UCL scientists have found a protein that could unlock the secret to quicker, more effective treatment of TB by waking TB bacteria in the body. Once the TB bacteria are active again, the disease becomes treatable using common drugs like antibiotics. Scientists believe that uncovering the molecular structure of this protein will lead the way to designing drugs which enable treatment of dormant and multidrug resistant TB.
In England and Wales around 400 people die each year from the disease. The top challenge for TB control in the European region is multidrug-resistant TB (MDR-TB). Eight per cent of the bacteria causing TB in patients are resistant to one or more drugs and one per cent show multidrug resistance. Left untreated, a person with infectious TB of the lungs infects around 10 to 15 people every year.
In a study published on 1st March 2005 in Nature Structural & Molecular Biology, a combined team discovered the structure of a protein known as resuscitation promoting factor (Rpf). Five versions of the Rpf protein exist in TB bacteria. The paper’s unveiling of the molecular structure of Rpf could be crucial to the treatment of TB in the future.
Alexandra Brew | alfa
Climate Impact Research in Hannover: Small Plants against Large Waves
17.08.2018 | Leibniz Universität Hannover
First transcription atlas of all wheat genes expands prospects for research and cultivation
17.08.2018 | Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung
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Scientists at the University of California, Los Angeles present new research on a curious cosmic phenomenon known as "whistlers" -- very low frequency packets...
Scientists develop first tool to use machine learning methods to compute flow around interactively designable 3D objects. Tool will be presented at this year’s prestigious SIGGRAPH conference.
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Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
Actin is the most abundant protein in highly developed cells and has diverse functions in processes like cell stabilization, cell division and muscle...
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