Article
Chemistry, Multidisciplinary
Kevin A. Murray, Declan Evans, Michael P. Hughes, Michael R. Sawaya, Carolyn J. Hu, Kendall N. Houk, David Eisenberg
Summary: Recent studies have revealed that some amyloid-like structures are reversible and derived from protein low-complexity domains involved in cellular metabolism. The finding of unique structural features of reversible amyloid fibrils suggests the involvement of intraresidue interactions known as C5 hydrogen-bonds in stabilizing these structures.
Review
Biochemistry & Molecular Biology
Anna Sulatskaya, Anastasiia O. Kosolapova, Alexander G. Bobylev, Mikhail Belousov, Kirill S. Antonets, Maksim Sulatsky, Irina M. Kuznetsova, Konstantin K. Turoverov, Olesya Stepanenko, Anton A. Nizhnikov
Summary: Both amyloids and beta-barrel proteins have beta-sheet-rich structures, with the latter being able to form functional amyloids in vivo. These beta-barrel amyloid proteins can interact with each other and form toxic oligomers, potentially contributing to the development of amyloidoses. Rapidly growing discoveries suggest that the number and diversity of functions of amyloid-forming beta-barrel proteins are significantly greater than currently understood.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Review
Biochemistry & Molecular Biology
Lucia Gallego Villarejo, Lisa Bachmann, David Marks, Maite Brachthaeuser, Alexander Geidies, Thorsten Mueller
Summary: Intracellular amyloid beta (iAβ) plays a crucial role in neurodegeneration and serves as a pathological marker. Modulating iAβ through pharmacological treatment has shown beneficial effects on cognitive properties. Future research should focus on the impact of viral infections on iAβ generation.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2022)
Article
Biochemistry & Molecular Biology
Zigmantas Toleikis, Mantas Ziaunys, Lina Baranauskiene, Vytautas Petrauskas, Kristaps Jaudzems, Vytautas Smirnovas
Summary: The presence of S100A9 alters the aggregation kinetics of alpha-synuclein and stabilizes a specific amyloid fibril structure. The ionic strength of the solution influences the interaction between S100A9 and alpha-synuclein, stabilizing a different structure of alpha-synuclein fibrils.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Clinical Neurology
Yalun Zhang, Yi Zhang, Yahyah Aman, Cheung Toa Ng, Wing-Hin Chau, Zhigang Zhang, Ming Yue, Christopher Bohm, Yizhen Jia, Siwen Li, Qiuju Yuan, Jennifer Griffin, Kin Chiu, Dana S. M. Wong, Binbin Wang, Dongyan Jin, Ekaterina Rogaeva, Paul E. Fraser, Evandro F. Fang, Peter St George-Hyslop, You-Qiang Song
Summary: Research has shown that the transcription factor PAX6 is increased in Alzheimer's disease, playing a key role in the hyperphosphorylation of tau protein induced by amyloid-beta. Downregulation of PAX6 can protect against amyloid-beta-induced neuronal death. This study provides novel potential targets for pharmaceutical intervention by modulating signaling pathways involving CDK/pRB/E2F1.
Article
Biodiversity Conservation
Marcy Summers, Matthew Geary, Nurlin Djuni, Pandji A. Kresno, Agustian Laya, Stallin Sawuwu, Adrianus Bawotong, Wiranto Abas, Vivi Megayanti Tan Oga, Ahmad Muh. Nur, Moh. Isfandri, Galen V. Priest, Philip J. K. McGowan, Johny S. Tasirin, Nigel J. Collar
Summary: The decline of the culturally iconic and critically endangered maleo in Sulawesi, Indonesia has never been systematically analyzed, and nesting grounds have not been comprehensively surveyed. However, this study visited numerous sites and collected data to assess the causes of decline and predict nesting ground success. The results showed that egg-taking by humans is the main driver of decline, and protecting eggs in situ is more effective than using hatchery methods.
BIODIVERSITY AND CONSERVATION
(2023)
Article
Biochemistry & Molecular Biology
Danielle M. Williams, David C. Thorn, Christopher M. Dobson, Sarah Meehan, Sophie E. Jackson, Joanna M. Woodcock, John A. Carver
Summary: 14-3-3 proteins are important in cellular signal transduction and act as molecular chaperones to maintain the protein structure of Aβ and α-syn by interacting preferentially with hydrophobic regions. The zeta isoform of 14-3-3 inhibits fibril formation of Aβ but has little effect on α-syn aggregation. These proteins play a role in the progression of Alzheimer's and Parkinson's diseases by interacting with amyloid-forming proteins.
