Articles tagged with Protein Structure
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A team of researchers at Duke University has determined the structure of the TRPM8 protein, which is responsible for sensing cold and menthol. The findings suggest that PIP2 and cooling agents like menthol cooperate to control structural changes in TRPM8, potentially leading to new treatments for chronic pain and migraine.
Researchers discovered that PRIMA-1 reverses mutant p53 aggregate accumulation, leading to the restoration of native protein function. The compound's potential as an anticancer drug is highlighted by its phase II clinical trials and positive results in breast and ovarian cancer cell lines.
Researchers at UT Austin develop a new method to build synthetic protein structures, allowing for the creation of nanomachines and other complex systems. The 'SUpercharged PRotein Assembly' (SuPrA) method mimics nature's way of forming molecular machines, enabling flexible and self-assembling structures.
Researchers at the University of Liverpool have synthesized a flexible crystalline porous material that can change its structure in response to its environment, mimicking the properties of proteins. This breakthrough enables the design of materials that can dynamically select the structure needed for specific tasks.
A research team has identified the early neuropathology mechanism of structural characteristics of polyglutamine toxic protein on neurodegenerative brain disorders. The coiled-coil structure causes rapid deformation of neurons and leads to diseases like Huntington's chorea and spino-cerebellar ataxias.
Researchers solved the structure and elucidated the function of photosynthetic complex I, a key element in dynamic rewiring of photosynthesis. The complex plays a major role in cyclic electron transport, allowing for efficient energy production.
A newly discovered protein from the bacterium Methylobacterium extorquens has been found to be 100 million times better at binding to lanthanides than to other metals. The protein's unique structure may explain its remarkable selectivity, which could provide insights into detecting and targeting rare-earth metals for industrial purposes.
Researchers have developed an innovative 'elastic' contrast media that enhances MRI diagnostics without increasing contrast medium use. The new method utilizes a self-regulating protein structure that absorbs xenon to improve image quality, allowing for better detection of disease markers in low concentrations.
Research reveals that a genetic mutation in Filamin A protein impairs cellular force transmission, leading to valvular heart disease. The study provides new insights into the molecular mechanisms of the disease and paves the way for developing new treatments.
Researchers at Scripps Research have identified a novel class of mechanosensitive ion channels, called OSCAs and TMEM63s, which convert physical forces into biochemical signals. The study provides a structural snapshot of an OSCA channel, revealing potential mechanisms for force sensation.
Researchers at the University of Eastern Finland have developed novel antibacterial compounds targeting LsrK kinase, a key player in bacterial quorum sensing. The identified LsrK inhibitors have shown micromolar activity and will be further optimized to improve understanding of inhibition of LsrK in the AI-2 pathway.
Scientists at the University of Leeds have used powerful microscopy techniques to reveal the structure of amyloid proteins, a build-up of abnormal proteins that causes disease. The research has provided significant insights into how these proteins form aggregates and contribute to disease, paving the way for potential treatments.
Researchers from Clemson University and Stony Brook University reveal a 3-D structure of a protein fragment that could serve as a drug target in treating stroke patients. The protein, PSD-95, plays a crucial role in maintaining neural connections and facilitating communication, learning, and memory.
Scientists developed a new method to analyze and reconstruct super-resolution images into a 3D volume with multiple colors. This technique enables the observation of complex molecular structures in cells, resolving protein complexes previously invisible.
Scientists have solved the structure of two proteins that control DNA packaging, potentially providing insights into why some people are at risk of developing specific cancers. The findings also shed light on how these proteins' mutations contribute to various types of cancer, including mesothelioma and leukemia.
The study revealed the atomic-level structure of TRPM2, a protein involved in regulating body temperature and mediating immune responses. The findings provide valuable details that could inform the design of therapeutic drugs to treat temperature-related diseases and prevent neuronal death.
A team of scientists has discovered the atomic-resolution structure of a specialized ribosome in Trypanosomes, a parasitic disease-causing organism. The study reveals that these ribosomes are composed primarily of proteins, unlike other ribosomes which are dominated by RNA.
Researchers at Washington University in St. Louis create 'blink' method to image amyloids, allowing for non-invasive visualization of these problematic proteins. The technique uses temporary fluorescence, causing amyloids to flash and enabling researchers to better understand their structure and behavior.
Researchers used a super-resolution microscope to observe viral assembly, finding that envelope proteins are randomly scattered on the cell membrane rather than recruited by matrix proteins. This discovery could lead to more effective vaccines for enveloped viruses like influenza and HIV.
