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News Article | May 19, 2017
Site: news.europawire.eu

HEIDELBERG, 19-May-2017 — /EuropaWire/ — The German National Academy of Sciences, Leopoldina, today welcomes EMBO Director Maria Leptin as one of its members. Election to the Leopoldina membership is the highest academic honour awarded by an institution in Germany and it is bestowed on scientists who are experts in their fields. Maria Leptin, together with 14 other eminent researchers from Germany and abroad, was elected in 2016, and will today be officially welcomed at a ceremony in Halle (Saale), Germany. Following the presentation of the membership certificates, Maria Leptin will deliver a lecture on the role of cellular coordination during the development of organs and whole organisms. Through her election, Maria Leptin became part of a membership of over 1,500 individuals from more than 30 countries. Other EMBO Members elected to the Leopoldina Membership in 2016 include Aaron Ciechanover, Haifa, Israel, Veit Hornung, Munich, Germany, Edvard Moser, Trondheim, Norway, May-Britt Moser, Trondheim, Norway, Christian Spahn, Berlin, Germany. For more information (in German): https://www.leopoldina.org/de/presse/pressemitteilungen/pressemitteilung/press/2487/ Maria Leptin received her PhD in 1983 for work on B cell activation carried out at the Basel Institute for Immunology under the supervision of Fritz Melchers. She switched to the study of development in Drosophila when she joined the laboratory of Michael Wilcox at the Medical Research Council’s Laboratory of Molecular Biology (LMB) in Cambridge, UK, for her postdoctoral work on Drosophila integrins. After a research visit at the lab of Pat O’Farrell at the University of California San Francisco (UCSF), where she began studying gastrulation, she spent the years from 1989 to 1994 as a group leader at the Max Planck Institute in Tübingen. In 1994, she became Professor at the Institute of Genetics University of Cologne. In January 2010 Maria Leptin became the Director of EMBO and established a research group in Heidelberg at the European Molecular Biology Laboratory (EMBL). The group studies the development of complex cell shapes in the respiratory system of Drosophila and the role of RNA localisation in generating cell shape. Professor Leptin is an elected member of EMBO, the Academia Europaea and the German National Academy of Sciences (Leopoldina). She also serves on the editorial boards of Developmental Cell, Developmental Biology and on advisory boards of several academic institutions.


News Article | February 15, 2017
Site: www.newscientist.com

Targeting tangles of tau protein in mice with Alzheimer’s-like symptoms has reversed their brain damage, halting memory loss and extending their lives. Clumps of two types of sticky protein build up in the brains of people with Alzheimer’s disease: beta-amyloid plaques, and tangles of tau. While many attempts to develop drugs to treat Alzheimer’s have targeted beta-amyloid, tau protein tangles have long been suspected to play a role in memory loss. “Tau is what correlates with memory problems, so one hypothesis is that lowering tau could be beneficial,” says Tim Miller of Washington University in St Louis, Missouri. Now Miller’s team has purged tau tangles from the brains of Alzheimer’s-like mice for the first time. They used fragments of RNA called antisense oligonucleotides to sabotage the gene that makes tau, preventing it from being fully translated into protein. Once a day for four weeks, the team injected the antisense treatment, named Tau-ASO12, into the fluid at the base of each mouse’s spine. The mice had been genetically engineered to make a rogue form of tau similar to what is seen in people with Alzheimer’s, predisposing the mice to developing tau-related brain problems. The drug successfully spread throughout the brain, and was linked to a reduction in levels of tau that was made. It also seemed to destroy existing tau tangles, and prevent tau from spreading around the brain in older mice. Overall, mice that got Tau-ASO12 lived up to 50 days longer than those that didn’t, and were able to retain important abilities, such as nest-making skills, that were lost in mice that received a sham treatment. When Miller’s team gave the antisense treatment to cynomolgus monkeys, they saw around a 20 per cent reduction in the amount of tau detected in spinal fluid samples, with no apparent side effects – early evidence that the therapy may hold promise for treating humans. Before testing the treatment in people, the team will further assess its safety and efficacy in larger primate animals. One concern is that lowering levels of a brain protein like tau could affect normal brain function. “We don’t know for sure what tau does in the brain,” says Michel Goedert at the Laboratory of Molecular Biology in Cambridge, UK, who showed in 2009 that tau can spread from one brain cell to another. However, mice that are genetically modified not to produce any tau are healthy for most of their lifespan, he says. “We believe that reducing tau levels by something like 30 per cent will not cause any ill effects, but will be beneficial in terms of preventing neurodegeneration.” Miller says any human Tau-ASO12 treatment would likely be injected into the cerebrospinal fluid at the base of the spine, and would probably have to be given around once a month. Similar antisense treatments have already been given safely to people with amyotrophic lateral sclerosis (motor neurone disease) and Huntington’s disease. Tau is implicated in several other neurodegenerative conditions, including progressive supranuclear palsy and frontotemporal dementia, and it’s possible that such a treatment could also benefit people with these conditions.


