Researchers used X-ray crystallography to determine the structure of COX-2 with arachidonic acid bound, gaining insights into its interaction with inhibitors. The study's findings may help guide future drug development for pain, inflammation, and cancer treatment.
Researchers at the Howard Hughes Medical Institute solved the structure of the reovirus core, a double-stranded RNA virus that bears similarity to pathogens such as rotavirus. The study reveals how the core synthesizes, modifies, and exports viral messenger RNA, ultimately leading to viral replication and takeover of host cells.
A team of scientists at Brookhaven National Laboratory has determined the atomic structure of cytochrome P450cam, an enzyme that performs several important chemical jobs in the body. The research could lead to new cancer therapies, pollution cleanup, and environmentally friendly manufacturing processes.
Scientists have mapped the structure of a protein complex believed to influence cancer cell transformation, enabling potential development of unique cancer-fighting drugs. The Cdc42/GDI complex is a key regulator in both normal and cancerous cells.
Researchers visualize radiation-induced breakage of specific chemical bonds in protein, revealing a highly specific phenomenon. The findings have direct implications for improving data collection using X-ray crystallography and developing pharmacological means to protect against radiation damage.
Researchers have produced the first 3-D structures of poliovirus in the moments after it attaches to and enters a host cell. The structures reveal tiny adjustments in the virus's protein shell that allow it to grab onto its host receptor more tightly.
The medical school will recruit four researchers in structural biology, including Michael Weiss, to study molecular processes leading to disease. The HHMI grant aims to enhance the medical school's research enterprise and develop scientific breakthroughs.
Researchers at Weizmann Institute have discovered the 3-D interaction between galanthamine and brain enzyme acetylcholinesterase (AChE), which breaks down neurotransmitter acetylcholine in Alzheimer's disease. This finding may lead to a new family of drugs with reduced side effects.
The Howard Hughes Medical Institute is investing $8.05 million in new 'superbend' beamlines at the Advanced Light Source, enabling protein crystallography research and advancing understanding of molecular function and interaction.
A team of scientists has unraveled key features of the small ribosomal subunit, including the site where protein biosynthesis begins. The study, which used novel experimental strategies and cryo-crystallography, provides a far-reaching glimpse into the microscopic world of ribosomes.
Researchers at Max-Planck-Gesellschaft have solved the three-dimensional structure of fumarate reductase dimer using X-ray crystallography. The enzyme plays a crucial role in anaerobic bacterial metabolism, and its structure reveals an electron transfer pathway from haem groups to FAD and then to fumarate reduction site.
Seattle researchers have described the structure of factor VIII, a key blood-clotting protein implicated in hemophilia A. The discovery provides a key to developing improved blood-thinning medications and clotting agents for hemophiliacs, as well as better treatments for those at risk of stroke and heart attack.
Researchers at Brookhaven National Laboratory have discovered the molecular mechanism by which adenovirus binds to human cells, paving the way for the development of drugs that block infection. This breakthrough could lead to more effective vaccines and targeted therapies for viral infections.
Researchers at Purdue University will study the three-dimensional structure of several types of viruses, including yellow fever and hepatitis C viruses, using a combination of X-ray crystallography and molecular biology techniques. The goal is to develop drugs that prevent infection by similar viral pathogens.
Harvard researchers have created the first atomic-resolution image of a donut-shaped enzyme that unwinds the DNA double helix for replication. The structure reveals how six individual polypeptide lobes arrange themselves to look like a ring of bread buns, providing new insights into the molecular motor's mechanism.
A team of researchers has identified several chemical compounds that can prevent HIV from fusing with human cells, a crucial step in the viral infection process. By targeting the gp41 protein, these compounds may provide a new avenue for treating HIV and potentially other viruses.
A team of researchers has produced high-resolution images of a complete ribosome complex using the Advanced Light Source (ALS), revealing more about its structure than previous observations. The new crystallographic images provide insights into how transfer RNA interacts with the ribosome and the molecular mechanisms of protein synthesis.
Researchers at Wistar Institute find parallels between PRD1 and human adenovirus coat protein structures, suggesting an evolutionary relationship. The discovery may lead to new research areas and therapies.
The discovery of Complex II's structure is crucial for understanding the energy production system in cells and may lead to therapies correcting defects. This breakthrough increases scientists' knowledge of fundamental processes and their role in diseases like diabetes and Alzheimer's.
Researchers used new techniques to study HDL particles, verifying the lipid bilayer structure and confirming a key finding about protein orientation. The study resolves a long-standing controversy over the structure of HDL, shedding light on its role in cardiovascular health.
