Cited by 208Parkinson's Disease Mechanisms and TreatmentsProtein Structure and DynamicsProtein purification and stability

The DOI matches its Crossref record; 33 of the 34 references it cites were found in a registry or an index.

Trimethylamine‐ N ‐oxide‐induced folding of α‐synuclein

Uversky, Vladimir N., Li, Jie, Fink, Anthony L.·2001·FEBS Letters

DOI 10.1016/s0014-5793(01)03121-0

Open this paper in CoChat — free account

Abstract

The effect of the natural osmolyte trimethylamine-N-oxide (TMAO) on the structural properties and fibril formation of the natively unfolded protein human alpha-synuclein was studied using several physico-chemical methods. TMAO induced folding of alpha-synuclein: at moderate concentrations, a partially folded intermediate with enhanced propensity for fibrillation accumulated; at higher concentrations, alpha-synuclein was tightly folded and underwent self-association to form oligomers. The latter conformation was significantly helical and probably represents the physiologically folded form of the protein.

Integrity signals

Registry

Crossref · 10.1016/s0014-5793(01)03121-0

Cites

33 of 33 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Small-Angle X-Ray Scattering
Bhushan, B. (2016) · Springer eBooks · doi:10.1007/978-94-017-9780-1_101037 · Cited by 3,800
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
Wright, P. E., & Dyson, H. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3110 · Cited by 2,968
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Why are ?natively unfolded? proteins unstructured under physiologic conditions?
Uversky, V. N., Gillespie, J. R., & Fink, A. L. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20001115)41:3 · Cited by 2,097
Fluorescence quenching studies with proteins
Eftink, M. R., & Ghiron, C. A. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90474-7 · Cited by 1,770
Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
Maroteaux, L., Campanelli, J., & Scheller, R. (1988) · Journal of Neuroscience · doi:10.1523/jneurosci.08-08-02804.1988 · Cited by 1,646
Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,559
NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded
Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., & Lansbury, P. T. (1996) · Biochemistry · doi:10.1021/bi961799n · Cited by 1,524
Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease
Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,519
The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
Iwai, A., Masliah, E., Yoshimoto, M., Ge, N., Flanagan, L., Rohan de Silva, H. A., Kittel, A., & Saitoh, T. (1995) · Neuron · doi:10.1016/0896-6273(95)90302-x · Cited by 1,316