Researchers at Shinshu University have developed proteins that can self-assemble into complex nanostructures, a breakthrough in biomolecular engineering and synthetic biology. The new protein complexes can be designed to produce various chain-like structures on demand, opening up possibilities for innovative applications in biotechnology.
Researchers at Ruhr-University Bochum developed a new infrared sensor method to analyze the structure of proteins affected by active agents. This method provides rapid measurements, allowing for the detection of structural changes within minutes and the identification of binding periods that determine drug efficacy.
Researchers have discovered how messenger RNAs are transported out of the nucleus through nuclear pore complexes, a process that occurs in just a fraction of a second. The study also sheds light on how mutations affect protein stability and could lead to the design of therapeutic drugs for motor neuron diseases.
A new German Research Foundation Priority Program explores how cells utilize phase separation to perform novel functions. The program aims to understand the collective behavior of intrinsically disordered proteins, which have been termed the dark proteome.
Beta peptides can self-assemble into robust biomaterials when placed inside other organic molecules. A new study has expanded their capabilities, allowing bioengineers to create more flexible materials for tissue engineering and biomedicine.
A human protein, teneurin, plays a key role in embryonic development and nervous system wiring by binding to other proteins on cell surfaces. Its unique structure, resembling a bacterial toxin, allows it to perform multiple functions through alternative splicing.
Researchers discovered that larger, more visible SOD1 protein aggregates are protective rather than harmful to neurons. The study suggests that these fibrils could be a solution to reduce toxicity in SOD1-ALS, and finding drugs to promote their formation may help mitigate the disease.
The study reveals that the circulating form of soluble a-Klotho can act as a co-receptor for FGF23, making every cell a potential target. This breakthrough challenges the long-held belief that only cell-attached a-Klotho can receive FGF23 signals.
The Protein Society has awarded Minfei Su and Chang-Ting Lin the 'Best Paper' award for their research on autophagy, a critical process in eukaryotic cells. The winners' work investigates the structural and thermodynamic details of protein interactions, shedding light on cellular homeostasis and evolution.
Researchers discovered that membrane proteins can recruit their own lipid microenvironments through allostery, enabling new possibilities for pharmaceutical drug design and delivery. This finding is critical to understanding how the lipid environment influences protein structure and function.
Researchers designed and expressed custom transmembrane proteins with new functions, overcoming challenges in studying these proteins. The advance enables the creation of multipass proteins with novel structures and functions.
Scientists have decoded the three-dimensional molecular structure of the healthy human huntingtin protein, enabling its functional analysis. This breakthrough could contribute to the development of new treatments for Huntington's disease.
Scientists at the University of Zurich have discovered a novel interaction mechanism for proteins, which can bind together despite being unstructured. This breakthrough has significant implications for understanding cellular processes and developing new therapies.
Excess calcium levels can lead to the formation of toxic clusters with alpha-synuclein, causing brain cell death. Understanding this interaction may aid in developing new treatments for Parkinson's disease.
Cyanobacterial clock proteins were found to dictate their function through internal motions, providing important mechanistic insights into biological timekeeping. This discovery has implications for understanding circadian clocks in eukaryotic organisms, such as animals and humans.
Researchers at UC San Francisco have uncovered the architecture of the spindle pole body in yeast, shedding light on its function and potential connections to human centrosomes. The study reveals that the Spc110 protein plays a crucial role in the SPB's structure and may provide a binding surface for its architecture.
Researchers at Penn develop a technology to track protein shape changes, which could lead to improved drug treatments and earlier detection of neurodegenerative diseases. By labeling proteins with probes, they can observe movement and create computational models for atomic-level detail.
The Biophysical Society has announced its new and notable symposium speakers for the 62nd Annual Meeting. The session will feature cutting-edge research on ultrafast glutamate sensors, dynamic chromatin fibers, and more. The meeting will take place from February 17-21, 2018.
The study's findings offer a blueprint for designing therapeutic drugs against common forms of lung and breast cancer. Understanding the structure of DHHC20 may aid in treatment of EGFR-driven cancers.
Researchers used cryo-electron microscopy to visualize the structure of the TRPV5 protein, which serves as a passageway for calcium across kidney cell membranes. The study reveals how inhibitor molecules attach to and close the channel, leaving calcium stranded in the urine where it can form kidney stones.
