Campbell Family Cancer Research Institute, Ontario Cancer Institute, Princess Margaret Hospital, University Health Network, Toronto, ON, Canada.
Published: December 2022
AI Article Synopsis
Article Abstract
Protein tyrosine phosphatases constitute a family of cytosolic and receptor-like signal transducing enzymes that catalyze the hydrolysis of phospho-tyrosine residues of phosphorylated proteins. PTP1B, encoded by , is a key negative regulator of insulin and leptin receptor signaling, linking it to two widespread diseases: type 2 diabetes mellitus and obesity. Here, we present crystal structures of the PTP1B apo-enzyme and a complex with a newly identified allosteric inhibitor, 2-(2,5-dimethyl-pyrrol-1-yl)-5-hydroxy-benzoic acid, designated as P00058. The inhibitor binding site is located about 18 Å away from the active center. However, the inhibitor causes significant re-arrangements in the active center of enzyme: residues 45-50 of catalytic Tyr-loop are shifted at their Cα-atom positions by 2.6 to 5.8 Å. We have identified an event of allosteric signal transfer from the inhibitor to the catalytic area using molecular dynamic simulation. Analyzing change of complex structure along the fluctuation trajectory we have found the large Cα-atom shifts in external strand, residues 25-40, which occur at the same time with the shifts in adjacent catalytic p-Tyr-loop. Coming of the signal to this loop arises due to dynamic fluctuation of protein structure at about 4.0 nanoseconds after the inhibitor takes up its space. Communicated by Ramaswamy H. Sarma.
Objectives: This narrative review aims to analyze mechanisms underlying Brain-Computer Interface (BCI) and Artificial Intelligence (AI) integration, evaluate recent advances in signal acquisition and processing techniques, and assess AI-enhanced neural decoding strategies. The review identifies critical research gaps and examines emerging solutions across multiple domains of BCI-AI integration.
Methods: A narrative review was conducted using major biomedical and scientific databases including PubMed, Web of Science, IEEE Xplore, and Scopus (2014-2024).
National Agri-Food Biotechnology Institute, Sahibzada Ajit Singh Nagar, Punjab 140306, India; Stress Physiology and Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India. Electronic address:
Background: Salinity stress affects plant growth, development, biomass, yield, as well as their survival. A series of signaling cascade is activated to cope the deleterious effect of salinity stress. Cytokinins are known for their regulatory roles from cell growth and expansion to abiotic stress signaling.
Key Laboratory of Optic-Electric Sensing and Analytical Chemistry for Life Science, MOE, College of Chemistry and Molecular Engineering, Qingdao University of Science and Technology, Qingdao 266042, P. R. China.
The classical electrochemiluminescence (ECL) reagent Ru(bpy) was first doped into CdSe QDs to prepare novel dual-potential color-resolved luminophore Ru-CdSe QDs. Ru-CdSe QDs emitted a strong red ECL signal at a positive potential with coreactant TPrA and a strong green ECL signal at a negative potential with coreactant KSO. As a proof-of-concept application, this work introduced Ru-CdSe QDs into a dual-channel closed bipolar electrode (CBPE) system to construct an ECL biosensor for simultaneous detection of chloramphenicol (CAP) and kanamycin (KAN).
Holographically designed aperiodic lattices (ALs) have proven to be an exciting engineering technique for achieving electrically switchable single- or multi-frequency emissions in terahertz (THz) semiconductor lasers. Here, we employ the nonlinear transfer matrix modeling method to investigate multi-wavelength nonlinear (sum- or difference-) frequency generation within an integrated THz (idler) laser cavity that also supports optical (pump and signal) waves. The laser cavity includes an aperiodic lattice, which engineers the idler photon lifetimes and effective refractive indices.
Autophagy is an essential cellular recycling process that maintains protein and organelle homeostasis. ATG9A vesicle recruitment is a critical early step in autophagy to initiate autophagosome biogenesis. The mechanisms of ATG9A vesicle recruitment are best understood in the context of starvation-induced non-selective autophagy, whereas less is known about the signals driving ATG9A vesicle recruitment to autophagy initiation sites in the absence of nutrient stress.
