Articles tagged with Protein Structure
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Researchers at Tohoku University used cryo-electron microscopy to determine the high-resolution 3D structure of human SPCA1a, a protein pump involved in calcium and manganese ion transport. The study provided insights into how the protein works and how mutations can cause Hailey-Hailey disease and other neurodegenerative disorders.
The study resolves a long-standing question about the structure of respiratory supercomplexes in unicellular eukaryotic organisms. Complex II is found to be part of the supercomplex in these organisms, optimizing ATP formation and revealing a surprising variety in supercomplex construction.
A cross-disciplinary team developed a convolutional neural network to analyze microscopy images of chromosomes with cohesion defects. The algorithm achieved 73.1% accuracy in classifying new images, streamlining experiments with chromosome analysis.
Scientists discovered the molecular basis of CAMSAP3's role in stabilizing microtubules, which is critical for cell survival and various cellular processes. The findings provide a key concept to understanding how microtubule dynamics control cellular phenomena.
Scientists have defined the full-length structure of p53, a crucial protein that regulates cell growth and division. The study reveals how mutations in p53 can lead to cancer by disrupting its ability to grasp DNA, highlighting potential new therapeutic approaches.
Researchers used machine-learning algorithms to design new light-emitting enzymes called luciferases that can efficiently recognize specific chemicals and emit light. This breakthrough could lead to custom enzymes for a wide range of applications in biotechnology, medicine, environmental remediation, and manufacturing.
The study reveals new details about the intraflagellar transport (IFT) complexes, including previously unknown zinc-binding sites in IFT-A. The high-resolution structures of IFT-A and Tubby-related protein 3 (TULP3) can now be used to investigate developmental diseases involving cilia.
Researchers discovered a causal mechanism behind BPTA syndrome by identifying a change in the HMGB1 protein that disrupts cellular self-organization. This disruption leads to developmental disorders and predisposition to cancer, with hundreds of comparable genetic changes associated with various conditions.
Scientists discovered a new hexameric structure of RepB protein, which initiates DNA replication for antibiotic resistance plasmids. The study highlights the importance of developing new antibiotics and understanding how resistance spreads.
Researchers at Universitat Autonoma de Barcelona solved the structure of a functional amyloid protein, hnRNPDL-2, which forms stable and non-toxic fibres in humans. The discovery changes the concept of disease origin and treatment, suggesting that molecules stabilising or facilitating fibre formation could be the key to therapy.
Researchers at La Jolla Institute for Immunology have discovered the detailed mechanism of action of Inmazeb, a three-antibody cocktail designed to combat Ebola virus infection. The study reveals new information about how the drug interacts with the virus and its potential effectiveness against additional species of Ebolavirus.
Researchers at Aston University are working with Isterian Biotech to develop small molecule inhibitors targeting transglutaminase 2, a key enzyme in fibrosis. The goal is to stop or reverse pathological crosslinking of proteins that lead to fibrotic diseases such as idiopathic pulmonary fibrosis.
Researchers successfully applied AlphaFold AI to an end-to-end platform, discovering a novel target and developing a potent hit molecule for liver cancer. The study demonstrates the potential of AI-powered drug discovery to accelerate treatment development.
Researchers from Tokyo Medical and Dental University found that PQBP5/NOL10 is a core structural element of the nucleolus, forming a meshwork that supports other nucleolar substructures. It remains in the nucleolus under osmotic stress conditions and anchors reassembly of the nucleolar structure.
A clinical trial found that boiling peanuts for up to 12 hours can desensitize children with peanut allergies. The therapy involved sequential doses of boiled and roasted peanuts, achieving high success rates in participants. While promising, the study's findings require confirmation in larger trials.
Scientists at IRB Barcelona have detailed the atomic scale mechanism of action for FoxH1, a key transcription factor in embryonic development and cancer. The study reveals an unusual binding mechanism to compacted DNA, shedding light on its role in disease progression.
Researchers have discovered the three-dimensional structure of phosphoinositide 3-kinase alpha (PI3Kα) and how it changes with cancer-associated mutations. This knowledge enables the design of targeted drugs that can specifically bind to mutated versions, potentially eliminating side effects associated with current PI3Kα inhibitors.
Researchers modeled how genetic changes affecting protein synthesis speed can lead to misfolding and altered activity levels in proteins. This finding suggests the importance of kinetics alongside sequence for determining protein structure and function, with potential implications for fields such as biopharmaceutics and medicine.
A Collaborative Research Centre investigates animal navigation using the Earth's magnetic field. The study focuses on vertebrates, including birds and fish, aiming to protect endangered migratory species.
