Articles tagged with Protein Complexes
A new research training group will investigate intrinsically disordered proteins, crucial for human function and disease development. The group aims to unravel protein structures and functions using state-of-the-art techniques.
Researchers at the University of Leeds have identified a new internal regulator that helps control the body's response to fight infection. The discovery has the potential to help find new drugs to tackle autoimmune diseases, such as lupus and scleroderma, by suppressing the immune system.
Researchers discovered that a deficiency of TSC2 produces dysfunctional molecules leading to PAH. The protein's role in maintaining healthy pulmonary blood vessels has significant therapeutic implications.
Scientists have successfully assembled protein cages that can be readily disassembled yet withstand extreme conditions. The breakthrough uses gold to overcome geometrical and complexity challenges in creating these nanoscale structures.
Researchers at CNIO describe the RUVBL1-RUVBL2 ATPases as the 'energy engine' in the co-chaperone R2TP, regulating access to ATP for energy production. The study found a gate-like structure in RUVBL2 that controls energy exchange, coupled to the assembly of mTOR complexes.
Researchers at JILA have developed a fast and gentle method to prepare DNA samples for imaging in liquid, revealing detailed structures of protein-DNA complexes. The process, which takes just five minutes, preserves the mechanical properties of DNA and produces high-resolution images of DNA's iconic double helix structure.
A team of researchers has identified a protein complex called Lubac that marks misfolded proteins, stopping them from interacting with other proteins and directing them towards disposal. This discovery holds promise for the development of new therapeutic approaches to treat neurodegenerative diseases such as Alzheimer's and Parkinson's.
Researchers at Berkeley Lab have revealed the structure of the NADH dehydrogenase-like complex (NDH), a crucial protein in photosynthesis. This breakthrough will allow scientists to explore how the complex functions and could lead to improvements in sustainable bioproducts, including plastic alternatives and biofuels.
Researchers at Penn State have identified a complex of proteins crucial for the maturation of the malaria parasite's sexual stage, which is required for transmission to mosquitoes. Disrupting this complex inhibits the parasite's ability to mature and infect mosquitoes, offering a new tool in the fight against malaria.
Researchers discovered a new class of complex folding molecules that form spontaneously without evolution or design. The molecules' unique structure suggests that complexity can emerge on its own, potentially revolutionizing our understanding of molecular folding and the origin of life.
Researchers have discovered a mechanism that enables flowering plants to 'remember' changes in their environment, triggering flowering in response to stress or seasonal changes. The PRC2 complex, containing the VRN2 protein, detects environmental signals and becomes stable under challenging conditions.
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 team of researchers has uncovered a critical mechanism for transporting proteins into the mitochondria, which are responsible for producing energy in cells. The discovery reveals that two J-proteins play a key role in targeting precursor proteins to specific receptors on the outer mitochondrial membrane.
A study published in Nature Cell Biology reveals the importance of the CENP-T pathway in ensuring accurate and timely chromosome segregation during cell division. The research, led by Osaka University, shows that this pathway is essential for successful mitosis and could lead to therapeutic options for diseases involving dysfunctional ...
Researchers have unraveled the complex process of how black widow spiders transform proteins into steel-strength fibers. They found that spider silk proteins form hierarchical nano-assemblies, potentially required for creating strong fibers.
Scientists have imaged the Ebola virus protein structure at near-atomic resolution, revealing a complex with individual RNA nucleotides and amino-acid side chains. This clarity may help find targets for antiviral drugs, one step closer to understanding how the whole virus works.
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.
A study published in Nature Structural & Molecular Biology reveals that the Arp8 module of the INO80 complex serves as a linker DNA sensor driving chromatin remodelling. This process enables gene expression adaptations by stimulating nucleosome repositioning, which has implications for cancer therapy.
A Kanazawa University-led team used high-speed atomic force microscopy to study GroEL's mechanism, finding two alternative pathways for the protein-GroES interaction. The research suggests a more active role for the football-shaped structure in protein folding, challenging conventional models of molecular chaperone function.
Researchers discover mTORC1 regulates cell growth and metabolism in developing T cells, favoring development of unconventional T cells. Disrupting mTORC1 leads to metabolic changes, altering T cell fate.
