Articles tagged with Membrane Proteins
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Researchers at UVA Health System develop novel approach to create less resistant and more effective antibiotics by targeting integral membrane enzyme DsbB. The breakthrough uses nuclear magnetic resonance spectroscopy to understand protein structure and function.
Researchers at the University of Cambridge and Bristol have successfully maintained membrane complexes intact in a mass spectrometer, enabling the study of previously unexplored interactions. This breakthrough discovery has significant implications for understanding cellular security and drug resistance.
Researchers developed MAPAS to predict protein contact surfaces, which can guide new treatments for devastating diseases. The tool uses supercomputers to analyze protein shapes and energy, revealing key details of membrane interactions.
Scientists at the University of Illinois have created novel biomimetic membranes that can efficiently transport water, making them ideal for desalination and wastewater purification. The membranes' high permeability and selectivity could also be useful for drug delivery applications.
Researchers have determined the first known structure of a human G protein-coupled receptor (GPCR), specifically the beta2-adrenergic receptor. This breakthrough promises to speed the discovery of new and improved drugs, as well as broaden our understanding of human health and disease.
The University of Leeds is partnering with Dr Tony Marchington's M2 Ventures to offer outsourced research and development in membrane biology to industries. Membrane biology research plays a crucial role in developing pharmaceutical drugs, and the partnership aims to capitalize on this expertise.
Researchers used solid-state NMR spectroscopy to create high-resolution images of cytochrome b5 in its membrane environment, revealing its helical shape and interaction with cytochrome P450. This breakthrough sheds light on the complex dynamics between these two proteins.
Researchers in Molecular & Cellular Proteomics have identified key proteins involved in schistosomiasis, a tropical disease affecting up to 200 million people. The study also reveals the structural proteome of a lethal shrimp viral disease and unique proteins allowing algae to thrive in salty environments.
Researchers have identified common attributes in viral replication machinery that could be vulnerable to disruption, potentially leading to broad-spectrum antiviral agents. A study on flock house virus reveals a new compartment for RNA synthesis, where the virus can collect components and carry out processes efficiently.
Researchers at the European Synchrotron Radiation Facility (ESRF) solved the 3D structure of LTC4 synthase, a protein targeted for asthma treatments. The breakthrough allows for the development of new and more effective medications against airway inflammation.
Researchers at Karolinska Institutet have elucidated the crystal structure of LTC4 synthase, a major influence on asthma development. The study enables the development of new therapeutics by tailoring molecules to block the enzyme's active sites.
A team of scientists has developed a new method to analyze the development of cortical polarity in cell membranes, which is essential for various cellular processes. They combined experiments with living cells and a mathematical model, showing that polarized regions are defined with near-optimal precision.
Researchers at Max Planck Institute successfully integrated in-vitro synthesized membrane proteins into artificial lipid membranes, overcoming previous difficulties due to protein solubility. This breakthrough enables the creation of biosensors that can detect poisons, explosives, or drugs.
Researchers mapped zebrafish axonal projections to reveal dual receptor expression and epigenetic programming. The study also explores the interaction of 'liking' and 'wanting' responses associated with compulsive behaviors, and investigates the role of ADAM10 in APP processing.
A novel method developed by Illinois researchers allows for the visualization of individual membrane fusion events, revealing unprecedented details about this fundamental life phenomenon. The technique, based on fluorescence resonance energy transfer (FRET), enables the study of SNARE-mediated membrane fusion at a single-vesicle level.
Researchers at the University of Illinois Chicago have discovered that spectrin can perform both structural and adhesive functions in cells, contradicting previous assumptions about its role. This finding has implications for understanding genetic diseases such as anemia and muscular dystrophy.
Researchers at IRB Barcelona have identified a crucial protein in building the nuclear envelope, a complex structure surrounding the nucleus. The discovery of MEL-28 sheds light on how this envelope is assembled and regulated.
Researchers discovered that bacteria employ a bungee-like structure called fimbriae with an adhesive protein at their tip to cling to mucous membranes. The mechanical properties of these structures allow them to grip even more tightly under force, helping bacteria persist in the human body.
The signal recognition particle (SRP) complex plays a crucial role in sorting secretory and membrane proteins, determining their final destination within or outside the cell. By understanding its structure, researchers can uncover key events during protein sorting, essential for expressing these proteins correctly.