Show all 34 references

Research works printed but not linked: 1

Naiki H., 1990, Lab. Invest., 62, 768

Sorted by citations

Conformational constraints for amyloid fibrillation: the importance of being unfolded
Uversky, V. N., & Fink, A. L. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2003.12.008 · Cited by 1,022
Implication of Trimethylamine N-Oxide (TMAO) in Disease: Potential Biomarker or New Therapeutic Target
Janeiro, M., Ramírez, M., Milagro, F., Martínez, J., & Solas, M. (2018) · Nutrients · doi:10.3390/nu10101398 · Cited by 631
Neuropathology, biochemistry, and biophysics of α‐synuclein aggregation
Uversky, V. N. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04764.x · Cited by 591
What Macromolecular Crowding Can Do to a Protein
Kuznetsova, I. М., Константинович, Т. К., & Uversky, V. N. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms151223090 · Cited by 574
Raman Spectroscopic Characterization of Secondary Structure in Natively Unfolded Proteins: α-Synuclein
Maiti, N. C., Apetri, M. M., Zagorski, M. G., CAREY, P. R., & Anderson, V. E. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0356176 · Cited by 523
α-Synuclein misfolding and aggregation: Implications in Parkinson’s disease pathogenesis
Mehra, S., Sahay, S., & Maji, S. K. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.03.001 · Cited by 527
The Aggregation and Fibrillation of α-Synuclein
Fink, A. L. (2006) · Accounts of Chemical Research · doi:10.1021/ar050073t · Cited by 511
A Protein-Chameleon: Conformational Plasticity of α-Synuclein, a Disordered Protein Involved in Neurodegenerative Disorders
Uversky, V. N. (2003) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2003.10506918 · Cited by 514
Practical considerations in refolding proteins from inclusion bodies
Tsumoto, K., Ejima, D., Kumagai, I., & Arakawa, T. (2003) · Protein Expression and Purification · doi:10.1016/s1046-5928(02)00641-1 · Cited by 452
Structure and Energetics of the Hydrogen-Bonded Backbone in Protein Folding
Bolen, D. W., & Rose, G. D. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061306.131357 · Cited by 408
Intrinsically Disordered Proteins and Their Environment: Effects of Strong Denaturants, Temperature, pH, Counter Ions, Membranes, Binding Partners, Osmolytes, and Macromolecular Crowding
Uversky, V. N. (2009) · The Protein Journal · doi:10.1007/s10930-009-9201-4 · Cited by 367
Biophysics of Parkinsons Disease: Structure and Aggregation of α- Synuclein
Uversky, V. N., & Eliezer, D. (2009) · Current Protein and Peptide Science · doi:10.2174/138920309789351921 · Cited by 326
Lipid Binding Inhibits α-Synuclein Fibril Formation
Zhu, M., & Fink, A. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210136200 · Cited by 321
Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go?
Uversky, V. N. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-003-3096-6 · Cited by 322
Unstructural biology coming of age
Tompa, P. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.03.012 · Cited by 292
Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease
Dev, K. K. (2003) · Neuropharmacology · doi:10.1016/s0028-3908(03)00140-0 · Cited by 265
The therapeutic potential of chemical chaperones in protein folding diseases
Cortez, L. M., & Sim, V. L. (2014) · Prion · doi:10.4161/pri.28938 · Cited by 254
Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)
Ma, J., Pazos, I. M., & Gai, F. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403224111 · Cited by 253
Conformational Behavior and Aggregation of α-Synuclein in Organic Solvents: Modeling the Effects of Membranes
Munishkina, L. A., Phelan, C., Uversky, V. N., & Fink, A. L. (2003) · Biochemistry · doi:10.1021/bi027166s · Cited by 247
Role of Protein−Water Interactions and Electrostatics in α-Synuclein Fibril Formation
Munishkina, L. A., Henriques, J., Uversky, V. N., & Fink, A. L. (2004) · Biochemistry · doi:10.1021/bi034938r · Cited by 217
Guiding Protein Aggregation with Macromolecular Crowding
Munishkina, L. A., Ahmad, A., Fink, A. L., & Uversky, V. N. (2008) · Biochemistry · doi:10.1021/bi8008399 · Cited by 199
Amyloidogenesis of Natively Unfolded Proteins
Uversky, V. N. (2008) · Current Alzheimer Research · doi:10.2174/156720508784533312 · Cited by 188
Effects of in vivo conditions on amyloid aggregation
Owen, M. C., Gnutt, D., Gao, M., Wärmländer, S. K. T. S., Jarvet, J., Gräslund, A., Winter, R., Ebbinghaus, S., & Strodel, B. (2019) · Chemical Society Reviews · doi:10.1039/c8cs00034d · Cited by 181
