; Sidhu, A; Subramaniam, V1
Aigbirhio, FI; Buell, AK; Fisher, E; Janik, M; Richardson, R; Tóth, G; Zhao, Y1
Chen, Y; Jiang, F; Lei, H; Li, JD; Ma, YT; Tan, J; Zhang, J; Zhang, Y1
Kumar, H; Kumari, P; Singh, J; Udgaonkar, JB1
Davis, TP; Ding, F; Kakinen, A; Ke, PC; Nowell, CJ; Pilkington, EH; Sun, Y; Wang, B; Wang, M; Xing, Y1
Abeyawardhane, DL; Crozier, MK; Fernández, RD; Forney, AK; Heitger, DR; Lucas, HR; Murgas, CJ1
Antifeeva, IA; Kuznetsova, IM; Povarova, OI; Rodina, NP; Sulatskaya, AI; Sulatsky, MI; Turoverov, KK1
Baatsen, P; Herrebout, WA; Johannessen, C; Keiderling, TA; Lambeir, AM; Van de Vondel, E; Van Elzen, R1
Ahn, DR; Doohun Kim, T; Kim, KK; Kim, KR; Le, LTHL; Lee, JH; Ryu, BH; Toth, G; Wang, Y; Yoo, WK1
Blum, C; Segers-Nolten, I; Sidhu, A; Subramaniam, V; Vaneyck, J1
Bhaskar, K; Chi, EY; Fanni, AM; Lin, CY; Monge, FA; Thapa, A; Whitten, DG1
Anantharam, V; Hepker, M; Huang, X; Jin, H; Kanthasamy, A; Kanthasamy, AG; Kondru, N; Lewis, M; Manne, S1
Ghasemi, Y; Javdani, N; Raheb, J; Rahpeyma, SS1
Andreasen, M; Barker, RA; Fazal, SV; Fragniere, AMC; Scott, K; Stott, SRW1
Adame, A; Aguzzi, A; Boersema, PJ; Courtheoux, T; Enchev, RI; Gerez, JA; Herrmann, US; Masliah, E; Peter, M; Picotti, P; Prymaczok, NC; Riek, R; Rockenstein, E; Schwarz, P1
Abou-Zied, OK; Akhtari, K; Aziz, FM; Falahati, M; Mustafa, TA; Salihi, A; Shahpasand, K; Tahaei Gilan, SS; Yahya Rayat, D1
Alasady, AA; Aziz, FM; Falahati, M; Hasan, A; Khaki, PA; Qadir Nanakali, NM; Salihi, A; Shahpasand, K; Sharifi, M; Zand, Z1
Abdulqadir, SZ; Abou-Zied, OK; Akhtari, K; Alasady, AA; Aziz, FM; Falahati, M; Hasan, A; Jabbari, S; Naskhi, A; Othman, GQ; Salihi, A; Sari, S; Sharifi, M1
Chau, E; Kim, JR; Wood, A; Yang, Y1
Bondia, P; Del Valle, A; Flors, C; Kanai, M; Nonell, S; Sawazaki, T; Sohma, Y; Sot, B; Tone, CM; Torra, J1
Afitska, K; Priss, A; Shvadchak, VV; Yushchenko, DA1
Candreva, J; Chau, E; Kim, JR; Rice, ME1
Alijanvand, SH; Christensen, MH; Christiansen, G; Harikandei, KB; Moosavi-Movahedi, AA; Otzen, DE; Salehi, P; Schiøtt, B1
Ådén, J; Andersson, PO; Karlsson, BCG; Näsström, T; Shibata, F1
Amininasab, M; Davoodi, J; Saffari, B; Sheikhi, S1
Chang, KH; Chao, CY; Chen, CM; Chen, WL; Huang, YT; Lee-Chen, GJ; Lin, CH; Lin, CY; Lin, JL; Su, MT; Wu, YR; Yen, CY1
Chiki, A; De Simone, A; Fusco, G; Lashuel, HA; Mela, I; Moons, R; Phillips, JJ; Schierle, GSK; Seetaloo, N; Sobott, F; Stephens, AD; Woodhams, PJ; Zacharopoulou, M1
Barinova, K; Kudryavtseva, S; Melnikova, A; Muronetz, VI; Pozdyshev, D1
Dazzi, A; Deniset-Besseau, A; Raussens, V; Ruysschaert, JM; Van Hemelryck, V; Waeytens, J1
Genov, M; Hummel, T; Kasture, A; Krenn, L; Moloney, M; Pretsch, A; Pretsch, D; Rollinger, JM; Schmid, A; Wöhrer, T1
Bariås, E; Furse, S; George, V; Govasli, ML; Halskau, Ø; Iashchishyn, IA; Jakubec, M; Morozova-Roche, LA; Turcu, D1
Bertoni, M; Bezard, E; Claverol, S; Daniel, J; De Giorgi, F; Doudnikoff, E; Dutheil, N; Faggiani, E; Grélard, A; Habenstein, B; Ichas, F; Laferrière, F; Lends, A; Loquet, A; Morvan, E; Qin, C; Yu, X; Zinghirino, F1
Hongo, K; Ishii, A; Kawata, Y; Mizobata, T; Ogawa, K; Shindo, A; Sogon, T1
Mikalauskaite, K; Smirnovas, V; Sneideris, T; Ziaunys, M1
Hunter, CA; Kocsis, I; Sanna, E1
Baum, J; Hoop, CL; Wang, B; Williams, JK; Yang, X1
Jiang, L; Liu, F; Lu, F; Sang, J; Wang, F; Wang, W; Wang, X; Wang, Y1
Fukuhara, T; Hatano, T; Hattori, N; Imai, Y; Nukina, N; Okuzumi, A; Ueno, S1
Alijanvand, SH; Burdukiewicz, M; Christensen, LFB; Dueholm, MS; Herbst, FA; Kjeldal, H; Otzen, DE1
Buell, AK; Farzadfard, A; Galvagnion, C; Jensen, H; Larsen, JA; Norrild, RK; Petersen, D; Ray, S; Stender, EGP1
Aguayo, LG; Armijo-Weingart, L; Boopathi, S; Burgos, CF; Fernández-Pérez, EJ; González, W; Olivos, N; Pacheco, CR; Ramirez, AE1
Aguirre, C; Baba, K; Choong, CJ; Doi, J; Goto, Y; Hideshima, M; Ikenaka, K; Kakuda, K; Kimura, Y; Mochizuki, H; Nabekura, K; Nagai, Y; Nagano, S; Nakajima, K; Takeuchi, T; Yamaguchi, K1

Other Studies

125 other study(ies) available for thioflavin t and alpha-synuclein

ArticleYear
Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of alpha-synuclein protein implicated in Parkinson's disease.
    FEBS letters, 1998, Nov-27, Volume: 440, Issue:1-2

    Topics: alpha-Synuclein; Amino Acid Substitution; Amyloid; Benzothiazoles; Biopolymers; Circular Dichroism; Dimerization; Humans; Hydrogen-Ion Concentration; Lewy Bodies; Microscopy, Electron; Mutation; Nerve Tissue Proteins; Parkinson Disease; Protein Structure, Secondary; Recombinant Proteins; Synucleins; Thiazoles

1998
Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments.
    FEBS letters, 1998, Nov-27, Volume: 440, Issue:1-2

    Topics: alpha-Synuclein; Amyloid; Apoptosis; Benzothiazoles; Biopolymers; Cell Nucleus; Cell Survival; Circular Dichroism; Humans; Microscopy, Electron; Mutation; Nerve Tissue Proteins; Neuroblastoma; Neurodegenerative Diseases; Neurons; Parkinson Disease; Peptides; Protein Structure, Secondary; Synucleins; Thiazoles; Tumor Cells, Cultured

1998
Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.
    Proceedings of the National Academy of Sciences of the United States of America, 2000, Jan-18, Volume: 97, Issue:2

    Topics: Age of Onset; alpha-Synuclein; Amino Acid Substitution; Amyloid; Benzothiazoles; Chromatography, Gel; Circular Dichroism; Fluorescence; Humans; Microscopy, Atomic Force; Mutation; Nerve Tissue Proteins; Parkinson Disease; Protein Conformation; Synucleins; Thiazoles; Ultracentrifugation

2000
Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid.
    Biochemistry, 2000, Mar-14, Volume: 39, Issue:10

