Annual Report 1998
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December 2, 2014 u vol. 111 u no. 48 u 16975–17336 Cover image: Pictured is a vermillion sea star, Mediaster aequalis,inPorlierPass,British Columbia, that shows signs of sea-star wasting disease. As of June 2014, the disease had affected 20 species of sea stars from Alaska to Baja California, but its cause is unknown. Ian Hewson et al. surveyed sea-star populations and conducted laboratory infection studies. They found that sea-star wasting disease is likely caused by a virus and identified a densovirus as a potential infectious agent. See the article by Hewson et al. on pages 17278–17283. Image courtesy of Peter Luckham (www.divemaster.ca). From the Cover 17278 Potential cause of sea-star wasting disease 17075 Human ability to evaluate probabilities 17122 X-ray free crystallography 17140 DNA binding site recognition by regulatory proteins 17182 Ebola antibodies’ modes of action Contents COMMENTARIES 16982 Going viral and the fatal vulnerability of neurons from immunity, not from infection THIS WEEK IN PNAS Lawrence Steinman See companion article on page 16053 in issue 45 of volume 111 16975 In This Issue 16984 Fuzzy universality of probability judgment Valerie F. Reyna and Charles J. Brainerd See companion article on page 17075 INNER WORKINGS—An over-the-shoulder look at scientists at work 16986 Expanding the femtosecond crystallography toolkit Sol M. Gruner 16977 Inner Workings: Freeing the dinos within See companion article on page 17122 Stephen Ornes CORE CONCEPTS—A brief introduction to emerging topics in science PNAS PLUS 16978 Core Concept: Synthetic biology—change, accelerated 16988 Significance Statements Danielle Venton Brief statements written by the authors about the significance of their papers. -
Hria Medical Foundation 2012 Review
20․12 DI VISION REVIE W Where Science and Philanthropy Converge IN THIS ISSUE: About Us and Our Services / 2 Funding Opportunities Jeffress Trust /8 Hood Foundation /10 Noonan Memorial Research Fund /11 Klarman Family Foundation /12 King Trust /13 Thome Foundation /14 Smith Family Foundation /16 Davis Foundation /17 Lymphatic Research Foundation /18 Scientific Review Committees /19 Gene Discovery in Anorexia Nervosa / 6 The Medical Foundation, a division of HRiA About Us Since 1957, foundations, bank trusts and individuals have engaged us to create and manage customized biomedical research grant programs that accelerate the pace of scientific discoveries. As evidenced by the more than 145,000 visits to our website this year alone, our funding announcements reach thousands of potential applicants for every grant cycle. And, by building a distinguished Scientific Review Committee for each program, we ensure critical and unbiased selection of the best minds in science. In 2012, we were privileged to work with foundations and bank trust departments whose grant programs distributed more than $18 million to investigators and physician-scientists across the United States and worldwide. Sally E. McNagny, M.D., M.P.H., F.A.C.P., Vice President Since 2001, Dr. McNagny has served as Vice President and head of HRiA’s Medical Foundation division where she leads biomedical research grantmaking and life sciences consulting. Dr. McNagny also serves on the faculty at Harvard Medical School and is a Fellow of the American College of Physicians. She holds a B.S. in Biology from Stanford University, an M.D. from Harvard Medical School, an M.P.H. -
Medical Advisory Board September 1, 2006–August 31, 2007
