Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1038/s41592-021-01362-6 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Hydrodynamic cavitation induced fabrication of soy protein isolate-polyphenol complexes: Structural and functional properties.
Curr Res Food Sci
January 2025
School of Biological and Chemical Engineering, Guangxi University of Science and Technology, Guangxi Key Laboratory of Green Processing of Sugar Resources, Key Laboratory for Processing of Sugar Resources of Guangxi Higher Education Institutes, Liuzhou, 545006, China.
The combination of polyphenols and protein can improve the functional characteristics of protein. How to effectively promote the binding of polyphenols to protein is still a difficult topic. In this study, hydrodynamic cavitation (HC) was used to induce the fabrication of complexes between soy protein isolate (SPI) and different polyphenols (tannic acid (TA), chlorogenic acid (CGA), ferulic acid (FA), caffeic acid (CA), and gallic acid (GA)).
View Article and Find Full Text PDFMassive endocytosis mechanisms are involved in uptake of HIV-1 particles by monocyte-derived dendritic cells.
Front Immunol
January 2025
IrsiCaixa, Badalona, Spain.
Introduction: HIV-1 exploits dendritic cells (DCs) to spread throughout the body via specific recognition of gangliosides present on the viral envelope by the CD169/Siglec-1 membrane receptor. This interaction triggers the internalization of HIV-1 within a structure known as the sac-like compartment. While the mechanism underlying sac-like compartment formation remains elusive, prior research indicates that the process is clathrin-independent and cell membrane cholesterol-dependent and involves transient disruption of cortical actin.
View Article and Find Full Text PDFDevelopment and validation of a glycolysis-associated gene signature for predicting the prognosis, immune landscape, and drug sensitivity in bladder cancer.
Front Immunol
January 2025
Department of Urology, The Second Hospital of Tianjin Medical University, Tianjin, China.
Background: Bladder cancer (BCa) is one of the most common malignancies worldwide, and its prognostication and treatment remains challenging. The fast growth of various cancer cells requires reprogramming of its energy metabolism using aerobic glycolysis as a major energy source. However, the prognostic and therapeutic value of glycolysis-related genes in BCa remains to be determined.
View Article and Find Full Text PDFA recurrent variant c.5126C>T in a Han-Chinese family with tuberous sclerosis complex.
Pak J Med Sci
January 2025
Lamei Yuan, MD, PhD, Health Management Center, the Third Xiangya Hospital, Disease Genome Research Center, Center for Experimental Medicine, the Third Xiangya Hospital, Research Center of Medical Experimental Technology, the Third Xiangya Hospital, Xiangya School of Medicine, Central South University, Changsha 410013, Hunan, China.
Objective: To identify the disease-causing variant in a family with tuberous sclerosis complex (TSC).
Methods: This study including a Han-Chinese pedigree recruited from the Third Xiangya Hospital, Central South University, Changsha, Hunan, China was conducted between February, 2019 and January, 2023. Detailed clinical examinations were performed on the proband and other family members of a Han-Chinese family with TSC.
Computational identification of novel natural inhibitors against triple mutant DNA gyrase A in fluoroquinolone-resistant Typhimurium.
Biochem Biophys Rep
March 2025
Department of Integrative Biology, School of Biosciences and Technology, Vellore Institute of Technology (VIT), Vellore, 632014, Tamil Nadu, India.
The rising resistance to fluoroquinolones in Typhimurium poses a significant global health challenge. This computational research addresses the pressing need for new therapeutic drugs by utilizing various computational tools to identify potential natural compounds that can inhibit the triple mutant DNA gyrase subunit A enzyme, which is crucial in fluoroquinolone resistance. Initially, the three-dimensional structure of the wild-type DNA gyrase A protein was modeled using homology modeling, and followed by mutagenesis to create the clinically relevant triple mutant (SER83PHE, ASP87GLY, ALA119SER) DNA gyrase A protein structure.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!