Articles tagged with Protein Complexes
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Researchers have revealed the architecture of a protein complex called CCAN, which plays a foundational role in chromosome segregation during cell division. The study found that each subcomplex needs to touch many others to be functional, forming a mesh structure crucial for kinetochore assembly and stability.
Cell membranes deform when viruses detach and during cell division, thanks to the ESCRT-III protein complex forming a molecular spring. Researchers used high-speed atomic force microscopy to observe the complex's movements in real-time, validating their theoretical models.
Researchers led by Assia Shisheva found a novel interaction partner of the ArPIKfyve-Sac3 complex in the brain, which binds Synphilin-1 and prevents its aggregation. This discovery may lead to new therapeutic approaches for reducing cytoplasmic aggregates in Parkinson's disease.
Researchers at CNIO have identified the role of SMC5/6 protein complex in cancer suppression and premature aging, revealing its importance in limiting carcinogenesis and promoting healthy lifespan. The study found that mutations in this complex can lead to tumours and accelerated aging in mice.
Monash University researchers have discovered the mechanism behind how proteins enter mitochondria, a crucial step in cellular energy production. The breakthrough uses novel technology to visualize the process at an atomic level, enabling scientists to study fundamental biological pathways.
A study published in Nature has identified nearly 1,000 common protein complexes shared by most kinds of animals, revealing deep evolutionary relationships. These findings have significant implications for understanding the genetic basis of diseases such as Alzheimer's, Parkinson's, and cancer across different species.
Researchers have mapped the 3-D atomic structure of a two-part protein complex that controls the release of neurotransmitters from brain cells. This discovery could help launch new research on drugs for treating brain disorders such as depression, schizophrenia and anxiety.
Researchers have developed a new tool to study TORC2, a protein critical for cell growth and cancer development. By understanding its structure and function, scientists can identify potential inhibitors of this complex, which could lead to the development of new anti-cancer agents.
Researchers discovered that a protein called Tmem231 plays a crucial role in regulating ciliary membrane composition and function. This study sheds light on the mechanisms underlying Meckel syndrome and other human diseases characterized by defects in cilia.
Researchers at KAIST have solved the mystery of how NSF disassembles a SNARE complex. They found that NSF requires only one round of ATP hydrolysis to unwind the complex, contrary to previous theories. This discovery sheds new light on membrane fusion and vesicle traffic in cells.
Researchers at Johns Hopkins Medicine have created a 3D model of the ORC protein machine, which helps prepare DNA for duplication. The model reveals that ORC is not always 'on' as previously thought, and no one knows how it turns on and off.
Researchers have identified a protective mechanism for tail-anchored proteins, which are crucial for various cellular functions. The study reveals a dimeric structure of the transport molecule Get3 that shields these proteins from harmful aggregation and guides them to the correct membrane location.
Researchers at Johannes Gutenberg Universitaet Mainz identified RAB3GAP complex as a key factor in autophagy, a process that breaks down cellular proteins and organelles. This discovery may enable innovative approaches to treat neurodegenerative diseases like Alzheimer's.
Researchers at RIKEN have identified a key mechanism in which brassinosteroids, expensive plant hormones, control plant height and growth. The study reveals that BIL1, a master switch regulating 3,000 genes, interacts with BSS1 to regulate brassinosteroid signaling.
Researchers at Columbia University have developed a light microscopy method to image protein synthesis and degradation in living tissues and animals. The technique, coupling stimulated Raman scattering (SRS) microscopy with metabolic labeling of deuterated amino acids, allows non-invasive visualization of protein metabolism.
Biochemists elucidate protein complex structure in the respiratory chain, a crucial process for cellular energy production. The study reveals how complex I switches between active and inactive forms, shedding light on its role in disease, including Parkinson's and myocardial infarction.
Scientists used a modified form of superabsorbent chemical to expand brain structures, enabling the use of common microscopes for high-resolution imaging. This technique, called expansion microscopy, has potential to study diseases in human brain tissue and answer various scientific questions.
Researchers developed a new technique called proximity ligation assays (PLA) to analyze protein complexes in cancer specimens, which may aid in patient treatment decisions. By focusing on the epidermal growth factor receptor (EGFR), they discovered that patients with high amounts of EGFR protein complexes had a better prognosis when tr...
A team of researchers at Syracuse University developed a multilevel computational approach to simulate the formation and behavior of protein coronas on quantum dots. This breakthrough enables more accurate measurements in various biological applications, such as tumor cell imaging and biomolecule detection.
