Articles tagged with Bacterial Proteins
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Researchers have successfully developed a novel therapy that uses a fusion protein to selectively kill HIV-infected cells by triggering a chain of suicidal events. This approach has potential applications in treating other infectious diseases such as hepatitis C and malaria, and may also be used to target cancer cells.
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.
A recent study by UK researchers reveals how the Yersinia pestis bacterium uses its YopM toxin to target and destroy phagocytic cells, crippling the immune response. The findings provide new insights into bacterial causes of disease and cell biology, potentially leading to improved therapies for various diseases.
Scientists have identified a close evolutionary connection between the photosynthetic reaction centre of bacteria and that of higher plants. Photosystem II in plants is a multi-enzyme complex comprising over 25 different proteins, which work together to convert sunlight into biochemical energy.
Researchers found that when E. coli attaches to the bladder lining, it triggers a natural defense mechanism where bladder cells commit suicide and slough off, but some bacteria can avoid being removed by invading deeper tissue. This could explain why patients experience recurrent bladder infections despite antibiotic treatment.
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.
Scientists develop biosteel, a novel material produced by infusing goat's milk with spider proteins, offering improved strength and elasticity. The new material could be used in applications such as body armor, spacecraft, or commercial fishing nets.
Bacteriorhodopsin, a salt-loving organism's defense mechanism, is grown in space to produce stable crystals, offering new insights into complex membrane proteins and their applications in all-optical computing. The findings may lead to the development of battery-conserving computer displays.
Researchers have discovered a protein in bacteria that protects them from nitric oxide, a toxin produced by the immune system. This mechanism allows bacteria to survive and thrive, with implications for human health and the development of new antibiotics.
Researchers have successfully adapted a strain of E. coli bacteria to survive on a diet that includes fluorotryptophan, a synthetic amino acid that is toxic to Earth-based life. After multiple generations, the microbes developed mutations that enabled them to cope with the artificial compound and thrive.
Scientists have identified a powerful combination of heat shock proteins that can restore aggregated proteins to their functional states. The Hsp104-Hsp40-Hsp70 trio helps stabilize proteins during aggregation and refolding, providing essential protection against denaturation and promoting cell survival.
Researchers from Duke University and the University of Pennsylvania have gained crystal-clear insight into ribonuclease P, an enzyme that forms a crucial partnership with RNA to construct proteins. The findings suggest an ancient remnant of early life's evolution when RNA molecules were enzymatic workhorses.
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.
Dr. Hultgren's work on pilus genetics, biosynthesis and structure has contributed significantly to understanding bacterial adhesions critical to pathogenesis. His research applications have led to recognition nationally and internationally.
Researchers capture first 'snapshots' of protein molecule converting light into chemical energy in under one billionth of a second. The breakthrough could lead to new optical computer mechanisms and insights into biomolecules.
Hultgren's research focuses on understanding how bacteria attach to human tissue, a key event in disease onset. He has made significant breakthroughs in developing vaccines against urinary tract infections.
Researchers studied how embryos cope with stress, finding unique mechanisms such as toxin-repelling proteins and heat shock protection. These adaptations help embryos survive environmental insults, but may come at a cost in delayed development or growth restrictions.
Researchers use a non-invasive method to visualize genetic activity in living cells, shedding light on chromosome movements and folding. The technique has provided evidence of chromosomal fibers folding and unfolding during natural events.
Researchers have isolated a bacterial protein that allows Helicobacter pylori to attach to the gastric lining, a key step in developing a vaccine against peptic ulcers and gastric cancer. The discovery of BabA protein, found on the surface of H. pylori, could lead to an effective, cheap vaccine that boosts immunity after every exposure.
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 have discovered a chaperone protein from yeast that controls a new, protein-only form of inheritance called a yeast prion. The discovery links the mechanism responsible for this new form of inheritance to neurodegenerative diseases such as Alzheimer's and Creutzfeld-Jakob disease.
Researchers have developed a new protein, IL13-PE38QQR, that penetrates brain cancer cells and kills them without harming healthy cells. The protein is a combination of interleukin 13 and Pseudomonas exotoxin, which can be delivered through the skull via a needle, potentially allowing patients to remain awake during treatment.