Roles of osmolytes in protein folding and aggregation in cells and their biotechnological applications
Rabbani, G., & Choi, I.-H. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.12.100 · Cited by 162
The Role of Early Life Environmental Risk Factors in Parkinson Disease: What Is the Evidence?
Logroscino, G. (2005) · Environmental Health Perspectives · doi:10.1289/ehp.7573 · Cited by 151
LC–MS-Based Urinary Metabolite Signatures in Idiopathic Parkinson’s Disease
Luan, H., Liu, L., Meng, N., Tang, Z., Chua, K.-K., Chen, L., Song, J., Mok, V., Xie, L.-X., Li, M., et al. (2014) · Journal of Proteome Research · doi:10.1021/pr500807t · Cited by 134
Molecular Mechanisms Underlying the Flavonoid-Induced Inhibition of α-Synuclein Fibrillation
Meng, X., Munishkina, L. A., Fink, A. L., & Uversky, V. N. (2009) · Biochemistry · doi:10.1021/bi900506b · Cited by 132
Protein Interactions and Misfolding Analyzed by AFM Force Spectroscopy
McAllister, C., Karymov, M. A., Kawano, Y., Lushnikov, A. Y., Mikheikin, A., Uversky, V. N., & Lyubchenko, Y. L. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.10.012 · Cited by 129
When Does Trimethylamine N -Oxide Fold a Polymer Chain and Urea Unfold It?
Mondal, J., Stirnemann, G., & Berne, B. J. (2013) · The Journal of Physical Chemistry B · doi:10.1021/jp405609j · Cited by 117
Salt-Induced Modulation of the Pathway of Amyloid Fibril Formation by the Mouse Prion Protein
Jain, S., & Udgaonkar, J. B. (2010) · Biochemistry · doi:10.1021/bi100745j · Cited by 117
Amyloid Fibril Formation of α-Synuclein Is Accelerated by Preformed Amyloid Seeds of Other Proteins
Yagi, H., Kusaka, E., Hongo, K., Mizobata, T., & Kawata, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508623200 · Cited by 113
The Role of a Gut Microbial-Derived Metabolite, Trimethylamine N-Oxide (TMAO), in Neurological Disorders
Praveenraj, S. S., Sonali, S., Anand, N., Hediyal, T. A., Vichitra, C., Kalyan, M., Kanna, P. V., Chandana, K. A., Paneyala, S., Mahalakshmi, A. M., et al. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02990-5 · Cited by 116
Methionine oxidation stabilizes non-toxic oligomers of α-synuclein through strengthening the auto-inhibitory intra-molecular long-range interactions
Zhou, W., Long, C., Reaney, S. H., Monte, D. A. D., Fink, A. L., & Uversky, V. N. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.12.004 · Cited by 99
Limitations of Induced Folding in Molecular Recognition by Intrinsically Disordered Proteins
Házy, E., & Tompa, P. (2009) · ChemPhysChem · doi:10.1002/cphc.200900205 · Cited by 98
On the Mechanism of Nonspecific Inhibitors of Protein Aggregation: Dissecting the Interactions of α-Synuclein with Congo Red and Lacmoid
Lendel, C., Bertoncini, C. W., Cremades, N., Waudby, C. A., Vendruscolo, M., Dobson, C. M., Schenk, D., Christodoulou, J., & Tóth, G. (2009) · Biochemistry · doi:10.1021/bi901285x · Cited by 98
Labeling Proteins with Fluorophore/Thioamide Förster Resonant Energy Transfer Pairs by Combining Unnatural Amino Acid Mutagenesis and Native Chemical Ligation
Wissner, R. F., Batjargal, S., Fadzen, C. M., & Petersson, E. J. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4005943 · Cited by 94
The Effect of Osmolytes on Protein Fibrillation
Macchi, F., Eisenkolb, M., Kiefer, H., & Otzen, D. E. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13033801 · Cited by 93
Protein Disorder Prevails under Crowded Conditions
Szasz, C., Alexa, A., Tóth, K., Rakács, M., Langowski, J., & Tompa, P. (2011) · Biochemistry · doi:10.1021/bi200365j · Cited by 86
Phthalocyanine Tetrasulfonates Affect the Amyloid Formation and Cytotoxicity of α-Synuclein
Lee, E.-N., Cho, H.-J., Lee, C.-H., Lee, D., Chung, K. C., & Paik, S. R. (2004) · Biochemistry · doi:10.1021/bi0356707 · Cited by 86
DNA induces folding in α-synuclein: Understanding the mechanism using chaperone property of osmolytes
Hegde, M. L., & Rao, K. S. J. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.042 · Cited by 83
TMAO Promotes Fibrillization and Microtubule Assembly Activity in the C-Terminal Repeat Region of Tau
Scaramozzino, F., Peterson, D. W., Farmer, P. J., Gerig, J. T. C., Graves, D. J., & Lew, J. (2006) · Biochemistry · doi:10.1021/bi052167g · Cited by 85
Trimethylamine-N-Oxide (TMAO) as a Rising-Star Metabolite: Implications for Human Health
Caradonna, E., Abate, F., Schiano, E., Paparella, F., Ferrara, F., Vanoli, E., Difruscolo, R., Goffredo, V. M., Amato, B., Setacci, C., et al. (2025) · Metabolites · doi:10.3390/metabo15040220 · Cited by 93
