Regulation of α-synuclein by chaperones in mammalian cells

Neurodegenerative diseases and oxidative stress

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The many faces of α-synuclein: from structure and toxicity to therapeutic target

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Molecular Chaperone Functions in Protein Folding and Proteostasis

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The HSP90 chaperone machinery

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100 years of Lewy pathology

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Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

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Structural disorder of monomeric α-synuclein persists in mammalian cells

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Composition of isolated synaptic boutons reveals the amounts of vesicle trafficking proteins

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Structural basis for the dynamic chaperoning of disordered clients by Hsp90

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Chaperone-mediated autophagy in neurodegenerative diseases: mechanisms and therapy

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Insights Into Peptide Inhibition of Alpha-Synuclein Aggregation

Torpey, J. H., Meade, R. M., Mistry, R., Mason, J. M., & Madine, J. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.561462 · Cited by 18

Enhanced separation of emulsified oil from alkaline-surfactant-polymer flooding produced water by Gordonia sp. TD-4: From interactions to mitigation strategies and bio-demulsifying mechanisms

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Phloroglucinol, a clinical-used antispasmodic, inhibits amyloid aggregation and degrades the pre-formed amyloid proteins

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Concomitant protein pathogenesis in Parkinson’s disease and perspective mechanisms

Han, Y., & He, Z. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1189809 · Cited by 18

Establishing Order Through Disorder by the Hsp90 Molecular Chaperone

Babu, N. L., & Freeman, B. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168460 · Cited by 18

Hypoxia Pathways in Parkinson’s Disease: From Pathogenesis to Therapeutic Targets

Gao, Y., Zhang, J., Tang, T., & Liu, Z. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910484 · Cited by 22

Alpha-synuclein interacts with regulators of ATP homeostasis in mitochondria

Serdiuk, T., Fleischmann, Y., Ghosh, D., Delparente, A., Reber, V., Frey, L., Rhyner, D., Gerez, J., Volkmar, N., Kralickova, L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62895-4 · Cited by 16

Current Understanding of Protein Aggregation in Neurodegenerative Diseases

Hu, C., Lin, M., Wang, C., & Zhang, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110568 · Cited by 21

α-Synuclein in Parkinson’s Disease: Does a Prion-Like Mechanism of Propagation from Periphery to the Brain Play a Role?

Zheng, H., Shi, C., Luo, H., Fan, L., Yang, Z., Hu, X., Zhang, Z., Zhang, S., Hu, Z., Fan, Y., et al. (2020) · The Neuroscientist · doi:10.1177/1073858420943180 · Cited by 21

The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ

Williams, D. M., Thorn, D. C., Dobson, C. M., Meehan, S., Jackson, S., Woodcock, J. M., & Carver, J. A. (2021) · Molecules · doi:10.3390/molecules26206120 · Cited by 15

Structural determinants of the interactions of catechins with Aβ oligomers and lipid membranes

Ahmed, R., Huang, J., Lifshitz, R., Pomier, K. M., & Melacini, G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101502 · Cited by 15

Multi‐Dimensional Structure and Dynamics Landscape of Proteins in Mammalian Cells Revealed by In‐Cell NMR

Kadavath, H., Prymaczok, N. C., Eichmann, C., Riek, R., & Gerez, J. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202213976 · Cited by 16

UBL3 Interacts with Alpha-Synuclein in Cells and the Interaction Is Downregulated by the EGFR Pathway Inhibitor Osimertinib

Chen, B., Hasan, M. M., Zhang, H., Zhai, Q., Waliullah, A. S. M., Ping, Y., Zhang, C., Oyama, S., Mimi, M. A., Tomochika, Y., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11061685 · Cited by 16

Inhibition of toxic metal-alpha synuclein interactions by human serum albumin

Pomier, K. M., Ahmed, R., Huang, J., & Melacini, G. (2024) · Chemical Science · doi:10.1039/d3sc06285f · Cited by 16

DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular milieu

Costello, W. N., Xiao, Y., Mentink-Vigier, F., Kragelj, J., & Frederick, K. K. (2024) · Journal of Biomolecular NMR · doi:10.1007/s10858-024-00436-9 · Cited by 16