    Topics: Alanine; alpha-Synuclein; Amino Acid Sequence; Amyloid; Benzothiazoles; Binding Sites; Brain; Circular Dichroism; Congo Red; Endopeptidases; Humans; Hydrolysis; Immunohistochemistry; Lewy Bodies; Microscopy, Atomic Force; Microscopy, Polarization; Molecular Sequence Data; Mutation, Missense; Nerve Tissue Proteins; Parkinson Disease; Postmortem Changes; Proline; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Synucleins; Thiazoles; Threonine

2000
The A53T alpha-synuclein mutation increases iron-dependent aggregation and toxicity.
    The Journal of neuroscience : the official journal of the Society for Neuroscience, 2000, Aug-15, Volume: 20, Issue:16

    Topics: alpha-Synuclein; Benzothiazoles; Cell Survival; Free Radicals; Humans; Inclusion Bodies; Iron; Lewy Bodies; Mutation; Nerve Tissue Proteins; Neuroblastoma; Neurons; Oxidative Stress; Parkinson Disease; Synucleins; Thiazoles; Tumor Cells, Cultured; Ubiquitins

2000
Multiple ligand interaction of alpha-synuclein produced various forms of protein aggregates in the presence of Abeta25-35, copper, and eosin.
    Brain research, 2001, Jul-20, Volume: 908, Issue:1

    Topics: alpha-Synuclein; Amyloid beta-Peptides; Benzothiazoles; Cells, Cultured; Copper; Eosine Yellowish-(YS); Fluorescent Dyes; Ligands; Microscopy, Electron; Nerve Tissue Proteins; Neurodegenerative Diseases; Peptide Fragments; Polymers; Protein Structure, Tertiary; Synucleins; Thiazoles

2001
Concurrence of alpha-synuclein and tau brain pathology in the Contursi kindred.
    Acta neuropathologica, 2002, Volume: 104, Issue:1

    Topics: Adult; alpha-Synuclein; Archives; Benzothiazoles; Brain; Fluorescent Antibody Technique; Fluorescent Dyes; Humans; Male; Microscopy, Immunoelectron; Nerve Degeneration; Nerve Tissue Proteins; Neurons; Parkinson Disease; Synucleins; tau Proteins; Thiazoles

2002
Dependence of alpha-synuclein aggregate morphology on solution conditions.
    Journal of molecular biology, 2002, Sep-13, Volume: 322, Issue:2

    Topics: alpha-Synuclein; Benzothiazoles; Circular Dichroism; Humans; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Ions; Kinetics; Magnesium; Microscopy, Atomic Force; Microscopy, Electron; Nerve Tissue Proteins; Osmolar Concentration; Protein Binding; Protein Structure, Quaternary; Sodium; Solutions; Synucleins; Thiazoles

2002
The ceruloplasmin and hydrogen peroxide system induces alpha-synuclein aggregation in vitro.
    Biochimie, 2002, Volume: 84, Issue:7

    Topics: alpha-Synuclein; Benzothiazoles; Ceruloplasmin; Humans; Hydrogen Peroxide; Hydroxyl Radical; Immunoblotting; Microscopy, Electron; Nerve Tissue Proteins; Protein Folding; Spectrometry, Fluorescence; Staining and Labeling; Synucleins; Thiazoles

2002
Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes.
    Biochemistry, 2003, Mar-11, Volume: 42, Issue:9

    Topics: Alcohols; alpha-Synuclein; Benzothiazoles; Circular Dichroism; Ethanol; Fluorescent Dyes; Humans; Kinetics; Light; Models, Chemical; Nerve Tissue Proteins; Phospholipids; Propanols; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Scattering, Radiation; Solvents; Spectroscopy, Fourier Transform Infrared; Synucleins; Thiazoles; Trifluoroethanol

2003
A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein.
    Biochemistry, 2003, Jul-29, Volume: 42, Issue:29

    Topics: Alanine; alpha-Synuclein; Amino Acid Motifs; Benzothiazoles; Circular Dichroism; Escherichia coli; Glycine; Humans; Microscopy, Atomic Force; Mutagenesis, Site-Directed; Mutation; Nerve Tissue Proteins; Peptides; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Synucleins; Thiazoles; Time Factors; Valine

2003
Inhibiting aggregation of alpha-synuclein with human single chain antibody fragments.
    Biochemistry, 2004, Mar-16, Volume: 43, Issue:10

    Topics: alpha-Synuclein; Amino Acid Sequence; Benzothiazoles; Binding Sites, Antibody; Epitope Mapping; Fluorescent Dyes; Humans; Immunoglobulin Variable Region; Inovirus; Kinetics; Microscopy, Atomic Force; Molecular Sequence Data; Nerve Tissue Proteins; Peptide Library; Protein Structure, Tertiary; Recombinant Proteins; Solubility; Synucleins; Thiazoles

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
NMR of alpha-synuclein-polyamine complexes elucidates the mechanism and kinetics of induced aggregation.
    The EMBO journal, 2004, May-19, Volume: 23, Issue:10

    Topics: alpha-Synuclein; Amino Acid Sequence; Benzothiazoles; Binding Sites; Fluorescent Dyes; Humans; Molecular Sequence Data; Molecular Structure; Nerve Tissue Proteins; Nuclear Magnetic Resonance, Biomolecular; Parkinson Disease; Polyamines; Protein Structure, Secondary; Synucleins; Thiazoles

2004
alpha-synuclein is required for the fibrillar nature of ubiquitinated inclusions induced by proteasomal inhibition in primary neurons.
    The Journal of biological chemistry, 2004, Nov-05, Volume: 279, Issue:45

    Topics: Acetylcysteine; alpha-Synuclein; Animals; Apoptosis; Benzothiazoles; Blotting, Western; Cells, Cultured; Cytoplasm; Genotype; Lewy Bodies; Mice; Mice, Knockout; Microscopy, Fluorescence; Nerve Tissue Proteins; Neurons; Protease Inhibitors; Proteasome Inhibitors; Rats; Synucleins; Thiazoles; Time Factors; Ubiquitin

2004
Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species.
    The Journal of biological chemistry, 2005, Apr-15, Volume: 280, Issue:15

    Topics: alpha-Synuclein; Benzothiazoles; Chromatography, Gel; Circular Dichroism; Flow Cytometry; Genetic Vectors; HSP70 Heat-Shock Proteins; Humans; Lewy Bodies; Magnetic Resonance Spectroscopy; Microscopy, Electron; Microscopy, Fluorescence; Molecular Chaperones; Nerve Tissue Proteins; Protein Binding; Protein Folding; Protein Structure, Secondary; Subcellular Fractions; Synucleins; Thiazoles; Time Factors

2005
Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway.
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2005, Volume: 19, Issue:10

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Circular Dichroism; Dopamine; Ferric Compounds; Humans; Parkinson Disease; Protein Folding; Protein Structure, Secondary; Sodium Dodecyl Sulfate; Thiazoles

2005
Haploinsufficiency for trkB and trkC receptors induces cell loss and accumulation of alpha-synuclein in the substantia nigra.
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2005, Volume: 19, Issue:12

    Topics: Aging; Alkaloids; alpha-Synuclein; Animals; Axons; Benzothiazoles; Brain-Derived Neurotrophic Factor; Crosses, Genetic; Densitometry; Dopamine; Fluorescent Dyes; Heterozygote; Immunohistochemistry; Indoles; Ligands; Male; Mice; Mutation; Neurons; Parkinson Disease; Phenotype; Quinolines; Receptor, trkB; Receptor, trkC; Signal Transduction; Substantia Nigra; Thiazoles; Tyrosine 3-Monooxygenase

2005
Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases.
    The Journal of biological chemistry, 2005, Nov-18, Volume: 280, Issue:46

    Topics: alpha-Synuclein; Amyloid; Animals; Benzothiazoles; Biochemistry; Cattle; Chaperonin 10; Chickens; Circular Dichroism; Escherichia coli; Humans; Insulin; Lewy Bodies; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Microscopy, Fluorescence; Models, Biological; Molecular Chaperones; Muramidase; Parkinson Disease; Peptides; Protein Binding; Protein Conformation; Scattering, Radiation; Thiazoles; X-Rays

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
Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans.
    The Journal of biological chemistry, 2005, Dec-30, Volume: 280, Issue:52

