Researchers discovered novel approach using llama-derived antibodies to control deadly C. difficile infections by targeting the pathogen's toxin proteins. This breakthrough provides opportunities for creating more effective treatments.
Researchers have discovered the molecular structure of NMDA receptor blockers, which could lead to new treatments for depression, schizophrenia, and Alzheimer's diseases. The findings provide valuable insights into how these receptors work and offer hope for developing targeted therapies.
Chromosomes' characteristic shape is explained by self-organizing supramolecular structures formed by stacked layers of chromatin. The symmetry breaking due to different surface energies in telomeres and lateral surfaces justifies the elongated structure.
Researchers discovered how sodium controls opioid receptors, a major class of brain cell receptors. The findings suggest new therapeutic approaches to treat pain and mood disorders. Sodium's effect on receptor activity is crucial for developing better opioid-receptor-targeting drugs.
Wolfgang Peti, a Brown University biochemist, has received a $1.625-million New to Diabetes Research Accelerator Award to tackle type 2 diabetes. He aims to develop medicines that improve on the status quo, potentially making insulin injections unnecessary.
The study pioneers a new approach to forming a 2-D, single-atom sheet of two different materials with a seamless boundary. By rethinking traditional methods, researchers combined graphene and boron nitride into a single layer only one atom thick.
Researchers at Scripps Research Institute have discovered the atomic-level structure of a genetic defect causing myotonic dystrophy type 2, allowing them to design compounds that improve disease-associated defects in treated cells. The study's findings hold promise for treating this rare form of muscular dystrophy.
Researchers have determined the molecular structure of a Tet family member from Naegleria gruberi, providing insights into its role in regulating gene expression and potential therapeutic targets for cancer. The study sheds light on how Tet enzymes interact with DNA, enabling scientists to design drugs that manipulate them.
Researchers have predicted and confirmed the existence of unusual sodium chlorides that break traditional charge balance rules in chemistry. These compounds may have practical applications and could exist in planetary interiors under high pressure.
ASU researchers have successfully imaged G-protein-coupled receptors at room temperature using serial femtosecond crystallography. The new method allows for the study of human proteins without freezing, reducing radiation damage and enabling the observation of molecular dynamics.
Researchers at Stanford and Google have successfully simulated the transformation of a key drug receptor site using Google Exacycle's cloud computing platform. The simulation revealed thousands of possible configurations, providing scientists with a better jumping-off point for computational drug design.
Researchers from Argonne National Laboratory and the University of Washington have identified a method to minimize radiation damage in protein crystals using submicrometer line focusing. This technique enables scientists to collect better data while reducing time and cost associated with repeated experiments.
The Biotechnology and Biological Sciences Research Council (BBSRC) and Medical Research Council (MRC) have jointly awarded £1.43M to support the development of CCP4, a world-leading x-ray crystallography software resource. This funding renewal aims to further scientific knowledge and promote economic growth through innovative approache...
The H7N9 influenza virus is poorly adapted for sustained human-to-human transmission, suggesting a low risk of pandemic. The study's findings indicate that the current form of the virus would need significant mutations to become transmissible between humans.
Rice University researchers have developed a new method to identify previously hidden details about proteins' structures, potentially accelerating novel drug design. By combining structural data and genomic analysis, the team predicted intermediate configurations of proteins that were hard to detect.
DNA polymerase epsilon's unique P-domain enables it to build long DNA strands without falling off, a crucial property for genome reproduction. The study identifies specific mutations linked to colorectal and cervical cancers, offering insights into their development.
Researchers at SLAC's Linac Coherent Light Source (LCLS) X-ray laser used the technique to generate an accurate model of lysozyme, a well-studied enzyme found in egg whites. The study opens the door to new discoveries and explores the potential for LCLS to play a leading role in studying important biomolecules of unknown structure.
Researchers have reconstructed 'missing' global temperatures using a combination of satellite and surface data, revealing that the Arctic is warming rapidly. The new study suggests that the rate of warming since 1997 has been two and a half times greater than previously estimated.
The BioXFEL center will focus on developing new bio-imaging techniques using x-ray lasers to analyze biological molecules. Researchers will use this technique to study drug development, disease occurrence, and the structure of individual viruses.
Researchers have developed a new method to refine low-resolution X-ray crystallography data for biomolecules, combining PHENIX and Rosetta software. The new approach can aggressively optimize models to fit the data while presenting realistic geometry.
Researchers have developed a detailed picture of the HIV envelope trimer, critical for understanding how HIV enters cells and creating potential vaccines. Atomic-resolution imaging revealed the structure of the Env trimer, its assembly, and interaction with broadly neutralizing antibodies.
