This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:

"Learning something new not only changes our perspectives and behavior – it actually changes the structure of our brains. Memories and experiences are recorded in the brain by altering the physical connections between neurons. Until recently, however, the protein signals that cause these tiny structural changes were too small to measure with available imaging methods. But researchers at the Max Planck Florida Institute for Neuroscience created ultra-sensitive sensors and revealed the activity of two of the proteins that write memories into neural circuits in the brain. Individual neurons have many branches, or dendrites. And each dendrite can be covered with thousands of tiny bumps called spines, where messages are received from other neurons. Changes in spine size are one way memories are recorded-when lots of messages are being passed and a spine is very active, it gets bigger. Many proteins need to be activated to make spines grow..."

The rest of the transcript, along with a link to the research itself, is available on the resource itself.

This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:

"The pumping action of the heart is tightly regulated by many factors. For example, the ion channel proteins RyR2 and SERCA2a regulate cardiac contraction via the β adrenergic receptor (βAR) pathway and under stress conditions, βAR stimulation promotes the enzyme activity of PKA to ultimately enhance cardiac contraction and relaxation. However, it’s unclear exactly how βAR-stimulated PKA dynamically affects RyR2 and SERCA2a within their nano-scale subcellular domains. To learn more, researchers recently used biosensors to detect PKA activity at these nanodomains in heart cells from mice, rats, and rabbits. They found that the βAR subtype β₁AR signaled to both RyR2 and SERCA2a nanodomains via PKA, while β₂AR did not. Specifically, β₂AR signaling at these nanodomains was prevented by the enzymes PDE3 and PDE4, which controlled baseline PKA activity, but blocking an inhibitory G protein permitted β₂AR signaling at the RyR2 nanodomains..."

The rest of the transcript, along with a link to the research itself, is available on the resource itself.

This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:

"Chronic infection with the hepatitis C virus is a major cause of chronic liver disease, even after the virus has been eradicated by antiviral treatment. The problem appears to lie in the lingering activation of harmful Wnt/β-catenin signaling, which active viruses exploit for replication. A new study suggests the enzyme PKA could play a role. PKA is part of a signaling cascade that is activated during hepatitis C infection. To determine its role, researchers prevented PKA activation by treating cells with a PKA inhibitor. Inhibition was found to be beneficial. Inhibiting PKA reduced cells’ capacity to support both the hepatitis C virus and Wnt/β-catenin signaling, as mediated by another enzyme, GSK-3β. Interestingly, similar benefits were observed when another harmful effect of viral infection was repressed, namely, endoplasmic reticulum stress..."

The rest of the transcript, along with a link to the research itself, is available on the resource itself.

This guided inquiry learning activity is designed to be used in a large introductory chemistry course. By working in small groups to discuss the presented information and question prompts, students will engage in cycles of exploring and analyzing data, inventing new conceptual understandings, and applying those concepts. Students should be tasked with working together to complete the prompts in each section by a set time limit. After each section is completed, the entire class can share their answers via a personal response system, and the instructor can review and explain the correct responses, using the accompanying slide deck, which translates the problems into multiple-choice prompts.Instructional resources include 1) the learning activity (.docx and .pdf) 2) the learning objects (.docx and .pdf) and 3) the slide deck (.pptx).- Atomic Orbitals- Chemical Fuels- Gas Laws- Intermolecular Forces- pKa Trends- VSEPR

This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:

"Nerves, and the signals that modulate them, play critical roles during wound healing. CGRP (calcitonin gene-related peptide) is one such modulator and is a potential treatment target for chronic wounds, like ulcers. But CGRP doesn’t last long in blood samples, so researchers recently focused on RAMP1 (receptor activity-modifying protein 1), which is part of the CGRP receptor. First, in mouse experiments, they determined that RAMP1 expression was altered during skin wound healing. Then, they used mouse skin fibroblasts (MSFs) to determine the mechanisms at play. Overexpressing RAMP1 in MSFs promoted proliferation by increasing expression of YAP (Yes-associated protein). Subsequent experiments showed that overexpressed RAMP1 increased expression of Gαi3 (inhibitory G protein α subunit 3). While Gαi3 is typically inhibitory, here Gαi3 activated PKA (protein kinase A) through a non-classical pathway..."

The rest of the transcript, along with a link to the research itself, is available on the resource itself.