    Topics: 3-Hydroxybutyric Acid; alpha-Synuclein; Amino Acid Sequence; Animals; Animals, Genetically Modified; Antioxidants; Apoptosis; Benzoates; Benzothiazoles; Bile Acids and Salts; Caenorhabditis elegans; Cholagogues and Choleretics; Copper; Disease Models, Animal; Electron Transport Complex I; Gene Deletion; Gene Expression Regulation; Gene Library; Genetic Techniques; Humans; Immunoblotting; Intracellular Signaling Peptides and Proteins; Ions; Iron; Mitochondria; Molecular Sequence Data; Mutagenesis; Mutation; Neurons; Oncogene Proteins; Oxygen Consumption; Paraquat; Parkinson Disease; Polyenes; Probucol; Protein Deglycase DJ-1; Pyrazoles; Pyridazines; RNA, Small Interfering; Rotenone; Sequence Homology, Amino Acid; Sodium Azide; Taurochenodeoxycholic Acid; Thiazoles; Time Factors; Transgenes; Ubiquitin-Protein Ligases

2005
Proteasomal inhibition hypersensitizes differentiated neuroblastoma cells to oxidative damage.
    Neuroscience letters, 2006, May-15, Volume: 399, Issue:1-2

    Topics: alpha-Synuclein; Benzothiazoles; Cell Differentiation; Cell Line, Tumor; Cytoplasm; Ferrous Compounds; Humans; Immunohistochemistry; Molsidomine; Mutation; Neuroblastoma; Oxidative Stress; Parkinson Disease; Proteasome Inhibitors; Reactive Oxygen Species; Rotenone; Thiazoles; Ubiquitin

2006
Cerebrospinal fluid of Alzheimer's disease and dementia with Lewy bodies patients enhances alpha-synuclein fibril formation in vitro.
    Experimental neurology, 2007, Volume: 203, Issue:2

    Topics: Aged; Aged, 80 and over; alpha-Synuclein; Alzheimer Disease; Amyloid beta-Peptides; Apolipoproteins E; Benzothiazoles; Female; Humans; Immunoglobulin G; Lewy Body Disease; Male; Microscopy, Electron; Middle Aged; Psychiatric Status Rating Scales; Spectrometry, Fluorescence; tau Proteins; Thiazoles

2007
Vitamin A potently destabilizes preformed alpha-synuclein fibrils in vitro: implications for Lewy body diseases.
    Neurobiology of disease, 2007, Volume: 25, Issue:2

    Topics: alpha-Synuclein; Antioxidants; Benzothiazoles; beta Carotene; Coenzymes; Humans; Lewy Body Disease; Microscopy, Atomic Force; Microscopy, Electron; Microscopy, Fluorescence; Neurofibrils; Neuroprotective Agents; Parkinson Disease; Thiazoles; Ubiquinone; Vitamin A; Vitamins

2007
Anti-fibrillogenic and fibril-destabilizing activity of nicotine in vitro: implications for the prevention and therapeutics of Lewy body diseases.
    Experimental neurology, 2007, Volume: 205, Issue:2

    Topics: alpha-Synuclein; Benzothiazoles; Humans; Kinetics; Lewy Body Disease; Microfibrils; Microscopy, Atomic Force; Microscopy, Electron; Mutation; Nicotine; Nicotinic Agonists; Pyridines; Pyrrolidines; Reverse Transcriptase Polymerase Chain Reaction; Spectrometry, Fluorescence; Thiazoles

2007
Novel method for quantitative determination of amyloid fibrils of alpha-synuclein and amyloid beta/A4 protein by using resveratrol.
    Analytical biochemistry, 2007, Aug-15, Volume: 367, Issue:2

    Topics: alpha-Synuclein; Amyloid; Amyloid beta-Peptides; Amyloidosis; Benzothiazoles; Humans; Protein Structure, Quaternary; Resveratrol; Spectrometry, Fluorescence; Stilbenes; Thiazoles

2007
Differentiating Alzheimer disease-associated aggregates with small molecules.
    Neurobiology of disease, 2007, Volume: 28, Issue:3

    Topics: alpha-Synuclein; Alzheimer Disease; Amyloid beta-Peptides; Benzothiazoles; Dose-Response Relationship, Drug; Fluorescent Dyes; Humans; Mass Spectrometry; Neurofibrillary Tangles; Peptide Library; Plaque, Amyloid; tau Proteins; Thiazines; Thiazoles

2007
Sequence Determinants for Amyloid Fibrillogenesis of Human alpha-Synuclein.
    Journal of molecular biology, 2007, Nov-23, Volume: 374, Issue:2

    Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid; Benzothiazoles; beta-Synuclein; Fluorescence; Humans; Molecular Sequence Data; Mutation; Protein Conformation; Protein Folding; Sequence Deletion; Sequence Homology, Amino Acid; Thiazoles

2007
Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.
    The FEBS journal, 2007, Volume: 274, Issue:24

    Topics: alpha-Crystallin B Chain; alpha-Synuclein; Amyloid; Animals; Benzothiazoles; beta-Crystallins; Caseins; Cattle; Chromatography, High Pressure Liquid; Humans; Kinetics; Magnetic Resonance Spectroscopy; Microscopy, Electron, Transmission; Molecular Chaperones; Protein Binding; Recombinant Proteins; Temperature; Thiazoles

2007
Single particle characterization of iron-induced pore-forming alpha-synuclein oligomers.
    The Journal of biological chemistry, 2008, Apr-18, Volume: 283, Issue:16

    Topics: alpha-Synuclein; Benzothiazoles; Electrophysiology; Flavanones; Fluorescent Dyes; Gene Expression Regulation; Humans; Iron; Lipid Bilayers; Microscopy, Atomic Force; Microscopy, Confocal; Models, Biological; Parkinson Disease; Protein Binding; Solvents; Thiazoles

2008
Alpha-synuclein aggregation and cell death triggered by energy deprivation and dopamine overload are counteracted by D2/D3 receptor activation.
    Journal of neurochemistry, 2008, Volume: 106, Issue:2

    Topics: alpha-Synuclein; Analysis of Variance; Animals; Benzothiazoles; Cell Death; Cells, Cultured; Dopamine; Dopamine Agents; Dopamine Plasma Membrane Transport Proteins; Embryo, Mammalian; Formazans; Gene Expression Regulation; Glucose; Mesencephalon; Mice; Mitochondria; Nerve Degeneration; Nerve Tissue Proteins; Neurons; Protein Transport; Receptors, Dopamine D2; Tetrazolium Salts; Thiazoles

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
Aggregates assembled from overexpression of wild-type alpha-synuclein are not toxic to human neuronal cells.
    Journal of neuropathology and experimental neurology, 2008, Volume: 67, Issue:11

    Topics: alpha-Synuclein; Analysis of Variance; Benzothiazoles; Cell Count; Cell Differentiation; Cell Fractionation; Cell Line, Tumor; Dose-Response Relationship, Drug; Gene Expression Regulation; Humans; Microscopy, Electron, Transmission; Molecular Weight; Neuroblastoma; Neurofilament Proteins; Neurons; Tetracycline; Thiazoles; Time Factors; Transfection; Tretinoin

2008
Real-time analysis of amyloid fibril formation of alpha-synuclein using a fibrillation-state-specific fluorescent probe of JC-1.
    The Biochemical journal, 2009, Mar-01, Volume: 418, Issue:2

    Topics: alpha-Synuclein; Amyloid; Benzimidazoles; Benzothiazoles; Carbocyanines; Computer Systems; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Humans; Models, Biological; Protein Binding; Protein Multimerization; Substrate Specificity; Thiazoles

2009
Smoking and Parkinson's disease: does nicotine affect alpha-synuclein fibrillation?
    Biochimica et biophysica acta, 2009, Volume: 1794, Issue:2

    Topics: alpha-Synuclein; Amino Acid Sequence; Anabasine; Benzothiazoles; Chromatography, Gel; Cotinine; Humans; Hydroquinones; Microscopy, Atomic Force; Molecular Sequence Data; Mutation; Nicotine; Parkinson Disease; Protein Binding; Protein Multimerization; Smoking; Thiazoles

2009
Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease.
    The Journal of biological chemistry, 2009, May-08, Volume: 284, Issue:19

    Topics: alpha-Synuclein; Benzothiazoles; Circular Dichroism; Cross-Linking Reagents; Dimerization; Glutamine; Humans; Immunoblotting; Mutagenesis, Site-Directed; Mutation; Parkinson Disease; Protein Conformation; Spectrometry, Mass, Electrospray Ionization; Thiazoles; Transglutaminases

