Articles tagged with Membrane Proteins
Researchers found that as oil chains lengthened, the transformation occurred at lower temperatures. The team used Raman scattering and multivariate curve resolution to analyze water's subtle changes, finding a new structure when interacting with long-chain oils.
Researchers at Johns Hopkins Medicine found that the location of rhomboid proteases within membranes enables them to recognize and cut unstable proteins. This discovery has profound implications for understanding diseases like Alzheimer's and developing treatments.
Researchers explore how membranes influence self-assembly and structure formation in cells, revealing that membranes promote self-assembly and reproduce structures similar to those found in nature.
The European Drug Initiative on Channels and Transporters (EDICT) project has enabled a major step forward in understanding membrane protein structures and functions. Over 30 proteins have been studied, with at least six potential new drug compounds identified.
Researchers at EMBL develop method to follow molecules under light and electron microscope, revealing crucial protein interactions in endocytosis process. They discover actin scaffolding protein forms network pulling membrane inwards.
Recent studies have made significant progress in understanding GPCRs, shedding light on their structure and function. The high-resolution structures of several GPCR receptors, including the A2A adenosine receptor, have been determined, providing valuable insights into how these proteins interact with ligands.
Researchers at Salk Institute create cell-free expression system to synthesize and analyze integral membrane proteins, solving their three-dimensional structures in just 18 months. This breakthrough enables precise biochemical mechanisms understanding and targets the proteins with new drugs.
Michigan State University researchers Merlin Bruening and Greg Baker have invented a high-performance membrane protein purifier that can simplify the process of isolating desired proteins. This innovation has the potential to reduce costs, speed up new drug development, and improve pharmaceutical efficiency.
Researchers found that alpha-synuclein protein aggregates in ring structures within neuron membranes, causing cell damage and symptoms of Parkinson's disease. The study provides a step-by-step explanation of how these aggregates form and offers hope for developing drugs to slow disease progression.
Muscle cells have efficient systems to seal holes in their plasma membranes. Researchers at KIT and Heidelberg University observed membrane repair in real-time using a novel imaging method. They found that membrane vesicles form a repair patch, which is sealed off from the extracellular environment.
Rutgers researchers identified a Type III PI4-kinase as an excellent target for panviral therapeutics. Blocking the enzyme was effective in stopping virus replication and saving host cells. The study found that viruses hijack this enzyme to manufacture a lipid necessary for replication.
Researchers find tau proteins interact with negatively charged lipids on cell membranes, causing protein aggregation and neuronal death. Compounds that prevent protein interaction with membranes offer hope for Alzheimer's patients.
Researchers developed a new tool to study the impact of spatial patterns on living cells, allowing them to control protein placement and study their behavior. The technique enabled them to test breast cancer cells and demonstrate the importance of cell adhesion molecules.
Researchers at Berkeley Lab create a new device called the SheetRocker to study how shaking affects sheet formation in peptoid monolayers. They find that compression on the air-water interface produces free-floating, stable nanosheets in 95% yield, enabling scalable sensing and filtration applications.
A team of researchers led by Professor Rikard Blunck has discovered the molecular mechanism behind toxin proteins engineered into food to kill insects. The study uses a novel technique involving fluorescent light to analyze the protein's structure and behavior in artificial cell membranes.
The Biophysical Society has honored five researchers with its top awards for 2012, recognizing their innovative work on membrane proteins, lipid interactions, and single-molecule biology. The awardees include Charles R. Sanders, Huey W. Huang, Lucy R. Forrest, Sunny Xie, and Vijay Pande.
A team of researchers has reconstructed and tested a trafficking pathway for hundreds of cell proteins, finding that they can be delivered to the membrane via a simple three-part system. This discovery could have significance for the development of new drugs and bioengineering methods.
The research group has identified a new protein, Pinkbar, that creates planar membrane sheets, modifying the structure of plasma membranes in intestinal epithelial cells. This finding may be linked to various intestinal disorders.
A newly synthesized protein is fragile and requires chaperones for proper folding, which also escort it to its destination and aid in membrane insertion. The researchers identified key components responsible for TA protein sorting, including Get3 ATPase and receptors Get1 and Get2.