Scientists created a recombinant protein that fused heat shock proteins with ovalbumin, leading to immune response against ovalbumin-producing cancer cells. The technology could be used to develop vaccine candidates against infectious diseases like AIDS and stimulate CTL responses against cancer.
Researchers at UT Southwestern Medical Center have found a promising new treatment for meningococcemia, a deadly disease that affects children. The study, led by Dr. Brett Giroir, used bactericidal permeability-increasing protein (BPI) to treat severe cases of the disease and showed encouraging results.
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 discover byssal threads in marine mussels, which feature a mix of collagenous and elastin-like properties. The unique structure of these threads may inspire the development of biomimetic materials with improved stretchiness and toughness.
Tuberculosis bacteria use the C2a protein to lure macrophages to their death, a strategy that makes them effective pathogens. Understanding this mechanism may lead to the development of a novel vaccine to prevent tuberculosis.
Researchers discovered new clues to biological clocks that pace daily activities, including the role of two proteins regulating light responses. Their findings link evolutionary spectrum from light perception to time keeping, paving way for detailing modern clock mechanisms in various organisms.
Biological clocks are reset by slow action of White Collar-1 and White Collar-2 proteins; these proteins work in the dark without light stimulation. Their discovery provides a link between light perception and circadian rhythms, opening an evolutionary window into clock mechanisms.
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.
A new vaccine targeting the E. coli adhesin protein has shown promise in preventing urinary tract infections and bladder infections in mice. The vaccine works by blocking attachment of bacteria to bladder cells, preventing infection and reducing bacterial load.
A new protein, IL 13-PE38QQR, has shown high specificity and sensitivity to kill cancer cells, including those with Kaposi's sarcoma. The compound targets receptor sites on cancer cells, gaining access through interleukin 13.
Researchers have discovered a novel phosphorus compound, DIP, in bacteria Thermotoga maritima that thrive at high temperatures, challenging the previous understanding of its role in archaea. The study suggests that DIP may play a role in osmosis and potentially as a thermoprotectant.
Researchers at Johns Hopkins University discovered that RNA- and DNA-binding proteins have the same shape, a configuration of three coils called alpha helices. This similarity suggests that the protein could be an ancient ancestral form of other proteins crucial to embryonic development.
Scientists at Purdue University have uncovered the mechanism by which disease-resistant plants recognize disease-causing microbes. The discovery reveals that a protein-protein interaction between an enzyme called Pto kinase and a protein produced by the bacterium alerts the plant's defense mechanisms, leading to effective resistance.
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.
Researchers have exposed the precise interactions between antibiotics and bacterial ribosomes, revealing a 'lock-and-key' system that sheds light on antibiotic effectiveness and resistance. The study highlights the importance of targeting RNA in cells and provides potential strategies for designing new, less toxic drugs.
Researchers at Harvard Medical School have visualized the first image of a membrane-spanning molecule thought to transport proteins across cell membranes. The study reveals a dynamic structure that appears and disappears on demand, with the channel opening in two dimensions for different protein types.
Researchers found that nitric oxide activates genes directly, controlling basic life processes down to the gene level. The discovery suggests a universal signaling molecule with far-reaching implications for health and disease.
Researchers find nitric oxide controls genes, influencing myriad body functions. The discovery offers a new approach to developing antibiotic drugs to disarm invasive bacteria.
A new vehicle has been found to carry therapeutic proteins into living cells, overcoming a major hurdle in the delivery of protein-based drugs. The discovery uses small peptides to substitute for bulky components of bacterial toxins and deliver therapeutic proteins into cells.
Researchers at Rutgers University are developing metalloprotein models to emulate nature's energy conversion process using state-of-the-art equipment. The models have the potential to lead to efficient molecular-based solar-energy systems and possibly molecular-based computers that derive their energy from synthetic metalloproteins.
Researchers at Texas A&M University and MedImmune have developed a new vaccine candidate that appears to offer protection against Lyme disease. The vaccine is based on a protein from the Lyme-causing bacterium and has been shown to clear the disease-causing organisms from the body even after infection.
Scientists have long known that proteins like colicin Ia can punch holes in cell membranes to kill bacteria. Researchers at Albert Einstein College of Medicine mapped the structure of colicin Ia, revealing a massive chunk of protein must cross the membrane to form an open channel.