Articles tagged with Mutant Proteins
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Researchers at HHMI and Stanford University have developed a new method to engineer drug molecules that bind more effectively to their targets. By attaching small molecule inhibitors to larger proteins, the team increased the binding affinity of the inhibitor, making it easier to inhibit protein-protein interactions.
Researchers at Harvard Medical School have identified a key pathway linking the growth cone's membrane receptor to actin, the final agent of change. The study reveals an uninterrupted chain of signaling events that enables neurons to transmit information from the membrane to the cytoskeleton.
Geneticists at Duke University have discovered the functional interaction between myc and ras, two cancer-related genes. The study found that mutated ras causes myc protein to accumulate in cells, enhancing its growth-promoting abilities.
Researchers discovered a novel family of cell surface proteins that regulate nerve cell connections by inducing synapse formation. The Neuroligin/b-Neurexin junction is the core of this process, forming a transsynaptic cell-adhesion complex that initiates protein-protein-interaction cascades.
A newly discovered gene mutation has been found to shut down the MHC-I transport system in tumor cells, making them less recognizable to the immune system. This could lead to a way to increase the immune system's sensitivity to tumors, potentially improving cancer treatment options.
Recent discoveries in circadian rhythms research have identified a set of probably a dozen or so proteins that regulate the biological clock in flies and mammals. These proteins share a common molecular motif called the PAS domain, which instructs them to attach to other proteins and help set the clock's time.
Researchers at The Wistar Institute have identified a new mechanism of molecular recognition in which proteins regulate DNA transcription through asymmetric binding. This discovery sheds light on how homodimeric transcription factors can recognize their target DNA and has potential implications for drug design.
Researchers at the University of Chicago have discovered a molecular mechanism that allows organisms to evolve new traits in response to environmental stress. The mechanism involves the protein heat shock protein 90 (Hsp 90), which normally keeps genetic variations silent but can reveal them during times of stress.
Researchers have discovered a novel function of the Survival Motor Neuron (SMN) protein essential for mRNA production in all cells. This finding links SMN deficiency to spinal muscular atrophy, a leading genetic cause of infant death, and paves the way for potential therapeutic interventions.
Researchers have discovered a protein, gephyrin, crucial for central nervous system synapse development and molybdenum utilization. The absence of this protein leads to symptoms similar to human diseases, including stiff baby syndrome and molybdenum cofactor deficiency.
Researchers found a genetic mutation in the CCR5 gene promoter that significantly delays HIV disease progression, affecting approximately 20% of infected individuals. The mutant promoter is 45% less active, leading to slower disease progression and increased resistance to HIV infection.
Researchers have determined the first structure of a functional protein unit involved in neurofibromatosis, which regulates Ras and contributes to tumor growth. The study confirms mechanistic ideas about neurofibromin's function and links NF1 to cancerogenesis.
Scientists have identified SLP-76 as a critical protein for the development and activation of T cells, an essential part of the immune system. This finding provides valuable insights into the basic biology of immune system activation, which is crucial for understanding immunodeficiency disorders and autoimmune diseases.
Researchers discovered a new gene called double-time that regulates circadian rhythms in fruit flies, which may also influence human sleep patterns. The gene affects the pairing of proteins essential for maintaining daily cycles.
Researchers at Harvard Medical School have identified a new component of the circadian clock, BMAL1, which partners with CLOCK to regulate daily rhythms. The study shows how closely conserved genes are between different organisms and hopes to shed light on the negative feedback part of the circadian loop.
Scientists have isolated a novel gene involved in phosphorylating starch in potato tubers. Inhibiting its expression leads to reduced phosphate content and altered starch properties, resulting in improved degradation and reduced cold-induced sweetening. This discovery has significant implications for plant biotechnology.
UCSF researchers have identified a protein essential for forming concentrated urine in mice, which has potential implications for treating fluid retention diseases such as congestive heart failure and cirrhosis. The study shows that inhibiting the water channel with drugs could effectively treat these conditions.
Researchers at Yale University are using computer simulations to design more effective pharmaceuticals by optimizing chemical binding to target proteins. This approach has the potential to improve treatment outcomes for diseases such as dementia, diabetes, and spinal cord injuries.
The proteasome is a crucial macromolecular machine responsible for eliminating abnormal proteins. It plays a vital role in various biological processes, including the regulation of cell cycle, apoptosis, and immune response. The molecular architecture of the 20S proteasome is conserved from archaea to eukaryotes.
The study, led by Ming-Daw Tsai, used nuclear magnetic resonance spectroscopy to determine the 3D structure of the p16 protein. The researchers aim to develop a drug that mimics p16 to treat cancer, which is expected to target more than 70 different types of cancer.
Researchers discover two related versions of the LOV domain in a plasma membrane protein, which shares significant similarity with domains from various organisms. The LOV domain may play a crucial role in regulating the phototropic response and other cellular processes.
Researchers identified a specialized protein that catalyzes conformational change of mitotic proteins, allowing correct exit from mitosis. This finding has significant implications for understanding and developing anti-cancer agents targeting this mechanism.
Researchers at UNC Chapel Hill School of Medicine found that NF-kappa B, a natural protein, teams up with a cancer gene to prevent cell death in tumor cells. The team suggests using new drugs or therapies to turn off or neutralize NF-kappa B to control certain tumors.
