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:

"A team of researchers based at West Virginia University has devised an innovative way to potentially monitor enzyme activity in vivo using electron paramagnetic resonance imaging. The method could provide new insights into the molecular underpinnings of many types of disease. The team specifically focused on tracking enzymatic dephosphorylation. Abnormalities in dephosphorylation have been linked to disorders ranging from cancer to Alzheimer disease. Monitoring such malfunction in vivo can provide crucial details into disease state and progression, but direct measurement of enzyme activity within a living organism remains extremely challenging. Many imaging approaches that might be used for this purpose are hampered by concerns such as low sensitivity and penetration depth. Such limitations prompted the researchers to turn to EPRI – a method with high intrinsic sensitivity and specificity..."

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:

"Prostate cancer is one of the prevalent forms of cancer in men around the world. Prostate tumors become especially fatal when they spread to one and other vital organs. The main forces driving cell motility are the constant polymerization and depolymerization of actin filaments which lead to changes in cellular protrusions. This process is regulated by actin-binding proteins, such as capping proteins, which bind to the fast-growing ends of actin filaments. A new study shows that these capping proteins are substrates for cancer-inducing PIM kinases, proteins whose overexpression promotes cancer cell survival and motility. Phosphorylation of capping proteins decreases their ability to protect actin filament ends from disassembly, leading to enhanced cell motility. while PIM inhibitors or capping protein mutations have the opposite effect, reducing cell migration..."

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:

"Oncogenic PIM kinases and the tumor suppressor LKB1 regulate cell growth and metabolism in different directions. LKB1 suppresses tumorigenesis largely by phosphorylating and activating the energy sensing kinase AMPK. Anti-oncogenic PIM inhibitors also increase AMPK phosphorylation. However, the exact mechanism by which PIM inhibition affects AMPK remains unclear. A recent study explored the potential PIM-LKB1 interaction related to AMPK phosphorylation in prostate (PC3) and breast (MCF7) cancer cells. Inhibition of activity (by DHPCC9 or AZD1208) or expression (by triple knockout, TKO) of all three PIM kinases increases AMPK phosphorylation. These effects are LKB1-dependent, suggesting that PIM kinases regulate AMPK via LKB1. Additional assays confirmed that PIM kinases phosphorylate LKB1 to inactivate it, identifying LKB1 as a novel PIM substrate. In a chick embryo xenograft model, LKB1 knockout increased tumorigenic growth of prostate cancer cells..."

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 activation of toll-like receptors (TLRs) is critical to detecting potentially harmful microbes, but overactivation can be life-threatening, leading to autoimmune and inflammatory diseases. While much research has been dedicated to positive regulators of TLR signaling, such as protein serine/threonine kinases, much less has focused on phosphatases, which counterbalance and limit TLR signaling. Fortunately, a growing number of studies are exploring the roles of these enzymes and how they might be harnessed to prevent excessive immune activation. Two important families of protein phosphatases are phospho-protein phosphatases (PPPs) and metal-dependent protein phosphatases (PPMs). PPPs contain a highly conserved catalytic core domain, which can combine with regulatory subunits to home in on specific enzymatic targets. PPMs, on the other hand, rely on magnesium or manganese ions and do not form multi-subunit complexes..."

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:

"Medulloblastoma is the most common brain tumor of childhood. Precisely targeting the signaling pathways involved in medulloblastoma is needed to increase treatment efficacy. One promising treatment, inhibiting the protein Smoothened (SMO), downregulates the Hedgehog signaling pathway, but treatment resistance and severe side effects such as muscle spasms remain a concern for SMO inhibitors. In a new study, researchers sought to better understand Hedgehog signaling pathway regulation in medulloblastoma. Using quantitative phosphoproteomics to evaluate human medulloblastoma cells, they found that Hedgehog signaling via SMO affected ciliary assembly, trafficking, and signal transduction. Several signaling pathways were differentially regulated by SMO inhibitors, including ERK/MAPK, Protein Kinase A, and mTOR. These results help to elucidate the downstream signaling pathways triggered by SMO inhibitor treatment, providing important insight to help prevent adverse effects and therapeutic resistance..."

