Researchers at MD Anderson have discovered bacterial genetic and cellular elements within brain tumor cells, potentially influencing tumor behavior. Inflammation may also drive the earliest stages of lung cancer, with targeting proinflammatory pathways emerging as a potential early intervention approach
A POSTECH research team found that EGF/EGF-like domains interact with GlcNAc-based biopolymers to achieve strong underwater adhesion without oxidation, leading to durable and reversible bonds.
A massive study of human protein variants found that 61% of disease-causing mutations destabilize proteins, leading to cataracts, neurological disorders, and muscle-wasting diseases. The researchers created the Human Domainome 1 catalogue, which includes over half a million mutations across 522 human protein domains.
A recent study revises our understanding of the universal genetic code's evolution, suggesting that early life preferred smaller amino acids over larger ones. The researchers found that amino acids with aromatic ring structures were incorporated into the code later than previously thought, offering clues about other extinct genetic codes.
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Researchers uncover new insights into protein signal transduction, revealing key details about GRB2 and SOS1's role in passing signals. They discovered differences in the domains' dynamics and binding affinities, providing a more detailed mechanism for liquid-liquid phase separation.
Researchers found that Werner syndrome mice experience age-dependent and sex-specific changes in their livers and immune systems, including fatty liver accumulation and altered lipid metabolism. These findings suggest a potential link between immunoglobulin variants and fatty liver progression in the disorder.
Researchers have developed PaCS-Toolkit to facilitate accessible parallel cascade selection MD (PaCS-MD) simulations. The software package automates the simulation process via a single configuration file, allowing users to explore different conformations and investigate molecular interactions more efficiently.
Researchers at the University of Buffalo have discovered that fusion proteins hijack gene regulatory complexes through their unfolded domains, causing cancer. The study found that these disordered domains interact with high specificity and form liquid-like droplets, enabling cancerous genes to be activated.
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Researchers at Washington University School of Medicine discovered a decoy molecule that protects against the potentially deadly brain infection. The study advanced understanding of viral protein and receptor interactions, laying a foundation for treatments and vaccines.
Researchers at Tokyo Medical and Dental University have developed a novel method to characterize protein-binding interfaces, revealing complex protein geometries. The technique was validated by studying the homophilic interaction between LAMP2A molecules, which form a trimeric structure in mammalian cells.
A new study has uncovered the molecular causes of a rare developmental brain condition in children, known as Autosomal Recessive ACBD6-related disorder. The research team identified defects in the acyl-CoA-binding domain-containing protein 6 (ACBD6) gene as the underlying cause, leading to delays in cognitive and motor skills development.
Researchers developed a novel approach to predict therapeutic targets for aging and age-related diseases. They trained a domain-specific BioGPT model on biomedical literature, which improved its performance in identifying prospective targets.
Rice University scientists developed a tiny CRISPR-Cas13 system to shred viruses by targeting RNA. The system's unique mechanism and three-dimensional structure were mapped using cryo-electron microscopy, allowing researchers to engineer it for improved precision and specificity.
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Researchers from Nara Institute of Science and Technology developed a fluorescence-based monitoring system to study BAR protein assembly. The study found that WASP, Cdc42, and other proteins facilitate GAS7 assembly on lipid membranes, promoting cellular shape formation and protein signaling.
Researchers found that necroptosis promotes metastasis in breast cancer models, and blocking it leads to inhibition of metastasis. Necroptosis may be a key factor in tumor progression, and targeting its regulators could be critical for mitigating metastasis.
A study by Indian Institute of Science researchers found that enhanced recombination in the SARS-CoV-2 Omicron variant resulted in new mutations affecting viral proteins, particularly those involved in host-cell binding. These mutations enabled the virus to evade immune defenses and infect host cells more efficiently.
Researchers found that antibodies against one of the two main domains of the SARS-CoV-2 viral entry machinery elicit a broad antibody response against many variants. This suggests strategies for clinical development of variant-resistant vaccines.
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Researchers have identified a complex of proteins in a tiny marine invertebrate that share similarities with the human immune system, suggesting an earlier origin for the building blocks of our immune system. The study could ultimately guide the development of new immunotherapies and improve understanding of transplant rejection.
Researchers determined the cryo-EM structure of IGF Ternary complex and its assembly & activation mechanism. The study reveals how IGFBP3 and ALS form a stable complex with IGF1, regulating its activity. The findings provide new insights into growth-related diseases such as growth hormone deficiency and ALS deficiency.
Researchers at Johns Hopkins Medicine have probed the atomic structure of proteins, finding that wiggling and movement play a critical role in their ability to function. The study's findings may help scientists design new drugs that can modify or disrupt protein movements to alter their functions.