News Article | February 21, 2017
Site: www.businesswire.com

WATERTOWN, Mass.--(BUSINESS WIRE)--FORMA Therapeutics, a clinical-stage and fully integrated discovery and development company, announced today it has been awarded a research grant from The Michael J. Fox Foundation for Parkinson’s Research (“MJFF”) to further develop FORMA’s discovery program in protein homeostasis and ubiquitination for the treatment of Parkinson’s disease (PD). FORMA has established a research alliance with Professors Michael Clague and Sylvie Urbé from University of Liverpool, UK, and Dr. David Komander from Medical Research Council, Laboratory of Molecular Biology, Cambridge, UK, who will work alongside FORMA’s lead investigator, Dr. Stephanos Ioannidis, to advance the research plan subject to this prestigious award. Protein homeostasis and mitochondrial function are areas of biology that harbor promising new therapeutic targets for the treatment of PD. Recent research suggests that members of the deubiquitinase (DUB) family of proteins, which are critical in protein homeostasis, are also key modulators of mitophagy or mitochondrial clearance. The elimination of abnormal mitochondria by targeting DUB activity may be a route to intervene in the pathogenesis of PD. The grant from MJFF supports the advanced discovery and development of preclinical compounds targeting DUBs potentially relevant to PD. Shalini Padmanabhan, Ph.D., Associate Director of Research Programs at MJFF, said, “While accumulating evidence implicate defective mitochondria in PD pathology, exactly how DUBs regulate mitophagy is unclear. We hope this award will enable FORMA and its neurodegenerative disease alliance with leading investigators to understand the role of DUBs in clearance of damaged mitochondria and potentially lead to a promising treatment approach for PD patients.” “We are honored to receive recognition from MJFF for our research in protein homeostasis and to collaborate with its network in PD. This award provides support to further enable innovative research with our talented collaborators in the UK,” said John Hohneker, M.D., EVP and Head of Research and Development at FORMA. “We hope to gain a deeper understanding of the role of DUBs in PD that will ultimately facilitate the advancement of new therapies for patients.” As the world’s largest nonprofit funder of Parkinson’s research, The Michael J. Fox Foundation is dedicated to accelerating a cure for Parkinson’s disease and improved therapies for those living with the condition today. The Foundation pursues its goals through an aggressively funded, highly targeted research program coupled with active global engagement of scientists, Parkinson’s patients, business leaders, clinical trial participants, donors and volunteers. In addition to funding more than $650 million in research to date, the Foundation has fundamentally altered the trajectory of progress toward a cure. Operating at the hub of worldwide Parkinson’s research, the Foundation forges groundbreaking collaborations with industry leaders, academic scientists and government research funders; increases the flow of participants into Parkinson’s disease clinical trials with its online tool, Fox Trial Finder; promotes Parkinson’s awareness through high-profile advocacy, events and outreach; and coordinates the grassroots involvement of thousands of Team Fox members around the world. FORMA Therapeutics' scientists are passionate about discovering and developing medicines that will make a difference in oncology, inflammation & immunity, and other serious diseases. The Company’s fully integrated R&D team drives discovery and early clinical development of therapeutics for qualified targets in the areas of epigenetics, protein homeostasis and metabolism. Leveraging a world class network of academic investigators, clinical experts and partners, FORMA combines deep biology insight, chemistry expertise and early clinical development capabilities, to create drug candidates that will ultimately provide profound patient benefit. FORMA is headquartered in Watertown, MA near the epicenter of the Cambridge Life Sciences cluster, with additional chemistry operations in Branford, CT. www.formatherapeutics.com


