Researchers at OHSU Vollum Institute discovered the atomic structure of the serotonin transporter bound to SSRIs, revealing a pathway for developing new therapeutic agents. The study provides insight into how chemically diverse antidepressants interact with the protein that transports serotonin in the brain.
A Yale-led study reveals the intricate mechanism of beta-Klotho, a protein that regulates longevity and metabolism. The findings could lead to therapies for diabetes, obesity, and certain cancers.
The study reveals how fibroblast growth factor 23 (FGF23) signals to cells through its receptor and alpha-Klotho, reversing previous conjecture on alpha-Klotho's anti-aging role. The findings also shed light on kidney disease leading to heart hypertrophy.
RAS molecules act in pairs, known as dimers, to cause cancer and transmit signals that tell a cell to grow and divide. The study provides a foundation for further studies on RAS biology and could potentially pave the way to develop new cancer drugs.
Researchers at The Scripps Research Institute have discovered the workings of a promising treatment for Marburg virus, which has a mortality rate of up to 88 percent. The treatment, MR191, targets a conserved site on the virus and neutralizes it by mimicking the host receptor.
Researchers at Osaka University developed an acid-tolerant green fluorescent protein, Gamillus, that can withstand low pH environments. The protein exhibits superior acid tolerance and nearly twice the brightness of reported GFPs, making it a powerful tool for imaging in acidic organelles.
Researchers at Nagoya University and Tsinghua University have analyzed the crystal structure of LURE bound to its receptor protein PRK6, revealing a unique binding scheme that controls pollen tube growth. The study provides insights into the precise mechanism of direction control in fertilization.
Researchers at Scripps Research Institute use nuclear magnetic resonance spectroscopy to study the A2a adenosine receptor, revealing its dynamic structure and a
Researchers at Scripps Research Institute and Duke University have made the first determination of TRPM8's atomic structure using cryo-electron microscopy. The findings reveal unexpected binding pocket locations for menthol and other cold-sensing molecules, opening new avenues for drug development.
A team of scientists at Université de Montréal developed a novel strategy to block the transfer of antibiotic-resistant genes by binding molecules that target the TraE protein. This approach has the potential to reduce the spread of resistance genes, preserving the potency of antibiotics and improving human health.
A new study uses neutron analysis to understand the molecular mechanism of an oxygen-generating enzyme that breaks down chlorite, a industrial pollutant found in groundwater and drinking water. The research opens possibilities for future applications in bioremediation and biotechnology.
A new experimental setup allows for serial crystallography using broad-spectrum X-rays at synchrotron sources, enabling the study of proteins with smaller samples and shorter exposure times. This method reduces unwanted scattered radiation, making it possible to determine protein structures with high precision.
A new study from Scripps Research Institute reveals that egg-based production causes the virus to target bird cells, disrupting the major antibody target site on the surface. This mutation renders the flu vaccine less effective in humans, with recent vaccines proving only 33% effective against H3N2 viruses.
Researchers at Osaka University have developed a new method to model the structure of perovskite oxide interfaces using a Bayesian probability-based computer program. This approach provides fast and accurate results, allowing for easier analysis of complex structural data.
Scientists from Boston College and Harvard have successfully created a copper iridate metal oxide that meets the Kitaev model's standards, enabling a chemical entity known as a 'spin liquid' with free-flowing properties. The material's unique honeycomb structure disrupts natural magnetic order, producing geometric frustration.
Researchers at Oak Ridge National Laboratory use neutron crystallography to study the location of hydrogen atoms in aspartate aminotransferase, an enzyme vital to metabolism. This study could lead to new antibiotics and medicines against multidrug-resistant diseases.
The NIH has awarded a $6.5 million grant to Berkeley Lab to integrate existing synchrotron structural biology resources, establishing the ALS-ENABLE center to guide researchers in determining biological structures. The initiative will provide rapid response crystallography, high-quality small-angle X-ray scattering, and specialized cry...
Researchers solved the structure of mouse TRPML1 ion channel using UT Southwestern's cryo-EM facility, a breakthrough that may aid in treating mucolipidosis type IV, a rare neurodegenerative disease. The study utilizes a novel sample preparation technique and cutting-edge software to reveal atomic-level details of the protein.
Researchers used computational drug discovery and in vitro enzyme assays to identify potential therapeutic protein inhibitors for Chagas disease. The study successfully selected four drug-like compounds that interacted with a key amino acid, demonstrating the promise of docking simulation for identifying effective treatments.