hoWard hughes medical iNstitute 2007 annual report What’s Next h o W ard hughes medical i 4000 oNes Bridge road chevy chase, marylaNd 20815-6789 www.hhmi.org N stitute 2007 a nn ual report What’s Next Letter from the president 2 The primary purpose and objective of the conversation: wiLLiam r. Lummis 6 Howard Hughes Medical Institute shall be the promotion of human knowledge within the CREDITS thiNkiNg field of the basic sciences (principally the field of like medical research and education) and the a scieNtist 8 effective application thereof for the benefit of mankind. Page 1 Page 25 Page 43 Page 50 seeiNg Illustration by Riccardo Vecchio Südhof: Paul Fetters; Fuchs: Janelia Farm lab: © Photography Neurotoxin (Brunger & Chapman): Page 3 Matthew Septimus; SCNT images: by Brad Feinknopf; First level of Rongsheng Jin and Axel Brunger; iN Bruce Weller Blake Porch and Chris Vargas/HHMI lab building: © Photography by Shadlen: Paul Fetters; Mouse Page 6 Page 26 Brad Feinknopf (Tsai): Li-Huei Tsai; Zoghbi: Agapito NeW Illustration by Riccardo Vecchio Arabidopsis: Laboratory of Joanne Page 44 Sanchez/Baylor College 14 Page 8 Chory; Chory: Courtesy of Salk Janelia Farm guest housing: © Jeff Page 51 Ways Illustration by Riccardo Vecchio Institute Goldberg/Esto; Dudman: Matthew Szostak: Mark Wilson; Evans: Fred Page 10 Page 27 Septimus; Lee: Oliver Wien; Greaves/PR Newswire, © HHMI; Mello: Erika Larsen; Hannon: Zack Rosenthal: Paul Fetters; Students: Leonardo: Paul Fetters; Riddiford: Steitz: Harold Shapiro; Lefkowitz: capacity Seckler/AP, © HHMI; Lowe: Zack Paul Fetters; Map: Reprinted by Paul Fetters; Truman: Paul Fetters Stewart Waller/PR Newswire, Seckler/AP, © HHMI permission from Macmillan Page 46 © HHMI for Page 12 Publishers, Ltd.: Nature vol. -
Prion Diseases in Knock-In Mice Carrying Single Prp Codon Substitutions Associated with Human Diseases
Profoundly different prion diseases in knock-in mice carrying single PrP codon substitutions associated with human diseases Walker S. Jacksona,b,c,1, Andrew W. Borkowskia,b,c, Nicki E. Watsona, Oliver D. Kingd, Henryk Faase, Alan Jasanoffe,f, and Susan Lindquista,b,c,2 aWhitehead Institute for Biomedical Research, Cambridge, MA 02142; bHoward Hughes Medical Institute, cDepartment of Biology, and fDepartments of Biological Engineering, Brain and Cognitive Sciences, and Nuclear Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139; dDepartment of Cell and Developmental Biology, University of Massachusetts Medical School, Worcester, MA 01655; and eFrances Bitter Magnet Laboratory, Cambridge, MA 02139 Contributed by Susan Lindquist, July 9, 2013 (sent for review March 7, 2013) In man, mutations in different regions of the prion protein (PrP) linked to it, provides an important general model for such are associated with infectious neurodegenerative diseases that investigations. have remarkably different clinical signs and neuropathological There are several types of human prion diseases, each begin- lesions. To explore the roots of this phenomenon, we created ning with pathologic processes in a different brain region and fi – a knock-in mouse model carrying the mutation associated with leading to distinct functional de cits: cognition [Creutzfeldt – – one of these diseases [Creutzfeldt–Jakob disease (CJD)] that was Jakob disease (CJD)], movement control (Gerstmann Sträussler Scheinker syndrome), or sleep and autonomic functions [fatal exactly analogous to a previous knock-in model of a different fl prion disease [fatal familial insomnia (FFI)]. Together with the familial insomnia (FFI)] (7). Prion diseases also af ict animals WT parent, this created an allelic series of three lines, each express- and include bovine spongiform encephalopathy (BSE) of cattle, scrapie of sheep and goats, and chronic wasting disease (CWD) ing the same protein with a single amino acid difference, and with of deer and elk (1). -
Structure & Symmetry