WATERTOWN, Mass., Oct. 31, 2016 (GLOBE NEWSWIRE) -- Selecta Biosciences, Inc. (NASDAQ:SELB), a clinical-stage biopharmaceutical company developing a novel class of targeted antigen-specific immune therapies, today announced that results from preclinical studies involving SVP-Rapamycin, the company’s novel immunotherapeutic, were presented by its collaborators Ira Pastan, MD, Chief of the Laboratory of Molecular Biology, and Ronit Mazor, Ph.D., Postdoctoral Fellow at Center for Cancer Research at the National Cancer Institute (NCI), part of the National Institutes of Health. Through a collaboration under a Cooperative Research and Development Agreement (CRADA) between Selecta and NCI, the results were obtained by co-administration of SVP-Rapamycin with an investigational anti-cancer therapeutic, LMB-100. LMB-100 is a next-generation recombinant immunotoxin (rIT) developed in the Pastan Lab that is currently undergoing Phase 1 clinical trials at the NIH Clinical Center in patients with mesothelioma and pancreatic cancer. Dr. Pastan’s presentation at the Immunogenicity and Bioassay Summit 2016 in Baltimore, Maryland was entitled, “Strategies to Reduce Immune Response to Immunotoxins,” and Dr. Mazor’s presentation was entitled, “Induction of Tolerance to Immunotoxins Using Nanoparticle Delivery of Rapamycin.” Further, Dr. Mazor presented a poster with the title “Nanoparticle-Encapsulated Rapamycin Prevents Primary and Secondary Immune Responses in Murine Models.” LMB-100 is a next-generation immunotoxin comprised of a mesothelin-targeting antibody fragment linked to an engineered cytotoxic domain of Pseudomonas exotoxin A. The majority of mesothelioma patients treated with an earlier version of LMB-100, called SS1P, experienced dose-limiting immune responses despite the use of potent immunosuppressants. However, the few patients tolerating more than one treatment cycle in this trial showed marked antitumor activity in patients with chemotherapy-refractory mesothelioma. The co-administration of SVP-Rapamycin with LMB-100 in mice models prevented the formation of anti-LMB-100 antibodies and allowed for the administration of at least four treatment cycles, representing a marked increase in the number of effective doses that could be administrated without the onset of neutralizing antibodies. Further, in a tumor model, the addition of SVP-Rapamycin restored the beneficial effect of LMB-100 on controlling tumor growth. “These pre-clinical proof of concept data clearly demonstrate the potential benefit of co-administrating LMB-100 and SVP-Rapamycin, two products currently used in clinical trials,” said Peter Keller, M.Sc., Chief Business Officer at Selecta. “The program is part of our objective to extend our clinical pipeline by applying our SVP technology platform to oncology treatments. In oncology, the effectiveness of many therapies could be enhanced by antigen-specific mitigation of undesired immune responses.” Selecta is developing SVP-Rapamycin for co-administration with biologic therapies for the antigen-specific mitigation of undesired humoral and cellular immune responses.  The company is focused on three strategic areas: enzyme therapy, gene therapy and oncology. SVP-Rapamycin has the potential to be co-administered with a multitude of biologic drugs that have been identified in each of these areas to increase the number of treatable patients and/or enhance efficacy and safety. Selecta’s lead product candidate, SEL-212, applies SVP-Rapamycin to pegsiticase, a pegylated uricase. SEL-212 is designed to be the first non-immunogenic version of uricase, an immunogenic enzyme that targets uric acid. SEL-212 is in a Phase 2 clinical trial and is being developed for patients with chronic refractory and tophaceous gout. LMB-100 is a next generation immunotoxin comprised of a mesothelin-targeting antibody fragment linked to an engineered cytotoxic domain of Pseudomonas exotoxin A.  Mesothelin, a cell surface antigen discovered in Ira Pastan’s laboratory at NCI, is overexpressed in mesothelioma, pancreatic, ovarian and lung cancers.  Dr. Pastan is a world-renowned expert in the design and development of immunotoxins. A first generation mesothelin-targeted immunotoxin, SS1P, could only be given for 1 cycle because it was immunogenic, but showed marked antitumor activity in patients with chemotherapy-refractory mesothelioma, when combined with drugs to suppress the development of anti-drug antibodies.  LMB-100 was engineered to reduce immunogenicity and off target toxicity.  