Articles tagged with Protein Complexes
Scientists at Tufts University and the University of Pennsylvania have determined the unusual structure of a key member of the herpes virus protein complex that allows it to invade cells. The research provides a new target for antiviral drugs, which could prevent the virus's access to cells.
Researchers have discovered a domino effect in protein complexes that contribute to neurodegenerative diseases. The study, led by Dr. Aitor Hierro, reveals reduced levels of mutated protein Vps54 disrupt the GARP complex, leading to motorneurodegeneration.
Scientists have mapped the herpes virus protein complex that allows it to invade cells, revealing a new target for antiviral drugs. This breakthrough could lead to the development of new therapeutics to restrict herpes virus access to mammalian cells.
Researchers at EMBL identified a new Polycomb group complex, PR-DUB, which surprisingly removes the same gene-silencing tag as another complex. This unexpected behavior may be a case of fine-tuning to maintain optimal levels of chemical tagging.
Researchers have discovered that the byssal cuticle of mussels is a protein-based polymeric scaffold stabilized by dopa-iron complexes, enabling its unique hardness and extensibility. The cuticle's mechanical behavior allows it to dissipate energy from crashing waves while resisting abrasive damage.
A CSHL team discovered rules governing the processing and sorting of small RNAs in the RNAi pathway. The rules determine which strand of a duplex is chosen to interact with the Argonaute protein, affecting gene regulation and potential therapeutic applications.
Researchers found that BBS proteins remove excess signaling molecules to prevent damage to cilia, suggesting a new mechanism for the protein complex's function. The study suggests that BBS patients may experience cilia dysfunction due to the buildup of disruptive proteins.
Researchers have identified a molecular scaffold that bridges the two rare inherited disorders, revealing how cells repair damaged DNA. The study suggests that disruption of this interaction leads to similar chromosomal repair defects in both Fanconi anemia and Bloom's syndrome.
The article features laboratory methods for high-throughput genotyping, including single-nucleotide polymorphism (SNP) genotyping and next-generation sequencing. The tandem affinity purification (TAP) procedure is also presented as a method for protein purification.
Berkeley researchers have imaged the human RISC-loading complex for the first time, proposing a model of how small RNA molecules target specific messenger RNAs for silencing and/or destruction. This work provides new insights into RNA interference mechanisms and has significant implications for gene regulation in humans.
A $2.2 million NIH grant will enhance the lab's ability to rapidly detect protein clumps in Alzheimer's and other neurodegenerative diseases using a new high-resolution electron microscope. This technology will also enable researchers to study molecular motors in flagella, leading to a better understanding of these diseases.
Researchers have discovered the strongest protein bond yet found in nature, which anchors muscular strength. This discovery has significant implications for fields like medical research and nanotechnology.
Researchers at the University of Oregon have identified a key mechanism by which an enzyme (aPKC) directs the fate of daughter cells in stem cell divisions. This simpler process, rather than a long cascade of events, helps determine the fates of subsequent cells.
The May issue of Cold Spring Harbor Protocols features a set of methods to analyze protein complexes, including Blue-Native PAGE and differential in-gel electrophoresis. Additionally, researchers can generate viral vectors using adenovirus technology for efficient gene delivery.
Researchers at EMBL and PSI create ACEMBL, a new technology that produces multiprotein complexes with reduced effort and materials, speeding up structural studies and deciphering molecular mechanisms of health and disease. The system will be adapted for eukaryotic cells to study human origins and complex drug targets.
Scientists at Queen Mary University of London have discovered a PER:PER protein pair required for circadian clock function in fruit flies. This finding may also apply to mammals, including humans, with implications for regulating our biological clocks.
Scientists have decoded the structure of a needlelike protein complex on Shigella bacteria, essential for infection, revealing new insights into the mechanism of bacterial injection systems that could lead to new drugs.
Researchers at the University of Illinois have identified and visualized signaling pathways in protein-RNA complexes to understand how the genetic code is set in all organisms. The study uses molecular dynamics simulations and visualization software to analyze the optimal communication pathways, revealing modules and local communities ...
Researchers at VIB have identified a molecule that can form the basis for a new therapy for Alzheimer's disease. By targeting the Aph1B γ-secretase complex, they hope to develop a medicine that can prevent the formation of amyloid plaques and stop the progression of the disease.