HAPPY HOLIDAYS ASBMB MEMBERS December 2008 Structure & Symmetry American Society for Biochemistry and Molecular Biology J\\PfliGifk\`ej n`k_*.#'''>=G$kX^^\[FI=Zcfe\j 8 $@C- 9 "@C- : ; >=G$kX^^\[Kil\FI=Zcfe\jXi\kiXej]\Zk\[`ekf?<B)0* Z\ccjXe[k_\kX^^\[gifk\`ejXi\m`jlXc`q\[[li`e^@C$- `e[lZ\[elZc\XikiXejcfZXk`feJK8K*#gXe\c8Xe[9 Xe[`e Ôcfgf[`XXe[jki\jjÔY\i]fidXk`fe8Zk`e#gXe\c:Xe[; % Kil\FI= Fi`>\e\jXclk\j >\efd\n`[\FI=Zcfe\j k_\>=Gg`fe\\ij ]fik_\`iEfY\c ]fikX^^\[gifk\`e\ogi\jj`fe Gi`q\XnXi[ ×:$k\id`eXckX^f]>=G ×J\hl\eZ\m\i`Ô\[Xe[^lXiXek\\[ ×<Xj`cpj_lkkc\[`ekf)'[\jk`eXk`fem\Zkfij ×KiXej]\Zk`fe$i\X[p1('l^gcXjd`[;E8 fi`^\e\%Zfd&fi] ORG-041-GFPTaggedAd_ASBMB_v7.indd 1 10/20/08 12:29:39 PM contents DECEMBER 2008 ON THE COVER: Captivated by the symmetry society news of molecular structure, Sung-Hou Kim has been a 2 From the Editor leader in revealing symmetry 3 President’s Message through his studies in crystallography and 5 Letters to the Editor structural genomics. 30 6 Washington Update 12 Retrospective: Anthony G. San Pietro FASEB releases new Breakthroughs in special interest Bioscience. 6 13 Science’s Role in Foreign Policy 14 ASBMB Round Table: Jim Wells and Mary Woolley 16 Keeping Women in Science 19 Grammar and Writing Tips 2009 meeting 20 The 2009 Fritz Lipmann Lectureship: Douglas C. Rees 21 The 2009 ASBMB Merck Award: John Kuriyan 22 The 2009 FASEB Excellence in Science Award: Susan Lindquist science focus 30 Sung-Hou Kim: Consummate Crystallographer departments 7 News from the Hill 10 Member Spotlight 23 Education and Training A leaky pipeline for women scientists. -
Susan Lee Lindquist (1949–2016)
In Memoriam Sue was a spectacular scientist who com- at the University of Chicago, where she bined a searing intellect with deep wis- would later join the faculty (1978) and rise Susan Lee Lindquist (1949–2016) dom, sagacious intuition, and limitless to full professor (1988). While at the Uni- creativity. These characteristics enabled versity of Chicago, Sue married Edward Sue to make connections across dispa- Buckbee and would have two wonderful 1, James Shorter * rate disciplines that nobody else could daughters, Alana and Nora. She also make. Her infectious esprit for scientific launched a remarkable and radical series Lindquist was a visionary and pio- discovery was combined with disarming of trailblazing discoveries. These contin- neer who transformed our under- warmth, positivity, openness, directness, ued when Sue moved her research pro- standing of how protein folding and generosity, which made her an inspi- gram to the Whitehead Institute for rational, nurturing, and indefatigable men- Biomedical Research at Massachusetts sculpts biology, evolution, and dis- tor. These synergistic traits empowered Institute of Technology (MIT), which is ease. She revealed several unantici- extraordinarily effective collaborations where I trained with Sue as a postdoctoral pated mechanisms by which protein between scientists from diverse back- fellow (2002–2007). Sue would spend the folding can buffer, release, and grounds and disciplines. Indeed, rest of her career at the Whitehead Insti- potentiate genetic variation in researchers from diverse backgrounds – tute as Director (2001–2004), Institute response to environmental stress, physicists, chemists, biochemists, biolo- Member (2001–2016), and Professor of thereby enabling the rapid evolution gists, mathematicians, and physicians – Biology at MIT (2001–2016). -
Wang-Cv-July2017.Pdf
CURRICULUM VITAE Samuel Sheng-Hung Wang, Ph.D. Born: May 4, 1967 Address: Neuroscience Institute, Princeton University, Princeton, NJ 08544 Telephone: (609) 258-0388 FAX: (609) 258-1028 E-mail: sswang [at] princeton.edu Web: http://synapse.princeton.edu Research interests 1) Neuroscience – integrative role of the cerebellum in sensory learning and autism 2) Optical methods for observing and manipulating living brain tissue 3) Statistical analysis of data in neuroscience, development, and politics Education 1980-1982 Riverside Poly High School, Riverside, California 1982-1986 B.S. with honor, Physics, California Institute of Technology 1986-1993 Ph.D., Neurosciences, Stanford University (advisor: Stuart H. Thompson) Professional positions 1994-1995, 1996-1997 Postdoctoral fellow, Duke University (with George J. Augustine) 1995-1996 Congressional Science Fellow, Senate Committee on Labor and