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| http://dx.doi.org/10.21037/atm-23-522 | DOI Listing |
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Zn(TFSI)-Mediated Ring-Opening Polymerization for Electrolyte Engineering Toward Stable Aqueous Zinc Metal Batteries.
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Department of Chemistry and Shanghai Key Laboratory of Molecular Catalysis and Innovative Materials, Institute of New Energy, iChEM (Collaborative Innovation Center of Chemistry for Energy Materials), Fudan University, Shanghai, 200433, People's Republic of China.
Practical Zn metal batteries have been hindered by several challenges, including Zn dendrite growth, undesirable side reactions, and unstable electrode/electrolyte interface. These issues are particularly more serious in low-concentration electrolytes. Herein, we design a Zn salt-mediated electrolyte with in situ ring-opening polymerization of the small molecule organic solvent.
View Article and Find Full Text PDFHIV Molecular Transmission Networks Among Students in Guangxi: Unraveling the Dynamics of Student-Driven HIV Epidemic.
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Guangxi Key Laboratory of AIDS Prevention Control and Translation, Guangxi Zhuang Autonomous Region Center for Disease Control and Prevention, Nanning, Guangxi, China.
In Guangxi, the number of newly diagnosed HIV-1 infections among students is continuously increasing, highlighting the need for a detailed understanding of local transmission dynamics, particularly focusing on key drivers of transmission. We recruited individuals newly diagnosed with HIV-1 in Nanning, Guangxi, and amplified and sequenced the HIV-1 pol gene to construct a molecular network. Bayesian phylogenetic analysis was utilized to identify migration events, and multivariable logistic regression was employed to analyze factors influencing clustering and high linkage.
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Yusuf Hamied Department of Chemistry, University of Cambridge Cambridge CB2 1EW, UK; UK Dementia Research Institute at University of Cambridge Cambridge CB2 0XY, UK. Electronic address:
Synaptic dysfunction is a primary hallmark of both Alzheimer's and Parkinson's disease, leading to cognitive and behavioral decline. While alpha-synuclein, beta-amyloid, and tau are involved in the physiological functioning of synapses, their pathological aggregation has been linked to synaptopathology. The methodology for studying the small-soluble protein aggregates formed by these proteins is limited.
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