HIV-1 virus uses ATP to remove AZT, a widely used AIDS treatment, allowing it to replicate itself. This discovery helps researchers understand why anti-AIDS treatments can fail, enabling the development of more effective treatments for HIV patients.
McGill researchers discovered how cells identify and recycle proteins by capturing an image of the UBR box component. This finding holds promise for understanding and treating Johanson-Blizzard syndrome, a rare disease causing deformations and mental retardation.
Researchers have identified Csy4 as the enzyme responsible for producing CRISPR-derived RNAs, which target and silence invading viruses and plasmids. The discovery sheds light on how microbes use CRISPR to acquire immunity from future invasions.
Researchers at Scripps Research Institute have discovered the underlying mechanisms that activate gamma delta T cells in the skin and other organs. These cells play a unique role in recognizing damage or disease in epithelial tissues, and their activation is crucial for wound healing.
Biophysicists at Ruhr-University Bochum discovered a proton diode in proteins that allows protons to pass through cell membranes in one direction. Water molecules play a crucial role in this process, supporting the hypothesis that protein-bound water molecules are essential for protein function.
Researchers at Scripps Research Institute have determined the atomic structure of a human adenovirus, leading to insights into its assembly and potential applications in gene therapy. The largest complex ever solved at atomic resolution, this discovery may lead to more effective treatments for diseases such as cystic fibrosis and cancer.
Researchers at Penn State University have created the first image of a protein interacting with DNA packed tightly into space-saving bundles. The discovery is expected to aid future investigations into diseases such as cancer and provide new insights into how cells regulate gene expression.
The study aims to understand how enzymes activate molecular oxygen and attach it to substrate molecules to synthesize siderophores, essential for the microbes' metabolic needs. The researchers will use protein crystallography training to train global scientists and students.
A new experimental antibiotic has been shown to be effective against bacteria that are resistant to existing treatments. The compound works by targeting a specific enzyme in the bacteria's internal machinery, preventing it from reproducing.
A team of scientists has provided the first atomic-level glimpse of the proton-driven motor from ATP synthases, enzymes central to cellular energy conversion. The study revealed a water molecule in the critical rotor element of a bacterial nano-motor that shares common features with human mitochondria and bacteria.
A BU team led by Prof. Adrian Whitty aims to create 'drug-like' small molecule inhibitors targeting challenging protein-protein interactions with a $1.6M NIH grant. The goal is to develop new approaches for discovering inhibitors against intracellular proteins critical to human inflammatory diseases and cancers.
Scientists at Tufts University and the University of Pennsylvania have determined the unusual structure of a key member of the herpes virus protein complex that allows it to invade cells. The research provides a new target for antiviral drugs, which could prevent the virus's access to cells.
The study reveals how HIV protein Tat interacts with the human protein P-TEFb, altering its shape. This knowledge may lead to the design of inhibitors that target P-TEFb only when it is interacting with Tat, potentially reducing viral replication without harming normal cell function.
Researchers use X-ray diffraction microscope to image the 3D internal structure of yeast spores and cells. The technique overcomes limitations of previous methods, enabling quantitative 3D imaging of whole biological specimens at nanometer-scale resolutions.
Researchers have deciphered the molecular structure of phytochrome, a key 'light switch' in plant growth. The study reveals a twisted area of contact between two units, suggesting that light adjusts its strength and orientation to transmit signals.
A team of researchers has resolved the structural, electronic, and optical properties of a chiral gold nanocluster after ten years of mystery. The cluster, composed of 38 gold atoms and 24 organothiolate molecules, exhibits unique chiral properties that influence its response to circularly polarized light.
The National Institute of General Medical Sciences has granted $1.18 million to the University of Missouri to improve their protein prediction software, MULTICOM. The system can help scientists design drugs by predicting protein structures in diseases.
Researchers discovered a specific mutation that promotes fibril development, leading to organ damage and death. The study suggests this finding could be a target for future drug development in treating the fatal condition.
Researchers design compound that effectively blocks BCL6's cancer-causing actions, killing off cancer cells with minimal toxicity. The discovery opens possibilities for treating other tumor types and improving survival rates for patients with non-Hodgkin's lymphoma.
Researchers from Ontario Cancer Institute and US scientists have discovered a compound that blocks protein BCL6, a cancer-causing culprit in about half of all non-Hodgkins lymphoma cases. This breakthrough accelerates developing targeted drugs to fight the most common form of non-Hodgkins lymphoma.
Researchers at IRB Barcelona have developed a new method to study intrinsically disordered proteins, crucial for designing drugs against Alzheimer's disease and prostate cancer. The approach uses computational predictions and laboratory experiments to obtain structural information about dynamic proteins.