Stability prediction of canonical and non-canonical structures of nucleic acids in various molecular environments and cells
Takahashi, S., & Sugimoto, N. (2020) · Chemical Society Reviews · doi:10.1039/d0cs00594k · Cited by 80
Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape
Ferreon, A. C. M., Moosa, M. M., Gambin, Y., & Deniz, A. A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201802109 · Cited by 74
Hydrogen Bonding Progressively Strengthens upon Transfer of the Protein Urea-Denatured State to Water and Protecting Osmolytes
Holthauzen, L. M. F., Rösgen, J., & Bolen, D. W. (2010) · Biochemistry · doi:10.1021/bi9015499 · Cited by 74
Gut Microbiota-Derived Metabolite Trimethylamine N-Oxide as a Biomarker in Early Parkinson’s Disease
Chung, S. J., Rim, J. H., Ji, D., Lee, S., Yoo, H. S., Jung, J. H., Baik, K., Choi, Y., Ye, B. S., Sohn, Y. H., et al. (2021) · Nutrition · doi:10.1016/j.nut.2020.111090 · Cited by 74
The osmolyte betaine promotes protein misfolding and disruption of protein aggregates
Natalello, A., Liu, J. L., Ami, D., Doglia, S. M., & de Marco, A. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22266 · Cited by 74
The Brain–Gut Axis, an Important Player in Alzheimer and Parkinson Disease: A Narrative Review
Caradonna, E., Nemni, R., Bifone, A., Gandolfo, P., Costantino, L., Giordano, L., Mormone, E., Macula, A., Cuomo, M., Difruscolo, R., et al. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13144130 · Cited by 79
A Chemical Chaperone Decouples TDP-43 Disordered Domain Phase Separation from Fibrillation
Choi, K., Tsoi, P. S., Moosa, M. M., Paulucci-Holthauzen, A. A., Liao, S.-C. J., Ferreon, J. C., & Ferreon, A. C. M. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b01051 · Cited by 67
Clinical significance and potential role of trimethylamine N-oxide in neurological and neuropsychiatric disorders
Mudimela, S., Vishwanath, N. K., Pillai, A., Morales, R., Marrelli, S. P., Barichello, T., & Giridharan, V. V. (2022) · Drug Discovery Today · doi:10.1016/j.drudis.2022.08.002 · Cited by 71
The aggregation of alpha‐synuclein is stimulated by FK506 binding proteins as shown by fluorescence correlation spectroscopy
Gérard, M., Debyser, Z., Desender, L., Kahle, P. J., Baert, J. H., Baekelandt, V., & Engelborghs, Y. (2006) · The FASEB Journal · doi:10.1096/fj.05-5126fje · Cited by 66
The Gut Metabolite Trimethylamine N‐oxide Is Associated With Parkinson's Disease Severity and Progression
Chen, S., Kuo, C., Kuo, H., Chen, C., Wu, W., Liou, J., Wu, M., & Lin, C. (2020) · Movement Disorders · doi:10.1002/mds.28246 · Cited by 65
Effects of Osmolytes on Protein Folding and Aggregation in Cells
Ignatova, Z., & Gierasch, L. M. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)28021-8 · Cited by 66
Disulfide bonds in amyloidogenesis diseases related proteins
Li, Y., Yan, J., Zhang, X., & Huang, K. (2013) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24338 · Cited by 65
Relationship between functional activity and protein stability in the presence of all classes of stabilizing osmolytes
Jamal, S., Poddar, N. K., Singh, L. R., Dar, T. A., Rishi, V., & Ahmad, F. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07317.x · Cited by 64
Osmolytes Induce Structure in an Early Intermediate on the Folding Pathway of Barstar
Pradeep, L., & Udgaonkar, J. B. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406323200 · Cited by 62
Modulation of human IAPP fibrillation: cosolutes, crowders and chaperones
Gao, M., Estel, K., Seeliger, J., Friedrich, R. P., Dogan, S., Wanker, E. E., Winter, R., & Ebbinghaus, S. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp04682j · Cited by 62
Forty years of research on osmolyte-induced protein folding and stability
Singh, L. R., Poddar, N. K., Dar, T. A., Rahman, S., Kumar, P., & Ahmad, F. (2011) · Journal of the Iranian Chemical Society · doi:10.1007/bf03246197 · Cited by 61
Coordination abilities of N-terminal fragments of α-synuclein towards copper(II) ions: A combined potentiometric and spectroscopic study
Kowalik‐Jankowska, T., Rajewska, A., Wiśniewska, K., Grzonka, Z., & Jezierska, J. (2005) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2005.08.008 · Cited by 59
Natural Osmolytes Remodel the Aggregation Pathway of Mutant Huntingtin Exon 1
Borwankar, T., Röthlein, C., Zhang, G., Techen, A., Dosche, C., & Ignatova, Z. (2011) · Biochemistry · doi:10.1021/bi1018368 · Cited by 60
Osmolytes: Wonder molecules to combat protein misfolding against stress conditions