HSP90 Co-Chaperone, CacyBP/SIP, Protects α-Synuclein from Aggregation

Bohush, A., & Filipek, A. (2020) · Cells · doi:10.3390/cells9102254 · Cited by 15

Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases

Muronetz, V. I., Kudryavtseva, S. S., Leisi, E. V., Kurochkina, L. P., Barinova, K. V., & Schmalhausen, E. V. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052747 · Cited by 15

The role of structural dynamics in the thermal adaptation of hyperthermophilic enzymes

Fusco, G., Bemporad, F., Chiti, F., Dobson, C. M., & Simone, A. D. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.981312 · Cited by 15

Heat Shock Protein 90 in Parkinson’s Disease: Profile of a Serial Killer

Mansour, H. M., Mohamed, A. F., Khattab, M. M., & El-Khatib, A. S. (2023) · Neuroscience · doi:10.1016/j.neuroscience.2023.11.031 · Cited by 15

Solid-state NMR approaches to investigate large enzymes in complex with substrates and inhibitors

Schütz, A. K. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200099 · Cited by 15

Listerin promotes α-synuclein degradation to alleviate Parkinson’s disease through the ESCRT pathway

Qin, F., Cao, R., Cui, W., Bai, X., Yuan, J., Zhang, Y., Liu, Y., Cao, N., Dong, N., Zhou, M., et al. (2025) · Science Advances · doi:10.1126/sciadv.adp3672 · Cited by 16

Polymorphic USP8 allele promotes Parkinson’s disease by inducing the accumulation of α-synuclein through deubiquitination

Wu, S., Lin, T., & Xu, Y. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-05006-0 · Cited by 14

Development of a novel method for the quantification of tyrosine 39 phosphorylated α- and β-synuclein in human cerebrospinal fluid

Na, C. H., Sathe, G. J., Rosenthal, L. S., Moghekar, A., Dawson, V. L., Dawson, T. M., & Pandey, A. (2020) · Clinical Proteomics · doi:10.1186/s12014-020-09277-8 · Cited by 14

Unexpected Implication of SRP and AGO2 in Parkinson’s Disease: Involvement in Alpha-Synuclein Biogenesis

Hernandez, S. M., Tikhonova, E. B., Baca, K. R., Zhao, F., Zhu, X., & Karamyshev, A. L. (2021) · Cells · doi:10.3390/cells10102792 · Cited by 14

Gastric Enteric Glial Cells: A New Contributor to the Synucleinopathies in the MPTP-Induced Parkinsonism Mouse

Heng, Y., Li, Y., Wen, L., Yan, J., Chen, N., & Yuan, Y. (2022) · Molecules · doi:10.3390/molecules27217414 · Cited by 15

α-Synuclein and biological membranes: the danger of loving too much

Mansueto, S., Fusco, G., & Simone, A. D. (2023) · Chemical Communications · doi:10.1039/d3cc01682j · Cited by 15

Truncation-Driven Lateral Association of α-Synuclein Hinders Amyloid Clearance by the Hsp70-Based Disaggregase

Franco, A., Cuéllar, J., Fernández-Higuero, J. Á., de la Arada, I., Orozco, N., Valpuesta, J., Prado, A., & Muga, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312983 · Cited by 13

Keeping α-Synuclein at Bay: A More Active Role of Molecular Chaperones in Preventing Mitochondrial Interactions and Transition to Pathological States?

Aspholm, E. E., Matečko‐Burmann, I., & Burmann, B. M. (2020) · Life · doi:10.3390/life10110289 · Cited by 13

The role of heat shock proteins in preventing amyloid toxicity

Törner, R., Kupreichyk, T., Hoyer, W., & Boisbouvier, J. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1045616 · Cited by 12

Intrinsically disordered Pseudomonas chaperone FapA slows down the fibrillation of major biofilm‐forming functional amyloid FapC

Byeon, C., Hansen, K. H., Jeffrey, J., Saricayir, H., Andreasen, M., & Akbey, Ü. (2024) · FEBS Journal · doi:10.1111/febs.17084 · Cited by 12

Visualizing alpha‐synuclein and iron deposition in M83 mouse model of Parkinson's disease in vivo