A recommended nomenclature for 2D carbon materials has been published by the Editorial Board of Journal Carbon, aiming to standardize definitions and promote precise ideas. The new guidelines suggest using 'graphene materials' as an overarching term, including morphological descriptors for shape and size.
Bacteria use TamA protein to channel protein domains across the outer membrane, overcoming additional barrier for nutrient and toxin transport. This process is crucial for infections by pathogens like Yersinia, Salmonella, and Cholera.
Researchers used X-ray crystallography to visualize how brominated flame retardants bind to proteins like estrogens, potentially disrupting the body's natural hormones. The study sheds light on the effects of flame retardants on human health and provides insights for developing safer alternatives.
University of Alberta researchers have made a breakthrough in understanding prion protein interactions, paving the way for designing molecules that can block prion infection. The discovery opens up possibilities for treating human victims and preventing livestock diseases such as BSE.
Researchers at EMBL used super-resolution microscopy to determine the arrangement of Y-shaped molecules in the nuclear pore complex, resolving a decade-old controversy. The study found that the Ys lie in an orderly circle around the opening, with all arms pointing towards the centre.
Researchers at the University of Leicester have made a groundbreaking discovery into the regulation of a key cancer drug target. The study, funded by £2.4 million from the Wellcome Trust, reveals that signalling molecules called inositol phosphates play a crucial role in controlling gene expression.
Researchers at Berkeley Lab have created an atomic-scale structure of a ribosome attached to a molecule that controls its motion, shedding light on how bacterial ribosomes work. This breakthrough could lead to the development of new antibiotics that target the specific weaknesses of bacterial ribosomes.
Researchers at UC Santa Cruz have trapped the ribosome in a key transitional state, allowing them to see how it translates genetic code into proteins without mistakes. Understanding this process is crucial for developing new antibiotics and has significant implications for the origin of life.
Researchers at Brown University used a novel approach to nuclear magnetic resonance spectroscopy to resolve the key interaction between two proteins. The study reveals that the GroEL chaperone is a permissive captor, allowing the smaller protein to bind at two hydrophobic sites and detach, resulting in conformational heterogeneity.
Scientists have determined the precise chemical structure of the HIV capsid using a combination of laboratory techniques and computational simulations. The resulting structure revealed 216 protein hexagons and 12 protein pentagons, which work together to form the cone-shaped capsid.
Researchers develop a new method to model large biomolecules in their native state using X-ray flash data, providing insights into protein structures and dynamic behavior. This technique promises to solve the shapes of more than 80,000 proteins in a static state and offer clues on individual components of mixtures.
A team of researchers is studying the protein structure and reaction dynamics of a key photosynthesis catalyst. They aim to understand the intermediate stages necessary for the oxidation of water, which could help develop sustainable solar energy solutions.
Researchers used a microwave oven to produce a nanocrystal semiconductor for more efficient photovoltaic solar cells and LED lights, biological sensors, and systems to convert waste heat to electricity. The method produces the material quickly and uses less toxic metals than other semiconductors.
Scientists have identified a key gateway to the brain that is affected by alcohol, which could lead to the development of drugs that disrupt this interaction. The breakthrough was made using rare alpine bacteria, and the researchers plan to use mice to study the effects of altering this protein on behavior.
Researchers at Duke University Medical Center discovered a three-dimensional image of beta-arrestin1, a protein that regulates GPCRs, revealing a striking difference in its active and inactive states. This finding suggests the presence of a general molecular mechanism controlling the activation of beta-arrestin1.
Researchers have discovered a target for Schmallenberg virus treatment by identifying the nucleocapsid protein as a key building block that can be blocked to kill the virus. The study, published in Nucleic Acids Research, provides insight into the structure and function of the protein.
A research team developed a new protocol for X-ray single-crystal diffraction analysis that doesn't require crystallisation of the target molecule. This method allows for the analysis of scarce marine natural products and characterises many compounds previously impossible to analyze crystallographically.
Researchers have developed antiviral drugs for other enteroviruses that cause the common cold. The new work obtained a near-atomic-scale resolution three-dimensional structure of enterovirus 71 binding with an inhibitor called WIN 51711. This study provides a structural basis for development of antienterovirus 71 capsid-binding drugs.
Scientists have determined the exact structure of humulones, substances derived from hops in beer, which could be used to develop new pharmaceuticals. The findings overturn previous results and provide insights into the beneficial effects of moderate beer consumption on health.
A research team has described the architecture of human transcription factor TFIID, revealing its inner workings for the first time. The study used a novel approach inspired by viral replication to produce highly abundant and correctly assembled complexes of the core scaffold.
