Research on how proteins bind and work together. Covers membrane-protein assembly, viral infection, molecular imaging, and drugging difficult targets.
A new 3D-structure study reveals BRD4's unexpected ability to bind to chromosomes without a molecular signal, shedding light on its role in cancer and potential treatments. The discovery could lead to a better understanding of BRD4's function and its interaction with other proteins.
Supercomputer simulations reveal the high-confidence structure of kinesin's neck region, which interacts with the microtubule track to bias stepping trajectory. The study provides a vital foundation for understanding cellular transport, with future studies aiming to refine the structural framework.
A team of researchers has shed light on the mechanism of outer membrane protein assembly in bacteria, revealing key conformational changes made by a chaperone protein. The study's findings may help identify new targets for antibacterial agents and improve our understanding of Gram-negative bacteria's resistance to antibiotics.
A study by Goethe University and Universitätsmedizin Frankfurt has found that seminal fluid can facilitate infection of skin cells with the monkeypox virus. The researchers discovered that protein fragments in seminal fluid form fibers that promote attachment of the virus to human cells, increasing the risk of transmission through sexu...
Researchers at Salk Institute develop novel 'dye-cycling' strategy to measure RNA polymerase movement along DNA with unprecedented lengths of time. This breakthrough provides critical mechanical insights into how genes are transcribed in cells, shedding light on the fundamental processes of life.
Researchers at the University of British Columbia have developed a new method to target intrinsically disordered proteins, which are difficult to treat with medication. The approach has shown promise in slowing prostate cancer growth and could lead to new treatments for various diseases.
Scientists at the University of Virginia Health System have developed a suite of AI-powered tools, called YuelDesign, YuelPocket and YuelBond, to transform how new drugs are created. These tools can design drug molecules tailored to fit their protein targets exactly, even accounting for protein flexibility.
HSE researchers train a neural network, GSMFormer-PPI, to predict protein–protein interactions by integrating three types of data: sequence, structure, and surface properties. The model achieves 95.7% accuracy, outperforming popular graph-based models.
TOR protein's molecular switch regulator, SEA complex, has been structurally solved by CNIO researcher Lucas Tafur. The study reveals that SEA doesn't regulate TOR in the way previously thought, providing new insights into understanding cancer and disease prevention.
Researchers have developed a device that cuts sample consumption by as much as 97% while producing high-quality structural data for X-ray crystallography. This innovation enables the study of rare proteins and accelerates drug discovery, unlocking new insights into disease mechanisms.
Researchers have identified a new class of small molecules that boost the cell's natural recycling machinery to destroy an immune-modulating enzyme called IDO1. This approach takes a bolder approach than traditional drug design, eliminating disease-causing proteins altogether and opening up new possibilities for cancer treatment.
Researchers at the University of Plymouth investigate why drugs used to treat other tumours are ineffective against NF2-related schwannoma and meningioma tumours. They explore repurposing clinically tested cancer drugs to target MDR mechanisms, which may lead to effective therapies for patients with these tumours.
Researchers identified a targeted drug that blocks a specific genetic pathway to reverse tumor-driving cellular interactions, potentially restoring DNA function and benefiting patients with synovial sarcoma. The study's findings endorse a promising strategy to improve outcomes for this rare but deadly cancer.
Researchers at the University of Bath develop a peptide fragment that locks alpha-synuclein into its healthy shape, blocking toxic clumps that cause nerve cell death. The breakthrough demonstrates the potential of rational peptide design to transform large proteins into compact drug-like molecules.
Researchers from the Stowers Institute for Medical Research have identified a common process that powers the creation of protein formations that assemble like a 3D puzzle, triggering inflammation and cell death. This 'Catch-22' mechanism may be one of the fundamental reasons why we age.
Researchers developed photo-inducible binary interaction tools (PhoBITs) to precisely control gene expression, cell signaling, and immune responses. PhoBITs enable targeted treatment with minimal side effects, opening new avenues for cancer therapy, immunotherapy, and regenerative medicine.
Researchers found that Fen1 protein improves cell tolerance to alovudine by counteracting the toxic effect of 53BP1. This discovery promises new cancer treatments and biomarkers for cancerous cells with Fen1 deficiency.
The study reveals that four units of ZapA protein form an asymmetric ladder-like structure with FtsZ protofilaments, impacting the alignment of the Z-ring. The interaction between ZapA and FtsZ is dynamic, with cooperative binding and structural alterations, enabling the maintenance of FtsZ mobility.
Researchers have identified a hidden molecular mechanism involving two proteins that allows tumors to resist treatment. A new gelatin-based nanoparticle has been developed to shut down both proteins simultaneously, showing promising results in early studies with mice.