Researchers at Osaka University developed a novel chimeric antibody fragment to aid in the structural determination of 'uncrystallizable' target proteins. The Fv-clasp design improved production compatibility and stability while maintaining binding ability, enabling successful crystallization of biologically important proteins.
Researchers discovered how a bacterial protein loosely binds to a mineral, allowing the bacterium to breathe in oxygen-deprived conditions. The study revealed that this protein interacts relatively weakly with the mineral, requiring less binding energy than typical proteins.
A team of researchers at Penn State University has discovered a new pathway for nonstandard RNA transcription using high-resolution crystal structure. This finding provides insights into the mechanism of reiterative transcription, which plays a key role in controlling gene expression.
Korean researchers used protein crystallography to study the three-dimensional structure of proteins regulating neuronal cell connections. They identified MDGA1 protein's role in inhibiting inhibitory synapse formation and verified its control mechanism, providing insights into autism and brain diseases.
Physicists from FAU and DESY have developed a method to improve X-ray image quality, enabling the visualization of individual atoms in molecules at higher resolutions. The new technique uses incoherent radiation and time-resolved snapshots to overcome limitations of conventional coherent imaging methods.
Research provides molecular blueprints for bacterial enzymes, enabling targeted drug development. Key differences between bacterial and human enzymes offer a potential solution to antibiotic resistance.
Researchers at Sanford Burnham Prebys Medical Discovery Institute have published a study on K-80003, an anti-cancer agent that prevents activation of the PI3K pathway, resulting in inhibition of cancer cell growth.
The Rice lab has produced the first full-length structure of a salmon virus protein, shedding light on its role in viral assembly and potentially informing strategies to treat human influenza viruses. The discovery could lead to new antiviral treatments by targeting the protein's interaction with other viral components.
Researchers discovered how Cas1-Cas2 proteins insert viral DNA into CRISPR region by relying on flexible Cas1 protein, IHF binding, and DNA bending, allowing proper storage of 'memories' of prior viral infections. This finding opens doors for modification of the proteins to redirect them to other sequences.
Researchers at Cornell University and Harvard Medical School have observed the bacterial defense mechanism against invaders, revealing how CRISPR sites store molecular memories of invaders. The study provides structural data to improve CRISPR operations' efficiency and accuracy.
Researchers have discovered how Cpf1, a new molecular scissor, can act like a GPS to identify its destination in the genome, enabling precise genome modification and repair. The high precision of Cpf1 will improve the use of this technology in repairing genetic damage and other medical applications.
Research sheds light on how conserved mechanism regulates development and cancer; implications for new cancer therapies. TUTase enzymes interact with let-7, a small RNA molecule important in development and cancer.
Researchers used 3D printing to create optimized milling jars for X-ray powder diffraction experiments. The new design improves background and angular resolution, reducing scattering from jar walls and milling balls.
Scientists at the University of Konstanz and Umea University have successfully generated a structural model of the adenylate kinase enzyme in its closed state. This breakthrough allows researchers to analyze the precise moment when the enzyme is biochemically active, shedding light on its biochemical mechanisms.
Scientists used an X-ray free-electron laser to determine the atomic structure of an intact virus particle on a microchip containing thousands of tiny pores. This new method allows for faster and more efficient analysis, reducing sample material waste.
Scientists have discovered that organic crystals send out acoustic signals when their crystal structure changes, providing insight into the phenomenon. The crystals' rapid transformation of heat into movement is potentially useful for developing artificial muscles or microscale robotic arms.
Researchers at Argonne National Laboratory used X-ray crystallography to solve the structure of Lassa virus glycoprotein, a key component in vaccine development. The study provides valuable insights into how the virus enters human cells, paving the way for the design of an effective vaccine.
Researchers at KFU's Structural Biology Lab have made significant breakthroughs in understanding Staphylococcus ribosomes using cryo-electron microscopy. This discovery holds great promise for developing new treatments against deadly infections, such as pneumonia and septicemia.
Materials scientists at Duke University have resurrected an online cookbook of crystalline structures, featuring 288 entries with data on symmetry, properties, and unit cells. The revamped website provides a flexible platform for researchers to explore and create new materials.
Researchers at Fred Hutchinson Cancer Center have identified key mutations that allow HIV to escape a broadly neutralizing antibody. The study's findings could inform the development of more effective vaccines against this notoriously difficult-to-target virus.
A team led by Kathryn Hastie and Erica Ollmann Saphire at The Scripps Research Institute has solved the structure of Lassa virus's surface glycoprotein, a key step in developing a vaccine. The breakthrough provides a blueprint to design a Lassa virus vaccine, which could help combat the deadly arenavirus family.