Researchers solved the structure of a viral harpoon protein, revealing its role in viral entry and fusion with host cells. The discovery sheds light on how viruses hijack cellular machinery to produce and spread more virus, and may lead to new treatments for infections caused by enveloped RNA viruses.
Scientists have discovered that Streptococcus mutans, a decay-causing organism, can survive without the SRP pathway. The bacteria altered to lack SRP components were able to adapt and survive gradual increases in acid resulting from their own metabolism.
Researchers at the University of Kentucky developed carbon nanotube membranes that allow for fast transit approaching the speed of biological channels. The membranes' scalable fabrication enables industrially useful chemical separations.
Researchers at UCLA and NIH have discovered a new compound that can block viruses from entering cells, providing potential relief for conditions like HIV, herpes, and the flu. The compound also shows promise in combating antibiotic-resistant bacteria.
The Protein Structure Initiative (PSI) has reached its rapid production phase, aiming to determine thousands of protein structures using innovative approaches and tools. The new centers will use methods developed during the pilot period to rapidly generate protein structures found in organisms ranging from bacteria to humans.
Researchers at the University of Illinois discovered that macromolecules on the surface can modify the mobility of underlying lipids in phospholipid bilayers. The adsorption of larger polymers slows down lipid movement, while smaller ones have a minimal effect.
Researchers found that a novel form of restricted complement activation occurs on viable sperm upon exposure to follicular fluid, aiding in the fusion process between sperm and egg. This targeted activation may have implications for other cell-cell interactions.
The ASBMB-Avanti award recognizes Dr. Dowhan's work on lipid-protein interactions, which has expanded our understanding of lipids' roles in cellular processes. His research has established the molecular basis for new lipid functions and impacts a wide range of investigators.
Researchers discovered mitochondria can fuse without additional proteins, revealing new insights into the aging process and potential treatments for age-related diseases. This understanding is crucial for developing new therapies for optic atrophy, Charcot-Marie-Tooth disease, and neurodegenerative disorders.
Researchers found a novel rhodopsin protein in bacteria that can distinguish between blue and orange light, enabling more efficient harvesting of light for photosynthesis. This discovery sheds light on the role of cell membranes in biological functions and has potential applications in nano-machinery as a color-sensor.
Researchers at UT Southwestern Medical Center have refined the description of a bacterial protein that regulates salt and solute flow. By understanding how this protein functions, scientists may be able to design new antimicrobial agents by manipulating its gating mechanism.
Researchers discovered a protein, TgGAP50, that anchors myosin in the parasite's membrane, crucial for motility. This understanding may lead to new ways to interfere with parasite control mechanisms, potentially treating malaria.
Researchers at U.Va. Health System devise method to extract membrane proteins by using chemicals that allow them to be reversibly folded and refolded. This allows for structural and functional studies of the proteins using crystallography or nuclear magnetic resonance imaging.
Researchers determined the structure and behavior of a protein receptor complex in E. coli, revealing a 'two-receptor approach' to bring substances into the cell's cytoplasm. This discovery could provide insights into cellular metabolism and how proteins are transported across membranes.
A team of Purdue biologists has determined the structure of the cytochrome protein complex, critical for photosynthesis in a blue-green bacterium. The study reveals the entire mechanism of photosynthesis and its energy flow, shedding light on animal metabolism.
Researchers develop technique to visualize individual vesicles after release, discovering three modes of recycling: kiss-and-run, compensatory and stranded. The study reveals the rate of synaptic vesicle recycling determines information transmission in nerve cells.
Researchers observe temporary structure during membrane fusion, forming hourglass-shaped stalk connecting two membranes. This discovery may lead to understanding of viral infection and designing new drug delivery methods.
A new technique uses ESR to measure distances between atoms in proteins, revealing the overall structure of a molecule. This method is particularly useful for studying larger protein assemblies and membrane-embedded proteins, which are challenging to study using traditional methods.
Researchers visualized the enzyme formate dehydrogenase-N to a resolution of 1.6 angstroms, providing valuable insight into nitrate respiration and the molecular machinery of life. The discovery supports Peter Mitchell's 'chemiosmotic' theory, which describes how cells convert energy into usable form.
The center will provide cutting-edge instrumentation and theoretical expertise to researchers worldwide, focusing on biochemistry and molecular biology. Researchers will utilize state-of-the-art ESR spectrometers to study dynamic molecular processes and develop new methods for measuring distances in biomolecules.