The Deutsche Forschungsgemeinschaft will establish 21 new Collaborative Research Centers (CRCs) as of July 2011, focusing on topics such as additive manufacturing, biological systems, and quantum physics. The centers aim to improve manufacturing methods, investigate novel materials, and explore social structures.
Two studies provide the first detailed view of the chemical and mechanical interactions between the ribosome and membrane proteins. The researchers used cryo-electron microscopy to image the insertion process, revealing a
Researchers at NIST and University of California, Irvine, developed a way to magnify cell membranes up to 1,000 times resolution, revealing the importance of cholesterol in maintaining membrane order. The findings suggest that cholesterol may have profound consequences for gatekeeper proteins, which interact constantly with the membrane.
A new laser technique, called backscattering interferometry (BSI), measures the binding force between proteins and biological molecules in a natural environment. This technology has potential applications in drug discovery, particularly for targeting membrane proteins.
Researchers at Scripps Institute develop a novel technology that synthesizes complex cellular structures from simple starting materials, creating uniform cell-like compartments. The new process is highly efficient and customizable, revolutionizing the field of synthetic biology.
Scientists design artificial protocells with bait proteins that mimic henipavirus receptors, successfully entraping and deactivating experimental analogs of Nipah and Hendra viruses. This innovative technique could lead to the development of new antiviral drugs by exploiting the virus's basic infection mechanism.
Researchers found excessive calcification of fetal membranes may lead to preterm premature rupture of the membranes (PPROM) and preterm birth. Lower fetuin levels in amniotic fluid were linked to women at risk of PPROM.
Researchers at Arizona State University developed a new method to determine biomolecule structures, achieving over 3 million clear diffraction patterns with the Linac Coherent Light Source. This milestone has significant potential for discoveries in biology, medicine, clean energy, and the development of targeted cancer drugs.
Researchers use X-ray laser to determine 3D structures of proteins and capture single-shot images of viruses, paving the way for snapshots and movies of molecules and microbes in action. The technique has the potential to decipher tens of thousands of protein structures and study infectious diseases.
Australian researchers have developed a method to analyze X-ray scattering data from XFELs, enabling the measurement of membrane protein structures even with significant electronic damage. This breakthrough will help fast-track the development of targeted drugs.
EMBL scientists first to visualize the structure of a ribosome-protein complex involved in carrying nascent proteins out of the cell. The discovery could increase understanding of illnesses such as cystic fibrosis and Parkinson's disease, where improper protein targeting leads to harmful accumulation inside cells.
A novel lab-on-chip device has been developed to screen sensitive membrane proteins in parallel, utilizing a nano-fabricated chip with 50,000 nanopores. This technology preserves protein structure without organic solvents or solid support, enabling simultaneous analysis and preserving fragile protein function.
Researchers have developed a simple method to fabricate free-standing polymer membranes with precisely patterned holes, opening up potential applications in microfluidics. The technique uses photolithography and prepolymer, allowing for easy fabrication of membranes with accurate sizes and shapes.
Researchers discovered that cell membranes behave as viscoelastic materials, bouncing back like rubber when quickly perturbed. This finding challenges the long-held notion of biological membranes being simple Newtonian fluids.
A team of researchers has created a technology to extract complex membrane proteins without distorting their shape, enabling scientists to better understand the properties and functions of these proteins. This breakthrough could facilitate research at the biomedical frontier.
The NIH has awarded a $7.7 million grant to Arizona State University to unravel the structures of membrane proteins that play a key role in protecting against infectious diseases. The ASU center will target membrane proteins of key viral and bacterial pathogens, their infectious pathways and molecules involved in host defense.
The NIH has awarded $290 million in grants for structural biology research, focusing on determining protein shapes and functions. Four large-scale centers will operate pipelines for protein structure determination, including centers for mitochondria and membrane proteins.
Researchers at Helmholtz Association have developed a unique X-ray measuring chamber, LiXEdrom, which enables the study of liquids without membrane distortion. This breakthrough allows for precise information about material structure and has significant implications for protein studies.