Researchers at Umeå University have successfully mapped the structure and function of a transient enzyme state using X-ray crystallography and NMR spectroscopy. The study reveals that the transient state is essential for enzyme function and provides clues on how enzymes speed up reactions with incredible specificity and efficacy.
A Los Alamos research team used neutron crystallography to determine the three-dimensional structure of a protein that breaks down cellulose, a key step in creating biofuels. The findings suggest that understanding the mechanism of this enzyme could lead to more efficient and cost-effective production of ethanol.
Researchers at University of Illinois create first significant examples of optical crystallography for nanomaterials, improving precision of nanocrystal engineering and understanding of reactions. The new technique uses absorption spectroscopy to identify crystal type in liquid-dispersed nanomaterials, offering simple, accurate analysis.
Researchers discovered iodide phasing is universally applicable to membrane protein structure determination, enabling a molecular-level understanding of biomolecules. This breakthrough accelerates computer-aided drug development and makes it cheaper.
Scientists at Diamond Light Source developed a new Pan-DDAA method to extract clear detail from X-ray diffraction data. The approach identifies noise sources and removes them, exploiting the ability of Diamond's beamline to repeat measurements quickly.
Researchers studied halogen-bonding interactions in co-crystals with bromide ions, leading to honeycomb structures and variable geometry. The findings suggest potential gas storage applications and facilitate directional multidentate interactions.
Scientists have gained insight into the NS5 protein of Zika virus, a crucial enzyme involved in viral replication. The study reveals its structure and function, as well as comparisons with other related viruses, which will aid in the search for compounds to halt virus reproduction.
Rutgers scientists determine the structure of tuberculosis drug target Mtb RNA polymerase and discover a new class of compounds, Na-aroyl-N-aryl-phenylalanamides (AAPs), that potently inhibit it. The findings reveal potential for developing improved anti-tuberculosis drugs.
The University of Utah will receive a cryo-electron microscope, enabling precise imaging of life's building blocks at an atom-by-atom scale. The instrument will help researchers study protein complexes and understand biological processes.
Researchers have made a breakthrough in understanding the production of bilirubin, a substance responsible for yellowing of the skin in jaundiced patients. By studying the biliverdin reductase enzyme, they discovered that two molecules of biliverdin are used to produce bilirubin.
Berkeley Lab researchers develop first 3-D atomic-scale model of P22 virus that identifies critical protein interactions crucial for its stability. The successful rendering allows peeking inside the virus' protein coats at resolution.
CuanTec develops durable, antimicrobial, and biodegradable food packaging for seafood using a biopolymer from shellfish. The company aims to reduce £60 million annual losses in the seafood sector by converting waste into valuable products.
Researchers at Tokyo Institute of Technology have discovered how gold nanoparticles form within protein nanocages, revealing a key process in biomineralization. The study reveals the role of sulfur-containing residues in enhancing Au uptake and agglomeration into nanoclusters.
Scientists developed a novel double flow-focusing nozzle to reduce protein crystal consumption in X-ray crystallography. The new device enables stable experimental conditions, increases the rate of high-quality diffraction patterns, and widens the spectrum of biomolecules that can be analysed.
Researchers have developed a mathematical foundation to explain the role of small molecules in promoting proper protein folding. This understanding has important implications for developing future therapies based on pharmacological chaperones to treat misfolding diseases.
A study published in PNAS reveals details about Apoptosis signal-regulating kinase 1 (ASK1), a signaling protein controlling cellular behavior. The research found unexpected parts of ASK1's structure that help control its activity, shedding new light on disease processes such as Parkinson's and melanoma.
Researchers found that viruses stimulate the assembly of light-harvesting complexes in host bacteria, allowing for efficient photosynthesis and energy production. This mechanism provides a selective advantage to the virus, enabling it to replicate quickly.
A new facility at Diamond Light Source allows for long-term experiments (weeks to years) in parallel, detecting phase evolution and structural changes. This addresses the need for studying slow processes like material hydration and metal-organic framework stability.
Researchers used high-intensity X-ray pulses to determine the structure of a viral cocoon down to a scale of 0.2 nanometres, approaching atom-scale resolution. The tiny viruses with their crystal casing are by far the smallest protein crystals ever analyzed using X-ray crystallography.
University of Toronto scientists have discovered a better way to extract proteins from membranes, making it easier to study cell communication and human health/disease. Using a type of polymer, they stabilized proteins while keeping fatty molecules attached.