Khan, S., Siraj, S., Shahid, M., Haque, M. M., & Islam, A. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123662 · Cited by 57
Real-time analysis of amyloid fibril formation of α-synuclein using a fibrillation-state-specific fluorescent probe of JC-1
Lee, J., Lee, I., Choe, Y., Kang, S.-S., Kim, H. Y., Gai, W.-P., Hahn, J., & Paik, S. R. (2008) · Biochemical Journal · doi:10.1042/bj20081572 · Cited by 57
Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis
Gadhe, L. G., Sakunthala, A., Mukherjee, S., Gahlot, N., Bera, R., Sawner, A. S., Kadu, P., & Maji, S. K. (2021) · Biophysical Chemistry · doi:10.1016/j.bpc.2021.106736 · Cited by 56
Under‐folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis
Uversky, V. N. (2013) · Biopolymers · doi:10.1002/bip.22298 · Cited by 56
In situ analysis of osmolyte mechanisms of proteome thermal stabilization
Pepelnjak, M., Velten, B., Näpflin, N. C., von Rosen, T., Palmiero, U. C., Ko, J. H., Maynard, H. D., Arosio, P., Weber-Ban, E. U., de Souza, N., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01568-7 · Cited by 58
The Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPP
Gao, M., & Winter, R. (2015) · Journal of Diabetes Research · doi:10.1155/2015/849017 · Cited by 54
Effects of the osmolyte trimethylamine-N-oxide on conformation, self-association, and two-dimensional crystallization of myelin basic protein
Hill, C. M., Bates, I. R., White, G. F., Hallett, F. R., & Harauz, G. (2002) · Journal of Structural Biology · doi:10.1016/s1047-8477(02)00513-0 · Cited by 53
Two Disaccharides and Trimethylamine N-Oxide Affect Aβ Aggregation Differently, but All Attenuate Oligomer-Induced Membrane Permeability
Qi, W., Zhang, A., Good, T. A., & Fernández, E. (2009) · Biochemistry · doi:10.1021/bi9006397 · Cited by 52
Gut microbial metabolites in Parkinson's disease: Association with lifestyle, disease characteristics, and treatment status
Voigt, R. M., Wang, Z., Brown, J. M., Engen, P. A., Naqib, A., Goetz, C. G., Hall, D. A., Metman, L. V., Shaikh, M., Forsyth, C. B., et al. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105780 · Cited by 51
Temperature‐induced reversible conformational change in the first 100 residues of α‐synuclein
McNulty, B. C., Tripathy, A., Young, G. B., Charlton, L. M., Orans, J., & Pielak, G. J. (2006) · Protein Science · doi:10.1110/ps.051867106 · Cited by 49
Inhibition of formation of α-synuclein inclusions by mannosylglycerate in a yeast model of Parkinson's disease
Faria, C., Jorge, C. D., Borges, N., Tenreiro, S., Outeiro, T. F., & Santos, H. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.04.015 · Cited by 50
Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models
Sedov, I. A., & Khaibrakhmanova, D. R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113428 · Cited by 48
Solute’s Perspective on How Trimethylamine Oxide, Urea, and Guanidine Hydrochloride Affect Water’s Hydrogen Bonding Ability
Pazos, I. M., & Gai, F. (2012) · The Journal of Physical Chemistry B · doi:10.1021/jp307414s · Cited by 48
Unravelling the role of gut microbiota in Parkinson’s disease progression: Pathogenic and therapeutic implications
Rani, L., & Mondal, A. C. (2021) · Neuroscience Research · doi:10.1016/j.neures.2021.01.001 · Cited by 48
Observation of molecular inhibition and binding structures of amyloid peptides
Wang, C., Yang, A., Li, X., Li, D., Zhang, M., Du, H., Li, C., Guo, Y., Mao, X., Dong, M., et al. (2012) · Nanoscale · doi:10.1039/c2nr11508e · Cited by 46
The effects of the flavonoid baicalein and osmolytes on the Mg 2+ accelerated aggregation/fibrillation of carboxymethylated bovine 1SS-α-lactalbumin
Bomhoff, G., Sloan, K., McLain, C., Gogol, E. P., & Fisher, M. T. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.02.001 · Cited by 44
Parkinsons Disease: Genetics and Beyond
Inamdar, N., Arulmozhi, D. K., Tandon, A., & Bodhankar, S. L. (2007) · Current Neuropharmacology · doi:10.2174/157015907780866893 · Cited by 46
Pharmacological chaperones for the misfolded melanocortin-4 receptor associated with human obesity
Huang, H., Wang, W., & Tao, Y. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.03.001 · Cited by 44
Molecular Crowding and Hydration Regulating of G-Quadruplex Formation
Miyoshi, D., Fujimoto, T. R., & Sugimoto, N. (2012) · Topics in current chemistry · doi:10.1007/128_2012_335 · Cited by 41
The Accumulation and Molecular Effects of Trimethylamine N-Oxide on Metabolic Tissues: It’s Not All Bad
