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
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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“When the concentration of TMAO is high enough, α-synuclein forms oligomers in which the subunits are folded and are not able to fibrillate [88].”
From Implication of Trimethylamine N-Oxide (TMAO) in Disease: Potential Biomarker or New Therapeutic Target (2018) · cites this paper as [88]
Citations
Cites
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
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
Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,519
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
Research works printed but not linked: 1
- Naiki H., 1990, Lab. Invest., 62, 768
Cited by
Sorted by citations
Items 101–200 of 208
Targeting the Chameleon: a Focused Look at α-Synuclein and Its Roles in Neurodegeneration
Silva, B. A., Breydo, L., & Uversky, V. N. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8334-1 · Cited by 25
Ferrie, J. J., Ieda, N., Haney, C. M., Walters, C. R., Sungwienwong, I., Yoon, J., & Petersson, E. J. (2017) · Chemical Communications · doi:10.1039/c7cc05492k · Cited by 25
Forced Folding of a Disordered Protein Accesses an Alternative Folding Landscape
Moosa, M. M., Ferreon, A. C. M., & Deniz, A. A. (2014) · ChemPhysChem · doi:10.1002/cphc.201402661 · Cited by 25
Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein
Ferrie, J. J., Haney, C. M., Yoon, J., Pan, B., Lin, Y., Fakhraai, Z., Rhoades, E. R., Nath, A., & Petersson, E. J. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.006 · Cited by 25
Venkatesh, Y., Narayan, K. B., Baumgart, T., & Petersson, E. J. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c17933 · Cited by 24
Ahanger, I. A., & Dar, T. A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102538 · Cited by 26
Solution Model of the Intrinsically Disordered Polyglutamine Tract-Binding Protein-1
Rees, M., Gorba, C., de Chiara, C., Bui, T. T. T., Garcia‐Maya, M., Drake, A. F., Okazawa, H., Pastore, A., Svergun, D. I., & Chen, Y. W. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.02.047 · Cited by 24
Dequalinium-induced Protofibril Formation of α-Synuclein
Lee, C., Kim, H. J., Lee, J., Cho, H.-J., Kim, J., Chung, K. C., Jung, S., & Paik, S. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505307200 · Cited by 24
Asthana, S., Bhattacharyya, D., Kumari, S., Nayak, P. S., Saleem, M., Bhunia, A., & Jha, S. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.01.269 · Cited by 23
Park, S. J., Kim, K. W., & Lee, E. J. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00994 · Cited by 27
Warepam, M., & Singh, L. R. (2015) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2015.03.017 · Cited by 22
Calibrated Langevin-dynamics simulations of intrinsically disordered proteins
Smith, W. W., Ho, P.-Y., & O’Hern, C. S. (2014) · Physical Review E · doi:10.1103/physreve.90.042709 · Cited by 22
Estrela, N., Franquelim, H. G., Lopes, C., Tavares, E., Macedo, J. A., Christiansen, G., Otzen, D. E., & Melo, E. P. (2015) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24921 · Cited by 21
Yang, Y., Mu, Y., & Li, W. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp01205a · Cited by 20
Probing the Nongeneralized Amyloid Inhibitory Mechanism of Hydrophobic Chaperone
Masroor, A., Zaidi, N., Chandel, T. I., Aqueel, Z., Malik, S., & Khan, R. H. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00593 · Cited by 20
Persistent homology analysis of osmolyte molecular aggregation and their hydrogen-bonding networks
Xia, K., Anand, D. V., Saxena, S., & Mu, Y. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp03009c · Cited by 17
Protein Fibrillation under Crowded Conditions
Gorensek‐Benitez, A. H., Kirk, B., & Myers, J. K. (2022) · Biomolecules · doi:10.3390/biom12070950 · Cited by 18