LMB-100 is currently in phase 1 clinical studies by CCR investigators at the NIH Clinical Center in Bethesda, Maryland. Selecta Biosciences, Inc. is a clinical-stage biopharmaceutical company developing targeted therapies that use immunomodulators encapsulated in nanoparticles to induce antigen-specific immune responses to prevent and treat disease. Selecta’s proprietary Synthetic Vaccine Particle (SVP) technology is a highly flexible nanoparticle platform, capable of incorporating a wide range of antigens and immunomodulators, allowing the SVP-based products to either induce antigen-specific tolerance or activate the immune system. Selecta's focus and strategy is to leverage its SVP immune modulating platform to develop and commercialize highly differentiated life-sustaining biologic drugs that are uniquely capable of mitigating the formation of anti-drug antibodies (ADAs). Proprietary programs that use SVP-Rapamycin to enhance efficacy and safety of therapy include SEL-212, Selecta’s lead Phase 2 clinical program in chronic refractory gout, and two gene therapies programs for genetic metabolic diseases. Tolerance-inducing SVP biological products also have potential applications in the treatment of allergies and autoimmune diseases. Selecta is also developing SVP products that activate the immune system to prevent and treat cancer, infections and other diseases. Selecta is based in Watertown, Massachusetts, USA. For more information, please visit http://selectabio.com. Forward-Looking Statements Any statements in this press release about the future expectations, plans and prospects of Selecta Biosciences, Inc. (the “Company”), including without limitation, statements regarding the impact of the Company’s initial public offering on its financial position and the development of its pipeline, the timing of the Phase 2 clinical trial of SEL-212, including initiation, announcement of data, conference presentations, the number of centers in the Phase 2 clinical trial of SEL-212, the ability of the Company’s SVP platform, including SVP-Rapamycin, to mitigate immune response and create better therapeutic outcomes, the potential treatment applications for SVP products, the sufficiency of the Company’s cash, cash equivalents, investments, and restricted cash and other statements containing the words “anticipate,” “believe,” “continue,” “could,” “estimate,” “expect,” “hypothesize,” “intend,” “may,” “plan,” “potential,” “predict,” “project,” “should,” “target,” “would,” and similar expressions, constitute forward-looking statements within the meaning of The Private Securities Litigation Reform Act of 1995. Actual results may differ materially from those indicated by such forward-looking statements as a result of various important factors, including, but not limited to, the following: the uncertainties inherent in the initiation, completion and cost of clinical trials including their uncertain outcomes, the availability and timing of data from ongoing and future clinical trials and the results of such trials, whether preliminary results from a particular clinical trial will be predictive of the final results of that trial or whether results of early clinical trials will be indicative of the results of later clinical trials, the unproven approach of the Company’s SVP technology, potential delays in enrollment of patients, undesirable side effects of the Company’s product candidates, its reliance on third parties to manufacture its product candidates and to conduct its clinical trials, the Company’s inability to maintain its existing or future collaborations or licenses, its inability to protect its proprietary technology and intellectual property, potential delays in regulatory approvals, the availability of funding sufficient for its foreseeable and unforeseeable operating expenses and capital expenditure requirements, substantial fluctuation in the price of its common stock, a significant portion of the Company’s total outstanding shares are eligible to be sold into the market in the near future, and other important factors discussed in the “Risk Factors” section of the Company’s Quarterly Report on Form 10-Q filed with the Securities and Exchange Commission, or SEC, on August 9, 2016, and in other filings that the Company makes with the SEC. In addition, any forward-looking statements included in this press release represent the Company’s views only as of the date of this release and should not be relied upon as representing its views as of any subsequent date. The Company specifically disclaims any obligation to update any forward-looking statements included in this press release.


