A team of scientists at UVA has obtained the crystal structure of a key Ebola virus protein, revealing a novel tertiary fold that could lead to insights into viral assembly and antiviral drug design. The study's results may provide a potential target for the development of new treatments for Ebola hemorrhagic fever.
Researchers have developed a new method to measure structurally modified proteins in complex biological samples, enabling the analysis of thousands of proteins. The method uses a combination of digestion enzymes and Selected Reaction Monitoring to quantify protein quantities and determine structural changes.
The team determined the high-resolution structure of Dbr1 enzyme, which breaks loops of ribonucleic acids and could be a new target for treating most cases of ALS. By inhibiting this enzyme's activity, researchers hope to prevent TDP-43 aggregates from forming in motor neurons.
Scientists have unraveled a molecular mechanism of mRNA recognition, essential for understanding differential gene regulation in male and female organisms. This principle represents an essential and widespread mechanism of gene regulation in higher organisms.
Scientists identified a compound that effectively inhibits an enzyme crucial to Middle East respiratory syndrome (MERS) and severe acute respiratory syndrome (SARS) viruses. The compound has a different mode of action for each virus due to slight differences in the enzyme.
Researchers at the University of Adelaide have made significant advances in crystallography, allowing them to study chemical reactions in their native state. The new technique uses a metal-organic framework to bind reactants and enables the examination of reaction products without isolating or growing crystals.
Scientists have obtained an atomic-level picture of the intact NMDA receptor, a massive multi-subunit complex that integrates chemical and electrical signals in the brain. The structure reveals how the receptor is regulated and offers new insight into its function, which is tightly controlled and associated with neurological diseases.
Scientists at Berkeley Lab and SLAC used a 'photon science speedway' to collect and analyze 114 terabytes of data on photosynthesis in just five days. The work led to new insights into how nature splits water molecules during photosynthesis, a key step towards developing artificial solar energy.
X-ray crystallography has revolutionized our understanding of molecular structures and their influence on various scientific fields. The technique's future holds intriguing possibilities, including potential transformations beyond its current form.
Scientists have identified key regions of the Cwp84 enzyme that could be targeted by drugs to prevent Clostridium difficile colonization and toxin production. The research may lead to the development of a new type of anti-colonization inhibitor to treat C. difficile infection.
The research reveals the viral capsid structure, showing similarities to other viruses, and identifies potential binding sites for modification. The findings may lead to new information on host-virus interactions and the development of custom-made viruses to target parasitic or pathogenic worms.
Researchers have better understood how bacteria can protect itself from harm, using X-ray crystallography to visualize the molecular machinery known as Cascade. The unique ladder-like structure allows RNA to scan DNA more efficiently than a double-helix structure, enabling faster recognition and destruction of viral invaders.
Researchers have solved a longstanding puzzle in neuroscience by revealing the three-dimensional atomic structure of netrin-1, a guidance protein that can attract or repel brain cells. By understanding how this protein works, scientists may be able to develop new ways to steer cell behavior and potentially treat diseases such as cancer.
Scientists at Montana State University have developed a detailed blueprint of a bacterial surveillance complex that detects and destroys viruses. The discovery could lead to new innovations in medicine, biotechnology, and agriculture, as CRISPR-associated machines are being repurposed for precision DNA editing.
Researchers at Saint Louis University have trapped the part of a virus responsible for inserting its DNA into human cells, a crucial step in understanding how HIV infects people. By capturing integrase with x-ray crystallography, scientists aim to develop new treatments and better understand how existing drugs work.
Researchers have found an irreversible inhibitor, SML-8-73-1, that selectively and irreversibly interferes with the activity of mutated KRAS genes. This breakthrough has significant potential to target cancer cells and improve treatment outcomes for patients with lung, pancreas, and colon cancers.
Researchers at Saint Louis University discovered that deleting disordered sections of a protein's structure reveals the molecular mechanism of blood clotting. By crystallizing prothrombin, they found that the deleted version is activated to thrombin faster and provides key information on the mechanism of prothrombin activation.
A team of scientists has revealed the molecular mechanisms underlying Roquin's role in preventing autoimmune diseases. The study found that Roquin recognizes a range of RNA binding partners to control T-cell functions, regulating a larger number of genes than previously thought.
Scientists successfully visualize crucial event in photosynthetic reaction, enabling study of protein complex that splits water. This breakthrough uses free-electron laser technique to collect data at room temperature.
An international team of researchers has solved a long-standing debate over the molecular structure of a vital biological chemical, identifying that the ferryl heme in Compound I is not protonated. However, one amino acid side chain is found to be doubly protonated, raising new questions about oxygen activation mechanisms.
