Articles tagged with Ligases
Researchers at St. Jude Children's Research Hospital have discovered the 'double-donut' structure of SPOP, a protein critical to regulating gene expression in cells. The study reveals how certain cancer mutations disrupt this balance, leading to disease progression.
Researchers developed a novel method to immobilize proteins onto magnetic microbeads, allowing precise measurement of binding strength and efficient selection of target peptides. The technique achieved a 10,000-fold concentration in a single sorting step, significantly enhancing the efficiency of drug discovery research.
Developing neurons rely on multiple signaling pathways to migrate from the germinal zone. An antagonistic circuit between Netrin-1 'pushing' and Siah2 'pulling' ensures proper cerebellum development by balancing adhesion and guidance cues.
Researchers developed a simple, cost-effective method to study ubiquitination, a critical protein modification process involved in diverse cellular functions. The Ub-POD method quickly labels targets of E3 ligase enzymes directly in human cells, allowing for the identification of new substrates and expanding therapeutic options for dis...
A new adapter molecule recruits a previously unknown E3 ligase for targeted protein degradation, expanding therapeutic options for cancer and rare diseases. The discovery offers advantages in development due to the molecule's smaller size and potential for tissue-specific application.
Thorsten Hoppe and Jens Brüning received 2.5 million euros in funding from the European Research Council to investigate protein degradation and neural circuits of metabolic control, respectively. Their projects focus on preventing neurodegeneration and developing new drugs for obesity treatment.
Researchers have pinpointed the molecular mechanism by which a large portion of BRCA1 mutations cause cancers in women. The study found that the E3 ligase activity of BRCA1 is crucial in several stages of DNA repair and tumor suppression, reinterpreting previous findings.
Scientists at the University of Illinois Chicago have found a way to selectively degrade disease-causing proteins in specific parts of cells. By studying the movement of enzymes inside cells, they discovered that attaching or detaching a fat molecule can direct where these enzymes go.
Researchers at KAUST have discovered the molecular mechanisms of DNA repair by studying the interaction between two enzymes, Lig1 and PCNA. Lig1 seals nicks in DNA by attaching to a ring-shaped protein called PCNA, which dislodges another enzyme FEN1 to prepare for sealing.
A study by CeMM researchers and the University of Dundee identifies mutations in E3 ligases that mediate resistances in cell cultures, but also finds that these mutations can be targeted by chemically modified degraders. This understanding has clinical relevance and enables further improvement of cancer therapy drugs.
A team of researchers at Osaka University has identified a specific enzyme complex that initiates the removal of damaged lysosomes from cells. The complex, composed of CUL4A, DDB1, and WDFY1 proteins, acts preferentially during lysophagy to facilitate the degradation process.
Researchers are exploring a novel approach to target disease-causing proteins in human cells. This method, utilizing ubiquitin ligases, aims to overcome traditional drug discovery limitations by targeting more disease-causing proteins, offering new therapeutic possibilities for various conditions.
Researchers found that Mind bomb-2 (MIB2) ubiquitinates and stabilizes the anti-apoptotic protein cFLIP, preventing excessive cell death. This discovery may lead to new therapeutic strategies for treating cancers and neurodegenerative diseases.
The study analyzes mechanisms regulating carcinogenesis and tumor progression, opening new perspectives in the fight against human cancer. HERC1 ligase is found to regulate the activation of ERK and p38 kinase through ubiquitination.
Scientists from Osaka University have discovered a molecular 'light switch' that helps control vision in response to changes in light intensity. The enzyme Cul3-Klhl18 ubiquitin ligase regulates photoreceptor cell adaptation, and its inhibition may help treat conditions like age-related macular degeneration and retinitis pigmentosa.
NTU Singapore scientists have developed a new lab-created peptide ligase based on genetic information from the Chinese violet, which may help speed up drug development and improve diagnostic imaging. The enzyme has exceptional binding properties and can be produced in large quantities without by-products.
Human embryonic stem cells are immortal due to a 'garbage disposal system' called the proteasome. Reducing E3-ubiquitin ligases levels does not affect their behavior, but impacts overall cell function.
Researchers have identified new potential drug targets for a rare kidney and liver disease by studying the molecular mechanisms underlying the disease. The study found that a protein complex, FPC, plays a key role in the development of cysts, fibrosis, and hypertension associated with ARPKD.
The new RNA ligase, KOD1Rnl, has been developed by Brown University researchers to enable high-temperature reactions and improve template specificity. It is the most active in the presence of certain RNA structures, making it useful for RNA sequencing and detection.