α-synuclein overexpression and the microbiome shape the gut and brain metabolome in mice
Morais, L. H., Boktor, J. C., MahmoudianDehkordi, S., Kaddurah‐Daouk, R., & Mazmanian, S. K. (2024) · npj Parkinson s Disease · doi:10.1038/s41531-024-00816-w · Cited by 24
Fully reduced granulin-B is intrinsically disordered and displays concentration-dependent dynamics
Ghag, G., Wolf, L. M., Reed, R. G., van der Munnik, N. P., Mundoma, C., Moss, M. A., & Rangachari, V. (2016) · Protein Engineering Design and Selection · doi:10.1093/protein/gzw005 · Cited by 17
Nascimento, C., Leandro, J., de Almeida, I. T., & Leandro, P. (2008) · The Protein Journal · doi:10.1007/s10930-008-9149-9 · Cited by 17
Ahmad, A. (2010) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2009.12.017 · Cited by 17
Liu, J., Ge, P., Luo, Y., Sun, Z., Luo, X., Li, H., Pei, B., Xun, L., Zhang, X., Jiang, Y., et al. (2025) · Drug Design Development and Therapy · doi:10.2147/dddt.s512207 · Cited by 20
Disorder-to-order transitions in the molten globule-like Golgi Reassembly and Stacking Protein
Mendes, L. F. S., Basso, L. G. M., Kumagai, P. S., Fonseca-Maldonado, R., & Costa-Filho, A. J. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.01.009 · Cited by 16
Mondal, B., & Reddy, G. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.8b11128 · Cited by 16
Cosolvent effects on the growth of amyloid fibrils
Reddy, G., Muttathukattil, A. N., & Mondal, B. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.12.011 · Cited by 15
Kumari, K., Warepam, M., Bansal, A. K., Dar, T. A., Uversky, V. N., & Singh, L. R. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04087-z · Cited by 16
Hazari, Y., Habib, M., Bashir, S., Bashir, A., Hilal, N., Irfan, S., Haq, E. U., & Fazili, K. M. (2016) · Life Sciences · doi:10.1016/j.lfs.2016.01.002 · Cited by 15
Yagi, H., Takeuchi, H., Ogawa, S., Ito, N., Sakane, I., Hongo, K., Mizobata, T., Goto, Y., & Kawata, Y. (2010) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2010.07.007 · Cited by 14
Mukherjee, S., Knop, J., Oliva, R., Möbitz, S., & Winter, R. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00108f · Cited by 15
Osmolyte Effects on the Growth of Amyloid Fibrils
Muttathukattil, A. N., & Reddy, G. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b09215 · Cited by 14
Kundu, A., Verma, P. K., & Cho, M. (2018) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.7b03297 · Cited by 14
Protein Misfolding in Lipid-Mimetic Environments
Uversky, V. N. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-17344-3_2 · Cited by 13
A chemical chaperone induces inhomogeneous conformational changes in flexible proteins
Hamdane, D., Velours, C., Cornu, D., Nicaise, M., Lombard, M., & Fontecave, M. (2016) · Physical Chemistry Chemical Physics · doi:10.1039/c6cp03635j · Cited by 12
Rajagopalan, L., Rösgen, J., Bolen, D. W., & Rajarathnam, K. (2005) · Biochemistry · doi:10.1021/bi051219z · Cited by 12
Structural and Conformational Prerequisites of Amyloidogenesis
Uversky, V. N., Fernández, A., & Fink, A. L. (2007) · Springer eBooks · doi:10.1007/0-387-25919-8_1 · Cited by 12
Gątarek, P., Pawelczyk, M., Bobrowska‐Korczak, B., Giebułtowicz, J., Glabinski, A. R., & Kałużna‐Czaplińska, J. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26104575 · Cited by 11
Devi, S., Garg, D. K., & Bhat, R. (2023) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2023.140917 · Cited by 11
Ølnes, Å. S., Teigen, M., Laerdahl, J. K., Leren, T. P., Strøm, T. B., & Bjune, K. (2023) · PLoS ONE · doi:10.1371/journal.pone.0294764 · Cited by 11
TMAO to the rescue of pathogenic protein variants
Kumari, K., Singh, K. S., Singh, K., Bakhshi, R., & Singh, L. R. (2022) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2022.130214 · Cited by 10
Disintegration of amyloid fibrils of alpha-synuclein by dequalinium.