2009
Anti-aggregation and fibril-destabilizing effects of sex hormones on alpha-synuclein fibrils in vitro.
    Experimental neurology, 2009, Volume: 217, Issue:2

    Topics: alpha-Synuclein; Benzothiazoles; Estradiol; Estriol; Gonadal Steroid Hormones; Humans; In Vitro Techniques; Lewy Bodies; Lewy Body Disease; Microscopy, Electron; Molecular Structure; Neurofibrils; Neuroprotective Agents; Parkinson Disease; Spectrometry, Fluorescence; Testosterone; Thiazoles

2009
Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation.
    Cell stress & chaperones, 2010, Volume: 15, Issue:4

    Topics: alpha-Synuclein; Benzothiazoles; Calorimetry; Humans; Protein Disulfide-Isomerases; Protein Structure, Tertiary; Recombinant Proteins; Thiazoles

2010
DnaK/DnaJ/GrpE of Hsp70 system have differing effects on alpha-synuclein fibrillation involved in Parkinson's disease.
    International journal of biological macromolecules, 2010, Mar-01, Volume: 46, Issue:2

    Topics: alpha-Synuclein; Amino Acid Sequence; Benzothiazoles; Chromatography, Gel; HSP40 Heat-Shock Proteins; HSP70 Heat-Shock Proteins; Molecular Sequence Data; Parkinson Disease; Protein Structure, Quaternary; Thiazoles; Time Factors

2010
A novel, high-efficiency cellular model of fibrillar alpha-synuclein inclusions and the examination of mutations that inhibit amyloid formation.
    Journal of neurochemistry, 2010, Volume: 113, Issue:2

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Calcium Phosphates; Cell Line, Transformed; Humans; Hydrophobic and Hydrophilic Interactions; Inclusion Bodies; Point Mutation; Thiazoles; Transfection

2010
Strategies to increase the reproducibility of protein fibrillization in plate reader assays.
    Analytical biochemistry, 2010, May-15, Volume: 400, Issue:2

    Topics: alpha-Synuclein; Benzothiazoles; Fluorescent Dyes; Humans; Kinetics; Parkinson Disease; Recombinant Proteins; Reproducibility of Results; Sodium Dodecyl Sulfate; Thiazoles

2010
The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.
    Biophysical journal, 2010, Mar-03, Volume: 98, Issue:5

    Topics: alpha-Crystallin B Chain; alpha-Synuclein; Amyloid; Benzothiazoles; Fluorescence; Kinetics; Magnetic Resonance Spectroscopy; Molecular Chaperones; Protein Binding; Protein Structure, Quaternary; Quartz; Thiazoles

2010
Characterization of Lewy body pathology in 12- and 16-year-old intrastriatal mesencephalic grafts surviving in a patient with Parkinson's disease.
    Movement disorders : official journal of the Movement Disorder Society, 2010, Jun-15, Volume: 25, Issue:8

    Topics: alpha-Synuclein; Benzothiazoles; Fetal Tissue Transplantation; Humans; Lewy Bodies; Longitudinal Studies; Male; Mesencephalon; Microscopy, Electron, Transmission; Middle Aged; Neurons; Parkinson Disease; Postmortem Changes; Thiazoles; Time Factors

2010
Burden of neurodegenerative diseases in a cohort of medical examiner subjects.
    Journal of forensic sciences, 2010, Volume: 55, Issue:3

    Topics: Adult; Aged; Aged, 80 and over; alpha-Synuclein; Alzheimer Disease; Atrophy; Benzothiazoles; Brain; Brain Edema; Cohort Studies; Coroners and Medical Examiners; Female; Forensic Pathology; Frontotemporal Lobar Degeneration; Humans; Hygiene; Ill-Housed Persons; Immunohistochemistry; Male; Malnutrition; Middle Aged; Neurofibrillary Tangles; Neuropil Threads; Plaque, Amyloid; Staining and Labeling; Tauopathies; Thiazoles; Young Adult

2010
Dose- and time-dependent alpha-synuclein aggregation induced by ferric iron in SK-N-SH cells.
    Neuroscience bulletin, 2010, Volume: 26, Issue:3

    Topics: alpha-Synuclein; Benzothiazoles; Cell Line, Tumor; Cell Survival; Dose-Response Relationship, Drug; Ferric Compounds; Humans; Iron; Thiazoles; Time Factors

2010
Isolation of short peptide fragments from alpha-synuclein fibril core identifies a residue important for fibril nucleation: a possible implication for diagnostic applications.
    Biochimica et biophysica acta, 2010, Volume: 1804, Issue:10

    Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid; Benzothiazoles; Circular Dichroism; Humans; Insulin; Lewy Bodies; Microscopy, Atomic Force; Molecular Sequence Data; Peptide Fragments; Thiazoles

2010
The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity.
    Biochemistry, 2010, Sep-21, Volume: 49, Issue:37

    Topics: alpha-Synuclein; Amyloid; Amyloid beta-Protein Precursor; Animals; Benzothiazoles; Catechin; Cell Culture Techniques; Diabetes Mellitus, Type 2; Flavonoids; Islet Amyloid Polypeptide; Microscopy, Electron, Transmission; Phenols; Polyphenols; Protease Nexins; Rats; Receptors, Cell Surface; Thiazoles

2010
Amyloid formation and disaggregation of α-synuclein and its tandem repeat (α-TR).
    Biochemical and biophysical research communications, 2010, Oct-01, Volume: 400, Issue:4

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Catechin; Flavanones; Humans; Imidazoles; Imides; Ionic Liquids; Microscopy, Electron, Transmission; Parkinson Disease; Sulfonamides; Tandem Repeat Sequences; Thiazoles

2010
Characterization of the non-fibrillar α-synuclein oligomers.
    Protein and peptide letters, 2011, Volume: 18, Issue:3

    Topics: alpha-Synuclein; Benzothiazoles; Cell Membrane; Dose-Response Relationship, Drug; Kinetics; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Secondary; Salts; Solubility; Thiazoles; Unilamellar Liposomes

2011
The role of the C-terminus of human α-synuclein: intra-disulfide bonds between the C-terminus and other regions stabilize non-fibrillar monomeric isomers.
    FEBS letters, 2011, Feb-04, Volume: 585, Issue:3

    Topics: alpha-Synuclein; Benzothiazoles; Circular Dichroism; Cysteine; Cystine; Fluorescent Dyes; Humans; Isomerism; Kinetics; Mutagenesis, Site-Directed; Mutant Proteins; Oxidation-Reduction; Parkinson Disease; Protein Denaturation; Protein Folding; Protein Stability; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Fluorescence; Thiazoles

2011
Coumarin 6 and 1,6-diphenyl-1,3,5-hexatriene (DPH) as fluorescent probes to monitor protein aggregation.
    The Analyst, 2011, May-21, Volume: 136, Issue:10

    Topics: alpha-Synuclein; Benzothiazoles; Carbonic Anhydrases; Coumarins; Diphenylhexatriene; Fluorescent Dyes; Proteins; Quantum Theory; Spectrometry, Fluorescence; Thiazoles

2011
Mechanically functional amyloid fibrils in the adhesive of a marine invertebrate as revealed by Raman spectroscopy and atomic force microscopy.
    Archives of histology and cytology, 2009, Volume: 72, Issue:4-5

    Topics: alpha-Synuclein; Amyloid; Animals; Benzothiazoles; Humans; Microscopy, Atomic Force; Platyhelminths; Protein Structure, Secondary; Spectrum Analysis, Raman; Thiazoles

2009
Designed hairpin peptides interfere with amyloidogenesis pathways: fibril formation and cytotoxicity inhibition, interception of the preamyloid state.
    Biochemistry, 2011, Sep-27, Volume: 50, Issue:38

    Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid; Animals; Benzothiazoles; Drug Design; Humans; In Vitro Techniques; Islet Amyloid Polypeptide; Microscopy, Electron, Transmission; Models, Biological; Models, Molecular; Molecular Sequence Data; Peptides; Protein Folding; Protein Multimerization; Rats; Recombinant Proteins; Thiazoles

2011
Effect of melatonin on α-synuclein self-assembly and cytotoxicity.
    Neurobiology of aging, 2012, Volume: 33, Issue:9