Article
Cell Biology
Abubakar Wani, Sweilem B. Al Rihani, Ankita Sharma, Brenna Weadick, Rajgopal Govindarajan, Sameer U. Khan, Parduman R. Sharma, Ashish Dogra, Utpal Nandi, Chilakala N. Reddy, Sonali S. Bharate, Gurdarshan Singh, Sandip B. Bharate, Ram A. Vishwakarma, Amal Kaddoumi, Ajay Kumar
Summary: This study found that crocetin can induce autophagy in Alzheimer's disease, helping to clear Aβ and improve memory function.
Article
Food Science & Technology
Junying Bai, Yan Li, Wenhui Zhang, Mingcong Fan, Haifeng Qian, Hui Zhang, Xiguang Qi, Li Wang
Summary: This study investigated the effect of gut microbial source on oat beta-glucan metabolism by using mice and human fecal microbiota in an in vitro fermentation experiment. The main end products from gut microbial fermentation of beta-glucan were acetate, propionate, and butyrate, with differences in the main product between the mice and human groups. The data suggested that beta-glucan could be completely hydrolyzed by human fecal microbiota but not thoroughly degraded by mice fecal microbiota.
Article
Geriatrics & Gerontology
Ya-Li Wang, Jian-Gang Wang, Shuling Guo, Fang-Li Guo, En-Jie Liu, Xin Yang, Bingyan Feng, Jian-Zhi Wang, Martin Vreugdenhil, Cheng-Biao Lu
Summary: Neuronal synchronization at gamma frequency is impaired in early-stage Alzheimer's disease. The study found that oligomeric A beta(1-42) reduces the strength and regularity of gamma oscillations while increasing its frequency. The mTOR/S6K1 signaling pathway plays a key role in the A beta(1-42)-induced suppression of gamma oscillations.
Article
Geriatrics & Gerontology
Yujia Zhang, Qiaoyan Huang, Sichen Wang, Ziqian Liao, Haichao Jin, Shuo Huang, Xiao Hong, Yiming Liu, Jie Pang, Qing Shen, Qingcheng Wang, Changyu Li, Liting Ji
Summary: Despite the extensive research on Alzheimer's disease (AD), there are currently no effective therapies available. This study investigated the neuroprotective effects of the food flavouring agent beta-caryophyllene (BCP) and found that inhibition of the JAK2-STAT3-BACE1 signalling pathway may be one of the mechanisms through which BCP protects neurons and counteracts the neurotoxicity of amyloid beta (Aβ).
FRONTIERS IN AGING NEUROSCIENCE
(2022)
Article
Chemistry, Physical
William B. Weeks, Lauren E. Buchanan
Summary: This article presents a method to distinguish multiple β-sheet structures within peptide and protein aggregates, and demonstrates its effectiveness through experiments. The method utilizes two-dimensional infrared spectroscopy to calculate the transition dipole strength (TDS) spectrum, which provides higher sensitivity to protein structure and can detect structural details that are not observable by other techniques.
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2022)
Article
Geriatrics & Gerontology
Xiaojie Wang, Mengxi Hu, Qian Xie, Chi Geng, Chen Jin, Wei Ren, Jiangpeng Fan, Tengfei Ma, Bin Hu
Summary: In this study, it was found that human amyloid beta (Aβ) oligomers negatively affect the excitability of pyramidal neurons in the anterior piriform cortex (PC) of adult mice. This effect is independent of glutamatergic and GABAergic transmission, but regulated by serotonin, 5-HT2C receptors, phospholipase C (PLC), and calcium-activated potassium (BK) channels. The findings suggest that serotonergic modulation could be a potential therapeutic target for olfactory damage in Alzheimer's disease.
NEUROBIOLOGY OF AGING
(2023)
Article
Multidisciplinary Sciences
Husnul Fuad Zein, Ibrar Alam, Piyapong Asanithi, Thana Sutthibutpong
Summary: Aggregation of unfolded or misfolded proteins into amyloid fibrils can cause diseases. This study used molecular dynamics simulations to investigate the mechanism of beta-sheet formation of a hen egg-white lysozyme under high temperature and low pH conditions. The simulations showed that the lysozyme unfolded faster and had higher beta-strand content at pH 2.
Article
Biochemistry & Molecular Biology
Ghislaine Guillemain, Jean-Jacques Lacapere, Lucie Khemtemourian
Summary: This article evaluates a new approach to preserve beta-cells by preventing the formation of hIAPP oligomers and fibrils, which can lead to beta-cell death. It also reviews the progress in understanding amyloidosis associated with neurodegenerative diseases and inflammation, and explores its potential implications in preserving pancreatic beta-cells.