Park, J.-W., Lee, I.-H., Hahn, J., Kim, J., Chung, K., & Paik, S. (2008) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagen.2008.07.006 · Cited by 10
Warepam, M., Sharma, G. S., Dar, T. A., Khan, M. K. A., & Singh, L. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109408 · Cited by 11
Trimethylamine-N-oxide modulates the reductive unfolding of onconase
Gahl, R. F., Narayan, M., Xu, G., & Scheraga, H. A. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.10.088 · Cited by 11
Oligomers, fibrils and aggregates formed by alpha-synuclein: role of solution conditions
Panuganti, V., & Roy, I. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1856721 · Cited by 10
Qin, Z., Wu, W., Yang, X., Wang, X., Ding, A., Huang, Y., Tang, J., Jiang, S., Zhang, P., Qian, C., et al. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1592524 · Cited by 13
Bhat, M. Y., Mir, I. A., Hussain, M. U., Singh, L. R., & Dar, T. A. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2053744 · Cited by 10
Siraj, S., Yameen, D., Shamsi, A., Khan, F., Islam, A., & Haque, M. M. (2023) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2023.121270 · Cited by 9
Effect of mammalian kidney osmolytes on the folding pathway of sheep serum albumin
Dar, M. A., Islam, A., Hassan, M. I., & Ahmad, F. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.01.090 · Cited by 10
Smith, W. W., Schreck, C. F., Hashem, N., Soltani, S., Nath, A., Rhoades, E. R., & O’Hern, C. S. (2012) · Physical Review E · doi:10.1103/physreve.86.041910 · Cited by 9
A Set of Reliable Samples for the Study of Biomarkers for the Early Diagnosis of Parkinson's Disease
Konjevod, M., Sáiz, J., Barbas, C., Bergareche, A., Ardanáz, E., Huerta, J. M., Vinagre‐Aragón, A., Erro, M. E., Chirlaque, M. D., Abilleira, E., et al. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.844841 · Cited by 9
Tulla‐Puche, J., Getun, I. V., Woodward, C. K., & Bárány, G. (2004) · Biochemistry · doi:10.1021/bi035301a · Cited by 9
Factors Affecting the Fibrillation of α-Synuclein, a Natively Unfolded Protein
Fink, A. L. (2006) · Springer eBooks · doi:10.1007/978-0-387-36063-8_12 · Cited by 8
Sankaranarayanan, K. (2015) · Biointerphases · doi:10.1116/1.4922291 · Cited by 8
Effect of osmolytes on the binding of EGR 1 transcription factor to DNA
Mikles, D. C., Bhat, V. S., Schuchardt, B. J., McDonald, C. B., & Farooq, A. (2014) · Biopolymers · doi:10.1002/bip.22556 · Cited by 8
Small angle X-ray scattering study of the yeast prion Ure2p
Zhu, L. Q., Kihara, H., Kojima, M., Zhou, J., & Perrett, S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.10.027 · Cited by 8
Ligand interactions and the protein order-disorder energetic continuum
Moosa, M. M., Ferreon, J. C., & Ferreon, A. C. M. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.05.007 · Cited by 8
Magsumov, T. I., Ibraev, I., & Sedov, I. A. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.4c04919 · Cited by 7
Role of Osmolytes in Amyloidosis
Khan, S., Mueed, Z., Deval, R., Rai, P. K., Prajapati, D. K., & Poddar, N. K. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.83647 · Cited by 7
Effects of Ions and Small Compounds on the Structure of Aβ42 Monomers
Mahmoudinobar, F., Nilsson, B. L., & Dias, C. L. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c09617 · Cited by 7