Researchers at Technical University of Munich discovered that Hsp12, a stress protein, folds into helical structures to stabilize cell membranes against leaks and ruptures under various types of stress including heat shock, oxidative stress, and osmotic stress
Researchers are leveraging decades-old ultrahigh pressure discoveries to advance proteomics, mass spectrometry, and protein extraction techniques. Pressure-cycling technology (PCT) accelerates glycan release, membrane protein extraction, and other complex processes.
The Membrane Protein Structural Dynamics Consortium aims to unite structure and function through dynamic studies of membrane proteins, enabling better drug development for diseases like heart disease and diabetes.
Research at Stanford University School of Medicine has pinpointed the molecular cause of Bardet-Biedl syndrome, a genetic disorder associated with obesity, retinal degeneration, and kidney cysts. The primary cilium acts as a communication hub where signaling pathways take place, influencing weight gain and fat storage.
Researchers at Emory University have discovered that simple peptides can organize into bi-layer membranes, a 'missing link' between pre-biotic Earth's chemical inventory and the scaffolding essential to life. This finding may also shed light on protein assemblies related to Alzheimer's disease, Type 2 diabetes, and other serious ailments.
Scientists at EMBL discovered membrane-coat proteins in bacteria from the PVC superphylum, which could aid in understanding eukaryotic cell evolution and structure. These findings provide molecular evidence that coat proteins shape eukaryotic endomembrane systems in prokaryotes.
Researchers discovered a crucial role of protein BAR in membrane vesicle binding, providing insights into nerve cell communication failures that lead to nerve pain. The findings have the potential to develop new treatments for nerve disorders.
Researchers found that a mutant ATPase blocks autophagy partway through, causing multi-tissue degenerative diseases. Mutations in VCP also accumulate p62 and LC3 in muscle tissue, suggesting frustrated autophagosomes. The study aims to determine the mechanism of VCP's promotion of final stages of autophagy.
A team of researchers has discovered the process by which new HIV virus particles are assembled at the membrane of infected cells and released to attack healthy cells nearby. The study, published in PLoS Pathogens, provides important insights into a crucial step in person-to-person transmission.
Researchers have discovered how critical proteins for eye lens transparency are sorted and concentrated in membrane bilayers. The study reveals that protein-lipid interactions play a key role in this process, with aquaporin clustering influencing its localization in lens cell membranes.
Researchers found that a disruption in the spectrin-actin network leads to irregularities in lens cell packing and shape. The study suggests that mechanical stresses during lens growth and eye movements cause this disorganization.
Researchers discovered that atlastin, a previously underappreciated protein, plays a critical role in building and maintaining healthy cells by fusing intracellular membranes. This process is essential for cell function and development.
A new study identifies alpha dystroglycan as a key protein that binds muscle membranes to the basal lamina, reinforcing membrane integrity. Injecting functional dystroglycan into muscle tissue restored membrane integrity and protected muscles from damage.
Three NTU proposals win up to S$30 million in funding for innovative biomedicine, energy, and materials research. The grants aim to address global climate change concerns and develop new technologies for energy generation and storage.
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 have developed a novel protein stabilisation technique using nanoparticles, enabling detailed analysis of previously inaccessible membrane proteins. This breakthrough could lead to more effective drugs and open up exciting possibilities in therapeutic drug discovery.
A research team at Goethe University Frankfurt has identified two proteins, Fcj1 and Su e/g, that regulate the shape of mitochondria's inner membrane. The protein Fcj1 promotes negative curvature, while the Su e/g protein induces positive bending, leading to the formation of cristae junctions.
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 have for the first time visualized the three-dimensional structure of a crucial subcomplex of the nuclear pore complex (NPC), a fundamental innovation in multicellular life. The findings support a common architecture between NPCs and coated vesicles, revealing an ancient evolutionary connection.
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.
Researchers found that curcumin acts as a disciplinarian, inserting itself into cell membranes and making them more orderly. This improves cells' resistance to infection and malignancy by controlling information flow through the membrane.
Researchers at University of Copenhagen have developed a general method to study membrane proteins, reducing the development time for useful drugs substantially. The method uses amphipols to immobilize membrane proteins on surfaces, allowing for faster and more accurate testing.
Researchers at Johns Hopkins University School of Medicine have discovered a potential new approach to cancer therapy by manipulating the tail of a tumor suppressor protein. By removing its tail, the protein becomes active and can effectively suppress cancer growth.