Researchers at the University of Minnesota have created a molecular image of a system that moves electrons between proteins in cells, offering insights into minimizing energy loss. This breakthrough has implications for improving energy efficiency in nanoscale devices and grid systems.
Researchers at Lawrence Berkeley National Laboratory have made the closest look yet at kinesin protein's structural changes as it ferries molecules within cells. The high-resolution snapshots show kinesin moving up and down like a seesaw, propelled by an energy-giving compound called ATP.
Researchers at Dartmouth College have discovered a protein structure controlling Vibrio cholerae's virulent nature. A fatty acid found within the protein appears to inhibit its function, preventing the bacteria from causing life-threatening diarrhea.
The California Institute of Technology has received a $3.9 million estate gift from Edward and Ruth Hughes, which will be used to fund highly innovative research proposals and eight graduate research fellowships. The gift is supported by a matching grant of $2 million from the Gordon and Betty Moore Matching Program.
Researchers found that lankacidin and lankamycin, two antibiotics produced by streptomyces, are more effective when used together against MRSA and other pathogens. The combination prevents protein assembly and inhibits bacterial growth, offering a new strategy for fighting antibiotic-resistant infections.
Researchers at University of Helsinki and Paul Scherrer Institute determine crystal structure of VEGF-C ligand binding domain with its receptor complex, providing new insights into cancer cell growth and metastasis. The findings support the use of blocking VEGFs as a strategy to inhibit tumor growth.
Researchers at Emerald BioStructures have developed new allosteric small molecule modulators of phosphodiesterase-4 (PDE4) with improved safety and efficacy. These discoveries validate the company's structure-based drug design capabilities for addressing previously undruggable targets in inflammatory diseases and cognitive impairments.
Researchers at UBC Centre for Molecular Medicine and Therapeutics report detailed structure and function of YEATS domain protein Yaf9, a key player in chromatin regulation. The study reveals conserved function from yeast to humans, shedding light on mechanisms of chromatin modification.
Scripps Research scientists have determined the structure of the Ebola virus's critical protein VP35, which blocks the human immune system. The discovery may lead to new drug therapies and vaccines for Ebola infection.
A Brandeis study directly visualizes protein structures crucial for enzyme catalysis at high-energy states, suggesting new molecular sites for potential drug targets. The research reveals the importance of protein dynamics in enzyme function, offering insights into protein function and potential avenues for targeted drug design.
Researchers are gaining insights into how Gram-negative bacteria infect host cells and spread antibiotic resistance. The crystal structure of the outer membrane part of type IV secretion systems has been revealed, offering potential targets for novel antibiotics.
Researchers have uncovered the critical action shapshot of an enzyme known as the Rho transcription termination factor, a remarkable class of ring-shaped protein motors. The study reveals a rotary engine-like mechanism that enables the motor to selectively terminate transcription at discrete points along the genome.
The studies used molecular dynamics flexible fitting (MDFF) to examine the interaction of the ribosome with EF-Tu and SecY, respectively. The researchers found structural evidence that when the ribosome recognizes the correct tRNA, it induces a change in the shape of EF-Tu, allowing chemical interactions to lead to protein assembly.
Scientists discovered how plant hormone ABA interacts with protein PYR1 to trigger drought response. This interaction enables PP2C molecules to be hijacked, allowing plants to increase water uptake and storage while decreasing water loss. The study offers new approaches for increasing crop tolerance to water shortages.
A $2.2 million NIH grant will enhance the lab's ability to rapidly detect protein clumps in Alzheimer's and other neurodegenerative diseases using a new high-resolution electron microscope. This technology will also enable researchers to study molecular motors in flagella, leading to a better understanding of these diseases.
Researchers at the University of Oregon have found that evolution can only go forward, as genetic mutations block paths to ancestral genes. The team resurrected ancient proteins and manipulated them to study reverse evolution, discovering that restrictive mutations act like an evolutionary ratchet, preventing reversal.
A new structure of the zinc transporter protein has been revealed, showing how it senses and regulates zinc levels in cells. The discovery suggests an auto-regulatory mechanism for zinc transport and may lead to the development of treatments for diseases like seizure disorders or diabetes.
Researchers at the University of Oregon have successfully demonstrated that specially synthesized boron compounds can be accepted by biologically active enzymes. This breakthrough could lead to new drug design strategies and boost boron's expanding use in medicine.
The Case Center for Synchrotron Biosciences will provide three Technology Cores to support the study of proteins and nucleic acids. The center's facilities will enable researchers to understand the structure and function of proteins, including in vivo studies, as well as investigate the role of metal atoms in proteins.