Researchers at ETH Zurich have identified 76 proteins that could serve as biomarkers for Parkinson's disease, with their molecular structures differing between healthy and diseased individuals. The study uses a unique method to analyze protein shapes in cerebrospinal fluid, providing a promising new approach for diagnosis and potential...
Scientists at KAUST have identified dynamic regions, called cryptic binding sites, that can be targeted by drugs to treat cancer. The study reveals how molecular motion influences ligand binding to BTB domains, a critical part of many proteins involved in disease.
Researchers developed IsoNet, a software package solving intrinsic 'missing-wedge' problem and low signal-to-noise ratio issues in cryoET. IsoNet uses iterative self-supervised deep learning to perform missing-edge correction and denoise tomographic data.
A new technological advancement at the University of Oklahoma will enable scientists to study whole macromolecular structures without deconstructing them. This breakthrough, supported by a $50,000 NIH grant, aims to analyze proteins as intact molecules, improving our understanding of their modifications and interactions.
The study reveals the structure of the 15-subunit IFT-B complex, a crucial component in cilia formation and maintenance. The complex's elongated and flexible nature is consistent with previous low-resolution reconstructions, and two configurations are identified that may drive bi-directional movement.
Researchers at UIC have developed a new method to study ribosome function by attaching peptides to tRNAs, providing high-resolution structures of the ribosome and its interactions with nascent chains. This breakthrough sheds light on protein synthesis and antibiotic resistance.
The research reveals PAPP-A's heart-shaped structure and its interaction with STC2, a key regulator of IGF conversion. The study suggests that complex formation between PAPP-A and STC2 is highly regulated, influencing height by up to 2.1 cm.
Filopodia contribute to building a barrier surrounding breast tumours, blocking their escape. Cancer cells lacking Myosin-10 cannot maintain this barrier, making it easier for them to spread.
A team from the University of Geneva has identified the structure of the SEA complex, a key regulator of cell growth, and how it controls the activity of the major regulator of cell growth, mTOR. The discovery provides new insights into how cells perceive nutrient levels to regulate their growth.
Researchers at the National Eye Institute have discovered a mechanism by which an area of the protein RPE65 converts vitamin A into a form usable by photoreceptor cells. This finding provides better understanding of RPE65's function and will inform potential treatments for vision disorders linked to gene mutations.
Scientists from NTU Singapore have discovered that telomeres are stacked in columns like a spring, leaving DNA exposed to damage. This finding could improve understanding of how humans age and develop cancer, with potential treatments for diseases caused by dysfunctional telomeres.
Researchers observe atomic-level structural changes in bacterial ribosomes and their response to antibiotics, shedding light on mechanisms of action and potential off-target effects. The study provides new insights into the complex interactions between ribosomes and other cellular complexes.
Researchers decode Sr35 wheat protein's structure and function, revealing its role in protecting Einkorn wheat from Ug99. The discovery provides a crucial tool for improving crop resistance and ensuring global food security.
Researchers have identified a complex of proteins in a tiny marine invertebrate that share similarities with the human immune system, suggesting an earlier origin for the building blocks of our immune system. The study could ultimately guide the development of new immunotherapies and improve understanding of transplant rejection.
A recent study by Texas Tech University Health Sciences Center researchers has shed light on the mechanisms of salt transport across membrane barriers. The findings have significant implications for treating cystic fibrosis, a disease caused by mutations in three types of sodium-potassium pumps.
Researchers create mammalian cells that synthesize a noncanonical amino acid, which can be used to make therapeutic proteins. The discovery could lead to the development of new treatments for various diseases.
Researchers developed a new software tool called ProteinMPNN to create protein molecules more accurately and quickly than before. The team used machine learning algorithms, including AlphaFold, to generate new protein shapes and sequences, paving the way for novel vaccines, treatments, and sustainable biomaterials.
Researchers at Case Western Reserve University have identified the structure of protein fibrils linked to a hereditary form of human prion disease, revealing the mechanism for interspecies transmission. The study suggests that disease transmission between species can be predicted based on structural information.
Scientists at SLAC National Accelerator Laboratory have seen the critical interaction between SARS-CoV-2 protein Mpro and human immune system protein NEMO. The study reveals that Mpro can cut NEMO, slowing down the immune response and allowing the virus to evade the body.
A new study from MIT reveals that computer models predicting molecular interactions, like AlphaFold, need improvement to help identify drug mechanisms of action. Researchers improved the performance of these models using machine-learning techniques, but more work is needed.
