98%
921
2 minutes
20
The in vitro generation of defined cellular populations from induced human pluripotent stem cells (iPSCs) provides the opportunity to work routinely with human material and, importantly, allows examination of material derived from patients with clinically and genetically diagnosed disorders. In this regard, the ability to derive oligodendrocytes in vitro represents an important resource to examine human oligodendrocyte-lineage cell biology in normal and disease contexts. Oligodendrocytes undergo characteristic physiological maturation during differentiation in vitro, and patch-clamp electrophysiology allows a detailed examination of maturation state and, potentially, pathologically related variations of ion channel expression and regulation. Here, we detail our methodology to generate oligodendrocyte precursor cells and oligodendrocytes and characterize them electrophysiologically.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1007/978-1-4939-9072-6_4 | DOI Listing |
Sci China Life Sci
September 2025
MOE Key Laboratory of Bioinformatics and Center for Plant Biology, School of Life Sciences, Tsinghua University, Beijing, 100084, China.
Tomato brown rugose fruit virus (ToBRFV) overcomes all known tomato resistance genes, including the durable Tm-2, posing a serious threat to global tomato production. Here, we employed in vitro random mutagenesis to evolve the Tm-2 leucine-rich repeat (LRR) domain and screened ∼8,000 variants for gain-of-function mutants capable of recognizing the ToBRFV movement protein (MP) and triggering hypersensitive cell death. We identified five such mutants.
View Article and Find Full Text PDFNat Cell Biol
September 2025
Department of Medicine, Division of Pulmonary and Critical Care Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, MA, USA.
Durotaxis, cell migration along stiffness gradients, is linked to embryonic development, tissue repair and disease. Despite solid in vitro evidence, its role in vivo remains largely speculative. Here we demonstrate that durotaxis actively drives disease progression in vivo in mouse models of lung fibrosis and metastatic pancreatic cancer.
View Article and Find Full Text PDFImmunol Lett
September 2025
Department of Clinical and Translational Science, College of Graduate Health Science, University of Tennessee Health Science Center, Memphis, Tennessee. Electronic address:
Background: Patients with chronic lung diseases often suffer from pulmonary aspergillosis, caused by Aspergillus fumigatus (AF). Alveolar macrophages play a key role in the initial immune response to AF. Azithromycin (AZM), commonly known for its immunomodulatory properties in reducing exacerbations and improving lung function, has mixed effects on the development of aspergillosis.
View Article and Find Full Text PDFBioorg Chem
September 2025
Post Graduate and Research Department of Botany, A.V.V.M. Sri Pushpam College (Affiliated to Bharathidasan University), Poondi 613 503, Thanjavur, India. Electronic address:
The research employed zirconyl oxychloride as a catalyst in a reaction involving pyrazole aldehyde, (thio)urea, and acetyl acetone to establish an aqueous approach for synthesizing 3,4-dihydropyrimidinone derivatives (compounds 4a-j) with potential claims as antidiabetic agents. FT-IR, HR-MS, H NMR and C NMR were employed to analyze the synthesized compounds. The HOMO-LUMO analysis was performed to evaluate the stability of the synthesized derivatives.
View Article and Find Full Text PDFBioorg Chem
September 2025
State Key Laboratory of Immune Response and Immunotherapy, School of Basic Medical Sciences, Division of Life Science and Medicine, University of Science and Technology of China, Hefei 230027, China; Institute of Health and Medicine, Hefei Comprehensive National Science Center, Hefei 230601, China;
3-Oxoacid CoA-transferase 1 (OXCT1) plays a crucial role in hepatocellular carcinoma (HCC) progression through its ketolytic and succinyltransferase activities. Despite its potential as a therapeutic target, no small molecules have been developed to inhibit the dual enzymatic activities of OXCT1 specifically. In this study, our structural analysis revealed that the active sites for both enzymatic functions of OXCT1 are located in the same pocket.
View Article and Find Full Text PDF