Straumann, N., Combes, B. F., Deán‐Ben, X. L., Sternke‐Hoffmann, R., Gerez, J., Dias, I., Chen, Z., Watts, B., Rostami, I., Shi, K., et al. (2024) · Brain Pathology · doi:10.1111/bpa.13288 · Cited by 13

Structural polymorphism of α-synuclein fibrils alters the pathway of Hsc70-mediated disaggregation

Jäger, S., Tittelmeier, J., Dang, T. L., Bellande, T., Redeker, V., Buell, A. K., Hennig, J., Melki, R., Nussbaum-Krammer, C. I., Bukau, B., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00573-3 · Cited by 13

Aromaticity at position 39 in α‐synuclein: A modulator of amyloid fibril assembly and membrane‐bound conformations

Buratti, F. A., Böffinger, N. M., Garro, H. A., Flores, J. S., Hita, F. J., Gonçalves, P. D. C., Copello, F. D. R., Lizárraga, L., Rossetti, G., Carloni, P., et al. (2022) · Protein Science · doi:10.1002/pro.4360 · Cited by 12

Efficient characterization of multiple binding sites of small molecule imaging ligands on amyloid-beta, tau and alpha-synuclein

Sobek, J., Li, J., Combes, B. F., Gerez, J., Nilsson, K. P. R., Henrich, M. T., Geibl, F. F., Shi, K., Rominger, A., Oertel, W. H., et al. (2024) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-024-06806-7 · Cited by 14

Deuterium Solid State NMR Studies of Intact Bacteria Treated With Antimicrobial Peptides

Booth, V. K. (2021) · Frontiers in Medical Technology · doi:10.3389/fmedt.2020.621572 · Cited by 12

Intrinsic Disorder in α-Synuclein Regulates the Exocytotic Fusion Pore Transition

Bartolo, A. L. D., Caparotta, M., & Masone, D. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00040 · Cited by 10

Navigating the Neurobiology of Parkinson’s: The Impact and Potential of α-Synuclein

Paulėkas, E., Vanagas, T., Lagunavičius, S., Pajėdienė, E., Petrikonis, K., & Rastenytė, D. (2024) · Biomedicines · doi:10.3390/biomedicines12092121 · Cited by 12

Calcium/calmodulin-dependent serine protein kinase exacerbates mitochondrial calcium uniporter-related mitochondrial calcium overload by phosphorylating α-synuclein in Parkinson’s disease

Zhang, Q., Huang, Y., Wu, A., Duan, Q., He, P., Huang, H., Gao, Y., Nie, K., Liu, Q., & Wang, L. (2023) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2023.106385 · Cited by 12

Stabilization of 14-3-3 protein-protein interactions with Fusicoccin-A decreases alpha-synuclein dependent cell-autonomous death in neuronal and mouse models

Vinueza‐Gavilanes, R., Bravo-González, J. J., Basurco, L., Boncristiani, C., Fernández‐Irigoyen, J., Santamaría, E., Marcilla, I., Pérez‐Mediavilla, A., Luquín, M. R., Vales, Á., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106166 · Cited by 11

Understanding chaperone specificity: evidence for a ‘client code’

Omkar, S., Rysbayeva, A., & Truman, A. W. (2023) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.05.008 · Cited by 11

Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells

Kragelj, J., Ghosh, R., Xiao, Y., Dumarieh, R., Lagasca, D., Krishna, S., & Frederick, K. K. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2500367122 · Cited by 11

Implications of intracellular protein degradation pathways in Parkinson's disease and therapeutics

Amrutha, K., Mishra, A., & Singh, S. (2022) · Journal of Neuroscience Research · doi:10.1002/jnr.25101 · Cited by 11

Nuclear structure opportunities with GeV radioactive beams at FAIR

Aumann, T., Bertulani, C. A., Duer, M., Galatyuk, T., Obertelli, A., Panin, V., Rodríguez-Sánchez, J. L., Roth, R., & Stroth, J. (2024) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2023.0121 · Cited by 10

Biomimetically Engineered Amyloid-Shelled Gold Nanocomplexes for Discovering α-Synuclein Oligomer-Degrading Drugs

Lee, D., Jung, H. G., Park, D., Bang, J., Hong, J. H., Lee, S. W., Roh, S., Jang, J. W., Kim, Y.-H., Hwang, K. S., et al. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c14650 · Cited by 10