Researchers at Sanford Burnham Prebys have discovered the flexible structure of a key blood protein involved in macular degeneration and other age-related diseases. The study reveals how this protein adapts to changing pressure, leading to calcified plaque deposits characteristic of these conditions.
Researchers successfully created a periodic rippled beta sheet layer configuration, as predicted by Linus Pauling and Robert Corey in 1953. The new findings enable the rational design of unique materials based on this novel protein structure.
Researchers at Washington University have developed a hydrogel system that preserves biochemistry and mechanical environments of cultured podocyte cells. This allows researchers to identify new ways to control mechanisms used by cells to heal themselves, potentially leading to therapies for currently incurable diseases.
A new mid-infrared sensor chip can accurately monitor liquid concentrations in real-time, enabling precise monitoring of chemical reactions. The sensor combines customized infrared technology and chemical robustness to deliver data within fractions of a second.
Researchers at UBC have discovered a key vulnerability across all major COVID-19 variants that can be targeted by neutralizing antibodies. The 'master key' identified is the antibody fragment V H Ab6, which effectively neutralizes SARS-CoV-2 by attaching to the epitope on the spike protein.
A recent international study has shed light on the inner workings of the adaptive immune response, revealing how killer T cells recognize viral invaders using molecular road signs. The study highlights the crucial role of chaperones in ensuring the stability and longevity of these road signs, allowing for more effective detection and d...
A research team led by Prof. Dr. Birte Höcker applied a computer-based natural language processing model to protein research, creating new proteins capable of stable folding and defined functions. The ProtGPT2 model generates proteins with differentiated structures, eliminating the need for functionalization processes.
Researchers at Ohio State University have developed an artificial protein that could provide new insights into chemical evolution on early Earth. The protein, inspired by a key enzyme in energy production, has been shown to build molecules one step at a time, shedding light on how organic chemistry matured on the planet.
The study reveals multiple dimeric structures of cadherins in solution, including W-, cross-, and S-shaped dimers. The researchers propose a novel conformation, the S-shaped dimer, and suggest that binding mechanism progresses through sliding motion followed by flipping motion to form stable SS-dimers.
Researchers at Johns Hopkins Medicine have probed the atomic structure of proteins, finding that wiggling and movement play a critical role in their ability to function. The study's findings may help scientists design new drugs that can modify or disrupt protein movements to alter their functions.
Researchers from Johannes Gutenberg University Mainz used AlphaFold to predict the structures of new protein knots, discovering the most complex knot and composite knots. These findings provide insight into folding mechanisms and evolutionary processes in proteins.
A Tokyo University of Science study found that fluoride nanoparticles enhance β-sheet formation in amyloid β proteins, a common feature of Alzheimer's disease. The researchers also discovered that surrounding ions can control this process, paving the way for targeted treatments.
Researchers discovered a molecular switch in flavivirus that controls virus assembly, maturation, and entry into new cells. This switch is triggered by pH-dependent conformational changes in viral envelope proteins.
Researchers discovered a new prion structure using electron microscopy, revealing key similarities and differences between distinct strains. This finding could lead to better understanding of how shape variations affect disease outcomes.
Researchers discovered that copper accelerates protein aggregation in Parkinson's disease, forming ring-shaped structures that can be used as therapeutic targets. The study provides new clues to the development of the neurodegenerative disease.
Scientists have determined the molecular structure of HIV Pol, a protein that plays a key role in the late stages of HIV replication. The discovery reveals a new vulnerability in the virus that could be targeted with drugs, and sheds light on how the protein breaks apart to advance the replication process.
Liu's three-year grant will pursue protein-derived cofactor studies to improve understanding of amino acids and their role in metabolism. The research aims to gain a quicker and more thorough understanding of amino acid function and purpose.
Rensselaer researchers will use a five-year grant to develop novel inhibitors of the SARS-CoV-2 virus's CLpro and PLpro proteases. The team aims to create an orally bioavailable drug that can be administered at home, with the potential for improved antiviral activity when combined with other drugs like remdesivir.
The study reveals how the protein binds to ligands and inhibitory antibodies, providing insights into its molecular function. The findings may lead to better targeted therapeutic approaches in the future.
Researchers have discovered the process of incorporating selenium into 25 specialized proteins, essential for various cellular and metabolic processes. The study provides critical insights into the workings of these vital mechanisms, which could lead to the development of new medical therapies.
Scientists have discovered a new, high-resolution view of the rabies virus glycoprotein, which could lead to more effective vaccines. The study's findings suggest that a better-shaped vaccine could provide lifelong protection against the deadly disease.