Researchers at Fujita Health University discovered benzaldehyde's mechanism to halt therapy-resistant pancreatic cancer growth and spread. Benzaldehyde prevents key interactions that enable cancer cells' survival and treatment resistance.
Researchers discovered that blocking PRDX1 protein can make ovarian cancer cells more responsive to DNA-damaging platinum therapies. The study suggests targeting PRDX1 could be a viable strategy to improve chemotherapy efficacy.
Göttingen University researchers have discovered previously undetected chemical bonds within archived protein structures, revealing an unexpected complexity in protein chemistry. These newly identified nitrogen-oxygen-sulphur (NOS) linkages broaden our understanding of how proteins respond to oxidative stress.
Researchers at ETH Zurich created an atlas of protein interactions in different tissues, revealing that every fourth interaction is tissue-specific. This knowledge helps identify disease genes and develop targeted drugs with increased specificity.
A new study reveals that protein sources in an animal's diet significantly alter the gut microbiome, with some having extreme effects. The researchers found that diets high in brown rice, yeast, or egg whites led to changes in amino acid metabolism and complex sugar degradation.
Scientists developed a data science framework to understand how cells travel through the body by analyzing chemokines and G protein-coupled receptors. They found that specific positions in structured and disordered regions determine how these proteins bind, allowing for rational alteration of cell migration.
The study reveals new insights into the 'language' of gene expression, identifying key motifs that influence human development and disease risk. By analyzing 58,000 pairs of transcription factors, researchers estimated they identified between 18 and 47% of all human transcription factor pair motifs.
Researchers used cryo-electron microscopy to visualize the dynamic motion of a human chromatin remodeler in action, capturing 13 distinct structures that reveal the full picture of nucleosome sliding. This comprehensive view sheds light on how chromatin remodeling affects gene access and expression.
A machine-learning algorithm named catGRANULE 2.0 ROBOT identifies molecular targets for further researches and therapies in neurodegenerative diseases. The algorithm analyzes protein-RNA interaction to predict potential harm and identify early pathological signals.
Researchers at UCalgary have discovered a protein called CD2AP that may hold the key to reducing Alzheimer's disease risk. Levels of this protein are lower in patients with AD, and its absence affects memory function, particularly in males. The study suggests a sex-dependent link between vascular system health and brain function.
Researchers at Kyoto University have captured the first high-resolution structure of Ebola's nucleocapsid using single-particle cryo-electron microscopy. This visualization reveals sophisticated interactions between structural components, including VP24 and NP proteins, which govern virus assembly, RNA synthesis, and transport.
Scientists at Sanford Burnham Prebys discovered novel fragments of future drugs that selectively inhibit the enzyme VHR, which plays a role in controlling the immune system's response to danger. The findings may lead to the development of new therapies for sepsis and septic shock.
Researchers at Kobe University discovered that the molecule afadin plays a crucial role in cell adhesion by facilitating droplet formation. This process is essential for organs to form properly and tissues to develop, with significant implications for cancer metastasis and tissue engineering.
This study identified PIBP4, a PRA protein, as a crucial component of the PigmR-mediated immune signaling pathway in rice. The absence of PIBP4 and its interacting partner OsRab5a compromised blast resistance by disrupting PigmR's microdomain localization.
Researchers at UCSF have discovered how a unique type of virus called a jumbo phage protects itself inside bacteria. The shield works via a set of secret handshakes that allow only useful proteins to pass through, giving the phage an advantage over regular phages when fighting infections.
A recent study published in Communications Biology reveals that the Sudan virus binds to human cells through a specific protein called NPC1, which enables it to attach with nine times greater affinity than Ebola. This discovery may contribute to the high fatality rate of the Sudan virus.
The dengue virus uses its envelope protein to capture human plasmin, enhancing the permeability of the mosquito midgut. This interaction is crucial for viral infection, and understanding it could lead to innovative approaches to tackle vector-borne viruses.
A new Weizmann Institute study identified all proteins in a stool sample – those from the microbiome, human body, and food – revealing secrets of the intestines and their impact on human disease. The method, dubbed IPHOMED, decodes microbiome activity by showing which proteins come from bacterial strains and amounts.
Proteins form complexes to fulfill their functions, with assembly often beginning during synthesis. Misfolded proteins can lead to cellular dysfunction and diseases; understanding co-translational assembly may help develop new therapeutic approaches.
Researchers have discovered a complex mechanism that allows bacteria to build resistance to antibiotics, involving a KorB-KorA regulatory system. This finding offers a fresh insight into long-range gene silencing in bacteria and provides a potential target for novel therapeutics.
A POSTECH research team found that EGF/EGF-like domains interact with GlcNAc-based biopolymers to achieve strong underwater adhesion without oxidation, leading to durable and reversible bonds.