A research team at TUM has reconstructed the protein complex responsible for transport within cilia, crucial for cellular movement and organ development. The study reveals a minimal combination of four proteins that start the engine of intraflagellar transport.
Researchers found that the yeast protein Nhp6 helps unfold nucleosomes in humans, similar to its function in yeast. The study suggests that humans may possess a homologue of Nhp6 that assists the FACT complex in regulating gene transcription and detecting damaged chromatin.
Scientists have identified a critical function of the PDK1 signaling pathway in cancer cells, which regulates the formation of a three-protein complex that facilitates purine production and thiamine synthesis. This discovery may lead to new insights into the causes of metastasis and potential ways to prevent it.
Researchers have identified a new gene, ari-1, linked to aortic aneurysms in humans through a fruit fly study. The study found that mutations in the ari-1 gene disrupt mechanical sensing mechanisms in the body, leading to abnormal nuclei shapes and potentially contributing to the development of aortic aneurysms.
Researchers have determined the high-resolution structure of R2TP, a complex involved in key processes for cell survival. The study reveals that R2TP forms complexes with mTOR and other related kinases by interacting with HSP90.
Researchers at Penn State have identified key steps and proteins involved in cellulose synthesis, a crucial process for biofuels. The study's findings may lead to more efficient breakdown of cellulose for renewable energy production.
Researchers from Delft University and EMBL Heidelberg witness the formation of DNA loops by a single protein complex called condensin, resolving a heated debate. The process involves condensin reeling in DNA to form loops, which are then extruded to compact the genome.
Researchers investigated the evolution of small heat shock proteins (HSPs) that regulate cell operations. They found that changes in protein structure and assembly affect their ability to assemble into dodecamers, revealing fundamental principles governing protein function and evolution.
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.
Researchers at the University of Wisconsin-Madison identified the structural basis for how tightly bound protein complexes are broken apart to become inactivated. The structure shows that TIRPL can attack active PP2A complexes, changing their conformation and making them fall apart robustly.
Researchers discovered that Tau protein interacts with and disrupts cell membranes, forming toxic complexes that induce neuronal toxicity. The complexes are made up of Tau proteins and phospholipids from the membrane, and can be taken up by neurons more readily than the fibril form of the protein.
Researchers from the University of Freiburg successfully identified the molecular composition of calcium-ATPases, crucial for controlling various Ca2+-dependent processes in cells. The discovery highlights the essential role of novel subunits Neuroplastin and Basigin in regulating Ca2+ clearance.
Researchers at the University of Würzburg have uncovered key details of how Myc proteins work inside tumor cells, revealing their crucial role in cancer development. The study found that an enzyme called polymerase-associated factor 1 (PAF1) plays a significant role in amplifying Myc protein activity.
Researchers at Cincinnati Children's Hospital Medical Center have identified Polycomb Repressive Complex 1 (PRC1) as a key molecular switch that activates healthy sperm production in males. The study reveals that PRC1 sheds reproductive germline gene components, allowing fertile sperm to develop when the time is right.
Researchers have obtained the highest resolution map yet of human proteins critical to DNA function, providing insights into gene research and drug development. The study used cryo-electron microscopy to resolve the structure of transcription factor IIH at near-atomic resolution.
A team of researchers led by Charles Weitz shows that a set of core clock proteins organize into molecular machines that control circadian rhythms. The findings provide a starting point for understanding the clock's machinery and its role in various conditions, including sleep disorders and cancer.
Researchers have discovered that self-assembling protein complexes can form long, stiff filaments through a single mutation. This phenomenon has implications for both biological research and nanoscience, as it may indicate that Lego-like assemblies are more common than previously thought.
Researchers at the Stowers Institute have solved the three-dimensional structure of the synaptonemal complex, a critical protein complex that ensures proper chromosome sorting during meiosis. The structure is composed of two railroad tracks stacked on top of each other, connecting homologous chromosomes and ensuring smooth cell division.
A new mechanism has been identified by researchers where a subset of free 40S ribosomes preserve genetic information needed to produce new ribosomes. This discovery may lead to new therapies for cancer and 5q- syndrome, conditions where cancer cells exploit ribosome biogenesis to proliferate.
The study revealed how Mis18 protein complex controls the accumulation of CENP-A, a protein that collects at the site where chromosomes connect and divide. Researchers determined the molecular mass of constituent proteins to form a functional Mis18 complex, shedding light on its assembly process.