News Article | April 15, 2016
Site: www.cemag.us

A sticky spaghetti and meatballs model may be sufficient to describe how the nucleus in each of our cells selectively allows the entrance and exit of certain molecules, while blocking others to protect genetic material and normal functions of the cell. That is the conclusion based on research by an international team of scientists, led by the London Centre for Nanotechnology and CIC biomaGUNE, and published in the journal eLife. Cells of humans, animals, and plants have a nucleus that contains most of their genetic material. For the appropriate use of this genetic material, it is essential that proteins and other molecules can only enter and exit the nucleus in a highly selective way, via channels in the protective membrane that surrounds the nucleus. Inside these tiny channels (nuclear pore complexes) reside specialized proteins (FG domains) that arrange similarly to sticky spaghetti, to act as a selective barrier. The molecules that cross the barrier can be thought of as meatballs. Some very particular meatballs are nuclear transport receptors, which shuttle rather freely into and out of the spaghetti-like FG domains, and enable other molecules to do so too. To study how these meatballs penetrate the channels, the scientists first made layers of FG domains of only 100,000th of a millimeter thick, and next measured how nuclear transport receptors bound to these layers. Since the results were highly similar for different FG domains and different nuclear transport receptors, the next step was to design a physical model that only included the features that were universal to all, namely that the FG domains behaved as rather sticky spaghetti interacting with the nuclear transport receptors as even stickier meatballs. This model was very successful in reproducing the experimental data. Moreover, and encouragingly, it is consistent with earlier, less quantitative work of the London team on the real channels. Given the enormous complexity of the biological structures and processes involved, it is remarkable that such a simple (polymer-physics) model applies. Its success implies that the basic mechanism underlying selective transport into and out of the cell nucleus could well be explained based on generic physical principles. Beside the London Centre for Nanotechnology and CIC biomaGUNE, the work included important contributions from the MRC Laboratory of Molecular Biology, Cambridge, the Max Planck Institute for Biophysical Chemistry in Germany, and the University of Osnabrück in Germany.


News Article | March 2, 2017
Site: www.businesswire.com

CAMBRIDGE, Mass. & CAMBRIDGE, England--(BUSINESS WIRE)--Bicycle Therapeutics, a biotechnology company pioneering a new class of therapeutics based on its proprietary bicyclic peptide (BicycleTM) product platform, announced today that Kevin Lee, Ph.D., Bicycle’s Chief Executive Officer, will present a company overview at the Cowen and Company 37th Annual Health Care Conference in Boston, MA. The presentation will take place at 8:30 a.m. ET on Tuesday, March 7, 2017 in the MIT Room at the Boston Marriott Copley Place. About Bicycle Therapeutics Bicycle Therapeutics is developing a new class of medicines to treat oncology and other debilitating diseases based on its proprietary bicyclic peptide (BicycleTM) product platform. BicyclesTM exhibit an affinity and exquisite target specificity usually associated with antibodies, while a low molecular weight delivers rapid and deep tissue penetration enabling more efficient tumor targeting. Their peptidic nature provides a “tuneable” pharmacokinetic half-life and a renal route of clearance, avoiding the liver and gastrointestinal tract toxicities often seen with other drug modalities. Bicycle Therapeutics is rapidly advancing towards the clinic with its lead molecule, BT1718, and is collaborating in oncology and other areas to realize the full potential of the technology. Bicycle Therapeutics’ unique intellectual property is based on the work initiated at the MRC Laboratory of Molecular Biology in Cambridge, U.K., by the scientific founders of the company, Sir Gregory Winter and Professor Christian Heinis. Bicycle Therapeutics is headquartered in Cambridge, U.K., with a U.S. subsidiary in Cambridge, Massachusetts. For more information, visit www.bicycletherapeutics.com.


