Articles tagged with Cryo Electron Microscopy
Researchers from IOCB Prague uncover the mechanism behind a unique termite defense, where worker termites sacrifice themselves to kill attackers. The discovery sheds light on the enzyme's durability and functionality in harsh conditions.
Researchers have used cryo-electron microscopy to reveal the structural basis of how cells regulate ferritin, a protein that stores iron. This understanding could lead to the development of drugs that block ferritin's interaction with NCOA4, slowing down aggressive cancer cells.
Researchers have visualized a molecular complex that loads a 'clamp' onto DNA to ensure accurate replication. This discovery sheds light on the intricate mechanisms of DNA replication and could improve understanding of related health conditions.
Researchers have identified the critical step in NMDAR's routine where it rotates into an open formation, enabling electrical signals crucial for cognitive functions. This discovery may pave the way for drug compounds that can correct faulty NMDARs, potentially treating conditions like Alzheimer's and depression.
Researchers at UNIGE have discovered how yeast cells respond to physical stress on their membranes. Cryo-electron microscopy revealed that specific lipid domains can stabilize and trigger cellular responses to mechanical stimuli. This study sheds light on the role of membrane compartmentalization in cell survival.
Researchers have discovered how a neutralizing antibody blocks measles virus infection by arresting the fusion process. The study's findings may also be relevant to other viruses with pandemic potential, such as Nipah and parainfluenza viruses.
Researchers used advanced imaging technology to reveal the atomic structure of an enzyme that neurons use to communicate. The study provides new insights into synaptic function and may lead to therapeutic targets for epilepsy and other neurological conditions.
Researchers identified a complex of two proteins called Gabija that enhances the blockage of phage replication in bacteria. The study found that one protein alone can disable a phage's DNA, but the complex formed with its partner protein is more effective at preventing phage takeover.
A study published in PNAS reveals the structure of a protein linked to neurodegenerative disease Niemann-Pick type C, which accumulates cholesterol within cellular compartments. The research sheds light on the complex mechanism of cholesterol distribution and its role in maintaining optimal levels.
Researchers at ISTA have discovered the composition of poxviral cores, a key factor in their infectivity. The study's findings could lead to the development of new therapeutics targeting the viral core.
Researchers have identified and detailed the structure of Mcf1, a bacterial toxin that kills insects by disrupting essential proteins in their cells. The discovery has implications for developing new organic pest control agents and may also shed light on human diseases.
Research reveals that a small subset of bacterial cells produces deadly toxins while sacrificing themselves for the benefit of their comrades. The bacteria use a temperature-sensitive genetic switch to synchronize toxin production with cell enlargement, ensuring an efficient strategy for infection.
Researchers have solved the molecular structure of a complete tailed virus with a flexible tail at unprecedented detail. This discovery has significant implications for phage therapies and the development of alternative treatments to antibiotics.
Researchers at Johannes Gutenberg University Mainz discovered a unique cryptochrome protein in marine bristle worms that distinguishes between sunlight and moonlight. The protein's structure reveals an unusual light-induced change from dimer to monomer arrangements, allowing it to synchronize reproduction with lunar phases.
Researchers at Max Planck Institute of Molecular Physiology developed an innovative imaging technique to visualize the cardiac thick filament in its native environment. The resulting high-resolution image reveals new insights into the molecular organization and function of the sarcomere, a crucial component of heart muscle contraction.
Researchers used cryo-electron microscopy to capture detailed images of key receptors, unveiling their interactions with molecules and signaling mechanisms. This study provides significant insights into a crucial receptor family within the immune system, potentially paving the way for innovative treatments.
The discovery sheds light on the mechanism of phosphate release from actin filaments, which is crucial for cell movement and disassembly. The researchers found that phosphate escapes through a molecular backdoor in the filament core, but the door remains closed for most of the time.
The study reveals a quantum switching mechanism of LHCII, which regulates energy transfer quantum channel in response to lateral pressure and conformational change. This mechanism enables high efficiency in photosynthesis and balanced photoprotection.
Researchers have discovered how plants pass along chemical markers that instruct cells on using DNA codes, a process known as epigenetic inheritance. The study reveals the role of protein DDM1 in making way for enzymes that add regulatory marks to new DNA strands, preserving genetic controls across generations.