Researchers at St. Jude Children's Research Hospital found that the ARF tumor suppressor interacts with the p53 gene, preventing cancer growth and development. The study identifies a single genetic locus, INK4a/ARF, which encodes two proteins regulating two key biochemical pathways.
A study led by Johns Hopkins Researchers found that a drug, sodium 4-phenylbutyrate (4PBA), may help cystic fibrosis patients with the deltaF508 mutation by allowing more CFTR proteins to reach cell surfaces. This phenomenon occurs at concentrations normally seen in patients taking the drug for urea cycle disorders.
Two repair proteins, Fpg and UvrA, have been found to 'block the road' to replication by physically attaching themselves to damaged DNA, preventing mutations. This discovery offers new insights into natural DNA repair mechanisms and potential avenues for cancer prevention.
Researchers describe a powerful new immunotherapeutic approach that uses heat shock protein complexes to stimulate the immune system against cancer cells, with 80% of treated mice surviving longer than control mice. The treatment has potential for treating various cancers and may be applied in conjunction with surgery and chemotherapy.
Researchers have discovered a new class of proteins that may provide insights into all dystonia disorders. The DYT1 gene codes for torsinA protein, which is mutated in patients with early-onset torsion dystonia, disrupting communication among neurons responsible for movement and muscle control.
Researchers have discovered how key molecules interact in the major pathway regulating cell division. Disrupting this pathway may force cancer cells to divide prematurely, favoring their death. A class of molecules that inhibit Cdc25C has also been identified, suggesting a potential target for cancer therapies.
Scientists have discovered a common mechanism underlying neurodegenerative diseases, where mutant proteins accumulate in nuclear spaces, recruiting normal proteins and disrupting cellular processes. This finding suggests a single disease mechanism may be responsible for several afflictions.
Researchers at Johns Hopkins Medicine found that the TSG101 gene, previously identified as a tumor suppressor, was consistently normal and undamaged in human breast cancer cells. The cells exhibited abnormal RNA splicing, which may be a result of cancer cells trying to activate normal cell behaviors in an abnormal way.
Researchers at MGH discovered that presenilin genes are involved in programmed cell death, a natural process where unneeded cells commit suicide. Mutations in these genes increase the propensity of nerve cells to undergo apoptosis, a process that can contribute to Alzheimer's disease.
The pickle plant mutation retains embryonic cells in its root, storing oil, proteins, and starch. Gibberellin plays a crucial role in switching from embryonic to adult cell program, but its absence during early growth amplifies the effect.
Researchers have discovered a novel protein, Vera, that plays a crucial role in RNA localization in oocytes. This process is essential for the development of embryogenesis and has broad implications for biology, as it occurs in many adult cell types.
Researchers developed a genetically-engineered protein biosensor that can identify the presence of maltose, a sugar compound, in blood. The biosensor uses a fluorophore reporter to signal its catch, providing instant analysis for various applications.
Researchers have identified a key protein in the telomerase enzyme that is selectively activated in many cancer cells. The discovery may lead to the development of new anti-cancer agents, including variants of existing pharmaceuticals.
The study, published in the EMBO Journal, shows that viral tails play a crucial role in controlling the shape and formation of new viral particles. The research demonstrates the importance of these protein parts in the development of the virus.
A team from the University of Rochester Cancer Center has identified the protein PP1c that activates the retinoblastoma (RB) gene, a key tumor suppressor. This finding offers a new avenue for controlling cancer cell growth and potentially treating various types of cancer.
Researchers at Rockefeller University have determined the three-dimensional structure of Hck, a cancer-causing protein that plays a key role in regulating cell behavior. The study reveals that the protein's shape is controlled by the SH3 domain, which enables it to transform cells into cancerous ones.
The study provides a three-dimensional view of molecular switch Src, assisting in the development of new drugs. The researchers discovered that Src has four lobes with interconnected linkers, which keep it idle until stimulation arrives, turning it on.
A new study has identified a common functional problem in enlarged heart disease that causes sudden death in athletes, regardless of the genetic cause. This finding suggests that a single therapeutic approach may be effective for all victims of hypertrophic cardiomyopathy (HCM), a leading cause of sudden death in young adults.
Scientists at Duke University have discovered that a bacterial protein structure plays a crucial role in preventing genetic flaws from translating into diseases. The research reveals that the protein interacts with helicases, which are involved in several genetic diseases, including Werner's syndrome and Cockayne's syndrome.
The study provides evidence that FMRP is transported into the cell's nucleus where it forms a complex with particular mRNAs and then is transported out of the nucleus to join ribosomes in the neuronal cytoplasm. The researchers discovered that free ribosomes, found in dendrites and dendritic spines, associate with FMRP.
Researchers at Johns Hopkins Medicine have identified a protein glitch as an early problem in inherited Alzheimer's disease. Presenilin normally cleaves in two, but a disease-causing mutation can prevent this crucial change. This study may lead to new treatments by targeting the point of cleavage with drugs or other interventions.
Scientists have discovered how p27 blocks cell growth in virtually all human cancers, providing new hope for developing drugs to halt uncontrolled cell division. The discovery uses X-ray crystallography to reveal the molecular structure of p27 and its interaction with cyclin-CDK complexes.
Scientists found a connection between triplet repeat genes and brain disorders like Huntington's disease, where proteins errantly stick to an enzyme crucial for energy production in brain cells. The discovery offers a potential treatment option by blocking protein interactions.