    Topics: alpha-Synuclein; Analysis of Variance; Animals; Antioxidants; Antiparkinson Agents; Benzothiazoles; Brain; Cells, Cultured; Dose-Response Relationship, Drug; Embryo, Mammalian; Melatonin; Mice; Mice, Inbred C57BL; Microscopy, Electron, Transmission; Neurons; Protein Structure, Secondary; Sincalide; Thiazoles; Time Factors; Trihexyphenidyl

2012
Detection of α-synuclein aggregates by fluorescence microscopy.
    Rejuvenation research, 2012, Volume: 15, Issue:2

    Topics: alpha-Synuclein; Benzothiazoles; Biomarkers; Circular Dichroism; Dopaminergic Neurons; Fluorescent Dyes; Humans; Hydrogen-Ion Concentration; Microscopy, Electron, Transmission; Microscopy, Fluorescence; Models, Biological; Neurodegenerative Diseases; Parkinson Disease; Recombinant Proteins; Surface Properties; Temperature; Thiazoles

2012
Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein.
    The Journal of biological chemistry, 2012, Aug-17, Volume: 287, Issue:34

    Topics: Acetylation; alpha-Synuclein; Animals; Benzothiazoles; Escherichia coli; HEK293 Cells; HeLa Cells; Humans; Mice; Mice, Knockout; Multiprotein Complexes; Parkinson Disease; Protein Binding; Protein Structure, Secondary; Saccharomyces cerevisiae; Thiazoles

2012
Cross-seeding effects of amyloid β-protein and α-synuclein.
    Journal of neurochemistry, 2012, Volume: 122, Issue:5

    Topics: alpha-Synuclein; Amyloid beta-Peptides; Animals; Benzothiazoles; Chromatography, Gel; Humans; Microscopy, Electron, Scanning; Peptide Fragments; Plaque, Amyloid; Protein Binding; Thiazoles

2012
Effects of intravenous immunoglobulin on alpha synuclein aggregation and neurotoxicity.
    International immunopharmacology, 2012, Volume: 14, Issue:4

    Topics: alpha-Synuclein; Benzothiazoles; Cell Line, Tumor; Humans; Immunoglobulins, Intravenous; Microscopy, Electron, Transmission; Neuroblastoma; Neurons; Protein Binding; Protein Conformation; Thiazoles

2012
Rational design of potent domain antibody inhibitors of amyloid fibril assembly.
    Proceedings of the National Academy of Sciences of the United States of America, 2012, Dec-04, Volume: 109, Issue:49

    Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid; Amyloid beta-Peptides; Benzothiazoles; Chromatography, Gel; Circular Dichroism; Cloning, Molecular; Drug Design; Electrophoresis, Polyacrylamide Gel; Fluorescence; Humans; Immunoblotting; Islet Amyloid Polypeptide; Microscopy, Atomic Force; Molecular Sequence Data; Protein Engineering; Single-Domain Antibodies; Thiazoles

2012
Triggering of inflammasome by aggregated α-synuclein, an inflammatory response in synucleinopathies.
    PloS one, 2013, Volume: 8, Issue:1

    Topics: alpha-Synuclein; Analysis of Variance; Benzothiazoles; Blotting, Western; Carrier Proteins; Chromatography, Reverse-Phase; DNA Primers; Humans; Inflammasomes; Inflammation; Interleukin-1beta; Lewy Bodies; Microscopy, Atomic Force; Microscopy, Confocal; Microscopy, Electron, Transmission; Neurons; NLR Family, Pyrin Domain-Containing 3 Protein; Parkinson Disease; Phagocytosis; Real-Time Polymerase Chain Reaction; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Thiazoles; Toll-Like Receptor 2

2013
A blood-brain barrier (BBB) disrupter is also a potent α-synuclein (α-syn) aggregation inhibitor: a novel dual mechanism of mannitol for the treatment of Parkinson disease (PD).
    The Journal of biological chemistry, 2013, Jun-14, Volume: 288, Issue:24

    Topics: alpha-Synuclein; Amyloid; Animals; Antiparkinson Agents; Benzothiazoles; Blood-Brain Barrier; Drosophila; Female; Fluorescent Dyes; Hippocampus; HSP70 Heat-Shock Proteins; Humans; Locomotion; Male; Mannitol; Mice; Mice, Inbred C57BL; Mice, Inbred DBA; Mice, Transgenic; Microscopy, Electron, Transmission; Neocortex; Parkinson Disease; Protein Multimerization; Protein Structure, Secondary; Thiazoles

2013
Wildtype and A30P mutant alpha-synuclein form different fibril structures.
    PloS one, 2013, Volume: 8, Issue:7

    Topics: alpha-Synuclein; Benzothiazoles; Escherichia coli; Fluorescent Dyes; Humans; Kinetics; Microscopy, Electron, Transmission; Mutation; Protein Multimerization; Protein Structure, Secondary; Recombinant Proteins; Scattering, Small Angle; Solutions; Spectrometry, Fluorescence; Thiazoles; X-Ray Diffraction

2013
Overexpression of synphilin-1 promotes clearance of soluble and misfolded alpha-synuclein without restoring the motor phenotype in aged A30P transgenic mice.
    Human molecular genetics, 2014, Feb-01, Volume: 23, Issue:3

    Topics: Aging; alpha-Synuclein; Animals; Autophagy; Benzothiazoles; Brain; Carrier Proteins; Gene Expression; Humans; Mice; Mice, Transgenic; Mutation; Nerve Tissue Proteins; Parkinson Disease; Protein Folding; Solubility; Thiazoles; Ubiquitin

2014
In vitro evidence that an aqueous extract of Centella asiatica modulates α-synuclein aggregation dynamics.
    Journal of Alzheimer's disease : JAD, 2014, Volume: 39, Issue:2

    Topics: alpha-Synuclein; Antiparkinson Agents; Benzothiazoles; Centella; Circular Dichroism; Electrophoresis, Polyacrylamide Gel; Fluorescence; Kinetics; Microscopy, Electron, Transmission; Plant Extracts; Polyphenols; Protein Multimerization; Thiazoles; Triterpenes; Water

2014
Neuronal inclusions of α-synuclein contribute to the pathogenesis of Krabbe disease.
    The Journal of pathology, 2014, Volume: 232, Issue:5

    Topics: alpha-Synuclein; Animals; Benzothiazoles; Brain; Case-Control Studies; Cognition; Disease Models, Animal; Fluorescent Dyes; Humans; Leukodystrophy, Globoid Cell; Lewy Bodies; Mice; Motor Activity; Mutation; Neurons; Psychosine; Thiazoles

2014
Complexation of amyloid fibrils with charged conjugated polymers.
    Langmuir : the ACS journal of surfaces and colloids, 2014, Apr-08, Volume: 30, Issue:13

    Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid; Benzothiazoles; Escherichia coli; Fluorocarbon Polymers; Gene Expression; Humans; Kinetics; Microscopy, Atomic Force; Molecular Sequence Data; Protein Aggregates; Recombinant Proteins; Solutions; Spectroscopy, Fourier Transform Infrared; Static Electricity; Thiazoles

2014
Gallic acid interacts with α-synuclein to prevent the structural collapse necessary for its aggregation.
    Biochimica et biophysica acta, 2014, Volume: 1844, Issue:9

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Flocculation; Fluorescent Dyes; Gallic Acid; Humans; Magnetic Resonance Spectroscopy; Microscopy, Electron, Transmission; Protein Binding; Recombinant Proteins; Spectrometry, Fluorescence; Thiazoles

2014
Pitfalls associated with the use of Thioflavin-T to monitor anti-fibrillogenic activity.
    Bioorganic & medicinal chemistry letters, 2014, Jul-15, Volume: 24, Issue:14

    Topics: alpha-Synuclein; Amyloid; Artifacts; Benzothiazoles; Humans; Protein Structure, Tertiary; Structure-Activity Relationship; Thiazoles

2014
β-cyclodextrin and curcumin, a potent cocktail for disaggregating and/or inhibiting amyloids: a case study with α-synuclein.
    Biochemistry, 2014, Jul-01, Volume: 53, Issue:25

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; beta-Cyclodextrins; Circular Dichroism; Curcumin; Drug Synergism; Fluorescent Dyes; Thiazoles

2014
Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers.
    Biophysical journal, 2014, Jun-17, Volume: 106, Issue:12