Researchers developed ProteinReDiff, an AI-powered method to redesign proteins for improved ligand binding. The approach uses initial protein sequences and ligand SMILES strings, reducing reliance on detailed structural data.
Researchers identify Fam102a as a key regulator of both osteoclast and osteoblast differentiation, leading to enhanced osteoblast formation and bone volume. The study reveals significant protein-protein interactions involving Fam102a and Kpna2, shedding light on the critical molecular interactions involved in bone remodeling.
The EPFL team has developed a deep-learning pipeline called MaSIF to design new proteins that interact with therapeutic targets. They have successfully designed novel protein binders that can recognize and bind to drug-protein complexes, offering potential applications in cell-based therapies and biosensors.
Researchers from the University of Guelph studied plant-based proteins and their interaction with fat matrices to improve the quality of vegan cheeses. They found that a blend of pea protein, sunflower oil, and coconut oil created a cheese with a firm texture and lower saturated fat content.
The Zika virus hijacks the host protein ANKLE2 to assist its own reproduction, which is important for brain development. This interaction allows the virus to hide from the immune system and replicate more efficiently.
Researchers developed a new super-resolution microscopic method to investigate the interactions of therapeutic antibodies with target molecules on tumour cells. The study reveals that all four antibodies crosslink CD20 molecules independently of type I or II classification, and that B cells take on a hedgehog shape after treatment.
Researchers at U of T have created SIMPL2, a platform that simplifies detection and improves accuracy of protein-protein interactions. The tool enables the rapid identification of protein interactions, including weak ones, for targeted drug therapies.
Research team at the University of Basel uncovers new mechanisms in blood vessel formation, highlighting the critical role of dynamic forces and protein regulation. The study reveals that contraction forces enable continuous vascular lumen formation, while Rasip1 plays a key role in initial steps of lumen formation.
Researchers found that flavonoids in everyday foods like green tea and dark chocolate regulate glucose levels through gut receptors, paving the way for better health management. The study highlights the potential of polyphenol-rich diets to improve public health and offers a foundation for developing new therapies.
The researchers have revealed the precise positioning of RNA molecules and their interactions with the protective coat. This breakthrough enables the design of new drug molecules capable of binding to the protein coat, weakening viral RNA and inhibiting influenza virus replication.
Researchers at Chung-Ang University have identified a crucial role for specific tRNA fragments in cancer progression, revealing their ability to regulate gene expression and influence tumor growth. The study suggests that these fragments could serve as biomarkers for early-stage cancer detection and targets for therapeutic interventions.
Researchers capture dynamic interplay between RNA polymerase and ribosome, revealing emergent behaviors and communication between the two molecular machines. The study offers new insights into how transcription and translation work together, potentially leading to new ways to fight bacterial pathogens.
Max Delbrück Center researchers have uncovered new features of the molecular architecture of synaptic vesicles using cryo-electron tomography. The study reveals a persistent association between V-ATPase and synaptophysin, suggesting an important function in neurotransmission.
Researchers found effective peptidomimetics that can bind to and inhibit Aurora-A's interaction with TACC3 without inhibiting its enzymatic function. This inhibition also showed promise in targeting a different protein-protein interaction between N-Myc and Aurora-A, which is crucial in childhood brain cancers.
The review explores the impact of extracellular matrix (ECM) geometry on immune cell behavior and treatment efficacy. Specific ECM configurations, known as Tumor-Associated Collagen Signatures (TACS), create physical barriers that limit immune cell access to tumors.
Researchers at The Jackson Laboratory have developed a new combination of imaging and computational methods to study immune cell interactions. The approach reveals that interactions between immune cells in the vicinity of breast cancer or melanoma can predict immune responses and patient outcomes.
A recent study published in Cell reveals that nearly one in six disease-causing mutations leads to proteins mislocalizing within the cell. The research team developed a high-throughput imaging platform to assess protein location and found that breakdowns in protein stability are a major driver of misplaced proteins.
A new AI tool called PIONEER has been developed to predict protein-protein interaction mutations in hundreds of diseases, including dozens of cancers. The tool allows researchers to navigate the interactome for over 10,500 diseases and identify potential drug targets.
Researchers developed TETRIS, a technology that maps out diverse protein interactions in cells using DNA barcodes, capturing higher-order interactions linked to aggressive cancers. This enables precise diagnostics and tailored therapies.
Researchers at UCSF used cryogenic electron microscopy to study the protein TGF-Beta, which plays a crucial role in development and cancer. They found that TGF-Beta can signal even when bound to a 'straitjacket' within the cell membrane, challenging decades-old dogma on its function.