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Researchers have created stem cell models that mimic the genetic disorder, revealing the role of WASP protein in regulating RNA splicing and finding potential therapeutic targets. These findings could lead to new treatments for Wiskott-Aldrich syndrome, a devastating immune deficiency disorder.
A new study by the University of Colorado Anschutz Medical Campus explores the effects of multiple mutations in SARS-CoV-2 variants. The findings suggest that certain mutations work together to improve virus fitness, making it challenging for antibody treatments to neutralize new variants.
Researchers characterized viral protein binding to sialic acids on animal and human coronaviruses, revealing host-specific patterns. This adaptation enables coronaviruses to quickly jump species, driving cross-species transmission.
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Researchers at University of Texas at Austin create first-ever biologically authentic computer model of HIV-1 virus liposome, shedding light on replication and infectivity. The study reveals key characteristics of the liposome's asymmetry and its role in shaping macroscopic properties.
Scientists have discovered a new layer of regulation in plant-microbe interactions using peanut studies. An antisense long-noncoding RNA, DONE40, was found to bind to a protein involved in epigenetic control, suggesting a conserved function across plants and animals.
Researchers identify a molecular culprit for COVID-19's seasonal nature, finding a galectin-like structure on the spike protein that responds to external seasonal patterns. This discovery could help predict future mutations and potentially pave the way for new therapeutics or vaccines.
Researchers at Arizona State University have refined cryogenic electron microscopy to produce more accurate structures of biological samples. The new method uses a statistical approach to model transitory structures, which can play a vital role in biological processes.
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Researchers used complex computer simulations to study the attachment of SARS-CoV-2 and its variants to human cells. They found that the virus has two main locations where it grabs onto the host cell receptor ACE2, with early strains having a slippery interaction at one region that becomes less slippery as variants evolve.
Researchers mapped protein domain evolution over 3.8 billion years, revealing a 'big bang' of domain combinations 1.5 billion years ago. This discovery could help understand and engineer proteins for disease management, vaccine design, and preventing pandemics.
A German-Japanese research team has deciphered the 3D structure of a metalloprotein that catalyzes RNA editing in all plant cells. The DYW domain's activation is triggered by a zinc atom and a gating domain, providing a sophisticated regulation mechanism for chloroplasts and mitochondria.
Researchers at Göttingen University have identified a completely novel on/off switch in proteins that controls their structure and function. The discovery of this lysine-cysteine redox switch has wide-ranging implications for protein design, medical applications, and drug development.
A team of scientists has developed a new time-resolved method to analyze the structural changes in egg whites when heated. The study reveals how proteins unfold and cross-link to form a solid structure, with implications for food industry applications.
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A team of researchers used a novel approach to study the human gene responsible for Meier-Gorlin syndrome, a rare genetic disorder causing dwarfism and skeletal abnormalities. They discovered that a mutation in this gene affects its ability to bind to DNA, leading to defective cell division and growth.
Researchers have discovered a family of plant immune proteins with striking resemblance to vertebrate MLKLs, triggering cell death in response to pathogens. These findings provide new insights into how plants protect themselves from microbial invaders and highlight the shared machinery involved in cell death across kingdoms.
The study reveals a unique RNA binding pocket in SARS-CoV-2 nucleocapsid protein, which could guide the design of novel antiviral agents. The crystal structure provides atomic resolution features that may lead to the development of specific targeting sites for SARS-CoV-2.
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A study published in The FASEB Journal identifies a protein encoded by SARS-CoV-2 that may facilitate the virus's quick spread through cells. The research highlights key characteristics of the virus that could aid in the development of treatments for COVID-19.
Scientists have generated near atomic resolution images of a viral protein complex responsible for replicating the RNA genome of positive-strand RNA viruses. The results provide mechanistic insights into the virus life cycle and aid development of new antivirals.
Researchers have solved the structure of a critical protein region in SMCHD1, which plays a key role in 'switching off' genes. The new map reveals how inherited changes in this region cause certain diseases, including muscular dystrophy and developmental disorders.
Stress granules and P-bodies are formed when external stress halts the RNA assembly line, clumping RNA together. Researchers discovered a simple principle underlying their assembly, revealing how protein-rich compartments condense from cytoplasm into liquid droplets. This understanding may lead to new therapeutics for diseases of aging.
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Biophysicists analyzed the mechanical stability of a protein-ligand complex, finding that geometry affects stability and forces required to extract ligand vary by barrel structure. This discovery may improve experimental data analysis and understanding of mechanosensitive proteins.