Scientists at Scripps Research Institute have discovered that two separate functions—alanine adding and editing—were joined together in a single enzyme during early evolution. The findings show that the C-Ala domain enhances collaboration between the aminoacylation and editing domains, making them work together synergistically.
Researchers have gained in-depth knowledge of pyruvate carboxylase's structure, a metabolic enzyme linked to genetic diseases like lactic acidaemia and hypoglycaemia. The study also sheds light on its potential role in obesity and diabetes treatments.
The study reveals the atomic structure of the hepatitis E protein shell, which could lead to new ways to stop the virus. Researchers have identified potential sites on the model for designing drugs that can interrupt the binding process and prevent the virus from attaching to cell receptors.
Researchers at Vanderbilt University Medical Center used NMR methods to determine the structure of diacylglycerol kinase (DAGK), a large bacterial protein that resides within the cell membrane. The study suggests that similar methods can be applied to other membrane proteins, including G protein-coupled receptors, which are targets for...
Scientists at the University of Gothenburg have discovered a 'water gate' in yeast cells that regulates water flow, which may lead to new cancer drugs. The discovery has potential applications in human cancer research and could result in inhibitors for human aquaporins.
Researchers have gained insight into the regulation of aquaporins in yeast cells, revealing a previously mysterious region that acts as a gate controlling water flow. This discovery may lead to the development of inhibitors for human aquaporins, which could slow down cancer tumor growth.
Researchers discovered the chlorophyll molecules' structure, enabling artificial photosynthetic systems. The chlorosomes contain up to 250,000 chlorophylls and have unique internal structures.
Researchers from Durham University have successfully mapped the high-resolution structure of the matrix protein, a critical component of enveloped viruses like RSV. This breakthrough could lead to the development of new biochemical tools to treat respiratory ailments and other viral infections.
A groundbreaking study at Brandeis University has shed light on a crucial step in the complex process of genetic encoding for the first time. The researchers report that they were able to crystallize a large complex of a macromolecular machine in the human cell and determine its structure, zeroing in on the process of RNA splicing.
Researchers at the University of Liverpool have determined the atomic structure of the binding between an antibody and a brain protein that could be key to treating vCJD. The study found that this antibody, ICSM18, has therapeutic potential in preventing brain cell infection and reversing early damage caused by the disease.
Researchers have detailed the molecular structure of Clostridium difficile's protective 'jacket', a surface layer that helps the pathogen colonize human gut cells and cause illness. Understanding this structure could lead to new treatments, including targeted drugs and vaccines, to combat the deadly superbug.
Researchers used Nuclear Magnetic Resonance spectroscopy to analyze the structure of Tau, identifying structural properties and fast motions. This breakthrough provides insights into how phosphorylation alters binding to microtubules, leading to nerve cell damage.
A groundbreaking study reveals how enzymes in the cell cooperate to make fat, providing insights into a potential target for developing new anti-obesity and anti-cancer drugs. The research used state-of-the-art electron microscopy to capture the complex movements of fatty acid synthase, a molecular structure that is extremely flexible.
Researchers identified key elements of dynein's structure and its winch-like mechanism, correcting some mistaken ideas. Dynein is responsible for transporting molecular cargo within cells, powering movement of sperm and eggs, and helping cells divide.
A team of scientists has successfully determined the structure of DFPase, an enzyme from the squid Loligo vulgaris that can rapidly detoxify chemical warfare agents like Sarin. The study used neutron diffraction and provides essential information about the reaction mechanism of DFPase.
Researchers have determined the three-dimensional structure of TIGAR, an enzyme that helps regulate energy production in cells. The discovery may lead to earlier cancer detection or preventative treatments.
Researchers have solved the structure of VP35, a key part of the Ebola protein that interferes with host cell defense mechanisms. This discovery paves the way for designing drugs that can bind to and inhibit VP35 function, potentially neutralizing the Ebola virus.
A team of Dartmouth researchers has found a new function for the protein NOD, which plays a crucial role in chromosome segregation during cell division. This discovery contributes to our understanding of how cell functions can go wrong, particularly in cancerous cells.
The Compact Light Source has achieved three key milestones: first scientific publication, micro-tomographic images, and protein crystallography data set. These results demonstrate its potential to transform biomedical research with high-intensity, tunable x-ray beams.
A computational method predicts bacterial protein interactions with remarkable accuracy, identifying critical residues that bind directly with other proteins. This breakthrough enables the development of new antibiotics targeting specific protein interactions vital to pathogenic bacteria survival.