Uversky, V. N., & Fink, A. L. (2005) · Wiley eBooks · doi:10.1002/9783527619344.ch11 · Cited by 7
Dollar, A. N., & Webb, I. (2026) · Analytical Chemistry · doi:10.1021/acs.analchem.5c05078 · Cited by 6
Ahanger, I. A., Hajam, I. B., & Wani, O. H. (2025) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.10.006 · Cited by 6
α-Synuclein Fibrils as Penrose Machines: A Chameleon in the Gear
Giorgi, F. D., Uversky, V. N., & Ichas, F. (2022) · Biomolecules · doi:10.3390/biom12040494 · Cited by 6
Ray, S., Banerjee, V., Blaise, M., Banerjee, B., Das, K. P., Kern, D., & Banerjee, R. (2014) · The Protein Journal · doi:10.1007/s10930-014-9546-1 · Cited by 6
Neto, D. P. A., de Godoy, J. V. P., Tostes, K., Bosque, B. P., Rodrigues, P. V., Rocco, S. A., Sforça, M. L., & Fonseca, M. D. C. (2023) · Neuroscience · doi:10.1016/j.neuroscience.2023.06.010 · Cited by 5
Factors responsible for alpha-Synuclein aggregation
Singh, K. S., Verma, R., Singh, N., Singh, L. R., & Gupta, A. (2025) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.11.004 · Cited by 7
Metabolomics: a new frontier in neurodegenerative disease biomarker discovery
Verma, K. K., Gaur, P. K., Gupta, S. L., Lata, K., Kaushik, R., & Sharma, V. M. (2025) · Metabolomics · doi:10.1007/s11306-025-02267-7 · Cited by 5
Phogat, P., Bansal, A., Nain, N., Khan, S., Saso, L., & Kukreti, S. (2025) · BioMolecular Concepts · doi:10.1515/bmc-2025-0053 · Cited by 5
Fazili, N. A., & Naeem, A. (2016) · Journal of Fluorescence · doi:10.1007/s10895-016-1856-6 · Cited by 5
Protein Refolding/Renaturation
Kumar, D. (2011) · Elsevier eBooks · doi:10.1016/b978-0-08-088504-9.00136-7 · Cited by 6
Vinje, T., Laerdahl, J. K., Bjune, K., Leren, T. P., & Strøm, T. B. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz114 · Cited by 5
Modifiers of Protein Aggregation—From Nonspecific to Specific Interactions
Levy‐Sakin, M., Scherzer‐Attali, R., & Gazit, E. (2012) · Wiley eBooks · doi:10.1002/9781118183373.ch15 · Cited by 5
Macromolecular crowding: how it affects protein structure, disorder, and catalysis
Gupta, M. N., & Uversky, V. N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-99533-7.00016-9 · Cited by 5
Halophilic Properties and their Manipulation and Application
Arakawa, T., Tokunaga, H., Ishibashi, M., & Tokunaga, M. (2012) · Extremophiles · doi:10.1002/9781118394144.ch4 · Cited by 4
Role of TMAO on Folding Behavior of Various Proteins Associated with Neurodegeneration
Kumari, K. (2024) · Springer eBooks · doi:10.1007/978-981-97-6001-5_3 · Cited by 4
Methods for measuring structural disorder in proteins
Gondelaud, F., Schramm, A., Brocca, S., Natalello, A., Grandori, R., Santambrogio, C., & Longhi, S. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-99533-7.00018-2 · Cited by 3
Effect of ethanol as molecular crowding agent on the conformational dynamics of α-synuclein
(2020) · Letters in Applied NanoBioScience · doi:10.33263/lianbs91.779783 · Cited by 4
Small Molecule Osmolytes Can Modulate Proteostasis
Sharma, G. S., Warepam, M., Singh, L. R., & Dar, T. A. (2015) · Springer eBooks · doi:10.1007/978-81-322-2467-9_3 · Cited by 3
Modulation of Protein Aggregation/Fibrillation by Osmolytes
Bhat, M. Y., Singh, L. R., & Dar, T. A. (2017) · Springer eBooks · doi:10.1007/978-981-10-3707-8_6 · Cited by 3
Devi, S., Garg, D. K., & Bhat, R. (2025) · Biochemistry · doi:10.1021/acs.biochem.5c00518 · Cited by 2