Scientists at Scripps Research Institute have solved the mystery of Piezo1's structure, revealing three curved blades that move in response to mechanical force. The findings point the way to targeting diseases where Piezo1 is mutated.
Researchers at Van Andel Research Institute have determined the atomic-level structure of TRPM4, a protein responsible for regulating blood flow to the brain. The 'crown-like' structure reveals new facets of its makeup and provides a molecular blueprint for designing effective medications with fewer side effects.
Researchers developed a new approach to identify protein structure from sole sequence information by analyzing paired mutations across thousands of protein family members. This method identified sequence covariations that uncover the protein's macrostructure and its fundamental structural and functional units.
A single amino acid change determines which species are vulnerable to a hereditary brain disease. The human, mouse and hamster forms of the protein have distinct three-dimensional structures at the atomic level.
Researchers at CNRS have identified a novel protein, KSRP, specific to the ribosomes of trypanosome parasites. Inhibiting its activity leads to parasite death. This discovery opens the path to developing new, safer therapies for Chagas disease and African sleeping sickness.
Exosomes secreted by cells in healthy individuals stop protein aggregation that leads to type 2 diabetes, but those in patients with the disease do not. This discovery provides new insights into the disease and may lead to the development of treatments.
Researchers from the University of Alabama at Birmingham have solved the last unknown protein structure of HIV-1, which helps understand how the virus infects human cells and assembles progeny viruses. The cytoplasmic tail of gp41 protein plays a crucial role in virus assembly and replication.
Researchers at the University of Notre Dame have developed a new analysis procedure to better understand how intrinsically disordered proteins (IDPs) function in cells. The study finds that most IDPs are more disordered than previously thought, which could lead to new strategies for preventing protein misfolding diseases.
Researchers at the University of Dundee have identified the 3D structure and inner workings of the PINK1 enzyme, a key player in protecting brain cells against stress. This breakthrough provides crucial insights into how PINK1 exerts its protective role in Parkinson's disease.
The 2017 Nobel Prize in Chemistry was awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson for developing cryo-electron microscopy. This technology allows researchers to freeze biomolecules mid-movement and define protein structures at atomic resolution.
Researchers developed a theoretical method to calculate biomolecule conformations and demonstrate consistency with experimental results. The model sheds light on the role of amino acid structures in protein functions, revealing potential for extrapolating properties to larger systems.
Researchers from MSU have discovered a novel mechanism of carotenoid transfer between two proteins, opening doors for the development of water-soluble protein complexes to deliver antioxidants to cells. This discovery may lead to new therapeutic applications, such as protecting healthy tissue during cancer treatment.
Researchers created three-dimensional structures that mimic natural enzymes, shedding light on folding processes and potential treatments for diseases like Alzheimer's and Parkinson's. The breakthrough allows for the analysis of misfolded proteins, a key factor in these conditions.
Researchers stopped FUS protein clumping using phosphorylation, a natural cellular process that increases protein charge and repels aggregation. The findings could have positive implications for treating ALS and dementia.
The Rice lab has produced the first full-length structure of a salmon virus protein, shedding light on its role in viral assembly and potentially informing strategies to treat human influenza viruses. The discovery could lead to new antiviral treatments by targeting the protein's interaction with other viral components.
A new tilted microscopy technique reveals better protein structures, resolving missing information and improving disease research. This approach could lead to a deeper understanding of proteins' conformations and their role in various diseases.
Researchers from the Bristol BioDesign Institute created a miniprotein with a stripped-down structure to investigate molecular forces that assemble and stabilize protein structures. They discovered subtle forces beyond hydrophobic interactions, which could lead to new drug targets.
A Los Alamos research team used neutron crystallography to determine the three-dimensional structure of a protein that breaks down cellulose, a key step in creating biofuels. The findings suggest that understanding the mechanism of this enzyme could lead to more efficient and cost-effective production of ethanol.
Research in The FASEB Journal reveals a key role for cilia structure in determining susceptibility to neural tube defects. Genetically modified mice studies found that methylation of the Septin2 protein affects neural tube closure, leading to an increased risk of birth defects.
A team of researchers at Hokkaido University has uncovered the structure of a protein called HLA-G2 that protects embryos from being attacked by their mothers' immune systems during pregnancy. The structure was found to be similar to another class of human leukocyte antigens, suggesting its evolutionary origin.
An international team of scientists has determined the 3-D atomic structure of over 1,000 proteins that are potential drug and vaccine targets. The experimentally determined structures have been deposited into the World-Wide Protein Data Bank, freely available to the scientific community.