Researchers used mass spectrometric methods to identify proteins influenced by SNPs relevant to type 2 diabetes and AMD. This study provides insights into the molecular mechanisms modulated by regulatory SNPs, contributing to personalized medicine.
Researchers have found a gene mutation that may contribute to unexplained female infertility, affecting DNA methylation and embryonic development. Women carrying the mutation are healthy but may experience recurrent pregnancy loss or developmental disabilities.
Researchers have made a groundbreaking discovery by directly observing the structure of protein machinery in living cells, allowing them to study its functions in unprecedented detail. This breakthrough has significant implications for understanding cellular biology and developing new therapeutic strategies for diseases.
Researchers at VIB and Ghent University have uncovered a novel protein complex that controls plant tissue repair. This breakthrough could enable the efficient cultivation of crops and make them more resistant to parasites like those found in rice, wheat, and bananas.
Researchers at the CNIC have defined the molecular organization underlying energy production in living cells. The discovery sheds light on the regulation of metabolism and reveals a new understanding of the mitochondrial electron transport chain's structure and function.
Researchers found a way to break up p97 complex into its subunits using ASPL protein, which could be a promising new approach to kill proliferating cancer cells. This discovery may lead to the identification of smaller molecules that can disrupt the structure of p97 in a targeted manner.
A team of Japanese researchers has elucidated the structure of the bacterial flagellar motor protein MotA from a hot spring bacterium. The study reveals that MotA forms a tetramer complex with a unique shape differing from previous predictions, and can exist independently of another transmembrane protein MotB.
Researchers have determined the detailed structure of Mitochondrial Complex I, the first and largest complex in the respiratory chain. This breakthrough allows for a deeper understanding of its intricate arrangements and interactions, enabling insights into disease-causing mutations and affected enzyme activity.
Heat shock proteins collide with protein complexes, generating a force that breaks apart damaged or dysfunctional proteins. This study provides new insights into the role of heat shock proteins in maintaining proper protein function and preventing disease.
Researchers created ten large, two-component protein complexes with icosahedral symmetry, capable of encapsulating materials and self-assembling at the atomic level. The structures can be genetically modified to serve as biomolecular machines for drug delivery, vaccines, and bioenergy applications.
Researchers at TUM identified the molecular mechanism of thalidomide, revealing a common link between its teratogenic and anti-cancer effects. The study found that disrupting the protein complex CD147-MCT1 leads to both developmental defects and tumor cell death.
Researchers at OIST Graduate University discovered how E. coli bacteria disassemble their protein complex after cell division, finding a controlled order similar to assembly, and identifying an inner and outer ring of proteins with unique interactions.
Research reveals gene expression is a two-way communication between nucleus and cytoplasm, controlled by the Ccr4-Not complex. This protein complex acts as a messenger to ensure transcription and translation levels are well-balanced.
The study reveals that MCUR1 acts as a scaffold for the MCU complex, binding to both MCU and EMRE to protect cells from calcium overload. MCU complex assembly is disrupted by mutations in MCUR1/MCU binding regions, but small molecules may promote MCU complex assembly despite these mutations.
Belgian scientists developed Virotrap, a viral particle sorting approach that preserves protein complexes during purification. This method catches bait proteins and their associated partners in virus-like particles budded from human cells.
A team of researchers has solved the three-dimensional structure of a gene repression complex, known as the NuRD complex, which plays a role in cancer. The study provides unprecedented detail about the interaction between its components and may help develop strategies to reduce the activity of the complex and combat cancer.
Scientists at Sanford Burnham Prebys Medical Discovery Institute have identified a protein complex that converts
Researchers have identified a crucial protein complex, ASC-1, that guides the development of motor neurons and their target muscles. This breakthrough could lead to new insights into general disease mechanisms and potentially regenerative therapies for conditions like paraplegia.
Researchers proposed a new mechanism for DNA replication called the 'pumpjack' mechanism, which involves a molecular machine with two distinct conformations that rock back and forth to split the DNA double helix. This linear translocation mechanism appears different from previously thought mechanisms in more primitive organisms.
Researchers found that brush border microvilli and stereocilia share strikingly similar interaction modes, despite different functions. The study reveals a common mechanism for the formation of tip-link complexes in both structures.