Trimethylamine N-oxide participates in human diseases by causing endoplasmic reticulum stress
Kumari, K., Arora, A., Natarajan, N., Ansari, N. A., & Singh, L. R. (2025) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2025.130900 · Cited by 2
Osmolyte-Mediated Protein Stabilization: Unraveling Interactions Across Conformational Landscapes
Warepam, M., Nongdam, P., & Rahaman, H. (2024) · Springer eBooks · doi:10.1007/978-981-97-6001-5_4 · Cited by 2
Therapeutic approaches in proteinopathies
Nabi‐Afjadi, M., Dabirmanesh, B., & Uversky, V. N. (2024) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.03.008 · Cited by 2
Yao, W., Liu, L., Wang, J., Chen, S., Zhang, C., Liao, R., Wang, Y., Ou, K., Jiang, L., Yu, Y., et al. (2026) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-026-01738-2 · Cited by 1
The gut–brain axis and trimethylamine N-oxide: an emergent biomarker in neurological diseases
Arangia, A., Paola, R. D., Cuzzocrea, S., Siracusa, R., D’Amico, R., & Impellizzeri, D. (2026) · Neuroscience · doi:10.1016/j.neuroscience.2026.05.005 · Cited by 1
Parkinson’s disease and inflammatory bowel disease: exploring the connection between the two
Zhou, X., Zhang, X., Liang, H., & Bi, Y. (2026) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2026.01 · Cited by 1
Amyloid Fibril Formation of Natively Unfolded Proteins
Uversky, V. N., & Fink, A. L. (2008) · Wiley eBooks · doi:10.1002/9783527610754.md15 · Cited by 1
Vlad, C. (2011) · KOPS (University of Konstanz) · Cited by 1
Apetri, M. M. (2006) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 1
Experimental Evidence for Phosphorylation-Driven Allosteric Regulation of Alpha Synuclein FunctionPreprint
Dollar, A. N., & Webb, I. K. (2025) · bioRxiv · doi:10.1101/2025.02.20.639338
Fundamentals of Protein Folding
Uversky, V. N. (2014) · Wiley eBooks · doi:10.1002/9781118845363.ch1
The Effects of Trimethylamine N-Oxide on the Structural Stability of Prion Protein
Yang, B. C., You, K.-H., Wang, S.-C., Chen, H., & Lee, C.-I. (2011) · InTech eBooks · doi:10.5772/28885
Marine Natural Products for Protein Misfolding Modulation
James, C., & Vanya, K. (2013) · InTech eBooks · doi:10.5772/54585
Dottorato di Ricerca in: Biologia Funzionale dei Sistemi Cellulari e Molecolari - Ciclo XXV
Aioanei, D., Scarlato, V., Samor, B., & Brucale, M. (2013)
Muralidhar, L. H. (2005) · CFTRI Institutional Repository
Rabbani, G. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.11.022
Retracted(2009) · Chapman & Hall/CRC eBooks · doi:10.1201/9781420078930.bmatt
Physicochemical Properties of Non‐canonical Nucleic Acids
Sugimoto, N. (2021) · doi:10.1002/9783527817856.ch4
Liu, A. Y. ‐., Mathew, A., Karim, C., Eshak, P., & Chen, K. Y. (2024) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.08.005
Effect of Organic Osmolytes on Protein Folding Intermediates
Singh, K. S., Mohanty, D., Meena, A., Singh, N. O., & Sharma, G. S. (2024) · Springer eBooks · doi:10.1007/978-981-97-6001-5_2
Metadata
- 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.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2001-11-09
- Volume
- 509
- Issue
- 1
- Pages
- 31-35
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- 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
- 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