Scientists at Stanford University School of Medicine have identified a protein complex that plays a pivotal role in controlling the ability of embryonic stem cells to become any cell type. The finding is an important advance in harnessing the unique abilities of embryonic stem cells to treat disease and generate replacement tissue.
Researchers at Penn School of Medicine found that cells reorganize their internal skeleton to adjust their shape in response to external forces. This discovery validates a common theory in cell biology and has implications for understanding certain diseases, including cancer.
The structure of the Mre11 protein bound to DNA has been revealed, showing how it recognizes and remodels broken DNA strands. This breakthrough provides insight into the essential function of Mre11 in homologous recombination, a critical method for repairing double-strand breaks.
Researchers at Stanford University have made significant progress in understanding how the TRiC molecule folds proteins, a crucial step for cellular health. The study reveals that the TRiC lid opens like an iris, transferring rotation to the interior of the chaperonin, where protein folding occurs.
Researchers identified a gene that controls the proper development of synapses in fruit flies, which may help explain how they go wrong in humans. The findings suggest that a protein complex helps regulate synaptic growth by decommissioning receptors that respond to pro-growth signals.
A team of Canadian researchers has completed a massive survey of the network of protein complexes that orchestrate the fundamental processes of life. The study reveals protein complexes never before observed, including those implicated in diseases such as cancers and degenerative neurological disorders like Alzheimer's and Huntington's.
The Stowers Institute's Workman Lab has characterized a novel histone acetyltransferase protein complex called ATAC, which plays a crucial role in regulating chromosome functions. The study provides insight into the ATAC complex's functions and its potential link to human diseases such as developmental defects and cancers.
A study published in PLOS Biology reveals that multiple Arp2/3 regulatory proteins play distinct roles in regulating actin networks, which are crucial for cellular processes such as cell migration and intracellular transport. The research provides new insights into the coordination of protein activities to generate complex actin networks.
A study at Cincinnati Children's Hospital Medical Center reveals that a protein recycling system failure may be linked to the development of certain diseases, such as cancer and heart disease, as well as birth defects. The Retromer Complex plays a critical role in delivering signaling proteins to tissue-building sites.
Researchers demonstrate ability to attach gold nanoparticles to proteins, forming protein-gold arrays for deciphering protein structures, identifying functional parts, and targeted drug delivery. Applications include catalysts for biomass energy conversion and precision vehicles for tumor targeting.
The study reveals that a combinatorial action of multiple protein domains is required to read histone modifications, targeting the Rpd3S complex to deacetylate transcribed chromatin. This finding has significant implications for understanding and treating Huntington's disease and other neurodegenerative disorders.
Researchers at the Salk Institute have discovered a novel RPA-like complex that specifically targets the short single-stranded DNA tail end of yeast chromosomes. This complex helps maintain telomere integrity and prevent premature senescence or cancer development.
Researchers at Brown University have solved the structure of a DNA-protein complex that aids in site-specific recombination, a process that allows mobile DNA to cut into chromosomes. The discovery provides new insights into how this process shapes species over time and its role in spreading antibiotic resistance and certain diseases.
Researchers can now identify protein-DNA interactions in complex organisms using a freely available protocol developed by Dr. Marian Walhout and her colleagues. Additionally, the MuDPIT method enables the identification of rare proteins in complex mixtures.
Researchers have discovered a protein complex called Smc5/6 that plays a crucial role in repairing damaged DNA and untangling chromosomes before cell division. The complex is involved in two distinct pathways, one for repair and the other for untangling, and its function has significant implications for understanding genetic stability.
Researchers have identified over 1400 proteins in liver cells of mice, mapping their locations in ten different compartments. The study's findings show that around 40% of these proteins also appear in other cell organs, suggesting a high degree of conservation across species.
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.
The study provides a nearly complete parts list of all the machines in yeast, including 257 previously unknown machines and new components of existing ones. It also reveals how cells dynamically assemble and disassemble machines to respond to environmental challenges.
A new mass spectrometer design will enable scientists to analyze intact protein complexes in seconds, avoiding sample loss and improving research efficiency. This breakthrough technology could revolutionize fields like proteomics, virology, and nanotechnology.
Recent studies have shed light on RISC assembly in humans, a process crucial for gene expression and regulation. The research found that RISC components are assembled from individual genes to form functional complexes.