Parkinson’s disease-associated genetic variants synergistically shape brain networksPreprint

Chen, Z., Wu, B., Li, G., Zhou, L., Zhang, L., & Liu, J. (2022) · medRxiv · doi:10.1101/2022.12.25.22283938 · Cited by 10

α-Synuclein acts as a cholesteryl-ester sensor on lipid droplets regulating organelle size and abundancePreprint

Jacob, R. S., Dema, A., Chérot, H., Dumesnil, C., Cohen, S., Shalom, H. S., Rimon, N., Sibony-Nevo, O., Beck, G., Ainbinder, E., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.19.599670 · Cited by 11

MAPT rs17649553 T allele is associated with better verbal memory and higher small-world properties in Parkinson’s disease

Chen, Z., Wu, B., Li, G., Zhou, L., Zhang, L., & Liu, J. (2023) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2023.06.006 · Cited by 10

Mutant mice with rod-specific VPS35 deletion exhibit retinal α-synuclein pathology-associated degeneration

Fu, C., Yang, N., Chuang, J.-Z., Nakajima, N., Iraha, S., Roy, N. S., Wu, Z., Jiang, Z., Otsu, W., Radu, R. A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50189-0 · Cited by 9

Salvage NAD+ biosynthetic pathway enzymes moonlight as molecular chaperones to protect against proteotoxicity

Pinkerton, M., Ruetenik, A., Bazylianska, V., Nývltová, E., & Barrientos, A. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab080 · Cited by 11

Dual client binding sites in the ATP-independent chaperone SurA

Schiffrin, B., Crossley, J. A., Walko, M., Machin, J. M., Khan, G. N., Manfield, I. W., Wilson, A. J., Brockwell, D. J., Fessl, T., Calabrese, A. N., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-52021-1 · Cited by 8

Multi‐Targeting Macrocyclic Peptides as Nanomolar Inhibitors of Self‐ and Cross‐Seeded Amyloid Self‐Assembly of α‐Synuclein

Hornung, S., Vogl, D. P., Naltsas, D., Volta, B. D., Ballmann, M., Marcon, B., Syed, M. M. K., Wu, Y., Spanopoulou, A., Feederle, R., et al. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202422834 · Cited by 11

An approach to characterize mechanisms of action of anti-amyloidogenic compounds in vitro and in situ

Stalder, P., Serdiuk, T., Ghosh, D., Fleischmann, Y., Ait‐Bouziad, N., Quast, J.-P., Malinovska, L., Ouared, A., Davranche, A., Haenseler, W., et al. (2025) · npj Parkinson s Disease · doi:10.1038/s41531-025-00966-5 · Cited by 8

C-Terminal Radical Oxidation Inhibits α-Synuclein Aggregation and Cytotoxicity via an Oxidative Oligomer-Disrupting Pathway

Wang, X., Liang, T., Jin, A., Zhang, C., Zhou, J., Li, M., Sun, Z., & Li, G. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c06792 · Cited by 8

Effects of the Polyphenols Delphinidin and Rosmarinic Acid on the Inducible Intra-cellular Aggregation of Alpha-Synuclein in Model Neuron Cells

Yamamoto, H., Matsumura, R., Nakashima, M., Adachi, M., Ogawa, K., Hongo, K., Mizobata, T., & Kawata, Y. (2023) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-023-04362-8 · Cited by 8

α-Synuclein pathology in Drosophila melanogaster is exacerbated by haploinsufficiency of Rop: connecting STXBP1 encephalopathy with α-synucleinopathies

Matsuoka, T., Yoshida, H., Kasai, T., Tozawa, T., Iehara, T., & Chiyonobu, T. (2024) · Human Molecular Genetics · doi:10.1093/hmg/ddae073 · Cited by 8

The chaperonin TRiC is blocked by native and glycated prion protein

Kudryavtseva, S. S., Stroylova, Y. Y., Kurochkina, L. P., & Muronetz, V. I. (2020) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2020.108319 · Cited by 8

Molecular chaperones and their denaturing effect on client proteins

Hiller, S. (2020) · Journal of Biomolecular NMR · doi:10.1007/s10858-020-00353-7 · Cited by 8