Krueger, E. S., Lloyd, T. S., & Tessem, J. S. (2021) · Nutrients · doi:10.3390/nu13082873 · Cited by 41
Proline to the rescue
Fisher, M. T. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606106103 · Cited by 40
The role of water in amyloid aggregation kinetics
Stephens, A. D., & Schierle, G. S. K. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.06.001 · Cited by 38
Weighted persistent homology for osmolyte molecular aggregation and hydrogen-bonding network analysis
Anand, D. V., Meng, Z., Xia, K., & Mu, Y. (2020) · Scientific Reports · doi:10.1038/s41598-020-66710-6 · Cited by 41
Protein Quality Control System in Neurodegeneration: A Healing Company Hard to Beat but Failure is Fatal
Chhangani, D., & Mishra, A. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8411-0 · Cited by 37
Modulation of the Polymerization Kinetics of α/β‐Tubulin by Osmolytes and Macromolecular Crowding
Schummel, P. H., Gao, M., & Winter, R. (2016) · ChemPhysChem · doi:10.1002/cphc.201601032 · Cited by 37
Small Molecules Attenuate the Interplay between Conformational Fluctuations, Early Oligomerization and Amyloidosis of Alpha Synuclein
Ghosh, S. K., Kundu, A., & Chattopadhyay, K. (2018) · Scientific Reports · doi:10.1038/s41598-018-23718-3 · Cited by 36
Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods
Bujalowski, P. J., & Oberhauser, A. F. (2013) · Methods · doi:10.1016/j.ymeth.2013.03.010 · Cited by 37
Effects of Hydrophobic Macromolecular Crowders on Amyloid β (16–22) Aggregation
Latshaw, D. C., & Hall, C. K. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.05.032 · Cited by 34
Solution NMR and CD spectroscopy of an intrinsically disordered, peripheral membrane protein: evaluation of aqueous and membrane-mimetic solvent conditions for studying the conformational adaptability of the 18.5 kDa isoform of myelin basic protein (MBP)
Libich, D. S., & Harauz, G. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0334-8 · Cited by 34
Osmolyte Trimethylamine N-Oxide Converts Recombinant α-Helical Prion Protein to its Soluble β-Structured Form at High Temperature
Nandi, P., Bera, A., & Sizaret, P.-Y. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.07.060 · Cited by 35
Biomolecular Crowding Arising from Small Molecules, Molecular Constraints, Surface Packing, and Nano-Confinement
Hilaire, M. R., Abaskharon, R. M., & Gai, F. (2015) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.5b00957 · Cited by 33
The Osmolyte TMAO Modulates Protein Folding Cooperativity by Altering Global Protein Stability
Jethva, P. N., & Udgaonkar, J. B. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00698 · Cited by 33
Phenylketonuria as a protein misfolding disease: The mutation pG46S in phenylalanine hydroxylase promotes self-association and fibril formation
Leandro, J., Simonsen, N., Saraste, J., Leandro, P., & Flatmark, T. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.09.015 · Cited by 33
Addressing Mechanism of Fibrillization/Aggregation and Its Prevention in Presence of Osmolytes: Spectroscopic and Calorimetric Approach
Choudhary, S., & Kishore, N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104600 · Cited by 29
Conformational Ensembles of α-Synuclein Derived Peptide with Different Osmolytes from Temperature Replica Exchange Sampling
Jamal, S., Kumari, A., Singh, A. P., Goyal, S., & Grover, A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00684 · Cited by 29
Effects of the osmolyte TMAO (Trimethylamine-N-oxide) on aqueous hydrophobic contact-pair interactions
Macdonald, R. D., & Khajehpour, M. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.10.001 · Cited by 29
TMAO-Protein Preferential Interaction Profile Determines TMAO’s Conditional In Vivo Compatibility
Hong, J., & Xiong, S. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.09.035 · Cited by 29
DJ-1 (Park7) affects the gut microbiome, metabolites and the development of innate lymphoid cells (ILCs)
Singh, Y., Trautwein, C., Dhariwal, A., Salker, M. S., Alauddin, M., Zizmare, L., Pelzl, L., Feger, M., Admard, J., Casadei, N., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-72903-w · Cited by 29
Dietary patterns affect Parkinson's disease via the microbiota-gut-brain axis
Chu, C., Yu, L., Chen, W., Tian, F., & Zhai, Q. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.07.004 · Cited by 27
The relationship between Parkinson’s disease and gastrointestinal diseases
Zeng, J., Wang, X., Pan, F., & Mao, Z. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.955919 · Cited by 26