Human Resources (with Senator Edward M. Kennedy) 1997-1999 Postdoctoral Member of Technical Staff, Biological Computation Res. Dept., Bell Labs Lucent Technologies (with David W. Tank and Winfried Denk) 2000-2006 Assistant Professor, Department of Molecular Biology, Princeton University 2006-2015 Associate Professor, Department of Molecular Biology and Princeton Neuroscience Institute, Princeton University 2013- Faculty associate, Princeton Program in Law and Public Affairs 2014- Faculty affiliate, Cognitive Science 2015- Professor, Princeton Neuroscience Institute and Department of Molecular Biology, Princeton University 2015- Faculty affiliate, Program -
Calcineurin Determines Toxic Versus Beneficial Responses to Α-Synuclein
Calcineurin determines toxic versus beneficial responses to α-synuclein Gabriela Caraveoa,b, Pavan K. Aulucka,c,1, Luke Whitesella, Chee Yeun Chunga, Valeriya Barua,b, Eugene V. Mosharovd, Xiaohui Yane, Manu Ben-Johnyf, Martin Sosteg, Paola Picottig, Hanna Kime, Kim A. Caldwelle, Guy A. Caldwelle, David Sulzerd,h, David T. Yuef, and Susan Lindquista,b,2 aWhitehead Institute for Biomedical Research, Cambridge, MA 02142; bHoward Hughes Medical Institute, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139; cDepartment of Pathology, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114; Departments of dNeurology and hPsychiatry, Columbia University Medical Center, New York, NY 10032; eDepartment of Biological Sciences, The University of Alabama, Tuscaloosa, AL 35487; fDepartments of Biomedical Engineering and Neuroscience, The Johns Hopkins University School of Medicine, Baltimore, MD 21205; and gDepartment of Biology, Institute of Biochemistry, Eidgenossische Technische Hochschule Zurich, Zurich CH-8093, Switzerland Contributed by Susan Lindquist, July 15, 2014 (sent for review May 7, 2014) + Calcineurin (CN) is a highly conserved Ca2 –calmodulin (CaM)- tigations, given their genetic tractability and the remarkable + + dependent phosphatase that senses Ca2 concentrations and trans- conservation of Ca2 -signaling pathways from yeast to humans duces that information into cellular responses. Ca2+ homeostasis (14, 15). Moreover, the expression of human α-syn in yeast leads is disrupted by α-synuclein (α-syn), a small lipid binding protein to cellular pathologies directly relevant to neurons and PD, in- whose misfolding and accumulation is a pathological hallmark of cluding nitrosative stress (16, 17), defects in vesicle trafficking several neurodegenerative diseases. We report that α-syn, from (18–20), and faulty mitochondrial function (21, 22). -
Division of Extramural Activities Annual Report 2002
Division of Extramural Activities Annual Report 2002 National Institutes of Health National Cancer Institute Molecular Diagnosis of Cancer Gene expression profiling using DNA microarrays is a technology that arose as a consequence of the Human Genome Project. With DNA microarrays, it is possible to determine the activity (“expression”) of tens of thousands of genes in parallel on microarray plates. The expression of genes influences the biological behavior of a cell because it dictates which proteins the cell can make and gives cells their unique characteristics. In the DNA microarray images shown at the bottom of the cover illustration, each spot represents a different human gene. Red, yellow, and green spots indicate that a gene is expressed at high, intermediate, and low levels, respectively. The pattern of expression of all of the genes in a cell constitutes its gene expression “profile.” Using DNA microarrays, different types of normal and malignant cells can be distinguished from one another because they have distinct gene expression profiles. Shown at the top of the cover illustration are photomicrographs of lymph node biopsies from two patients with diffuse large B cell lymphoma. The tumor at the right belongs to the germinal center B cell-like subgroup of diffuse large B cell lymphoma. Patients with this lymphoma type have a relatively favorable 5-year survival rate of 59% following multi-agent chemotherapy. The tumor at the left belongs to the activated B cell-like subgroup of diffuse large B cell lymphoma. Patients with this lymphoma type have a less favorable 5-year survival rate of 31%. Although the tumors from these patients were indistinguishable histologically, they had striking differences in their gene expression profiles, as exemplified by the microarray images shown below each lymphoma subgroup. -
