Chronic stress leads to persistent and contrasting stellate neuron dendritic hypertrophy in the amygdala of male and female rats, an effect not found in the hippocampus.

In males, chronic stress enhances dendritic complexity in the amygdala, a region important in emotion regulation. An amygdalar subregion, the basolateral amygdala (BLA), is influenced by the hippocampus and prefrontal cortex to coordinate emotional learning and memory. This study quantified changes in dendritic complexity of BLA stellate neurons ten days after an unpredictable chronic stressor ended in both male and female rats.

Best practices for artificial intelligence in life sciences research.

We describe 11 best practices for the successful use of artificial intelligence and machine learning in pharmaceutical and biotechnology research at the data, technology and organizational management levels.

Metal- and Oxidant-Free Alkenyl C-H/Aromatic C-H Cross-Coupling Using Electrochemically Generated Iodosulfonium Ions.

A three-step transformation consisting of 1) addition of electrochemically generated iodosulfonium ions to vinylarenes to give (1-aryl-2-iodoethoxy)sulfonium ions, 2) nucleophilic substitution by subsequently added aromatic compounds to give 1,1-diaryl-2-iodoethane, and 3) elimination of HI with a base to give 1,1-diarylethenes was developed. The transformation serves as a powerful metal- and chemical-oxidant-free method for alkenyl C-H/aromatic C-H cross-coupling.

Endorepellin laminin-like globular 1/2 domains bind Ig3-5 of vascular endothelial growth factor (VEGF) receptor 2 and block pro-angiogenic signaling by VEGFA in endothelial cells.

Endorepellin, a processed fragment of perlecan protein core, possesses anti-angiogenic activity by antagonizing endothelial cells. Endorepellin contains three laminin G-like (LG) domains and binds simultaneously to vascular endothelial growth factor receptor 2 (VEGFR2) and α2β1 integrin, resulting in dual receptor antagonism. Treatment of endothelial cells with endorepellin inhibits transcription of VEGFA, the natural ligand for VEGFR2, attenuating the pro-survival and migratory activities of VEGFA/VEGFR2 signaling cascade.

Endorepellin affects angiogenesis by antagonizing diverse vascular endothelial growth factor receptor 2 (VEGFR2)-evoked signaling pathways: transcriptional repression of hypoxia-inducible factor 1α and VEGFA and concurrent inhibition of nuclear factor of activated T cell 1 (NFAT1) activation.

Endorepellin, the angiostatic C-terminal domain of the heparan sulfate proteoglycan perlecan, inhibits angiogenesis by simultaneously binding to the α2β1 integrin and the vascular endothelial growth factor (VEGF) receptor 2 (VEGFR2) on endothelial cells. This interaction triggers the down-regulation of both receptors and the concurrent activation of the tyrosine phosphatase SHP-1, which leads to a signaling cascade resulting in angiostasis. Here, we provide evidence that endorepellin is capable of attenuating both the PI3K/PDK1/Akt/mTOR and the PKC/JNK/AP1 pathways.

Hydrophobic residues in small ankyrin 1 participate in binding to obscurin.

Abstract Small ankyrin-1 is a splice variant of the ANK1 gene that binds to obscurin A. Previous studies have identified electrostatic interactions that contribute to this interaction. In addition, molecular dynamics (MD) simulations predict four hydrophobic residues in a 'hot spot' on the surface of the ankyrin-like repeats of sAnk1, near the charged residues involved in binding.

Electrostatic interactions mediate binding of obscurin to small ankyrin 1: biochemical and molecular modeling studies.

Small ankyrin 1 (sAnk1; also known as Ank1.5) is an integral protein of the sarcoplasmic reticulum (SR) in skeletal and cardiac muscle cells, where it is thought to bind to the C-terminal region of obscurin, a large modular protein that surrounds the contractile apparatus. Using fusion proteins in vitro, in combination with site-directed mutagenesis and surface plasmon resonance measurements, we previously showed that the binding site on sAnk1 for obscurin consists, in part, of six lysine and arginine residues.

Characterization and comparison of two binding sites on obscurin for small ankyrin 1.

Obscurin A, an ∼720 kDa modular protein of striated muscles, binds to small ankyrin 1 (sAnk1, Ank 1.5), an integral protein of the sarcoplasmic reticulum, through two distinct carboxy-terminal sequences, Obsc(6316-6436) and Obsc(6236-6260). We hypothesized that these sequences differ in affinity but that they compete for the same binding site on sAnk1.

Specific protein domains mediate cooperative assembly of HuR oligomers on AU-rich mRNA-destabilizing sequences.

The RNA-binding factor HuR is a ubiquitously expressed member of the Hu protein family that binds and stabilizes mRNAs containing AU-rich elements (AREs). Hu proteins share a common domain organization of two tandemly arrayed RNA recognition motifs (RRMs) near the N terminus, followed by a basic hinge domain and a third RRM near the C terminus. In this study, we engineered recombinant wild-type and mutant HuR proteins lacking affinity tags to characterize their ARE-binding properties.

A calibration study of therapeutic ultrasound units.

Background And Purpose: Physiological effects of therapeutic ultrasound (US) are dependent on the intensity and duration of application. The purpose of this study was to test US machines used in clinical settings for proper calibration of time and power output.

Methods: Measurements of power output and timer accuracy were obtained from 83 US units in clinical use.