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We designed a copper‐based nanotube (NT) with copper ionophores to induce enhanced cuproptosis. In combination with starvation therapy, the NT significantly inhibited energy metabolism in HCC cells. Our results show that the depletion of GSH by Cu2+ intensified oxidative stress and cuproptosis, resulting in ROS generation and DLAT aggregation ...
Xuan Han+8 more
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A Salt Bridge and Disulfide Bond within the Lassa Virus Fusion Domain Are Required for the Initiation of Membrane Fusion. [PDF]
Pennington HN, Birtles D, Shi ZW, Lee J.
europepmc +1 more source
Cu5%‐MoS2 with dual Cu and Mo active sites enables efficient photothermal synergistic catalysis of the CO2–H2O system for ethanol production. The catalyst achieves a high ethanol yield of 3.1 mmol·g−1·h−1 with 88.35% selectivity, showcasing exceptional performance and selectivity under mild conditions. Abstract The catalytic conversion of CO2 into high‐
Yingao Luo+6 more
wiley +1 more source
Deciphering the Cofilin Oligomers via Intermolecular Disulfide Bond Formation: A Coarse-Grained Molecular Dynamics Approach to Understanding Cofilin's Regulation on Actin Filaments. [PDF]
Li C, Wei TY, Cheung MS, Tsai MY.
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The research team integrated a potentiometrically controlled pH electrode with carbon nanotube (CNT) field‐effect transistor (FET) biosensors on a single chip using compatible processes. By employing zonal modification and optimized pH‐sensitive probes, they achieved simultaneous quadruple‐target detection and tenfold reusability under physiological ...
Bo Xiao+6 more
wiley +1 more source
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Disulfide bond formation in prokaryotes
Nature Microbiology, 2018Interest in protein disulfide bond formation has recently increased because of the prominent role of disulfide bonds in bacterial virulence and survival. The first discovered pathway that introduces disulfide bonds into cell envelope proteins consists of Escherichia coli enzymes DsbA and DsbB.
Cristina Landeta+2 more
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Disulfide Bond Mimetics: Strategies and Challenges
Chemistry – A European Journal, 2017AbstractThe activity profile of many biologically relevant proteins and peptides often relies on a precise 3D structural organization. In this context, disulfide bonds are natural covalent constraints that play a key role in driving and stabilizing the folding pattern of these molecules.
Gori A, Gagni P, Rinaldi S
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ChemInform Abstract: Disulfide Bond Formation in Peptides [PDF]
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
George Barany, Lin Chen, Ioana Annis
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