WCBR Program3
Welcome to the Thirty-Fifth Annual Winter Conference on Brain Research The Winter Conference on Brain Research (WCBR) was founded in 1968 to promote free exchange of information and ideas within neuroscience. It was the intent of the founders that both formal and informal interactions would occur between clinical and laboratory based neuroscientists. During the past thirty years neuroscience has grown and expanded to include many new fields and methodologies. This diversity is also reflected by WCBR participants and in our program. A primary goal of the WCBR is to enable participants to learn about the current status of areas of neuroscience other than their own. Another objective is to provide a vehicle for scientists with common interests to discuss current issues in an informal setting. On the other hand, WCBR is not designed for presentations limited to communicating the latest data to a small group of specialists; this is best done at national society meetings. The program includes panels (reviews for an audience not neces- sarily familiar with the area presented), workshops (informal discussions of current issues and data), and a number of posters. The annual conference lecture will be presented at the Sunday breakfast on Sunday, January 27. Our guest speaker will be Dr. Donald Kennedy, Editor-in-Chief of Science. On Tuesday, January 29, a town meeting will be held for the Aspen/Snowmass commu- nity at which Dr. George Ricaurte, and WCBR participants will discuss drug addiction and toxicity of addictive drugs. Also, participants in the WCBR Outreach Program will present sessions at local schools throughout the week to pique students’ interest in science. -
NIH Conflict of Interest Regs Revised
OCTOBEROCTOBER 2005 www.asbmb.org Constituent Society of FASEB AMERICAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY NIH Conflict of Interest Regs Revised SEE PAGE 30 FOR NEW CLARA BENSON TRAVEL FELLOWSHIP AWARD Held in conjunction with EB2006 Custom Antibodies Your Way! Choose the protocol that is right for you! QwikScreen ™: 65 day, 2 rabbit protocol - 4 immunizations, 3 bleeds/rabbit (~100ml serum), customer supplied peptide/protein - Options: Peptide synthesis, immunograde Conjugation to carrier u ELISA u u Animal extensionsMS analysis $685 Standard: 80 day, 2 rabbit protocol - 5 immunizations, 5 bleeds/rabbit (~ 200ml ser Options: um), ELISA, customer supplied peptide/pr Peptide synthesis MS Check™ peptide sequence confirmation u HPLC purified peptide Affinity purification otein - Pinnacle: $975 u HPLC and MS analysis u Complete Affinity Purified Protocol- Animal extensions 2 rabbit pr 5 bleeds/rabbitotocol, (~ 200mlepitope serum), design, peptide PhD technical synthesis support, (up to 20mer),5 immunizations, HPLC purified to ~85%, 5+mg peptide to customer, ELISA, evaluation period, affinity purification, and morMS Check™ peptide sequence confirmationNo Hidden Charges! e… - Discounts for Multiple Protocols$1795 , Includes peptide sequencing by CID MS/MS– u Guaranteed Peptide Let our enthusiasm for scienceExpert workTechnical for SupportFidelity! P: 508.303.8222 www.21stcenturybio.com Toll-free: 877.217.8238 F: 508.303.8333 you! E: [email protected] www.asbmb.org AMERICAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY OCTOBER -
The New Eppendorf Micro Centrifuge
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