A biophysical toolset to probe the microscopic processes underlying protein aggregation and its inhibition by molecular chaperones

Ahmed, R., & Melacini, G. (2020) · Biophysical Chemistry · doi:10.1016/j.bpc.2020.106508 · Cited by 8

Pyrogallol, Corilagin and Chebulagic acid target the “fuzzy coat” of alpha-synuclein to inhibit the fibrillization of the protein

Bopardikar, M., Ainavarapu, S. R. K., & Hosur, R. V. (2022) · RSC Advances · doi:10.1039/d2ra04358k · Cited by 7

Thermodynamic stability modulates chaperone-mediated disaggregation of α-synuclein fibrils

Fricke, C., Kunka, A., Norrild, R. K., Wang, S., Dang, T. L., Folke, J., Shahnawaz, M., Soto, C. A., Aznar, S., Wentink, A. S., et al. (2025) · Chemical Science · doi:10.1039/d5sc04927j · Cited by 7

The Potential Role of Artemisinins Against Neurodegenerative Diseases.

Xia, L., Qiu, Y., Li, J., Xu, M., & Dong, Z. (2024) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x24500642 · Cited by 7

Bispecific Tau Antibodies with Additional Binding to C1q or Alpha-Synuclein

Quint, W. H., Matečko‐Burmann, I., Schilcher, I., Löffler, T., Schöll, M., Burmann, B. M., & Vogels, T. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-201334 · Cited by 7

Structural Context Modulates the Conformational Ensemble of the Intrinsically Disordered Amino Terminus of α-Synuclein

Dumarieh, R., Lagasca, D., Krishna, S., Kragelj, J., Xiao, Y., Ansari, S., & Frederick, K. K. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c15653 · Cited by 6

Modulation of Alpha-Synuclein Conformational Ensemble and Aggregation Pathways by Dopamine and Related Molecules

Natalello, A., Brocca, S., Ponzini, E., Santambrogio, C., & Grandori, R. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2810266 · Cited by 6

Megadalton-sized Dityrosine Aggregates of α-Synuclein Retain High Degrees of Structural Disorder and Internal Dynamics

Verzini, S., Shah, M., Theillet, F., Belsom, A., Bieschke, J., Wanker, E. E., Rappsilber, J., Binolfi, A., & Selenko, P. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.10.023 · Cited by 6

Characterization of a Novel Monoclonal Antibody for Serine-129 Phosphorylated α-Synuclein: A Potential Application for Clinical and Basic Research

Liu, W., Zhang, Q., Xing, H., Gao, G., Liu, J., Huang, Y. M., & Yang, H. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.821792 · Cited by 6

Alpha-Synuclein species in oral mucosa as potential biomarkers for multiple system atrophy

Zheng, Y., Cai, H., Zhao, J., Yu, Z., & Feng, T. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1010064 · Cited by 6

Sandwiched‐fusion strategy facilitates recombinant production of small labile proteins

Huang, L., Qu, X., Chen, Y., Xu, W., & Huang, C. (2021) · Protein Science · doi:10.1002/pro.4024 · Cited by 6

Mapping the Role of Monomer Conformation in the Amyloid Formation of α-Synuclein Splice Variants

Dewison, K. M., Taylor, A. I. P., Brockwell, D. J., & Radford, S. E. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c12366 · Cited by 6

In-Cell Residue-Resolved NMR of Micromolar α-Synuclein and Tau at 310 K

Chérot, H., Pred’homme, T., Thaï, R., Théodoro, F., Castelli, F. A., & Theillet, F. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c15061 · Cited by 5

Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells

Lagasca, D., Ghosh, R., Xiao, Y., & Frederick, K. K. (2024) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2025.107864 · Cited by 5

Radiosynthesis and Evaluation of [18F]FEHSP990 as Novel PET Tracer for Hsp90 PET Imaging

Cools, R., Vermeulen, K., Celen, S., Leitao, R. C. F., & Bormans, G. M. (2025) · Journal of Labelled Compounds and Radiopharmaceuticals · doi:10.1002/jlcr.4144 · Cited by 6

Targeting the pathogenesis and boosting the therapeutic efficacy of Parkinson's disease by advanced nanoparticles