    Topics: Adsorption; alpha-Synuclein; Amyloid; Benzothiazoles; Lipid Bilayers; Liposomes; Mutant Proteins; Phosphatidylcholines; Phosphatidylglycerols; Protein Aggregates; Protein Binding; Staining and Labeling; Thiazoles

2014
Soluble, prefibrillar α-synuclein oligomers promote complex I-dependent, Ca2+-induced mitochondrial dysfunction.
    The Journal of biological chemistry, 2014, Aug-01, Volume: 289, Issue:31

    Topics: alpha-Synuclein; Animals; Benzothiazoles; Biopolymers; Calcium; Electron Transport Complex I; Humans; Membrane Potential, Mitochondrial; Mice; Mitochondria; Thiazoles

2014
Early sodium dodecyl sulfate induced collapse of α-synuclein correlates with its amyloid formation.
    ACS chemical neuroscience, 2015, Feb-18, Volume: 6, Issue:2

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Circular Dichroism; Entropy; Escherichia coli; Fluorescence Resonance Energy Transfer; Glycerol; Microscopy, Electron, Transmission; Mutation; Protein Structure, Secondary; Recombinant Proteins; Sodium Dodecyl Sulfate; Solutions; Solvents; Spectrometry, Fluorescence; Thiazoles; Urea

2015
Pseudocatalytic Antiaggregation Activity of Antibodies: Immunoglobulins can Influence α-Synuclein Aggregation at Substoichiometric Concentrations.
    Molecular neurobiology, 2016, Volume: 53, Issue:3

    Topics: alpha-Synuclein; Antibodies; Benzothiazoles; Biocatalysis; Biological Assay; Circular Dichroism; Fluorescence; Kinetics; Protein Aggregates; Protein Aggregation, Pathological; Thiazoles

2016
Cu(II) promotes amyloid pore formation.
    Biochemical and biophysical research communications, 2015, Aug-14, Volume: 464, Issue:1

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Cations, Divalent; Copper; Flavanones; Humans; Kinetics; Microscopy, Electron, Transmission; Oxidation-Reduction; Protein Aggregates; Protein Structure, Secondary; Recombinant Proteins; Spectrometry, Fluorescence; Thiazoles

2015
Insulin-degrading enzyme prevents α-synuclein fibril formation in a nonproteolytical manner.
    Scientific reports, 2015, Jul-31, Volume: 5

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Calorimetry; Insulysin; Microscopy, Atomic Force; Protein Multimerization; Thiazoles

2015
Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants.
    Scientific reports, 2015, Nov-19, Volume: 5

    Topics: alpha-Synuclein; Amino Acid Sequence; Benzothiazoles; Biological Assay; Fluorescence Resonance Energy Transfer; Humans; Kinetics; Molecular Sequence Data; Mutant Proteins; Mutation, Missense; Parkinson Disease; Protein Multimerization; Thiazoles

2015
High-content analysis of α-synuclein aggregation and cell death in a cellular model of Parkinson's disease.
    Journal of neuroscience methods, 2016, Mar-01, Volume: 261

    Topics: alpha-Synuclein; Apoptosis; Benzothiazoles; Blotting, Western; Cell Count; Cell Culture Techniques; Cell Line, Tumor; Cell Survival; Genetic Vectors; Humans; Image Processing, Computer-Assisted; Immunohistochemistry; Indoles; Lentivirus; Microscopy, Fluorescence; Oxidative Stress; Parkinsonian Disorders; Protein Aggregation, Pathological; Protein Multimerization; Software; Thiazoles

2016
Conformational Compatibility Is Essential for Heterologous Aggregation of α-Synuclein.
    ACS chemical neuroscience, 2016, 06-15, Volume: 7, Issue:6

    Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid; Benzothiazoles; Circular Dichroism; Humans; Microscopy, Atomic Force; Molecular Conformation; Thiazoles

2016
Piceatannol and Other Wine Stilbenes: A Pool of Inhibitors against α-Synuclein Aggregation and Cytotoxicity.
    Nutrients, 2016, Jun-15, Volume: 8, Issue:6

    Topics: alpha-Synuclein; Animals; Benzothiazoles; Cell Survival; Electrophoresis, Polyacrylamide Gel; Flavonoids; Microscopy, Electron, Transmission; Parkinson Disease; PC12 Cells; Phenols; Rats; Stilbenes; Thiazoles; Wine

2016
Mechanistic study of the inhibitory activity of Geum urbanum extract against α-Synuclein fibrillation.
    Biochimica et biophysica acta, 2016, Volume: 1864, Issue:9

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Geum; Humans; Plant Extracts; Protein Aggregates; Solutions; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Thiazoles

2016
Analysis of sheep α-synuclein provides a molecular strategy for the reduction of fibrillation.
    Biochimica et biophysica acta. Proteins and proteomics, 2017, Volume: 1865, Issue:3

    Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid; Animals; Benzothiazoles; Humans; Hydrogen-Ion Concentration; Kinetics; Lewy Bodies; Mutation; Parkinson Disease; Protein Aggregation, Pathological; Sequence Alignment; Sheep; Solubility; Thiazoles

2017
Propagation of pathological α-synuclein in marmoset brain.
    Acta neuropathologica communications, 2017, Feb-02, Volume: 5, Issue:1

    Topics: alpha-Synuclein; Animals; Benzothiazoles; Brain; Callithrix; Female; Immunohistochemistry; Lewy Bodies; Microglia; Nerve Degeneration; Neurons; Parkinsonian Disorders; Protein Aggregation, Pathological; Recombinant Proteins; Sequence Homology, Amino Acid; Thiazoles; Tyrosine 3-Monooxygenase

2017
Distinct Mechanisms Determine α-Synuclein Fibril Morphology during Growth and Maturation.
    ACS chemical neuroscience, 2017, 03-15, Volume: 8, Issue:3

    Topics: alpha-Synuclein; Benzothiazoles; Circular Dichroism; Humans; Microscopy, Atomic Force; Multiprotein Complexes; Mutation; Protein Aggregation, Pathological; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thiazoles; Time Factors

2017
Detection and Characterization of Small Molecule Interactions with Fibrillar Protein Aggregates Using Microscale Thermophoresis.
    ACS chemical neuroscience, 2017, 09-20, Volume: 8, Issue:9

    Topics: alpha-Synuclein; Benzothiazoles; Binding, Competitive; Dose-Response Relationship, Drug; Drug Discovery; Humans; Indoles; Microscopy, Atomic Force; Optical Imaging; Protective Agents; Protein Aggregation, Pathological; Protein Binding; tau Proteins; Thermal Diffusion; Thiazoles

2017
Enzymatic O-GlcNAcylation of α-synuclein reduces aggregation and increases SDS-resistant soluble oligomers.
    Neuroscience letters, 2017, Aug-10, Volume: 655

    Topics: alpha-Synuclein; Benzothiazoles; Humans; N-Acetylglucosaminyltransferases; Protein Aggregates; Protein Multimerization; Protein Processing, Post-Translational; Sodium Dodecyl Sulfate; Solubility; Thiazoles

2017
Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T.
    The Journal of biological chemistry, 2017, 10-13, Volume: 292, Issue:41

    Topics: alpha-Synuclein; Benzothiazoles; Humans; Multiprotein Complexes; Protein Aggregation, Pathological; Protein Multimerization; Thiazoles

2017
Lysophosphatidylcholine modulates the aggregation of human islet amyloid polypeptide.
    Physical chemistry chemical physics : PCCP, 2017, Nov-22, Volume: 19, Issue:45

    Topics: alpha-Synuclein; Benzothiazoles; Diabetes Mellitus, Type 2; Humans; Insulin-Secreting Cells; Islet Amyloid Polypeptide; Kinetics; Lysophosphatidylcholines; Microscopy, Electron, Transmission; Molecular Dynamics Simulation; Thiazoles

2017
Iron Redox Chemistry Promotes Antiparallel Oligomerization of α-Synuclein.
    Journal of the American Chemical Society, 2018, 04-18, Volume: 140, Issue:15

    Topics: alpha-Synuclein; Benzothiazoles; Ferrous Compounds; Fluorescent Dyes; Humans; Oxidation-Reduction; Parkinson Disease; Thiazoles

2018
Investigation of α-Synuclein Amyloid Fibrils Using the Fluorescent Probe Thioflavin T.
    International journal of molecular sciences, 2018, Aug-23, Volume: 19, Issue:9