A mutation in ankyrin-B gene causes cardiac arrhythmia, leading to sudden death in young people. The disorder disrupts calcium balance in heart muscle cells, making patients vulnerable to arrhythmias.
A study has identified a new molecular chaperone involved in assembling the enzyme complex I of mitochondria. The research found that B17.2L is a key protein required for this process and that it is mutated in patients with progressive encephalopathy.
The discovery of CD147 reveals a new component regulating the production of A-beta peptides, which form amyloid plaques. The study highlights the importance of understanding membrane protein structures to combat Alzheimer's research.
In archaea, a specialized enzyme uses RNA as a guide to pseudouridylate specific RNA molecules. This modification impacts the stability, localization, and translation efficiency of target RNAs.
Researchers at the Weizmann Institute of Science have determined the structure of a protein complex on retroviruses that enables them to infect cells. The complex undergoes a radical change in shape as it attaches to cells, and its arrangement is unlike other known viral envelope protein structures.
Researchers at Purdue University have identified a plant protein complex that triggers cellular growth and development, similar to animal development. The discovery opens new avenues for understanding plant growth and potentially designing plants with enhanced protection against insects and disease.
Scientists at EMBL have developed a new model for protein-complex interactions in yeast, revealing that key components are produced ahead of time and assembled as needed. This discovery sheds light on the dynamic behavior of cellular machines and offers potential applications in studying human and animal biological systems.
Moleculizer is a powerful tool for simulating intracellular biochemical networks, enabling accurate prediction of protein complexes and reactions. The software meets a crucial need in biologists, providing meaningful data for research and analysis.
Researchers have discovered that actin acts as a binding protein in the nucleus, recruiting other proteins to facilitate DNA transcription. This process is crucial for cellular activity and understanding its dysregulation is essential for developing new treatments for diseases like cancer.
The National Institute of Standards and Technology (NIST) has issued a new clinical standard to help manufacturers develop and calibrate assays that measure specific protein concentrations in patient blood samples. This standard, SRM 2921, is expected to reduce variations in clinical test results by as much as 50-fold.
Researchers at Purdue University have successfully crystallized a fat-soluble protein using a synthetic detergent and synthetic fat, overcoming a 20-year hurdle. This breakthrough could lead to significant advances in understanding diseases by studying the structure of these proteins.
Researchers have solved the structure of the pre-budding complex, a set of proteins that plays a key role in forming vesicles on the cell's endoplasmic reticulum. The study reveals how the complex assembles on the ER membrane and initiates the process of membrane cargo capture and vesicle budding.
Researchers found that abnormally short DNA sequences on chromosome 4 interfere with the function of a protein complex, leading to over-activity of nearby genes. This discovery provides insights into novel ways genes can influence disease and may lead to new treatments for FSHD.
Researchers at Brown University have discovered that the Arp2/3 protein complex plays a critical role in regulating the first step of human blood clotting. The complex drives platelets to change shape, forming long arms that grab onto other cells and fibrin, ultimately leading to clot formation.
Researchers have identified 31 novel microRNAs and their associated protein complexes. The discovery reveals a possible link between the pathway of miRNA activity and the progression of spinal muscular atrophy, a common childhood neuromuscular disorder.
Scientists have identified over 100 new protein machines in baker's yeast, revealing a third of the genome's complex relationships between proteins. The study provides insights into cellular functions and tasks performed by molecules.
A team at Cellzome developed a novel approach to systematically use protein interaction maps in drug discovery, enabling researchers to better assess protein roles and predict drug effects. The yeast proteomic map provides a framework for integrating data from literature and experiments.
Researchers have determined the atomic structure of the Arp2/3 complex, a protein responsible for initiating actin filament growth in moving cells. This discovery provides insights into cellular movement mechanisms and has implications for understanding various biological processes, including immune responses and neural development.
The project aims to catalog the HLA gene complex and explore its differences among populations worldwide. The goal is to create a searchable database linking multiple interacting genes with function, ethnicity, and disease.
The BRCA1 protein is at the catalytic heart of a vital DNA control complex that coordinates physical access to DNA for gene transcription. Mutant BRCA1 can lead to cancer by interfering with this complex.
Researchers developed an algorithm to calculate protein association rates and increase affinity by genetically determining protein design. The new system may lead to diverse medicinal applications, including antibody detection.