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Showing results 41-51 of 53 for 'Proteins'


  • ron-diskin-tn
    The Man Who Studies Deadly Diseases

    Israel21c profiles Dr. Ron Diskin, whose expertise in x-ray crystallography made him a key member of a groundbreaking Caltech-Rockefeller University team researching HIV. Now, as a new scientist at the Weizmann Institute, he is building a lab to advance his structural research on HIV and tropical Arena viruses that cause fatal diseases.

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    Unfolding the Mysteries of Proteins

    WeizmannViews Issue No. 46 is about the research of new young scientist Dr. Rina Rosenzweig. She is expert in using super-powerful NMR machines, applying these skills to her studies of misfolded proteins and the clumps they form. These protein “aggregates” are involved in neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s.

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    New Clues Help Doctors Cure Patients, Not Diseases

    Israel21c covers the Nancy and Stephen Grand Israel National Center of Personalized Medicine at the Weizmann Institute, including discussion with Dr. Berta Strulovici, the center’s founding director. The G-INCPM is already studying acute myeloid leukemia, soft-tissue sarcoma, and retinitis pigmentosa.

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    Rare Genetic Defect May Lead to Cancer Drug

    The path to understanding what goes wrong in cancer could benefit from a detour through studies of rare childhood diseases. Dr. Ayelet Erez explains that cancer generally involves dozens – if not hundreds – of mutations, and sorting out the various functions and malfunctions of each may be nearly impossible. Rare childhood diseases, in contrast, generally involve mutations to a single gene.

    /news-media/news-releases/rare-genetic-defect-may-lead-to-cancer-drug
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    Programmed Proteins May Make Malaria Vaccine Possible

    A malaria vaccine based on stabilized proteins could be used in tropical places where there is no refrigeration. Despite decades of malaria research, the disease still afflicts hundreds of millions and kills around half a million people each year – most of them children in tropical regions. The best deterrent would be a vaccine composed of some of the parasite’s own proteins. However, those proteins identified as most promising for a malaria vaccine are unstable at tropical temperatures and require complicated, expensive cellular systems to produce them in large quantities.

    /news-media/in-the-news/programmed-proteins-may-make-malaria-vaccine-possible
  • Schuldiner Maya_EMBO_Gold_Medal (002).jpg
    Maya Schuldiner Receives EMBO Gold Medal 2017

    Heidelberg, 8 June 2017 – Maya Schuldiner from the Weizmann Institute of Science in Israel is the recipient of the 2017 EMBO Gold Medal. She receives the award for significantly advancing the understanding of protein synthesis, trafficking and quality control. The EMBO Gold Medal is awarded annually and recognizes outstanding contributions to the life sciences in Europe by young independent group leaders.

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  • shimanovich ulyana_crop.jpg
    Microscopic Cocoons Made of Silk Protein May Facilitate Drug Design

    Scientists have managed to design microscopic silk capsules that mimic, on a very small scale, the structure of silkworm cocoons. The capsules can serve as a protective environment for the transport of sensitive “cargo” such as natural silk proteins, antibodies, or other delicate molecules. The collaborative research – which was performed by an international team of academics from the Weizmann Institute of Science in Israel; the Universities of Cambridge, Oxford, and Sheffield in the UK; and the ETH in Switzerland – may lead to a host of applications in the cosmetics, food, and pharmaceutical industries, particularly in the delivery of drugs within the body. The findings were reported in Nature Communications.

    /news-media/news-releases/microscopic-cocoons-made-of-silk-protein-may-facilitate-drug-design
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    No Cell Left Behind: Mapping the Human Body

    Imagine walking into the doctor’s office, preparing for the worst. The doctor brings up surgery, vaguely motions to a chart on the wall, and points to certain printed organs. But what if he could show you which cells needed removal, what they looked like, and even why they caused your condition? Scientists may now have the means to determine the precise cellular structure of human organs, which could improve researchers’, doctors’, and patients’ understanding of human diseases.

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  • Shalev 2 (002).jpg
    Cell Economics 101

    Every time we swallow food, cells that line the intestines must step up their activity in a sudden and dramatic manner. According to a new study by Weizmann Institute of Science researchers, reported in Science, they rise to the challenge in the most economic fashion. In business or engineering, when one has to get production underway quickly, instant decisions are made. These might involve instantly throwing all one’s resources into boosting production with existing equipment, or else first spending all those resources to equip the plant with proper machinery. The latter might seem to be a less efficient production method but it can actually, in some cases, speed things up considerably. Dr. Shalev Itzkovitz and his team in the Department of Molecular Cell Biology discovered that this is just the method adopted in the lining of the intestinal wall.

    /news-media/news-releases/cell-economics-101
  • shutterstock_521067919_lego blocks.jpg
    LEGO Proteins Revealed

    The proteins in our bodies are social molecules. But now and again, new ties between proteins can get you into trouble. For example, when hemoglobin – the protein complex that carries oxygen in our blood – undergoes just one mutation, the complexes stick to one another, stacking like Lego blocks to form long, stiff filaments. These filaments, in turn, elongate the red blood cells found in sickle-cell disease. For over 50 years, this has been the only known textbook example in which a mutation causes these filaments to form. According to Dr. Emmanuel Levy and his group in the Weizmann Institute of Science’s Structural Biology Department, Lego-like assemblies should have formed relatively frequently during evolution, and so they asked: How easy is it to get proteins to stack into filaments? Their answer, which was recently published in Nature, may have implications for both biological research and nanoscience.

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