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Cloning, Molecular; Escherichia coli; Fluorescent Dyes; Gene Expression; Genetic Vectors; Humans; Kinetics; Microdialysis; Protein Binding; Recombinant Proteins; Reproducibility of Results; Solutions; Spectrometry, Fluorescence; Thermodynamics

2018
Vibrational Circular Dichroism Sheds New Light on the Competitive Effects of Crowding and β-Synuclein on the Fibrillation Process of α-Synuclein.
    Biochemistry, 2018, 10-16, Volume: 57, Issue:41

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; beta-Synuclein; Circular Dichroism; Humans; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Protein Structure, Quaternary

2018
Modulating α-synuclein fibril formation using DNA tetrahedron nanostructures.
    Biochimica et biophysica acta. General subjects, 2019, Volume: 1863, Issue:1

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Chromatography, Gel; DNA; Humans; Light; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Nanostructures; Nucleic Acid Conformation; Parkinson Disease; Scattering, Radiation

2019
Polymorph-specific distribution of binding sites determines thioflavin-T fluorescence intensity in α-synuclein fibrils.
    Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 2018, Volume: 25, Issue:3

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Binding Sites; Fluorescence; Humans; Microscopy, Atomic Force; Protein Binding

2018
High Selectivity and Sensitivity of Oligomeric p-Phenylene Ethynylenes for Detecting Fibrillar and Prefibrillar Amyloid Protein Aggregates.
    ACS chemical neuroscience, 2019, 03-20, Volume: 10, Issue:3

    Topics: alpha-Synuclein; Amyloid beta-Peptides; Amyloidogenic Proteins; Benzothiazoles; Fluorescent Dyes; Humans; Parkinson Disease; Protein Aggregates

2019
Ultrasensitive Detection of Aggregated α-Synuclein in Glial Cells, Human Cerebrospinal Fluid, and Brain Tissue Using the RT-QuIC Assay: New High-Throughput Neuroimmune Biomarker Assay for Parkinsonian Disorders.
    Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology, 2019, Volume: 14, Issue:3

    Topics: Age Factors; Aged; Aged, 80 and over; alpha-Synuclein; Alzheimer Disease; Animals; Benzothiazoles; Biomarkers; Brain Chemistry; Case-Control Studies; Computer Systems; Fluorescent Dyes; Fluorometry; High-Throughput Screening Assays; Humans; Lewy Body Disease; Mice; Microglia; Middle Aged; Neuroglia; Parkinsonian Disorders; Protein Aggregates; Recombinant Proteins; Reproducibility of Results; Sensitivity and Specificity; Single-Blind Method; Synucleinopathies

2019
Effect of superparamagnetic nanoparticles coated with various electric charges on α-synuclein and β-amyloid proteins fibrillation process.
    International journal of nanomedicine, 2019, Volume: 14

    Topics: alpha-Synuclein; Amyloid beta-Peptides; Benzothiazoles; Cell Line, Tumor; Electricity; Humans; Kinetics; Magnetite Nanoparticles; Spectrometry, Fluorescence

2019
Hyperosmotic stress induces cell-dependent aggregation of α-synuclein.
    Scientific reports, 2019, 02-19, Volume: 9, Issue:1

    Topics: alpha-Synuclein; Animals; Benzothiazoles; Blotting, Western; Cell Death; Cell Line; Cell Survival; Electrophoresis, Polyacrylamide Gel; HEK293 Cells; Hot Temperature; Humans; Hydrogen Peroxide; L-Lactate Dehydrogenase; Mice; Osmolar Concentration; Parkinson Disease; Sodium Chloride; Sodium Dodecyl Sulfate; Urea

2019
A cullin-RING ubiquitin ligase targets exogenous α-synuclein and inhibits Lewy body-like pathology.
    Science translational medicine, 2019, 06-05, Volume: 11, Issue:495

    Topics: alpha-Synuclein; Animals; Benzothiazoles; Cell Line, Tumor; Chlorocebus aethiops; COS Cells; Humans; Lewy Bodies; Mice; Neuroblastoma; Neurons; Parkinson Disease; Proteome; S-Phase Kinase-Associated Proteins; Ubiquitin; Ubiquitin-Protein Ligases

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
Cerium oxide NPs mitigate the amyloid formation of α-synuclein and associated cytotoxicity.
    International journal of nanomedicine, 2019, Volume: 14

    Topics: alpha-Synuclein; Amyloid; Apoptosis; bcl-2-Associated X Protein; Benzothiazoles; Cell Line, Tumor; Cerium; Congo Red; Humans; Kinetics; Molecular Docking Simulation; Molecular Dynamics Simulation; Nanoparticles; Necrosis; RNA, Messenger; Spectrometry, Fluorescence

2019
Vitamin K1 As A Potential Molecule For Reducing Single-Walled Carbon Nanotubes-Stimulated α-Synuclein Structural Changes And Cytotoxicity.
    International journal of nanomedicine, 2019, Volume: 14

    Topics: Adsorption; alpha-Synuclein; Benzothiazoles; Caspase 3; Cell Death; Cell Line, Tumor; Congo Red; Humans; L-Lactate Dehydrogenase; Molecular Docking Simulation; Molecular Dynamics Simulation; Nanotubes, Carbon; Spectrometry, Fluorescence; Vitamin K 1

2019
A KLVFFAE-Derived Peptide Probe for Detection of Alpha-Synuclein Fibrils.
    Applied biochemistry and biotechnology, 2020, Volume: 190, Issue:4

    Topics: alpha-Synuclein; Amyloid beta-Peptides; Benzothiazoles; Circular Dichroism; Humans; Hydrophobic and Hydrophilic Interactions; Microscopy, Electron, Transmission; Mutation; Peptides; Protein Binding; Protein Domains; Spectrometry, Fluorescence; Static Electricity

2020
Nanoscale View of Amyloid Photodynamic Damage.
    Journal of the American Chemical Society, 2020, 01-15, Volume: 142, Issue:2

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Lactoglobulins; Light; Microscopy, Atomic Force; Microscopy, Fluorescence; Reactive Oxygen Species; Singlet Oxygen; Spectroscopy, Near-Infrared

2020
Structural Optimization of Inhibitors of α-Synuclein Fibril Growth: Affinity to the Fibril End as a Crucial Factor.
    Journal of molecular biology, 2020, 02-14, Volume: 432, Issue:4

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Fluorescence Polarization; Humans; Kinetics; Protein Aggregates; Protein Binding; Structure-Activity Relationship

2020
Interactions between Soluble Species of β-Amyloid and α-Synuclein Promote Oligomerization while Inhibiting Fibrillization.
    Biochemistry, 2020, 02-04, Volume: 59, Issue:4

    Topics: alpha-Synuclein; Alzheimer Disease; Amyloid; Amyloid beta-Peptides; Benzothiazoles; Brain; Electrophoresis, Polyacrylamide Gel; Humans; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Neurodegenerative Diseases; Parkinson Disease; Peptide Fragments; Protein Aggregation, Pathological

2020
Novel noscapine derivatives stabilize the native state of insulin against fibrillation.
    International journal of biological macromolecules, 2020, Mar-15, Volume: 147

    Topics: alpha-Synuclein; Amyloid; Amyloid beta-Peptides; Benzothiazoles; Cell Death; Cell Line, Tumor; Cell Survival; Humans; Insulin; Kinetics; Molecular Docking Simulation; Noscapine; Protein Denaturation; Protein Structure, Secondary; Temperature

2020
A Capped Peptide of the Aggregation Prone NAC 71-82 Amino Acid Stretch of α-Synuclein Folds into Soluble β-Sheet Oligomers at Low and Elevated Peptide Concentrations.
    International journal of molecular sciences, 2020, Feb-27, Volume: 21, Issue:5

    Topics: alpha-Synuclein; Amyloid beta-Peptides; Benzothiazoles; Circular Dichroism; Fluorescence; Molecular Dynamics Simulation; Peptides; Protein Conformation, beta-Strand; Protein Folding; Solubility

2020
An efficient method for recombinant production of human alpha synuclein in
    Preparative biochemistry & biotechnology, 2020, Volume: 50, Issue:7

    Topics: alpha-Synuclein; Benzothiazoles; Chromatography, Affinity; Chromatography, High Pressure Liquid; Cloning, Molecular; Endopeptidases; Escherichia coli; Histidine; Humans; Industrial Microbiology; Potyvirus; Recombinant Fusion Proteins; Spectrometry, Fluorescence; Thioredoxins