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
(2022)
Article
Biochemistry & Molecular Biology
Edoardo Del Poggetto, Francesco Bemporad, Francesca Tatini, Fabrizio Chiti
ACS CHEMICAL BIOLOGY
(2015)
Article
Biochemistry & Molecular Biology
Predrag Kukic, Hoi Tik Alvin Leung, Francesco Bemporad, Francesco A. Aprile, Janet R. Kumita, Alfonso De Simone, Carlo Camilloni, Michele Vendruscolo
Article
Cell Biology
Manuela Leri, Francesco Bemporad, Reinier Oropesa-Nunez, Claudio Canale, Martino Calamai, Daniele Nosi, Matteo Ramazzotti, Sofia Giorgetti, Francesco S. Pavone, Vittorio Bellotti, Massimo Stefani, Monica Bucciantini
JOURNAL OF CELLULAR AND MOLECULAR MEDICINE
(2016)
Article
Biochemistry & Molecular Biology
Edoardo Del Poggetto, Angelo Toto, Chiara Aloise, Francesco Di Piro, Ludovica Gori, Francesco Malatesta, Stefano Gianni, Fabrizio Chiti, Francesco Bemporad
JOURNAL OF BIOLOGICAL CHEMISTRY
(2018)
Article
Multidisciplinary Sciences
Simone Luti, Federica Martellini, Francesco Bemporad, Lorenzo Mazzoli, Paolo Paoli, Luigia Pazzagli
Editorial Material
Biochemistry & Molecular Biology
Ursula Jakob
JOURNAL OF BIOLOGICAL CHEMISTRY
(2019)
Article
Multidisciplinary Sciences
Denisa Jazaj, Seyyed Abolghasem Ghadami, Francesco Bemporad, Fabrizio Chiti
SCIENTIFIC REPORTS
(2019)
Article
Biochemistry & Molecular Biology
Hassan Ramshini, Reza Tayebee, Alessandra Bigi, Francesco Bemporad, Cristina Cecchi, Fabrizio Chiti
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2019)
Article
Biochemistry & Molecular Biology
Seyyed Abolghasem Ghadami, Sean Chia, Francesco Simone Ruggeri, Georg Meisl, Francesco Bemporad, Johnny Habchi, Roberta Cascella, Christopher M. Dobson, Michele Vendruscolo, Tuomas P. J. Knowles, Fabrizio Chiti
Article
Biochemistry & Molecular Biology
Mirella Vivoli-Vega, Prandvera Guri, Fabrizio Chiti, Francesco Bemporad
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2020)
Article
Chemistry, Medicinal
Francesco Bemporad, Manuela Leri, Matteo Ramazzotti, Massimo Stefani, Monica Bucciantini
Summary: This study investigated the interaction between oleuropein derivative OleA and TTR protein. The results showed that OleA could stabilize TTR, prevent its dissociation into monomers, and subsequent misfolding. This finding suggests the potential use of OleA in preventing degenerative diseases associated with TTR misfolding.
Article
Biochemistry & Molecular Biology
Matteo Moretti, Isabella Marzi, Cristina Cantarutti, Mirella Vivoli Vega, Walter Mandaliti, Maria Chiara Mimmi, Francesco Bemporad, Alessandra Corazza, Fabrizio Chiti
Summary: TAR DNA-binding protein 43 (TDP-43) has been associated with amyotrophic lateral sclerosis and frontotemporal lobar degeneration. The N-terminal domain (NTD) of TDP-43 plays a crucial role in its function and the formation of intraneuronal inclusions. The study identified an alternative conformation of NTD in the presence of SB3-10, which led to a more α-helical structure. The results also showed that the aggregation of TDP-43 was slower when pre-incubated with SB3-10, indicating the disruption of oligomeric seeds by the alternative conformation conditions. These findings provide insights into the plasticity of TDP-43 NTD and suggest strategies for monomerising TDP-43 NTD for various applications.
Article
Biochemistry & Molecular Biology
Tommaso Garfagnini, Francesco Bemporad, Daniel Harries, Fabrizio Chiti, Assaf Friedler
Summary: Hydrophobicity is a key driving force for amyloid aggregation, and the presence of osmolytes in the cellular environment has a significant impact on this process. Hydrophobic mutations can increase the aggregation rate, but osmolytes can slow down the kinetics, especially when the mutation site is closer to the center of the protein sequence.
JOURNAL OF MOLECULAR BIOLOGY
(2023)
Article
Biochemistry & Molecular Biology
Seyyed Abolghasem Ghadami, Francesco Bemporad, Benedetta Maria Sala, Guido Tiana, Stefano Ricagno, Fabrizio Chiti
CELLULAR AND MOLECULAR LIFE SCIENCES
(2017)
Article
Biophysics
Francesco Elia, Francesca Cantini, Fabrizio Chiti, Christopher Martin Dobson, Francesco Bemporad
BIOPHYSICAL JOURNAL
(2017)