Researchers reconstructed six states of a rotary sodium ion pump using cryo-electron microscopy. The study found non-uniform rotation behavior due to structural interference between the rotor and stator components. This reveals a unique molecular mechanism of the rotary sodium ion pump.
Scientists have developed a way to program virus particles' size and shape using DNA origami nanostructures, potentially advancing vaccine development and drug delivery. The approach uses electrostatic interactions between DNA nanostructures and capsid proteins to create user-defined assemblies.
Researchers discovered that extracellular cytochrome nanowires are widespread in prokaryotic microbes, including both bacteria and archaea. The findings suggest that these nanowires, composed of a long chain of cytochrome proteins, play a crucial role in microbial metabolism by facilitating efficient electron transfer.
The study reveals that the GABA transporter structure is facing the cytosol and bound to a GABA molecule, sodium, and chloride ions. This binding mechanism is crucial for understanding GABA recognition and release into neurons.
Scientists have gained high-res structural insights into a key bacterial enzyme to develop new drugs that target its weaknesses and suppress disease-causing bacteria. The enzyme Lnt is not found in humans and has huge potential as a therapeutic target with fewer side effects for patients.
Researchers used cryo-electron tomography to study the dynein motor protein, revealing new details about how it generates force and coordinates with other proteins. This knowledge may help develop treatments for diseases related to cilia dysfunction, such as fertility issues and lung disease.
Researchers discovered a protein complex called FERRY that plays a crucial role in transporting messenger RNA in neurons. The study provided evidence of the transport of mRNA using Early Endosomes (EEs) and a novel mode of binding RNA via coiled-coil domains.
A team at Penn State has produced high-resolution images of SARS-CoV-2's protease protein and polyprotein complex. The research reveals a consistent order in which the proteins are cleaved, potentially supporting more efficient antiviral drugs.
Researchers at IOCB Prague have determined the first cryo-EM structures of a surface receptor of Trypanosoma brucei gambiense in complex with human complement factor C3. This discovery sheds light on how the parasite avoids clearance from the human bloodstream and survives within the immune system.
Researchers have identified the structure of the circadian rhythm photosensor and its target in fruit flies, revealing key components of the circadian clocks. The study also shed light on how DNA damage is repaired in a cell and found genetic variations that help flies adapt to changing latitudes.
Researchers use cryo-electron microscopy to visualize a sirtuin enzyme bound to a nucleosome, clarifying how it accesses DNA and histone proteins to modulate gene expression. The study provides insight into the function of SIRT6 in humans and other animals.
Researchers at the University of Tokyo have discovered the 3D structure of TnpB, a protein involved in genome editing and a probable precursor to the CRISPR-Cas12 enzyme. The study reveals how TnpB recognizes and cuts DNA using a unique pseudoknot shape similar to that found in guide RNAs of Cas12 enzymes.
Researchers from PSI deciphered the structure of an ion channel found in the eye while interacting with calmodulin, a protein that enables cell response to calcium fluctuations. This interaction is believed to be responsible for achieving remarkable sensitivity to dim light.
Researchers at UC San Francisco have created the first molecular-level picture of how an odor molecule activates a human odorant receptor, opening doors to creating novel smells. This achievement paves the way for new insights into biological processes, including fragrances and food science.
Scientists at Aarhus University and Berkeley Laboratory developed a method called RNA origami to design artificial RNA nanostructures. The technique allowed for the discovery of rules and mechanisms for RNA folding that will make it possible to build more ideal RNA particles for use in RNA-based medicine.
Researchers have unveiled the structure of DREADDs, a neural tool that enables precise control over neurons. The new findings will allow for further refinement and optimization of the tool, paving the way for innovative treatments for brain disorders such as schizophrenia, substance abuse, and Alzheimer's.
Researchers create advanced imaging-based method for studying mitochondria, enabling detailed mapping and measurement of structural changes. This technique has potential applications in understanding diseases such as Alzheimer’s, Parkinson’s, and cancers where mitochondrial function is disrupted.
The São Paulo School of Advanced Science on Cryogenic Electron Microscopy will be held at the University of São Paulo from July 10-27, 2023. The event will cover theoretical and practical foundations of advanced CryoEM techniques, featuring renowned researchers and hands-on practical sessions.
Researchers at Osaka University used cryogenic electron microscopy to study the structural change of the centromere during cell division. The study revealed a complex interaction between proteins involved in cell division, providing new insights into the correct division of chromosomes.
