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Rapid and dual-mode nitrite detection with improved sensitivity by nanointerface-regulated ultrafast Griess assay.
Anal Chim Acta
January 2025
College of Chemistry, Beijing University of Chemical Technology, Beijing, 100029, China. Electronic address:
Background: The rapid and sensitive detection of nitrite is important to human health protection due to its carcinogenic and teratogenic risks with excessive intake. The Griess assay is widely applied for the design of nitrite detection system. However, its relatively slow reaction kinetics and sole colorimetry mode might limit it's the sensitivity and practical application.
View Article and Find Full Text PDFElucidating the binding specificity of interactive compounds targeting ATP-binding cassette subfamily G member 2 (ABCG2).
Mol Divers
January 2025
Data Science, Amity Institute of Integrative Sciences and Health, Amity University Haryana, Gurugram, India.
The ATP-binding cassette transporter superfamily plays a pivotal role in cellular detoxification and drug efflux. ATP-binding cassette subfamily G member 2 (ABCG2) referred to as the Breast cancer resistance protein has emerged as a key member involved in multidrug resistance displayed by cancer cells. Understanding the molecular basis of substrate and inhibitor recognition, and binding within the transmembrane domain of ABCG2 is crucial for the development of effective therapeutic strategies.
View Article and Find Full Text PDFUnlocking dual-mode enzyme activities on bacterial surface: Directional recognition and swift capture of Alicyclobacillus acidoterrestris from fruit juices.
Food Res Int
January 2025
State Key Laboratory of Marine Food Processing and Safety Control, Dalian Polytechnic University, Dalian 116034, Liaoning, China. Electronic address:
The acidophilic and heat-resistant characteristics of Alicyclobacillus acidoterrestris (A. acidoterrestris) pose significant challenges to fruit juice production. Traditional thermal removal methods are often ineffective against this resilient bacterium.
View Article and Find Full Text PDFDecoding the Torsional Dynamics of Main-Chain Atoms Within CαNN Motif Facilitating Specific Anion Recognition.
Proteins
January 2025
Department of Biotechnology, Maulana Abul Kalam Azad University of Technology, Haringhata, India.
The structural plasticity of proteins at the molecular level is largely dictated by backbone torsion angles, which play a critical role in ligand recognition and binding. To establish the anion-induced cooperative arrangement of the main-chain (mc) torsion, herein, we analyzed a set of naturally occurring CαNN motifs as "static models" for their anion-binding competence through docking and molecular dynamics simulations and decoded its torsion angle influenced mc-driven anion recognition potential. By comparing a pool of 20 distinct sets of CαNN motif with identical sequences in their "anion bound/present, aP" and "anion free/absent, aA" versions, we could discern that there exists a positive correlation between the "difference of anion residence time (ΔR)" and "difference among the main-chain torsion angle" of the aP and aA population.
View Article and Find Full Text PDFRecognition and cleavage of human tRNA methyltransferase TRMT1 by the SARS-CoV-2 main protease.
Elife
January 2025
Department of Chemistry & Biochemistry, University of Delaware, Newark, United States.
The SARS-CoV-2 main protease (M or Nsp5) is critical for production of viral proteins during infection and, like many viral proteases, also targets host proteins to subvert their cellular functions. Here, we show that the human tRNA methyltransferase TRMT1 is recognized and cleaved by SARS-CoV-2 M. TRMT1 installs the ,-dimethylguanosine (m2,2G) modification on mammalian tRNAs, which promotes cellular protein synthesis and redox homeostasis.
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