The Howard Hughes Medical Institute has awarded $1.32 million to Cold Spring Harbor Laboratory to support advanced courses in molecular biology, neuroscience, and structural biology. The institution will also construct a new teaching laboratory and provide scholarships for scientists worldwide.
The National Science Foundation awards Cornell University $88 million to operate the Cornell Electron Storage Ring (CESR) accelerator for 54 months. The funding enables continued improvement of the facility for high-energy physics and X-ray research in various fields.
Scientists discovered a common viral harpoon protein structure among measles, mumps and respiratory syncytial viruses. This finding suggests that these viruses may be related to HIV, influenza and Ebola viruses, potentially leading to the development of new drugs.
The nuclear pore complex is a highly regulated structure composed of around 50-100 different proteins that control the transport of macromolecules between the nucleus and cytoplasm. Ran protein plays a crucial role in this process, binding selectively to transport factors to regulate cargo molecules across the nuclear pore.
A team of scientists has created a detailed model of the structure of a protein in photosynthetic bacteria, which can help explain how certain diseases such as Alzheimer's and Mad Cow Disease occur. The model shows how nature uses irregular forms to create complex structures that are effective at absorbing sunlight.
Researchers used x-ray crystallography to reveal the structure of HIV reverse transcriptase (RT) enzyme. The active form shows how genetic mutations confer resistance to antiviral drugs like AZT by preventing nucleotide analogs from binding, allowing RT to continue making DNA for the virus.
Researchers at Brandeis University have pinpointed a genetic repressor that can transform diphtheria into a lethal parasite. The discovery could lead to a novel class of antibiotics that prevent bacterial virulence without inducing resistance.
Scientists at Johns Hopkins Medicine solved a major mystery surrounding energy production by determining the molecular structure of adenosine triphosphate synthase (ATP synthase). The discovery explains how cells produce ATP, the common currency of energy, and offers new insights into why people get less energetic with age.
Researchers discover shared structure among 150 enzymes, promoting transfer of acetyl group and affecting antibiotics and neurotransmitters. The discovery provides a potential solution to emerging antibiotic resistance and sheds light on the fundamental structures of proteins.
Researchers have determined the complete crystal structure of cytochrome bc1, a crucial protein complex in the mitochondrial respiratory chain. This breakthrough has provided detailed images of the complex at an unprecedented resolution of 3 angstroms, shedding light on its role in energy production for living cells.
The crystal structure of gp120 in action provides valuable clues for vaccine design, revealing how the virus binds to T cells while maintaining changeability. Researchers can now use this information to create targeted compounds that interfere with the interaction between gp120 and CD4 receptors.
Scientists have discovered a novel form of vancomycin that may be effective against resistant bacteria. The findings suggest a new way for the drug to bind to bacteria, opening an avenue for developing next-generation antibiotics.
Researchers at Yale University are using computer simulations to design more effective pharmaceuticals by optimizing chemical binding to target proteins. This approach has the potential to improve treatment outcomes for diseases such as dementia, diabetes, and spinal cord injuries.
The research reveals the structure of T7 DNA polymerase, a protein crucial for DNA replication, showcasing its high accuracy and speed. The study provides insights into how this enzyme achieves its accuracy and could guide the development of better reagents for DNA sequencing.
Researchers at the University of Illinois used advanced computer modeling to study the purple bacteria Rhodobacter sphaeroides. The team created a three-dimensional model depicting how the light-harvesting complexes aggregate in a ring around the photosynthetic reaction center, shedding light on efficient energy capture. This breakthro...
Scientists created a 3D computer model of a glutamate receptor, which can be used to develop new drugs for Alzheimer's disease and other disorders. The model accurately represents the receptor's structure and behavior.
The Stanford research group synthesized a compound that replicates the chemical wizardry of cytochrome c oxidase, a vital biochemical process found in all oxygen-using organisms. The model converts oxygen molecules into water, releasing energy to charge biological batteries and generate heat.
Professors Fraser Stoddart and David Williams successfully link complex synthetic molecules, enabling the creation of molecular chains with various applications in information storage systems and molecular computing. The achievement represents a significant step towards storing data within molecules smaller than a grain of salt.
Scientists have discovered how p27 blocks cell growth in virtually all human cancers, providing new hope for developing drugs to halt uncontrolled cell division. The discovery uses X-ray crystallography to reveal the molecular structure of p27 and its interaction with cyclin-CDK complexes.
Researchers have discovered a novel 'left-handed' spiral structure in the protein enzyme LpxA, which could lead to the development of new antibiotics that target this unique structure. The discovery offers a promising approach to combating bacterial resistance to current antibiotics.