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 have shed new light on viral genome replication machinery, revealing its intricate structure at atomic resolution. The study, published in PNAS, provides essential insights into the assembly, dynamic operation, and potential therapeutic targets of this complex machine.
A potent plant toxin called albicidin has emerged as a strong new antibiotic candidate, effective in small concentrations and highly potent against pathogenic bacteria. Its unique mechanism targets the bacterial enzyme DNA gyrase, which is essential for cell function.
Researchers at St. Jude Children's Research Hospital used cryo-electron microscopy to capture the first 3D structure of SPOP, a protein mutated in prostate and endometrial cancers. The study revealed previously unknown interfaces that harbor cancer-causing mutations, shedding light on how SPOP drives cancer.
Researchers at Aston University have created the world's first computer reconstruction of a virus, including its complete native genome. This breakthrough could lead to the development of targeted treatments to kill bacteria that are dangerous to humans, reducing the threat of antibiotic resistance.
Researchers used high-voltage electron microscopy to image frozen tokyovirus particles in detail, revealing a novel capsid protein network and scaffold protein component. The study provides new insights into the structure and function of giant viruses, which are larger than small bacteria.
Researchers have gained a better understanding of the structures and functions of Andhra gene products, paving the way for custom phages for therapeutic applications. The high-resolution knowledge of the virus structure is crucial for developing targeted treatments against Staphylococcus epidermidis infections.
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.
Scientists have clarified the structure of a new protein complex that catalyses energy conversion processes in photosynthesis, known as Photosystem I. The research reveals that two monomers can join together as a dimer, leading to improved hydrogen production in certain plant species.
Poliovirus researchers at Umeå University have gained a new understanding of how the virus behaves in infected cells, revealing key protein roles and cellular processes involved. This breakthrough could lead to the development of new antiviral treatments and vaccines targeting the autophagy system.
Researchers used advanced imaging techniques to understand the structure of bacterial propellers, which are made of a single protein. The study reveals that bacteria push themselves forward by coiling these appendages into corkscrew shapes, and that similar structures have evolved independently in archaea.
Researchers developed a new method combining cryo-EM with iDPC-STEM, achieving sub-nanometer resolution for protein structures. This technique expands possibilities for structural analysis of heterogeneous and single-particle samples.
Researchers captured first image of antigen-bound T-cell receptor complex with bound antigen at atomic resolution. The study reveals no significant structural changes in the receptor after antigen binding, sparking further investigation into the signaling pathway activation mechanism.
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.
Researchers uncovered the sophisticated mechanism of bacterial Tc toxin's action by utilizing cryo-EM and protein NMR 3D snapshots. The subunits assemble like a syringe, triggering the release of toxic enzymes that disturb cytoskeleton regulation, leading to paralysis.
Researchers discovered that CAMSAP2 proteins utilize phase separation to form an 'aster' structure, which then organizes into a microtubule network. This process is crucial for the formation of specialized cell shapes, such as those found in heart muscle and nerve cells.
New study reveals how GABA A receptor antibodies inhibit neurotransmitter binding, leading to hyperexcitability and symptoms like twitching and seizures. The findings pave the way for developing effective therapies and further investigations into other diseases.
A research team led by Professor Youdong Mao has developed a new method using time-resolved cryo-electron microscopy and machine learning-based 4D reconstruction to visualize the USP14-proteasome system in atomic detail. This reveals a 'multiverse' of parallel reality pathways, allowing for targeted inhibition of cancer cells.
A team of researchers has combined expansion microscopy and stimulated Raman scattering microscopy to create a new imaging technique called MAGNIFIERS. This allows for the high-resolution imaging of biomolecules, including proteins, lipids, and DNA, at the nanoscale.
Researchers from Max Planck Institute have determined the 3D structural details of the human CCAN complex, highlighting its unique features and implications for interactions with centromere protein A. This discovery raises fundamental questions about creating artificial chromosomes.
Researchers find NLRP3 protein forms filament that grows in one direction, allowing for targeted treatment of chronic inflammatory diseases. The discovery could potentially stop inflammation at the 'growing end', bringing relief to those suffering from conditions like Alzheimer's disease.
Researchers have developed a new approach to studying RNA molecules using nanotechnology and cryo-electron microscopy (cryo-EM), enabling the analysis of RNA subunits with unprecedented resolution. This breakthrough has significant implications for fundamental research, drug development, and RNA therapeutics.