Authors: Uversky, V. N., Li, J., & Fink, A. L.
Affiliations: Russian Academy of Sciences (RU)
University of California, Santa Cruz (US)
Corresponding author: Fink, Anthony L.
ORCID: Uversky, Vladimir N.
Li, Jie
Venue: FEBS Letters
Publisher: Wiley
Published: 2001-11-09
Volume: 509
Issue: 1
Pages: 31-35
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/s0014-5793(01)03121-0
OpenAlex: W1988949963
Cited by: 208
References: 34
Citations by year: 2026: 9 · 2025: 13 · 2024: 11 · 2023: 5 · 2022: 12 · 2021: 8 · 2020: 10 · 2019: 7 · 2018: 8 · 2017: 8 · 2016: 8 · 2015: 8 · 2014: 12 · 2013: 10 · 2012: 11
FWCI: 3.54
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: FEBS Letters (publishedVersion)
PubMed (publishedVersion)
Digital Commons - University of South Florida (University of South Florida) (submittedVersion)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Keywords: trimethylamine N-oxide, alpha-synuclein, protein folding, osmolytes, intrinsically disordered proteins, fibril formation, folding intermediates, oligomerization, helical conformation, protein self-association
MeSH terms: Acrylamides, Circular Dichroism, Dose-Response Relationship, Drug, Methylamines, Nerve Tissue Proteins, Peptides, Protein Conformation, Recombinant Proteins, Scattering, Radiation, Spectrometry, Fluorescence, Time Factors, X-Rays, Oxidants, Protein Structure, Secondary, Protein Folding, Synucleins, alpha-Synuclein

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Trimethylamine‐ N ‐oxide‐induced folding of α‐synuclein

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks