Article
Biochemistry & Molecular Biology
Animesh Mondal, Sandip Dolui, Sukhamoy Dhabal, Shubham Kundu, Lopamudra Das, Ashish Bhattacharjee, Nakul C. Maiti
Summary: Parkinson's disease is associated with the aggregation of α-synuclein and the accumulation of amyloid in the substantia nigra region of the brain. This study identified two types of α-synuclein oligomers with different protein conformation and stability, and compared their toxic effects on neuronal cells. The lyophilized oligomer was highly toxic, while the heat-induced oligomer was less toxic. It was also found that the presence of molten globule-like conformation in the oligomer increased its toxicity to cultured neuronal cells.
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
(2023)
Article
Biochemistry & Molecular Biology
Edward Chau, Hyunjoo Kim, Jineun Shin, Alberto Martinez, Jin Ryoun Kim
Summary: The study found that AM17 can not only inhibit the aggregation of alpha S monomers, but also disaggregate alpha S oligomers and fibrils, independent of copper ions. Resveratrol also showed similar inhibitory effects on alpha S aggregation only in the presence of copper ions.
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
(2021)
Article
Biotechnology & Applied Microbiology
Edward Chau, Jin Ryoun Kim
Summary: In this study, a new molecular probe, PG65-MIMO, was developed and shown to provide comprehensive information on the aggregation states of alpha-synuclein (alpha S). It fills the technological gap in alpha S detection and offers a promising tool for studying Parkinson's Disease.
BIOCHEMICAL ENGINEERING JOURNAL
(2022)
Article
Biochemistry & Molecular Biology
Edward Chau, Jin Ryoun Kim
Summary: This study investigated the interactions between Aβ42 and αS in different conformations. It was found that αS monomers and oligomers promoted the oligomerization and stabilization of soluble Aβ42, while αS fibrils hindered the aggregation of Aβ42. These interactions may be achieved through direct binding or co-assembly, and different parts of Aβ42 mediated the interactions with αS.
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
(2022)
Article
Biochemistry & Molecular Biology
Vanderlei de Araujo Lima, Rodrigo Esquinelato, Phelippe Carmo-Goncalves, Lucas Alex do Nascimento, Hudson Lee, David Eliezer, Luciana Romao, Cristian Follmer
Summary: The study found that apomorphine (Apo) inhibits the fibrillation of alpha-synuclein (aSyn), leading to the formation of large toxic oligomeric species in mesencephalic dopaminergic neurons. Purified Apo-aSyn-O, even at low concentrations, seems capable of converting unmodified aSyn monomer into neurotoxic species.
Article
Clinical Neurology
Yasuo Miki, Kunikazu Tanji, Kana Shinnai, Makoto T. Tanaka, Firat Altay, Sandrine C. Foti, Catherine Strand, Takanori Sasaki, Tomoya Kon, Shuji Shimoyama, Tomonori Furukawa, Haruo Nishijima, Hiromi Yamazaki, Yasmine T. Asi, Conceicao Bettencourt, Zane Jaunmuktane, Mari Tada, Fumiaki Mori, Hiroki Mizukami, Masahiko Tomiyama, Hilal A. Lashuel, Tammaryn Lashley, Akiyoshi Kakita, Helen Ling, Andrew J. Lees, Janice L. Holton, Thomas T. Warner, Koichi Wakabayashi
Summary: This study investigated how abnormal alpha-synuclein in the hippocampus leads to memory impairment in multiple system atrophy (MSA). The results suggest that increased alpha-synuclein oligomers may be a pathological cause of memory impairment in MSA.
NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY
(2022)
Review
Biochemistry & Molecular Biology
Jin Ryoun Kim
Summary: This mini review summarizes the findings on the interactions between A beta and alpha S, which enhance oligomerization via co-assembly. It aims to provide a better understanding of the complex biology behind AD and PD and common pathological mechanisms among the major neurodegenerative diseases.
FRONTIERS IN MOLECULAR BIOSCIENCES
(2023)
Article
Multidisciplinary Sciences
Rohith K. Nellikka, Bhavya R. Bhaskar, Kinjal Sanghrajka, Swapnali S. Patil, Debasis Das
Summary: Alpha-synuclein plays a crucial role in the pathogenesis of Parkinson's disease by directly regulating individual exocytotic release events, controlling vesicular secretion. It forms an inhibitory complex to decrease the open probability of fusion pores, influenced by various factors. This study reveals the key role of alpha-synuclein in modulating pore properties and highlights its regulatory action in membrane fusion.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2021)
Article
Biochemistry & Molecular Biology
Tomohiro Umeda, Yukari Hatanaka, Ayumi Sakai, Takami Tomiyama
Summary: The study found that intranasal administration of rifampicin significantly reduced the levels of alpha-synuclein oligomers in DLB model mice and improved cognitive function, suggesting that rifampicin may be a promising remedy for preventing neurodegenerative dementia.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Review
Biochemistry & Molecular Biology
Marco Giampa, Maria J. Amundarain, Maria Georgina Herrera, Nicolo Tonali, Veronica I. Dodero
Summary: The aggregation of proteins into amyloid fibers is associated with various cellular and neurodegenerative diseases. Understanding the molecular mechanism of aggregation is crucial for finding new therapeutic targets. This review explores different approaches and theories for studying amyloid aggregation, with a focus on alpha-syn.
Article
Biochemistry & Molecular Biology
Tapojyoti Das, Meraj Ramezani, David Snead, Cristian Follmer, Peter Chung, Ka Yee Lee, David A. A. Holowka, Barbara A. A. Baird, David Eliezer
Summary: Alpha-synuclein plays an important role in regulating synaptic vesicle cycling, exerting both inhibitory and potentiating effects on vesicle release. The binding affinity of alpha-synuclein to isolated vesicles is a key determinant of its ability to potentiate release.
Article
Chemistry, Physical
Soham Maity, Kazuma Shimanaka, Laken N. Rivet, Malikah O'Dell, Anisa M. Rashid, Nurhanis B. M. Isa, Rachel S. Kepczynski, Ulf Dettmer, Babak Borhan, Jessica S. Fortin
Summary: This study focuses on the effectiveness of a novel family of molecules in inhibiting the aggregation of alpha-synuclein, a major pathogenetic contributor to diseases like Parkinson's Disease and multiple system atrophy. Compound 12 was identified as a promising inhibitor for late-stage fibril formation and also impeded early-stage oligomerization of alpha-synuclein. The compound showed potential as a valuable tool in abrogating alpha-synuclein aggregation at the early stage.
JOURNAL OF MOLECULAR STRUCTURE
(2022)
Article
Biochemistry & Molecular Biology
Pankaj Gaur, Maksym Galkin, Andrii Kurochka, Subrata Ghosh, Dmytro A. Yushchenko, Volodymyr V. Shvadchak
Summary: In this study, two molecular rotor-based probes RB1 and RB2 are presented, with RB1 showing outstanding absorption red-shift and high fluorescence enhancement, exhibiting high affinity and selective staining ability for alpha-synuclein fibrils in living cells. RB1 can be used for intracellular imaging of alpha-synuclein fibrils due to its strong binding affinity and cell-permeable nature.
ACS CHEMICAL NEUROSCIENCE
(2021)
Article
Chemistry, Multidisciplinary
Eun Ji Shin, Joon Won Park
Summary: The study used atomic force microscopy to examine the surface structure of hetero-oligomers derived from amyloid-beta and alpha-synuclein, finding that recognition probability of N-terminus or C-terminus in the former is higher than that in homo-oligomers, suggesting a new approach to elucidate the structure of such aggregates.
Article
Neurosciences
Tomohiro Umeda, Ayumi Sakai, Keiko Shigemori, Ayumi Yokota, Toru Kumagai, Takami Tomiyama
Summary: The combination of rifampicin and resveratrol showed improved cognition, reduced amyloid oligomer accumulation, and normalized liver enzyme levels in transgenic mice. Furthermore, the combination therapy enhanced brain-derived neurotrophic factor (BDNF) levels in the hippocampus and showed a synergistic effect in ameliorating mouse cognition. These results demonstrate the safety and efficacy advantages of this combinatorial medicine for preventing neurodegenerative dementia targeting toxic oligomers.
FRONTIERS IN NEUROSCIENCE
(2021)
Article
Biochemistry & Molecular Biology
Arshdeep Sidhu, Ine Segers-Nolten, Vincent Raussens, Mireille M. A. E. Claessens, Vinod Subramaniam
ACS CHEMICAL NEUROSCIENCE
(2017)
Article
Biophysics
Juan J. Dominguez Pardo, Jonas M. Dorr, Aditya Iyer, Ruud C. Cox, Stefan Scheidelaar, Martijn C. Koorengevel, Vinod Subramaniam, J. Antoinette Killian
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
(2017)
Article
Chemistry, Multidisciplinary
Pravin Kumar, Nathalie Schilderink, Vinod Subramaniam, Martina Huber
ISRAEL JOURNAL OF CHEMISTRY
(2017)
Article
Chemistry, Physical
Kristian L. Goeken, Richard B. M. Schasfoort, Vinod Subramaniam, Ron Gill
Article
Chemistry, Multidisciplinary
D. Wasserberg, J. Cabanas-Danes, V. Subramaniam, J. Huskens, P. Jonkheijm
CHEMICAL COMMUNICATIONS
(2018)
Article
Physics, Multidisciplinary
Slav A. Semerdzhiev, Saskia Lindhoud, Anja Stefanovic, Vinod Subramaniam, Paul van der Schoot, Mireille M. A. E. Claessens
PHYSICAL REVIEW LETTERS
(2018)
Article
Multidisciplinary Sciences
G. C. Hassink, C. C. Raiss, I. M. J. Segers-Nolten, R. J. A. van Wezel, V. Subramaniam, J. le Feber, M. M. A. E. Claessens
Article
Biophysics
Gerardo Abbandonato, Barbara Storti, Ilaria Tonazzini, Martin Stoeckl, Vinod Subramaniam, Costanza Montis, Riccardo Nifosi, Marco Cecchini, Giovanni Signore, Ranieri Bizzarri
BIOPHYSICAL JOURNAL
(2019)
Article
Chemistry, Physical
Jord C. Prangsma, Robert Molenaar, Laura van Weeren, Daphne S. Bindels, Lindsay Haarbosch, Jente Stouthamer, Theodorus W. J. Gadella, Vinod Subramaniam, Willem L. Vos, Christian Blum
JOURNAL OF PHYSICAL CHEMISTRY B
(2020)
Article
Chemistry, Physical
Theresa S. Braun, Juliane Stehle, Sylwia Kacprzak, Patrick Carl, Peter Hoefer, Vinod Subramaniam, Malte Drescher
Summary: Protein-membrane interactions are crucial for cellular processes, and the study of these interactions presents a challenge in modern biophysical chemistry. By employing rapid-scan electron paramagnetic resonance spectroscopy, the interaction between αS and negatively charged vesicles in vitro was studied, with reflections observed in cells as well.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2021)
Review
Neurosciences
Aditya Iyer, Arshdeep Sidhu, Vinod Subramaniam
Summary: N-alpha-acetylation is a common post-translational modification in eukaryotic proteins, which has significant effects on protein regulation and function. However, the precise mechanisms and implications of N-alpha-acetylation of alpha-synuclein (alpha S) are not fully understood. This review provides an overview of current knowledge and discusses the impact of N-alpha-acetylation on the conformational, oligomeric, and fibrillar states of alpha S, as well as its relevance to Lewy body formation and synucleinopathies.
FRONTIERS IN NEUROSCIENCE
(2022)
Article
Chemistry, Physical
Himanshu Chaudhary, Vinod Subramaniam, Mireille M. A. E. Claessens
Meeting Abstract
Biophysics
Pravin Kumar, Maryam Hashemi Shabestari, Nathalie Schilderink, Ine M. J. Segers-Nolten, Mireille M. A. E. Claessens, Vinod Subramaniam, Martina Huber
BIOPHYSICAL JOURNAL
(2017)
Article
Materials Science, Textiles
Kumarasamy Subbiah, Bhaarathi Dhurai, Venkatraman Subramaniam
FIBRES & TEXTILES IN EASTERN EUROPE
(2017)
Article
Biochemistry & Molecular Biology
Arshdeep Sidhu, Jonathan Vaneyck, Christian Blum, Ine Segers-Nolten, Vinod Subramaniam
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
(2018)
Article
Biochemistry & Molecular Biology
Ankita Chadda, Alexander G. Kozlov, Binh Nguyen, Timothy M. Lohman, Eric A. Galburt
Summary: In this study, it was found that the DNA damage response in Mycobacterium tuberculosis differs from well-studied model bacteria. The DNA repair helicase UvrD1 in Mtb is activated through a redox-dependent process and is closely associated with the homo-dimeric Ku protein. Additionally, Ku protein is shown to stimulate the helicase activity of UvrD1.
JOURNAL OF MOLECULAR BIOLOGY
(2024)