Liu, H., Hua, M., Zheng, Q. Y., Gao, Y., & Li, Z. (2023) · MedComm – Biomaterials and Applications · doi:10.1002/mba2.47 · Cited by 5

Targeting pathological brain activity-related to neuroinflammation through scRNA-seq for new personalized therapies in Parkinson’s disease

Mîrzac, D., Bange, M., Kunz, S., Jager, P. L. D., Groppa, S., & González‐Escamilla, G. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02086-7 · Cited by 5

Bioreactor in-cell NMR: A powerful tool for observing intracellular biological events

Nishida, N., Zhao, Q., & Shimada, I. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103086 · Cited by 5

Behind closed gates – chaperones and charged residues determine protein fate

Koopman, M. B., & Rüdiger, S. (2020) · The EMBO Journal · doi:10.15252/embj.2020104939 · Cited by 5

Efficient characterization of multiple binding sites of small molecule imaging ligands on amyloid-beta, 4-repeat/full-length tau and alpha-synucleinPreprint

Sobek, J., Li, J., Combes, B. F., Gerez, J., Nilsson, K. P. R., Henrich, M. T., Geibl, F. F., Shi, K., Rominger, A., Oertel, W. H., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.12.531651 · Cited by 5

Nanodiamond-based hyperpolarization for in-situ magic-angle-spinning nuclear magnetic resonance spectroscopy of proteinsPreprint

Kato, K., Takahashi, H., Tamaki, H., Fujiwara, T., & Matsuki, Y. (2023) · ChemRxiv · doi:10.26434/chemrxiv-2023-x9m17-v2 · Cited by 5

Intact cells selectively amplify and structurally remodel amyloid fibrilsPreprint

Ansari, S., Lagasca, D., Dumarieh, R., Xiao, Y., Krishna, S., Li, Y., & Frederick, K. K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.09.612142 · Cited by 5

Unraveling the Relation of Parkinson's Disease and Metabolites: A Combined Analysis of Stool and Plasma Metabolites Based on Untargeted Metabolomics Technology

Liu, S., Zhao, Q., Tang, J., Li, X., Wang, J., Zhao, Y., Yang, Z., Pan, X., Xiang, R. H., Tian, J., et al. (2025) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.70424 · Cited by 4

Genetic modifiers of synucleinopathies—lessons from experimental models

Lee, R. M. Q., & Koh, T. (2023) · Oxford Open Neuroscience · doi:10.1093/oons/kvad001 · Cited by 4

Molecular-level interplay between intrinsically disordered clients and Hsp90

Ramirez, L. M., & Zweckstetter, M. (2023) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2023.102304 · Cited by 4

Chaperones as Potential Pharmacological Targets for Treating Protein Aggregation Illness

Rani, S., & Tuteja, M. (2025) · Current Protein and Peptide Science · doi:10.2174/0113892037338028241230092414 · Cited by 6

Triple gene expressions in yeast, Escherichia coli, and mammalian cells by transferring DNA fragments amplified from a mother yeast expression plasmid

Nakamura, M., Kikuta, H., Misumi, Y., Suzuki, A., Hoshida, H., & Akada, R. (2022) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2022.03.002 · Cited by 4

Advanced NMR spectroscopy methods to study protein structure and dynamics

Kawale, A. A., & Burmann, B. M. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-99127-8.00010-6 · Cited by 7

Synergistic Multi-Pronged Interactions Mediate the Effective Inhibition of Alpha-Synuclein Aggregation by the Chaperone HtrA1Preprint

Chinchilla, P., Wang, B., Lubin, J. H., Yang, X., Roth, J., Khare, S. D., & Baum, J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.25.624572 · Cited by 4

Dopaminergic Neuron‐Specific Tfam Knockout Links Inter‐Organelle Miscommunication to Early‐Onset Parkinsonism

Shen, W., Zheng, M., Zhao, Y., Ni, F., & Zhu, X. (2025) · The FASEB Journal · doi:10.1096/fj.202501454rr · Cited by 3

Cardiolipin and mitochondrial membrane integrity in neurodegeneration: insights from α-synuclein-driven Parkinson’s disease

Ruiz, E., Wilkaniec, A., Juárez, J., & Adamczyk, A. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02190-x · Cited by 4

Bridging the gap in Parkinson’s disease research: from general pathophysiology to advanced 3d cell culture models

