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Urinary obstruction causes injury to the renal medulla, impairing the ability to concentrate urine, and increasing the risk of progressive kidney disease. However, the regenerative capacity of the renal medulla after reversal of obstruction is poorly understood. To investigate this, we developed a mouse model of reversible urinary obstruction.

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Background: Peripheral nerve sheath tumors (PNSTs) encompass entities with different cellular differentiation and degrees of malignancy. Spatial heterogeneity complicates diagnosis and grading of PNSTs in some cases. In malignant PNST (MPNST) for example, single cell sequencing data has shown dissimilar differentiation states of tumor cells.

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Multifunctional Artificial Electric Synapse of MoSe-Based Memristor toward Neuromorphic Application.

J Phys Chem Lett

January 2025

Key Laboratory of Atomic and Molecular Physics and Functional Materials of Gansu Province, College of Physics and Electronic Engineering, Northwest Normal University, Lanzhou 730070, China.

Research on memristive devices to seamlessly integrate and replicate the dynamic behaviors of biological synapses will illuminate the mechanisms underlying parallel processing and information storage in the human brain, thereby affording novel insights for the advancement of artificial intelligence. Here, an artificial electric synapse is demonstrated on a one-step Mo-selenized MoSe memristor, having not only long-term stable resistive switching characteristics (reset 0.51 ± 0.

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Fully Atomistic Molecular Dynamics Simulation of Ice Nucleation Near an Antifreeze Protein.

J Am Chem Soc

January 2025

Department of Materials Science and Engineering, City University of Hong Kong, Hong Kong, Kowloon 999077, China.

Heterogeneous ice nucleation is a widespread phenomenon in nature. Despite extensive research on ice nucleation near biological antifreeze proteins, a probe for ice nucleation and growth processes at the atomic level is still lacking. Herein, we present simulation evidence of the heterogeneous ice nucleation process on the ice-binding surface (IBS) of the antifreeze protein (TmAFP).

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