News Article | March 2, 2017
Site: www.businesswire.com

CAMBRIDGE, Mass. & CAMBRIDGE, England--(BUSINESS WIRE)--Bicycle Therapeutics, a biotechnology company pioneering a new class of therapeutics based on its proprietary bicyclic peptide (BicycleTM) product platform, announced today that Kevin Lee, Ph.D., Bicycle’s Chief Executive Officer, will present a company overview at the Cowen and Company 37th Annual Health Care Conference in Boston, MA. The presentation will take place at 8:30 a.m. ET on Tuesday, March 7, 2017 in the MIT Room at the Boston Marriott Copley Place. About Bicycle Therapeutics Bicycle Therapeutics is developing a new class of medicines to treat oncology and other debilitating diseases based on its proprietary bicyclic peptide (BicycleTM) product platform. BicyclesTM exhibit an affinity and exquisite target specificity usually associated with antibodies, while a low molecular weight delivers rapid and deep tissue penetration enabling more efficient tumor targeting. Their peptidic nature provides a “tuneable” pharmacokinetic half-life and a renal route of clearance, avoiding the liver and gastrointestinal tract toxicities often seen with other drug modalities. Bicycle Therapeutics is rapidly advancing towards the clinic with its lead molecule, BT1718, and is collaborating in oncology and other areas to realize the full potential of the technology. Bicycle Therapeutics’ unique intellectual property is based on the work initiated at the MRC Laboratory of Molecular Biology in Cambridge, U.K., by the scientific founders of the company, Sir Gregory Winter and Professor Christian Heinis. Bicycle Therapeutics is headquartered in Cambridge, U.K., with a U.S. subsidiary in Cambridge, Massachusetts. For more information, visit www.bicycletherapeutics.com.


News Article | March 4, 2016
Site: cen.acs.org

There is an urgent need for new antimalarial drugs because the malaria parasite has developed resistance to the most widely used therapies—combinations of artemisinin and other drugs—and most treatments don’t prevent transmission, which allows resistance to spread. Researchers now report a small molecule that can kill the parasite in mice with few side effects (Nature 2016, DOI: 10.1038/nature16936). The molecule works by inhibiting the proteasome, the cell’s protein-degrading machine, in the parasites but to a much lesser extent in the host. Such selective proteasome inhibitors could complement current antimalarial drugs and lead to medications for other infectious diseases. The malaria parasite has a complex life cycle, in which it morphs through nine forms in mosquitoes and people. Researchers have been actively investigating proteasome inhibitors as antimalarial agents because inhibiting the proteasome can kill all stages of the parasite, reducing the possibility that one or more will survive treatment. Also, recent findings suggest proteasome inhibitors suppress artemisinin-resistant strains. But the inhibitors developed to date hit both the malarial and human proteasomes to a similar extent, making them toxic to people. In the new study, Matthew Bogyo and coworkers at Stanford University School of Medicine first screened a library of peptides to determine sequences favored for degradation by parasite proteasomes but not human ones. They used that information to design selective inhibitors. Then the Stanford team and Paula C. A. da Fonseca of the MRC Laboratory of Molecular Biology used cryoelectron microscopy to obtain a structure of the parasite proteasome bound to a designed inhibitor. This structure of the malarial proteasome at the inhibitor-binding site provided a guide for further optimization of the inhibitor structures. Malaria treatment specialist Benjamin Mordmüller of the University of Tübingen says the development is promising because previous studies have shown that proteasome inhibitors have the potential to kill all the different stages of the malaria life cycle. No current antimalaria drugs hit all stages, and existing drugs that do hit more than one stage aren’t equally effective against the different ones. Parasite proteasome expert Karine G. Le Roch comments that a selective proteasome inhibitor such as WLL-vs could be combined with artemisinin to decrease the spread of malarial drug resistance, if it can pass efficacy and toxicity trials. Puran S. Sijwali of the Centre for Cellular & Molecular Biology, in Hyderabad, India, a parasite drug-target specialist, notes that the general design strategy could also lead to proteasome-specific drug leads for other infectious diseases, such as trypanosome and amoeba infections, leishmaniasis, and toxoplasmosis. This article has been translated into Spanish by Divulgame.org and can be found here.