Researchers have developed a theoretical methodology to solve the 'counting problem,' allowing for the analysis of protein groups in living cells. The study's findings could lead to advancements in disease diagnosis and understanding of protein function.
A team of Penn State researchers has developed a thermoplastic material from squid protein, which can be used in 3D printing and has tunable properties for medical or cosmetic applications. The semi-crystalline thermoplastic exhibits high tensile strength and is a wet adhesive.
Purdue researchers have discovered the structure of the enzyme responsible for producing cellulose, a key breakthrough in understanding plant cell wall composition. The findings could lead to improved methods for breaking down plant materials and creating sustainable biofuels.
Researchers have developed a new method to measure structurally modified proteins in complex biological samples, enabling the analysis of thousands of proteins. The method uses a combination of digestion enzymes and Selected Reaction Monitoring to quantify protein quantities and determine structural changes.
Researchers have uncovered how the NF-κB protein complex is activated, a pivotal step in developing cancer, viral infection and autoimmune diseases. The discovery reveals that two additional events are necessary to switch on NF-κB, paving the way for new drug targets.
A team of researchers found that inflammasomes remain active even after cell death, triggering a rapid inflammatory reaction. This discovery offers potential novel approaches for therapies against diseases such as gout, atherosclerosis, and Alzheimer's disease.
Scientists have determined the three-dimensional structure of a Type VI secretion system export complex in bacteria, offering a potential target for novel antibiotics. The contractile sheath complex functions like a nanosyringe to expel toxins from cells, and its mechanism has been elucidated at sub-nanometer resolution.
Researchers at the University of Toronto have identified a complex of three proteins that regulate brain function and may lead to improved treatments for epilepsy. The discovery has major implications for understanding neurological disorders such as schizophrenia, autism, and neuropathic pain.
The researchers identified the molecular structure of a protein complex that plays an important role in regulating the circadian rhythm. The complex contains a zinc ion, which stabilizes it and may play a key role in regulating metabolic processes.
Researchers have identified a novel protein complex, TPLATE, essential for plant endocytosis, which is unique to plants. The discovery sheds light on the process of endocytosis and its importance in plant cells.
Researchers at Rutgers University–Camden studied microRNAs in common fruit flies to understand the connection between aging and diseases like Alzheimer's. They found that as fruit flies age, more microRNAs accumulate on a protein complex, impacting age-associated events and leading to shorter lifespans.
Researchers at ETH Zurich deciphered the structure of the large subunit of the mitochondrial ribosome, a complex enzyme that deciphers genetic code and assembles amino acids into proteins. The study's success relies on a combination of high-resolution cryo-electron microscopy and chemical cross-linking combined with mass spectrometry.
Researchers have discovered a novel protease complex in bacteria that operates as a molecular motor, with a constant revolutions per minute (RPM) and varying gears to shred proteins. This 'cellular shredder' plays a crucial role in DNA damage repair, gene expression, and protein quality control.
UC Irvine scientists have identified a key molecular gateway for the botulinum neurotoxin, which can be blocked by inhibitor molecules to prevent the toxin from entering the bloodstream. The discovery provides a vital first step toward a pharmaceutical intervention and could lead to preventive treatments for botulism.
The researchers determined the structure of NatA, a protein complex modifying nearly 85% of human proteins, and found it essential for cancer cell proliferation. The team believes their findings will allow them to create an inhibitor that can knock out NatA, potentially curbing cancer growth.
The newly found CLAMP protein plays a crucial role in regulating the X chromosome in male fruit flies, enabling them to develop and survive. By working together with the MSL complex, CLAMP creates a self-reinforcing feedback loop that enhances gene expression, providing a model for understanding how proteins govern gene transcription.
For the first time, a large complex of proteins and RNA has been identified in chloroplasts, which cuts non-coding regions out of messenger RNA to create a protein blueprint. The study reveals that this splicing complex contains 23 different proteins encoded in the cell nucleus.
Researchers developed a structural comparison map for small angle X-ray scattering (SAXS), enabling quick identification of protein structures under various conditions. This technique highlights factors making the biggest difference in structural conformations, allowing for high-throughput screening and tracking of trends.
Scientists have identified a complex of three molecules that regulates the production of defective Huntingtin protein, a key contributor to Huntington's disease. By targeting this complex with pharmaceuticals, it may be possible to directly affect the production of defective proteins and treat the underlying causes of the disease.
A research team has described the architecture of human transcription factor TFIID, revealing its inner workings for the first time. The study used a novel approach inspired by viral replication to produce highly abundant and correctly assembled complexes of the core scaffold.
