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A Jekyll-and-Hyde enzyme's role in Alzheimer's

Researchers discovered that a Jekyll-and-Hyde enzyme plays a crucial role in Alzheimer's disease. Transient production of the enzyme p25 enhances learning and memory, whereas chronic expression impairs these cognitive functions. The study uses mice to demonstrate the dual effects of p25 on neural mechanisms.

SourceCell Press·JournalNeuron·DateDec 7, 2005

Potential malaria drug target identified

A team of researchers has discovered a parasite enzyme, PfSUB2, that sheds sticky surface proteins, allowing the parasite to invade red blood cells. The discovery could lead to the development of new antimalarial drugs that target this enzyme.

SourcePLOS·JournalPLOS Pathogens·DateNov 24, 2005

New discovery: If it weren't for this enzyme, decomposing pesticide would take millennia

Researchers at UNC Chapel Hill have discovered a new enzyme that can break down chloroacrylate pesticide residue in just 10,000 years, significantly longer than other environmental pollutants. This enzyme is found in bacteria that thrive on the pesticide and has implications for designing more efficient enzymes.

SourceUniversity of North Carolina at Chapel Hill·JournalProceedings of the National Academy of Sciences·DateOct 24, 2005

Proofreading and error-correction in nanomaterials inspired by nature

Researchers at the University of Illinois have developed a novel method for proofreading and error-correction in nanomaterials, utilizing catalytic DNA to detect and remove incorrect particles. This approach mimics nature's accuracy mechanisms in protein synthesis and holds promise for precise control over nanoparticle assembly.

Mitochondrial biology gets a new chaperone

A study has identified a new molecular chaperone involved in assembling the enzyme complex I of mitochondria. The research found that B17.2L is a key protein required for this process and that it is mutated in patients with progressive encephalopathy.

SourceJCI Journals·JournalJournal of Clinical Investigation·DateOct 3, 2005

The link between fasting and acute attacks of porphyria

A team of researchers has discovered a molecular missing link that explains why fasting brings on acute attacks of the genetic disease hepatic porphyria. Fasting increases levels of PGC-1a, which regulates the activity of an enzyme in the heme production pathway, leading to toxic buildup of precursor molecules.

SourceCell Press·JournalCell·DateAug 25, 2005

Predicting the outcome of drug-induced liver disease

A study analyzing reports of suspected drug-induced liver injury found that AST and bilirubin levels are key predictors of death or liver transplant in patients with severe drug-induced liver disease. Patients with hepatocellular liver damage had a higher mortality rate, highlighting the importance of monitoring these biomarkers.

SourceWiley·JournalHepatology·DateJul 18, 2005

Rice unveils 'green' microcapsule production method

The new process, developed by Michael Wong and his team, involves mixing polymer, salt, and tiny silica particles to create hollow spheres that can encapsulate drugs, flavor compounds, and other molecular cargo. The microcapsules have potential applications in drug delivery, medical imaging, and enzyme protection.

SourceRice University·JournalAdvanced Materials·DateMay 26, 2005

Automated imaging screen reveals promising drug candidates

A high-throughput screening method using automated imaging and bioinformatics has identified a novel compound with promising potential as an anticancer agent. The compound, hydroxy-PP, targets carbonyl reductase 1, an enzyme involved in chemotherapy-related cardiotoxicity.

SourcePLOS·JournalPLOS Biology·DateApr 4, 2005

Scientists find missing enzyme for tuberculosis iron scavenging pathway

Researchers have identified a missing enzyme in M. tuberculosis that plays a crucial role in the bacterium's ability to acquire iron through mycobactin synthesis. This discovery highlights the importance of understanding the iron scavenging pathway in TB and provides new avenues for developing effective anti-TB drugs.

SourceAmerican Society for Biochemistry and Molecular Biology·JournalJournal of Biological Chemistry·DateMar 30, 2005

Key target for Foot and Mouth drug revealed

Researchers at Imperial College London have solved the structure of the Foot-and-Mouth Disease Virus enzyme, revealing its atomic details and potential target for anti-viral drugs. The discovery could lead to the development of a vaccine that can be administered quickly to control outbreaks.

SourceImperial College London·JournalJournal of Biological Chemistry·DateMar 21, 2005