HOBOKEN, N.J.--(BUSINESS WIRE)--The Wiley Foundation, part of John Wiley & Sons, Inc. (NYSE: JWa and JWb) today announced the 16th annual Wiley Prize in Biomedical Sciences will be awarded to Joachim Frank, Richard Henderson, and Marin van Heel for pioneering developments in electron microscopy that are transforming structural studies of biological molecules and their complexes. Dr. Joachim Frank is an HHMI investigator, a Professor of Biochemistry and Molecular Biophysics and of Biological Sciences at Columbia University, and Distinguished Professor of the State University of New York at Albany. Dr. Richard Henderson is a scientist at the MRC Laboratory of Molecular Biology in Cambridge, UK. He was Director from 1996 to 2006, and is a fellow of the Royal Society and a Foreign Associate of the US National Academy of Sciences. Dr. Marin van Heel is a visiting Professor at the National Nanotechnology Laboratory – LNNano/CNPEM, Campinas, Brazil. He is an Emeritus Professor at the Institute of Biology Leiden (NeCEN) and the Department of Life Sciences, Imperial College London. “The 2017 Wiley Prize honors scientists who have developed cryo-electron microscopy to be the most important new tool for establishing atomic structures of large molecular complexes," said Dr. Günter Blobel, Chairman of the awards jury for the Wiley Prize. First awarded in 2002, The Wiley Prize in Biomedical Sciences is presented annually to recognize contributions that have opened new fields of research or have advanced concepts in a particular biomedical discipline. Among the many distinguished recipients of the Wiley Prize in Biomedical Sciences, six have gone on to be awarded the Nobel Prize in Physiology or Medicine. “The Wiley Foundation honors leadership and innovation in the development of techniques that greatly advance scientific discovery. The work of the 2017 Wiley Prize recipients Joachim Frank, Richard Henderson, and Marin van Heel truly upholds this mission,” said Deborah E. Wiley, Chair of the Wiley Foundation. “We are pleased to highlight the impact that cryo-electron microscopy has had in advancing knowledge of molecular structure and resulting cellular functions.” This year’s award of $50,000 will be presented to the winners on April 7, 2017 at the Wiley Prize luncheon at The Rockefeller University. The winners will then deliver an honorary lecture as part of The Rockefeller University Lecture Series. This event will be live streamed via the Current Protocols’ Webinar Series and registration is free. Wiley, a global company, helps people and organizations develop the skills and knowledge they need to succeed. Our online scientific, technical, medical, and scholarly journals, combined with our digital learning, assessment and certification solutions help universities, learned societies, businesses, governments and individuals increase the academic and professional impact of their work. For more than 200 years, we have delivered consistent performance to our stakeholders. Dr. Joachim Frank is an HHMI investigator, a Professor of Biochemistry and Molecular Biophysics and of Biological Sciences at Columbia University, and Distinguished Professor of the State University of New York at Albany. He is a Member of the National Academy of Sciences, and Fellow of the American Academy of Arts and Sciences, the American Association for the Advancement of Science, and the Biophysical Society. In 2014 he received the Franklin Medal in Life Science, bestowed by the Franklin Institute in Philadelphia. Dr. Richard Henderson is a scientist at the MRC Laboratory of Molecular Biology in Cambridge, UK. He was Director from 1996 to 2006, and is a fellow of the Royal Society and a Foreign Associate of the US National Academy of Sciences. Dr. Marin van Heel is a visiting Professor at the National Nanotechnology Laboratory – LNNano/CNPEM, Campinas, Brazil. He is an Emeritus Professor at the Institute of Biology Leiden (NeCEN) and the Department of Life Sciences, Imperial College London. After studying theoretical optics at the University of Groningen, his PhD thesis marked the beginning of a career in methodology development in structural biology by cryo-EM. He received the Ernst Ruska Prize 1987.