2020
Lactulose and Melibiose Inhibit α-Synuclein Aggregation and Up-Regulate Autophagy to Reduce Neuronal Vulnerability.
    Cells, 2020, 05-16, Volume: 9, Issue:5

    Topics: alpha-Synuclein; Amino Acid Sequence; Antioxidants; Autophagy; Benzothiazoles; Cell Line; Cell Survival; Dopaminergic Neurons; Fluorescence; Green Fluorescent Proteins; Humans; Lactulose; Melibiose; Neuronal Outgrowth; Neurons; Neuroprotective Agents; Oxidative Stress; Protein Aggregates; Trehalose; Up-Regulation

2020
Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity.
    Nature communications, 2020, 06-04, Volume: 11, Issue:1

    Topics: alpha-Synuclein; Benzothiazoles; Calcium; Humans; Kinetics; Mutant Proteins; Mutation; Phosphorylation; Protein Aggregates; Protein Conformation; Proton Magnetic Resonance Spectroscopy; Structure-Activity Relationship

2020
α-Synuclein Overexpression in SH-SY5Y Human Neuroblastoma Cells Leads to the Accumulation of Thioflavin S-positive Aggregates and Impairment of Glycolysis.
    Biochemistry. Biokhimiia, 2020, Volume: 85, Issue:5

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Cell Line, Tumor; Glyceraldehyde-3-Phosphate Dehydrogenases; Glycolysis; Humans; Neuroblastoma; Oxidation-Reduction

2020
Characterization by Nano-Infrared Spectroscopy of Individual Aggregated Species of Amyloid Proteins.
    Molecules (Basel, Switzerland), 2020, Jun-24, Volume: 25, Issue:12

    Topics: alpha-Synuclein; Amyloid; Amyloid beta-Peptides; Benzothiazoles; Fluorescence; Microscopy, Atomic Force; Peptide Fragments; Protein Structure, Secondary; Selenium Compounds; Spectrometry, Fluorescence; Spectrophotometry, Infrared; Spectroscopy, Fourier Transform Infrared; Zinc Compounds

2020
Prolongation of metallothionein induction combats Aß and α-synuclein toxicity in aged transgenic Caenorhabditis elegans.
    Scientific reports, 2020, 07-16, Volume: 10, Issue:1

    Topics: Aging; alpha-Synuclein; Alzheimer Disease; Amyloid beta-Peptides; Animals; Animals, Genetically Modified; Benzothiazoles; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Clioquinol; Disease Models, Animal; Emodin; Gene Knockdown Techniques; Homeostasis; Metallothionein; Metals; Neuroprotective Agents; Parkinson Disease; Quercetin; Signal Transduction

2020
Cholesterol-containing lipid nanodiscs promote an α-synuclein binding mode that accelerates oligomerization.
    The FEBS journal, 2021, Volume: 288, Issue:6

    Topics: Algorithms; alpha-Synuclein; Benzothiazoles; Cholesterol; Humans; Kinetics; Lipid Bilayers; Magnetic Resonance Spectroscopy; Maleates; Membrane Lipids; Microscopy, Atomic Force; Nanostructures; Protein Binding; Protein Multimerization; Styrene; Surface Plasmon Resonance

2021
Novel self-replicating α-synuclein polymorphs that escape ThT monitoring can spontaneously emerge and acutely spread in neurons.
    Science advances, 2020, Volume: 6, Issue:40

    Topics: alpha-Synuclein; Amyloid; Animals; Benzothiazoles; Mice; Neurons; Synucleinopathies

2020
Spearmint Extract Containing Rosmarinic Acid Suppresses Amyloid Fibril Formation of Proteins Associated with Dementia.
    Nutrients, 2020, Nov-13, Volume: 12, Issue:11

    Topics: alpha-Synuclein; Alzheimer Disease; Amyloid; Amyloid beta-Peptides; Benzothiazoles; Cell Line; Cell Survival; Cinnamates; Dementia; Depsides; Humans; Mentha spicata; Plant Extracts; Polyphenols; Rosmarinic Acid

2020
Effect of Ionic Strength on Thioflavin-T Affinity to Amyloid Fibrils and Its Fluorescence Intensity.
    International journal of molecular sciences, 2020, Nov-24, Volume: 21, Issue:23

    Topics: alpha-Synuclein; Alzheimer Disease; Amyloid; Animals; Benzothiazoles; Binding Sites; Fluorescence; Humans; Insulin; Kinetics; Mice; Osmolar Concentration; Parkinson Disease; Prion Proteins; Protein Aggregates; Protein Aggregation, Pathological; Protein Binding

2020
Liposome Enhanced Detection of Amyloid Protein Aggregates.
    Organic letters, 2021, 02-05, Volume: 23, Issue:3

    Topics: alpha-Synuclein; Amyloid; Amyloid beta-Peptides; Benzothiazoles; Fluorescence; Fluorescent Dyes; Liposomes; Molecular Structure; Protein Aggregates; Protein Binding

2021
NMR unveils an N-terminal interaction interface on acetylated-α-synuclein monomers for recruitment to fibrils.
    Proceedings of the National Academy of Sciences of the United States of America, 2021, 05-04, Volume: 118, Issue:18

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; Binding Sites; Humans; Intrinsically Disordered Proteins; Magnetic Resonance Imaging; Magnetic Resonance Spectroscopy; Nuclear Magnetic Resonance, Biomolecular; Parkinson Disease

2021
The food additive fast green FCF inhibits α-synuclein aggregation, disassembles mature fibrils and protects against amyloid-induced neurotoxicity.
    Food & function, 2021, Jun-21, Volume: 12, Issue:12

    Topics: alpha-Synuclein; Amyloid; Animals; Benzothiazoles; Cell Survival; Food Additives; Hydrogen Bonding; Lissamine Green Dyes; Molecular Dynamics Simulation; Neurons; Neurotoxicity Syndromes; Parkinson Disease; PC12 Cells; Protective Agents; Protein Aggregates; Rats; Static Electricity

2021
α-Synuclein Seeding Assay Using RT-QuIC.
    Methods in molecular biology (Clifton, N.J.), 2021, Volume: 2322

    Topics: alpha-Synuclein; Benzothiazoles; Biological Assay; Brain; Humans; Kinetics; Prion Proteins; Protein Aggregates; Synucleinopathies

2021
Identification of amyloidogenic proteins in the microbiomes of a rat Parkinson's disease model and wild-type rats.
    Protein science : a publication of the Protein Society, 2021, Volume: 30, Issue:9

    Topics: alpha-Synuclein; Amino Acid Sequence; Amyloid; Amyloidogenic Proteins; Animals; Bacterial Proteins; Benzothiazoles; Biofilms; Disease Models, Animal; Endopeptidase K; Feces; Female; Formates; Gastrointestinal Microbiome; Humans; Hydrogen-Ion Concentration; Microbial Consortia; Parkinson Disease; Protein Aggregates; Rats; Rats, Transgenic; Urea

2021
Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation.
    Nature communications, 2021, 12-15, Volume: 12, Issue:1

    Topics: alpha-Synuclein; Amyloid; Benzothiazoles; DEAD-box RNA Helicases; Kinetics; Peptides; Phase Transition; Thermodynamics

2021
The Stimulatory Effects of Intracellular α-Synuclein on Synaptic Transmission Are Attenuated by 2-Octahydroisoquinolin-2(1H)-ylethanamine.
    International journal of molecular sciences, 2021, Dec-09, Volume: 22, Issue:24

    Topics: alpha-Synuclein; Animals; Benzothiazoles; Cells, Cultured; Humans; Hydrophobic and Hydrophilic Interactions; Isoquinolines; Mice; Molecular Docking Simulation; Molecular Dynamics Simulation; Neurons; Protein Binding; Protein Domains; Rats; Synaptic Transmission

2021
Two-step screening method to identify α-synuclein aggregation inhibitors for Parkinson's disease.
    Scientific reports, 2022, 01-10, Volume: 12, Issue:1

    Topics: alpha-Synuclein; Animals; Animals, Genetically Modified; Antiparkinson Agents; Benzothiazoles; Biological Assay; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Disease Models, Animal; Drug Repositioning; HeLa Cells; High-Throughput Screening Assays; Humans; Mice, Inbred C57BL; Neurons; Parkinson Disease; Protein Aggregates; Protein Aggregation, Pathological; Spectrometry, Fluorescence; Tannins

2022