Scientists solved the long-standing question of whether ferryl heme in Compound I involves just an oxygen atom or a hydroxyl group, with implications for drug development. The study used neutron crystallography to determine the structure of Compound I at cryogenic temperatures.
Researchers captured the first molecular-level images of photosynthesis, revealing how water is split into oxygen and hydrogen. The breakthrough could lead to the development of artificial systems that mimic and surpass the efficiency of natural photosynthesis.
Scientists at Berkeley Lab and SLAC have taken detailed snapshots of the four photon-step cycle of photosynthetic water oxidation in photosystem II. The study provides information that should be useful for designing artificial solar-energy based devices to split water, a crucial step towards clean energy.
A group of scientists have revealed the structure of two proteins involved in liver and colon cancers, opening up research opportunities for drugs that can inhibit cancer cell growth. By blocking a specific region of these proteins, it is possible to prevent tumour cell reproduction without affecting other life-sustaining functions.
Alicia Boole Stott and Ludwig Schlaefli showed that six platonic solids have four-dimensional counterparts, featuring strange symmetries. The spinorial construction explains these symmetries, shedding new light on both three- and four-dimensional geometries.
Researchers develop a crowdsourcing game to tackle the phase problem, achieving successful results in low-resolution phasing puzzles. The approach leverages human pattern recognition capabilities to guide the search process.
Researchers used X-ray crystallography to study how tubulin acetyltransferase (TAT) interacts with microtubules, revealing that TAT only labels stable microtubules. This discovery may help cells distinguish between stable and unstable microtubules, influencing nerve cell health and behavior.
Researchers at the University of Colorado School of Medicine have solved a biochemical mystery surrounding viral RNA molecules. The study reveals how these molecules mimic cellular RNAs as part of their strategy to infect cells and multiply, offering insights into potential treatments or vaccines against infectious diseases.
Researchers from the University of Freiburg have made significant progress in understanding how the antimalarial drug atovaquone works. By analyzing its molecular structure, they have identified key binding sites and revealed the underlying mechanism of resistance to mutations. This breakthrough could lead to the development of more ef...
The study's findings highlight the importance of API hydration in determining physical properties, such as stability and solubility. The research provides valuable insights into the mechanistic relationships between dehydration stages and lattice structure changes.
Scientists have developed a method to study protein crystals inside cells using X-ray analysis, bypassing complex sample preparation. This breakthrough enables the analysis of micron-scale in vivo samples with improved signal-to-noise ratio.
The UK has invested £5.64M in the European X-ray Free Electron Lasers (XFEL) project, allowing UK researchers to use serial femtosecond crystallography for high-resolution biological molecule determination. This cutting-edge technology will enable scientists to study the smallest building blocks of life at unprecedented speeds and reso...
Researchers at Cold Spring Harbor Laboratory have obtained an unprecedented view of a type of brain-cell receptor implicated in neurological illnesses. The team's atomic-level picture of the intact NMDA receptor should serve as a template and guide for the design of therapeutic compounds.
Researchers have resolved the crystal structure of sulfamidase, a key enzyme in Sanfilippo A syndrome. The discovery provides insights into the molecular consequences of genetic mutations and will aid in developing novel therapeutic molecules to manage the devastating disease.
University of Missouri researchers have completed a 3D map of the Proline utilization A (PutA) enzyme, which facilitates metabolism by adding oxygen to molecules. This understanding will help drug manufacturers create more effective treatments for diseases like h. pylori infection.
Researchers identified a mutated enzyme called LovD9 that produces simvastatin 1,000 times more efficiently than the natural enzyme. The team used computer simulations and X-ray crystallography to determine the molecular structures of both enzymes, revealing subtle variations in their behavior when immersed in water.
The Protein Data Bank has surpassed 100,000 entries, providing a wealth of structural data for researchers to understand biological mechanisms and discover new medicines. The archive's growth is driven by the efforts of structural biologists worldwide, who continue to deposit new structures and improve the resource.
Rotational X-ray tracking (RXT) measures slow dynamics in disordered systems, overcoming limitations of previous techniques. The new method reveals unique rotational motion and nanoscale elastic properties of gel networks.
Scientists at the University of York studied how Staphylococcus aureus attaches to human blood proteins fibronectin and fibrinogen. The research reveals how binding of these proteins cooperates to cause life-threatening infections, including infective endocarditis.
Scientists at Harvard University have created a magnetic resonance imaging (MRI) system that can produce nano-scale images, potentially allowing researchers to peer into the atomic structure of individual molecules. The system uses a miniaturized magnet and quantum computing technology to achieve high spatial resolution.