News Article | February 15, 2017
Site: www.newscientist.com

Can tiny brains grown in a dish reveal the secrets of sociability? Balls of brain tissue generated from stem cells are enabling us to understand the underlying differences between people who struggle to be sociable and those who have difficulty reining themselves in. Alysson Muotri at the University of California, San Diego, and his team created the mini-brains by exposing stem cells taken from the pulp of children’s milk teeth to cocktails of growth factors that help them mature. Eventually, they can develop as many as six layers of cerebral cortex – the outer surface of the brain. This region is much more sophisticated in humans than in other animals, and houses important circuitry governing our most complex thoughts and behaviours, including socialising with others. Each mini-brain is approximately 5 millimetres across. “Though they’re not as well defined as they are in a real brain, they resemble what you find in an embryonic fetus,” says Muotri. To understand how brain development affects sociability, the team used donated cells from children with autism and Rett syndrome, both of which are associated with impaired communication skills. They also used cells from children with Williams syndrome, a condition characterised by a hyper-sociable nature. People with Williams syndrome can be unable to restrain themselves from talking to complete strangers. The team found that mini-brains grown using stem cells from children with autism form fewer neural connections, while those from Williams syndrome children have an abnormally high number. When cells from the teeth of children with none of these conditions were used, the resulting mini-brains were somewhere in between these two extremes. “The differences are striking, and go in opposite directions,” says Muotri. “In Williams syndrome, one of the cortical layers makes large projections linking into many other layers, and these are important for sociality,” he says. “By comparison, autism-linked brains are more immature, with fewer synapses,” he says. When Muotri’s team examined donated brains from deceased people with these disorders, they found similar patterns. Research by other teams working with similar “organoids” suggests that the brains of people with autism also seem to have a higher number of inhibitory neurons, cells that act to damp down the signals transmitted through the brain. Later this week, Muotri will discuss the results and outline the team’s future plans to probe sociability at a conference on stem cells in Olympic Valley, California. Ultimately, he wants to be able to understand how humans evolved to be so social, he says. The team has begun comparing human mini-brains with ones made from chimpanzee and bonobo stem cells. “The most striking observation so far is that monkey brains mature way faster,” says Muotri. Next, Muotri wants to try stimulating the mini-brains to see how they react. To do this, the team plans to develop eye-like tissue that can sense light, and hook this up to the mini-brains. “We hope to have projections from the retina going to the visual cortex in the mini-brain,” says Muotri. “We can then stimulate the eye and see what happens in the brain.” As well as illuminating what makes us so sociable, the work may lead to treatments for conditions that affect sociability. Muotri has found that a growth factor called IGF1 can prompt mini-brains derived from cells from children with Rett syndrome to make extra neural connections. “Other people are now moving this into clinical trials in Rett syndrome,” he says. Muotri’s work is a nice demonstration of the power of mini-brains to help understand the early, cellular features of neurological disorders, says Madeline Lancaster at the MRC Laboratory of Molecular Biology in Cambridge, UK, who developed the organoid-growing method Muotri used. But studying this tissue cannot reveal the features of such disorders that are more related to behaviour, she says. “The human organoids are good for studying the very early stages of brain development, but may not reveal much about later, more mature stages on which things like sociality depend,” says John Mason at the University of Edinburgh, UK.

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