Researchers at SLAC National Accelerator Laboratory have identified a new way to attack Helicobacter pylori, a bacterium that causes ulcers and stomach cancer. By pinpointing the Achilles' heel of this tough bacteria, scientists hope to develop specific and effective treatments.
Researchers at Scripps Research Institute determine the structure of two proteins that form specialized subunits within cells, crucial for maintaining cell health. This discovery has implications for developing new cancer therapies by inhibiting autophagosome formation.
Researchers have discovered how a particular type of carbapenemase enzyme reorients bound antibiotics to destroy their antimicrobial activity. This understanding could lead to the design of new drugs that can resist being broken down by such enzymes, helping combat increasing antibiotic resistance.
The Johns Hopkins team used X-ray crystallography to map the arrangement of atoms in the enzyme that forms unique molecular bonds within the cell wall of Mycobacterium tuberculosis. This structure reveals a distinct pattern of bonds, creating a new target for TB drug development.
Researchers will use x-ray crystallography and NMR to understand the structural rules governing nuclear receptors' activity. The goal is to fill gaps in knowledge about these proteins' role in metabolism, cancer, inflammation, and bone health.
Dr. Gordon E. Brown, Jr. receives the prestigious AGI Ian Campbell Medal for his groundbreaking work on synchrotron technology and its applications in environmental science. His research has focused on addressing societal issues through innovative geochemical reactions and remediation of contaminated sites.
Researchers have published a detailed description of neurotensin's interaction with its receptor, suggesting a novel binding mechanism that may activate G-protein coupled receptors. This knowledge could lead to the development of better drugs for conditions such as Parkinson's disease and schizophrenia.
Researchers at UMass Amherst have identified two small molecule chaperones that can stabilize the defective alpha-NAGAL enzyme, offering hope for developing the first drug treatment for Schindler/Kanzaki disease. These molecules, DGJ and DGJNAc, can increase the amount of functional enzyme in cells.
Researchers describe experiments exploring multi-drug tolerance, a phenomenon that allows bacteria to outwit antibiotics. By analyzing HipA protein's structure and biochemical components, they gained insight into how this mechanism enables bacterial dormancy.
Research reveals that approximately 30-40% of eukaryotic proteomes consist of intrinsically disordered proteins, playing crucial roles in signaling and regulation. These proteins' unique characteristics enable them to interact with multiple molecules, facilitating efficient information exchange through networks.
Andrew Lovering, a renowned structural biologist, has received the ICAAC Young Investigator Award for his seminal research on bacterial cell wall synthesis and modification. His work has significantly advanced our understanding of antibacterial targets and membrane-anchored proteins in bacteria.
At the annual meeting of crystallographers, researchers presented groundbreaking studies on X-ray laser technology, deep-sea bacteria's pressure tolerance, and molecular mechanisms underlying bacterial resistance to antibiotics. The discoveries have significant implications for fields such as medicine, genomics, and material science.
A Japanese research team identified a structural change in a protein that confers pressure-resistant properties on deep-sea bacteria. This finding may help guide the design of enzymes for use in high-pressure chemical industrial processes, exploiting the unique adaptation mechanisms of these organisms.
An international research team has developed a new nanocrystallography technique that captures 3D images of biomolecules in action using the Linac Coherence Light Source X-ray laser. This method allows scientists to study molecules at room temperature without radiation damage, enabling the creation of atomic-scale resolution models.
Berkeley Lab's Laser Ablation Molecular Isotopic Spectrometry (LAMIS) technology enables remote chemical analysis on other planets, while the Compact Variable Collimator (CVC) improves X-ray beam shaping for protein crystallography. The Multinozzle Emitter Array (MEA) accelerates biomedical research by analyzing biomolecules in microfl...
Scientists have discovered a new way to inactivate the disease-causing ability of Helicobacter pylori by disrupting its acid-sensing receptor. The study reveals that urea binding is crucial for the protein's function and could lead to potential treatments.
Saskia B. Neher, a UNC School of Medicine assistant professor, is one of 22 promising scientists to receive the 2012 Pew Scholars award, supporting her research on LPL regulation and its implications for cardiovascular disease.
Researchers create DCA-fold tool to spot subtle interactions between amino acids in proteins, refining methods for predicting protein form and function. The new method uses genomic sequence information to eliminate possibilities from the range of forms a protein might take.
Researchers at two structural genomics centers determined 1,000 protein structures from infectious disease organisms, providing crucial insights into the deadliest diseases. The knowledge gained will aid in developing new interventions and therapeutic agents for drug-resistant strains of TB, MRSA, and other pathogens.