Keleş, B. S., Rumman, B., Samarie, M. A. J. A., Özdemir, Y., Çakmak, Ö. Ö., Akyoldaş, G., Ertan, S., & Sokullu, E. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02461-z · Cited by 3

High-affinity binding of celastrol to monomeric α-synuclein mitigates in vitro aggregation

Kavya, R., Aouti, S., Jos, S., Prasad, T. K., Kumuda, K. N., Unni, S., Padmanabhan, B., Kamariah, N., Padavattan, S., & Mythri, R. B. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2175379 · Cited by 3

Structure and dynamics of the mitochondrial DNA-compaction factor Abf2 from S. cerevisiae

Lidman, J., Sallova, Y., Matečko‐Burmann, I., & Burmann, B. M. (2023) · Journal of Structural Biology · doi:10.1016/j.jsb.2023.108008 · Cited by 3

Quantification of CH and NH/π-Stacking Interactions in Cells Using Nuclear Magnetic Resonance Spectroscopy

Chen, X., Zhang, X., Chen, J., Wang, M., Yang, Y. K., An, L., Liu, Z., Song, X., & Yao, L. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c00688 · Cited by 3

Inhibition of α-Synuclein Misfolding into β-Sheet Domains on Medium-Sized Gold Nanoclusters: Evidence from Enhanced Sampling MD Simulations

Gong, S., Gao, G., Sun, T., & Shen, L. (2024) · ACS Macro Letters · doi:10.1021/acsmacrolett.4c00533 · Cited by 3

From molecular descriptions to cellular functions of intrinsically disordered protein regions

Chen, W., Fraser, O. A., George, C., & Showalter, S. A. (2024) · Biophysics Reviews · doi:10.1063/5.0225900 · Cited by 3

Cytotoxicity of α-synuclein amyloid fibrils generated with phage chaperonin OBP

Pozdyshev, D. V., Leisi, E. V., Muronetz, V. I., Golyshev, S. A., & Kurochkina, L. P. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.151127 · Cited by 3

An Overview of Alpha Synuclein Protein and Its Role in Parkinson’s disease

Kaya, Z. B., & Atilla, P. (2021) · Acta Medica · doi:10.32552/2021.actamedica.510 · Cited by 3

Identifying interaction interface between Pseudomonas major biofilm forming functional amyloid FapC and disordered chaperone FapA during fibrillation decelerationPreprint

Byeon, C., Saricayir, H., Hansen, K. H., Jeffrey, J., Andreasen, M., & Akbey, Ü. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.14.530334 · Cited by 3

Visualizing alpha-synuclein and iron deposition in M83 mouse model of Parkinson’s disease in vivoPreprint

Straumann, N., Combes, B. F., Deán‐Ben, X. L., Sternke‐Hoffmann, R., Gerez, J., Dias, I., Chen, Z., Watts, B., Rostami, I., Shi, K., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.06.28.546962 · Cited by 3

Keeping α-Synuclein at Bay: A More Active Role of Molecular Chaperones in Preventing Mitochondrial Interactions and Transition to Pathological States?

Aspholm, E. E., Matečko‐Burmann, I., & Burmann, B. M. (2020) · Life · doi:10.3390/life10110289 · Cited by 13

Identification of Protein Interfaces between α-Synuclein, the Principal Component of Lewy Bodies in Parkinson Disease, and the Molecular Chaperones Human Hsc70 and the Yeast Ssa1p

Redeker, V., Pemberton, S., Bienvenut, W. V., Bousset, L., & Melki, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.387530 · Cited by 51

Exploring the Formation of Neuronal Inclusions in Parkinson’s Disease using Single Molecule Fluorescence Spectroscopy

Leitao, A. (2022) · UNSWorks (University of New South Wales, Sydney, Australia) · doi:10.26190/unsworks/22070

Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone Activity

Rekas, A., Adda, C. G., Aquilina, J. A., Barnham, K. J., Sunde, M., Galatis, D., Williamson, N. A., Masters, C. L., Anders, R. F., Robinson, C. V., et al. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.054 · Cited by 226

Molecular Chaperones, Alpha-Synuclein, and Neurodegeneration

Witt, S. N. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8325-2 · Cited by 68