Researchers found that female mice with a mutated ITCH gene had reduced implantations and corpora lutea, as well as extended estrous cycles. The study suggests a potential role for ITCH in regulating reproductive function.
Scientists at Sanford Burnham Prebys Medical Discovery Institute have solved the atomic structure of a unique ubiquitin ligase complex, which plays a key role in modulating the immune system. The study reveals significant therapeutic potential for developing novel drug targets for cancer and inflammatory diseases.
A new study has identified partner molecules of cell-waste disposal proteins, which regulate the body's clock. The researchers found that ligase Fbxl3 regulates Cry proteins and Seven in absentia 2 (Siah2) targets RevErbα on a 24-hour cycle.
Researchers have identified a specific gene required for human cells to survive chromosomal defects that occur as cells divide over time. The discovery sheds light on the mechanisms behind cancer cell survival and holds promise for developing new treatments.
Researchers at Michigan State University found that cells can grow normally without a crucial component needed to duplicate their DNA. This discovery suggests that cells are more flexible in managing their DNA than previously thought.
Researchers at Scripps Research Institute discover that parkin enzyme loss leads to reduced levels of protective protein Fbw7β, causing neuronal stress and death. Targeting Fbw7β may offer a new neuroprotective strategy for Parkinson's disease and other neurodegenerative disorders.
Abnormalities in DNA repair mechanisms are a hallmark of cancer cells, leading to increased errors and genetic mutations. The UNM Cancer Center researcher is investigating the role of enzymes that repair DNA damage, aiming to identify new targets for cancer therapy.
Researchers at St. Jude Children's Research Hospital have discovered a new mechanism for eliminating unneeded proteins in cells, which could lead to new treatments for rare blood vessel disorders. The study reveals how a protein called Glomulin disrupts the ubiquitin system, marking potentially thousands of proteins for destruction.
The MDC researchers have discovered a crucial scaffold regulating the identification and disposal of defective proteins. The study reveals that the flexible Usa1 subunit tethers specific modules of the enzyme complex, connecting them to form a larger complex to degrade insoluble membrane proteins.
Researchers from Caltech have developed a new method to view the process of adding ubiquitin chains to cell-cycle proteins, revealing that enzymes add ubiquitins one at a time. This discovery could lead to the development of targeted cancer therapies by understanding how ubiquitin ligases work.
Researchers at Helmholtz Centre for Infection Research identify enzyme that requires acids and dissolved metals to function, repairing genetic damage under extreme conditions. This discovery opens up new possibilities for biotechnological applications and potential treatments for diseases characterized by over-acidification.
A new study identifies CUL7 E3 ubiquitin ligase as a key regulator of protein degradation linked to cellular senescence. The researchers found that the enzyme targets insulin receptor substrate 1 (IRS-1) for degradation, leading to oncogene-induced senescence.
Scientists have found a new approach to treating human cancers by understanding how a plant hormone, auxin, interacts with its receptor, TIR1. This discovery may lead to the development of new cancer drugs by targeting ubiquitin ligases, which are involved in various human diseases.
Researchers discovered that a genetic repair mechanism enables the dynamic assembly and change of shape in proteins to join DNA ends during replication and repair. This mechanism allows DNA ligases to switch between open and closed conformations, enabling efficient ligation of DNA.
A team of researchers has discovered that DNA ligase changes shape from an open to a closed conformation as it joins DNA strands together. This finding reveals new insights into the genetic repair mechanism and its potential as a target for cancer treatment.
Researchers have discovered a cullin-dependent E3 ligase as a crucial component of the Clr4 methyltransferase complex, controlling histone methylation and heterochromatin assembly. The study suggests that polyubiquitylation of regulatory proteins may play a key role in regulating these processes.
Scientists at UNC have discovered a basic mechanism in cell growth control involving damaged DNA, pointing to a potential target for drug development. The study found that the cellular enzyme family Cullin4 plays a crucial role in preventing replication of damaged genomic material.
Researchers at Virginia Tech have identified two enzymes in Methanococcus jannaschii that may predate the cell's use of ribosomes to build proteins. These discoveries provide insight into how peptides were formed before ribosomes, expanding our knowledge of gene function and the evolution of life.
Stanford researchers have identified a potential cause of prion disease, linking it to a mutation in a ubiquitin ligase that flags proteins for destruction. The study suggests that the buildup of cellular trash may contribute to the development of spongy degeneration, leading to neuronal death.
Researchers created a tiny computer using DNA molecules and enzymes, performing a billion operations per second with high accuracy. The device can be programmed to perform simple tasks and may pave the way for future computers that can operate within the human body.