Researchers have devised a new type of chimeric antigen-receptor (CAR) T cell that can be reversibly inactivated with small molecules, offering novel solutions to the safety concerns of CAR-T therapies. The 'STOP-CAR-T' system has been shown to work as well as traditional CAR-T systems and can be controlled by an approved drug.
MIB2 promotes proteasomal degradation of CYLD, activating NF-κB signaling and enhancing inflammation. Mib2-knockout mice show reduced serum IL-6 and suppressed inflammatory responses.
Scientists have detailed the structure of calcium-calmodulin-dependent kinase II (CaMKII), a key protein involved in encoding memories. The study reveals how CaMKII binds to actin filaments, forming rigid bundles that support dendritic spines and enable cognitive functions.
Scientists have solved the X-ray crystal structure of an enzyme that produces a broad-spectrum antibiotic called obafluorin. This breakthrough provides a detailed molecular structure of the enzyme's three-dimensional space and sheds light on its mechanism, which could lead to the creation of new antibiotics with novel structural classes.
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A deep learning-powered computational framework called DeepEC has been developed to predict enzyme commission numbers with high accuracy and efficiency. It uses convolutional neural networks and homology analysis to identify EC numbers, which is essential for understanding enzyme functions.
A new study demonstrates how ankyrin repeat and KH domain-containing protein 1 (ANKHD1) forms the early endosome, enabling cellular transport. The ARD of ANKHD1 contains 25 ankyrin repeats that have different roles in vesiculation and dimerization.
A study by EPFL researchers found that the KRAB domain-containing zinc finger protein Zfp30 initially repressed a retrotransposon, but later evolved to activate genes involved in fat-cell formation instead, surprising scientists
A recent study discovered that the nascent polypeptide-associated complex (NAC) plays a key role in preventing protein aggregation associated with neurodegenerative diseases. NAC suppresses PolyQ aggregation and enhances organismal fitness, according to tests using animal models such as C. elegans.
Researchers at University of Alabama at Birmingham discover how Avian Sarcoma Virus binds to cell membrane, providing insights into HIV-1 replication and potential treatment strategies. The study reveals a crucial cluster of four lysine amino acids that interact with acidic membrane lipids.
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The study provides new insights into targeting the human T-cell immunoglobulin and mucin domain containing protein-3 (hTIM-3) for treating various cancers. The high-resolution structure of hTIM-3 will help develop useful therapeutics.
Researchers from the University of Würzburg have provided new insights into the molecular-level structural details responsible for spider silk's exceptional strength, extensibility, and biodegradability. The study suggests that a molecular clamp connecting protein building blocks contributes to the material's flexibility.
Researchers have created biomaterials that combine ordered and disordered segments to form a stable, porous scaffold that promotes cell growth and vascularization. The material's unique properties enable it to integrate into tissue with minimal inflammation and hold its volume well.
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Researchers from Clemson University and Stony Brook University reveal a 3-D structure of a protein fragment that could serve as a drug target in treating stroke patients. The protein, PSD-95, plays a crucial role in maintaining neural connections and facilitating communication, learning, and memory.
Researchers have identified two protein domains that mediate toxicity in ALS and FTLD, revealing a key role for stress granules in disease progression. The study provides new insights into the molecular mechanisms underlying these neurodegenerative diseases.
Researchers discovered that porcine deltacoronavirus can infect human cells by binding to aminopeptidase N, which is conserved across animal species; this suggests a possible mechanism of transmission from pigs to other animals and potentially humans.
Researchers developed a process to observe lipid-flipping enzymes' activity in conjunction with membrane deformation. They found that ATP10A enzyme flips phosphatidylcholine lipids, causing curvature changes that trigger tubule formation, enhancing endocytosis and membrane dynamics.
A recent study has found that plants share defensive proteins through evolutionary pick 'n' mix, allowing them to respond effectively to emerging diseases. The research identified diverse groups of genes in various wild and domestic grasses, including wheat and barley, which can be used to engineer resistant crops.
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Mutations in p63 protein lead to severe genetic disease AEC syndrome, which resembles Alzheimer's, Parkinson's or ALS more closely than other syndromes. The research lays groundwork for causal therapies by showing that protein aggregates underlie the disorder.
A team of researchers has described atom-by-atom changes in a family of proteins linked to amyotrophic lateral sclerosis (ALS), a group of brain disorders. The study suggests that small chemical changes can lead to big changes in assembly and disease-associated aggregation, offering new insights into disease mechanisms.
The protein Trigger factor recognizes a partner with unstable domains to form a stable protein duo. Chaperones like TF help folding of other proteins.