Researchers have created the first detailed 3D model of the PRC2 protein complex, shedding light on its role in embryonic development and cancer. The model reveals how PRC2 interacts with chromatin and other proteins to regulate gene expression.
Researchers at Aarhus University have solved the long-standing puzzle of haemoglobin structure using high-resolution three-dimensional mapping. This discovery provides essential information on how haptoglobin captures and neutralizes toxic haemoglobin, which can cause kidney damage in diseases like malaria.
Researchers have mapped the molecular-level details of how protein machinery binds and wraps DNA to start replication, a crucial process for cell division. The study sheds light on how this complex choreography is orchestrated by intricate cellular proteins, potentially leading to new ways to fight cancer.
A team from UNC Chapel Hill discovered how a long-studied protein complex influences cell movement and how cells respond to external cues. Cells without the protein complex exhibit altered structure and movement, affecting their ability to sense chemical cues and navigate surfaces.
Researchers at EMBL and IGBMC discovered a ring-like structure in the Elongator protein complex, which holds tRNA in place while introducing chemical modifications to DNA. This ensures accurate protein production. The findings also suggest that the complex employs tools and tricks to perform its tasks inside cells.
Researchers identify genetic alterations in T-ALL that work together to cause the devastating childhood cancer, providing new potential treatment strategies. The study reveals a dynamic interplay between Notch and PRC2 function, showing how deregulation of PRC2 fuels the development of T-ALL.
Researchers at Karolinska Institutet have discovered a new player in the body's defense against cancer, VCP/p97 complex. This complex plays a crucial role in regulating the recruitment of tumor suppressor protein 53BP1 to damaged DNA.
Researchers at University of Georgia discovered that GAUT1 and GAUT7 proteins form a critical part of pectin-synthesizing protein complexes in plant cells. This fundamental discovery opens a new door to converting plants to biofuels and other carbon-based products.
Researchers from CSHL and St. Jude's Research Hospital have discovered new details of how a protein complex contributes to heterochromatin assembly and gene silencing in fission yeast. The team identified a previously unknown substructure at the end of Chp1, which plays a crucial role in heterochromatin formation at telomeres.
Researchers have defined a specific protein complex that allows cells to remove damaged mitochondria via autophagy, a process crucial for maintaining cellular integrity. This discovery highlights the interaction between Hsp90-Cdc37 and Ulk1, which is essential for efficient mitochondrial clearance.
A team of researchers led by Professor Karl-Peter Hopfner has clarified the structure and function of Mot1, a Swi2/Snf2 remodeler that regulates gene expression by removing TBP from DNA. This process enables genes to be transcribed into messenger RNA.
A new study suggests that structural weaknesses in proteins, rather than natural selection, may have led to the evolution of biological complexity. Flaws in protein packing make them more unstable in water, promoting interactions and intracellular teamwork.
Scientists at Yale University used fluorescent stains to create movies of cellular actin filaments disassembling, shedding light on their mysterious process. The study reveals the location of breaks along the filaments, crucial for cell movement and maintenance.
Rockefeller scientists have developed a new polarized microscopy technique that can help deduce the orientation of specific proteins within cells. By harnessing the unique properties of polarized light, researchers have filled in the gaps left by other techniques and made important new discoveries about protein complexes.
A newly discovered biomarker could help doctors diagnose meniscal tears with high accuracy, avoiding unnecessary surgery and medical scans. The biomarker, a fibronectin-aggrecan complex, was found in the knee fluid of patients with painful meniscal tears but not in asymptomatic individuals.
A team of scientists discovered remnants of a protein-chitin complex in Paleozoic-era arthropod fossils, which could revolutionize our understanding of organic fossilization. The findings were made possible by advanced analytical instruments and suggest that the complex may play a critical role in preserving fossils.
A new theory of energy transfer in photosynthesis is being developed based on experimental findings that challenge the traditional dipole-based mechanism. Energy is rapidly and efficiently transferred when dipoles are orthogonally disposed, contrary to previous assumptions.
Researchers watched a fundamental process of cellular organization in living plant cells, where protein complexes create the microtubule cytoskeleton. They observed that these complexes are distributed at the cell membrane and interact with other microtubules to organize the cell shape and structure.
A study by Dr. Klaus Hansen's group at BRIC, University of Copenhagen, reveals that external stressors can activate genes responsible for cellular development and function.
Researchers found a unique genome structure formed by protein complexes that regulate cell-type-specific genes, leading to developmental diseases. Deficiencies in these complexes can cause syndromes like Opitz-Kaveggia syndrome and schizophrenia.
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.