New research reveals a fresh understanding of the structure of sodium channels, with particular focus on the β3-subunit's role in regulating heart cell activity. The study suggests that these channels may be functionally connected, leading to more efficient action potential initiation.
Researchers have developed a novel method to help doctors diagnose and treat kidney stones more effectively. By analyzing the behavior of nanocrystals and crystallites under different chemical conditions, they found that certain methods can reduce stone size and change its shape, improving treatment outcomes.
Researchers developed new mathematical tools to understand virus symmetry, revealing insights into viral genome and protein capsid interaction. This work also applies to carbon onions, providing a basis for nanotechnology applications.
Scientists have discovered the atomic-scale mechanism of action for NpmA, an enzyme that imparts chemical changes to bacterial ribosomes, making them resistant to aminoglycoside antibiotics. This finding poses a significant threat to public health, but also reveals potential targets for developing new drugs.
Researchers at Saint Mary's University and the University of Jyväskylä have isolated cyanoformate, an ion that can deactivate cyanide's toxic capabilities, using crystallography and computational chemistry. This discovery highlights the importance of applied chemistry in understanding carbon-capture processes.
Researchers in France have developed a new technique for studying solar panel absorber materials, which could lead to non-toxic and readily available alternatives. The technique involves resonant diffraction of single crystals, allowing for the creation of high-quality material samples.
Researchers in China have developed a convenient way to selectively prepare germanium sulfide nanostructures, including nanosheets and nanowires. These nanostructures show outstanding photoresponsive behavior, indicating their potential use in solar energy conversion systems and optoelectronics.
Dr. Ira Kurtz's research aims to understand the molecular processes affecting kidney function, with a focus on designing specific drugs targeting disease-causing proteins. The goal is to reduce side effects and costs associated with current treatments, which affect millions of people worldwide.
The NIH has awarded a five-year grant of up to $28 million to establish a center for excellence in finding an antibody cocktail to fight the deadly Ebola virus. Researchers from 15 institutions, led by Erica Ollmann Saphire at Scripps Research Institute, will collaborate on definitive experiments.
Biophysicists at Rice University developed a computational technique that combines genetic and structural data to analyze complex molecular machines. The technique, called DCA, reveals previously unknown details about protein transitions between functional states.
Researchers at Karolinska Institutet have successfully produced a molecule that blocks LTA4 hydrolase from producing LTB4, while maintaining the inactivation of Pro-Gly-Pro. This could lead to new hopes for treating chronic obstructive pulmonary disease (COPD) and various types of inflammatory skin diseases.
Researchers have identified specific behavior of PP1 by analyzing binding motifs with regulatory proteins. This discovery allows them to predict interactions with a significant number of proteins without resolving their structure.
Tc toxin complexes, used by bacteria like Yersinia pestis and Photorhabdus luminescens, have been imaged with atomic detail. The complexes use an elastic band-like protein chain to penetrate cell membranes, depositing toxic enzymes. This mechanism has potential applications in medicine, including selectively targeting cancer cells.
Researchers studying cow antibodies have gained insights into the diversity of human antibodies, which is crucial for recognizing and neutralizing pathogens. The unique structure of these cow antibodies may also be useful for antibody-based therapies or diagnostics.
The Vanderbilt team has deciphered the 3-D structure of a key MRSA protein, FosB, which inactivates an antibiotic called fosfomycin. This discovery may enable the design of inhibitors that can improve the effectiveness of fosfomycin and combat MRSA infections.
Researchers have successfully imaged a single layer of proteins using exceptionally bright and fast X-rays, significantly broadening the number and type of proteins that can be studied. This new method, based on XFEL technology, opens up possibilities for understanding protein structures and their role in disease and toxicity.
Researchers used computer simulation to analyze X-ray crystallographic data and found that current software programs underestimate the level of dynamics in proteins. This could lead to more accurate pictures of protein structures and improved development of medicines.
Berkeley researchers provide detailed picture of Cas9's three-dimensional shape, showing radical change in structure upon binding to guide RNA. This breakthrough enables rational design of new and improved versions of Cas9 enzymes for basic research and genetic engineering.
A team of scientists has discovered the structure of the NS1 protein, which helps dengue and West Nile viruses replicate and evade the immune system. The researchers believe this breakthrough could lead to the development of a vaccine that protects people without increasing their risk.
Researchers have determined the complex structure of a key cell membrane protein involved in sterol metabolism and resistance in a yeast model. The study's findings provide new insights into mechanisms underlying fungal resistance to triazole drugs, which can help develop new broad-spectrum drugs with minimal side effects.