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:

"Bladder cancer is the 10th most frequent malignancy in the world. Despite the availability of several treatment options, including surgery, chemotherapy, and radiotherapy, outcomes for patients with bladder cancer remain poor. Fortunately, a growing understanding of the molecular origins of the disease is revealing new targets for treatment. Among the most promising are a family of enzymes called tyrosine kinases. Tyrosine kinases modify the structure and function of tyrosine-containing proteins. This action helps regulate cellular processes such as growth, migration, differentiation, and metabolism. Dysregulation of tyrosine kinases is part of the pathway that leads to signs and symptoms of bladder cancer. Abnormal tyrosine kinase function can be caused by mutations, amplification, and chromosomal abnormalities. Ongoing studies are discovering how tyrosine kinases can serve as early markers of bladder cancer and how they might be manipulated to stop the progression of bladder tumors..."

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:

"A change in temperature can easily alter the course of our day. But for some reptiles and fish, it can set the course of their lives—deciding whether they emerge as male or female when they hatch. Basically, temperature affects whether the early gonad becomes a testis (making male hormones) or an ovary (making female hormones). It’s called temperature-dependent sex determination, and it was first described in the late 1960s. But only now are researchers close to understanding how this phenomenon works on a molecular level. A new study reveals the genetic circuitry behind this type of sex determination in red-eared slider turtles. Researchers recently discovered the role played by an epigenetic regulator known as KDM6B, which can control whether a gene is turned on or off. KDM6B is required for the expression of the sex-determination gene Dmrt1, which leads to a male anatomy..."

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:

"Calcineurin is a serine/threonine phosphatase that serves as a critical bridge between calcium signaling and the phosphorylation states of numerous important substrates. But despite being studied for approximately 40 years, exactly how calcineurin is activated in humans and other organisms is not yet fully understood. Structurally, calcineurin is a heterodimer expressed as three different isoforms: α, β, and γ each featuring a catalytic domain, a B chain binding helix, the regulatory domain, an autoinhibitory domain, and an unstructured C-terminal domain of unknown function. Disorder is a key hallmark of calcineurin’s structure. The intrinsically disordered regulatory domain could facilitate the rapid activation of calcineurin during calcium signaling. Increasing evidence suggests that calcineurin is a vital component of various signaling pathways. But even more work is needed to understand calcineurin’s versatility including how certain substrates bind to calcineurin..."

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:

"RNA base editing has great potential for use in research for cell functions and genetic disease. Unlike DNA editing, which can cause unwanted mutations in other parts of the genome, RNA editing may allow researchers to mimic genetic variants that provide a health advantage. Two main RNA base editors have been used in vitro: REPAIR, which mediates A-to-I editing, and RESCUE, which can perform both C-to-U and A-to-I editing. Unfortunately, although RESCUE is more versatile, its low editing efficiency limits its applications. Now, researchers have developed an enhanced RESCUE (eRESCUE) system. eRESCUE was generated by fusing inactivated PspCas13b with ADAR2. In tests using human cell lines, eRESCUE mediated more efficient A-to -I and C-to-U RNA editing than the original RESCUE editor. eRESCUE editing of IKKβ successfully converted 177Ser to Gly, resulting in decreased phosphorylation and downregulation of downstream IKKβ-related genes..."

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:

"Normally bound to the microtubules that give neurons their structure, the protein tau becomes detached in the brains of patients with Alzheimer’s disease. That leads to the fibrillary tangles that have become the hallmark of the disease. Most textbooks explain that post-translational modifications, or PTMs, in the form of excessive phosphorylation trigger the formation and growth of these bundles. But new findings propose a subtle though crucial refinement. Researchers from the Brain Mind Institute at the EPFL in Switzerland have discovered that while phosphorylation does trigger tau detachment, it doesn’t appear to promote tangle growth. It actually protects against it. Their findings offer a new perspective on the role of phosphorylation in tau pathologies, while encouraging the design of therapeutics that target tau detachment. Numerous studies have homed in on hyperphosphorylation as a trigger for tau pathologies. Unfortunately, they’ve done so with relatively poor resolution..."

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