Themysterious Centromere
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Caso Relativamente Recente
Perché chiamiamo “fondamentale” la Cenerentola della ricerca? (di M. Brunori) Neanche nel Pnrr si trovano speranze di cambiamento e iniziative coraggiose per la ricerca di base. Ma nelle scienze della vita non sono rare le scoperte nate da progetti di ricerca curiosity driven che richiedono tempo per portare risultati Soci dell'Accademia dei Lincei. (a cura di Maurizio Brunori, Prof. emerito di Chimica e Biochimica, Sapienza Università di Roma, Presidente emerito della Classe di Scienze FMN dell’Accademia dei Lincei) Nelle scienze della vita non sono infrequenti le scoperte innovative nate da progetti di ricerca di base, iniziati per cercare di comprendere qualche importante proprietà di un essere vivente, misteriosa ma ovviamente necessaria se è stata conservata nel corso dell’evoluzione. Questi progetti sono quelli che si iniziano per curiosità intellettuale, ma richiedono libertà di iniziativa, impegno pluriennale e molto coraggio in quanto di difficile soluzione. Un successo straordinario noto a molti è quello ottenuto dieci anni fa da due straordinarie ricercatrici, Emmanuelle Charpentier e Jennifer Doudna; che a dicembre hanno ricevuto dal Re di Svezia il Premio Nobel per la Chimica con la seguente motivazione: “for the development of a new method for genome editing”. Nel 2018 in occasione di una conferenza magistrale che la Charpentier tenne presso l’Accademia Nazionale dei Lincei, avevo pubblicato sul Blog di HuffPost un pezzo per commentare l’importanza della scoperta di CRISPR/Cas9, un kit molecolare taglia-e-cuci che consente di modificare con precisione ed efficacia senza precedenti il genoma di qualsiasi essere vivente: batteri, piante, animali, compreso l’uomo. NOBEL PRIZE Nobel Chimica Non era mai accaduto che due donne vincessero insieme il Premio Nobel. -
[email protected] (609) 258-5981 Jonikaslab.Princeton.Edu Updated 3/10/2021
Martin Casimir Jonikas, Ph.D. Assistant Professor, Department of Molecular Biology Princeton University, Princeton, NJ 08544 [email protected] (609) 258-5981 jonikaslab.princeton.edu updated 3/10/2021 VISION My group seeks to advance the basic understanding of cell biology. We study the pyrenoid, a fascinating phase-separated organelle that enhances CO2 capture in nearly all eukaryotic algae. Understanding the pyrenoid is important for three reasons: (1) the pyrenoid plays a central role in our planet’s carbon cycle, (2) the pyrenoid embodies fundamental questions in organelle biogenesis, and (3) engineering a pyrenoid into land plants could dramatically increase crop yields. To accelerate progress, we are developing community resources for the unicellular green alga Chlamydomonas reinhardtii as a model system for photosynthetic organisms. My group also seeks to nurture and train future world-leading scientists. EDUCATION 2004 B.S., Aerospace Engineering, Massachusetts Institute of Technology 2009 Ph.D., Biochemistry and Molecular Biology, University of California, San Francisco. Research advisors: Dr. Jonathan Weissman and Dr. Peter Walter PROFESSIONAL POSITIONS 2010-2016 Young Investigator (faculty position equivalent to Assistant Professor), Department of Plant Biology, Carnegie Institution for Science, Stanford, CA 2011-2016 Assistant Professor by courtesy, Department of Biology, Stanford University, Stanford, CA 2016-present Assistant Professor, Department of Molecular Biology, Princeton University, Princeton, NJ 2019-present Affiliated Faculty, Princeton Quantitative and Computational Biology Program AWARDS AND HONORS 2002 1st place, MIT 2.007 Robotics Competition 2005 National Science Foundation Graduate Research Fellowship 2009 Harvard Bauer Fellowship (declined) 2010 Air Force Office of Scientific Research Young Investigator Award 2015 National Institutes of Health Director's New Innovator Award 2016 HHMI-Simons Faculty Scholar Award 2020 Vilcek Prize for Creative Promise in Biomedical Science Martin Casimir Jonikas, Ph.D. -
Quantum Objects: Sculpture Inspired by the Deeper Nature of Reality
Article Frontispiece: Birth of an Idea, steel, glass, and wood, 60 x 32 x 32 in (150 x 80 x 80 cm), 2007. (<c> Julian Voss-Andreae. Photo: Dan Kvitka. Collection of Roderick MacKinnon, Rockefeller University, New York City, N.Y.) This sculpture, based on the structure of the potassium channel protein, was commissioned by Roderick MacKinnon, who won the 2003 Nobel Prize in Chemistry for his work on this structure. Ion channels function as our nervous system’s smallest logical units, controlling the nerve cells’ ability to fire. For a color image see the artist’s website [1]. 1 Unraveling Life's Building Blocks: Novel Sculpture Inspired by Proteins December 23, 2010 Julian Voss-Andreae Artist/Scientist 1517 SE Holly Street, Portland, OR 97214, USA Email: [email protected] Website: www.JulianVossAndreae.com Abstract The foundation of life is explored through art. Inspired by life’s molecular building blocks, the presented work recreates the emergence of three-dimensional bodies from one-dimensional DNA. Utilizing an algorithmic approach as his point of departure, the artist follows his vision freely, creating sculptures which bring life’s isolated components emotionally back to life. In this sequel to an earlier Leonardo article, which covers the inception of his protein-inspired sculptures [2], the author presents the unfolding of his vision: Large-scale works of increasing formal and conceptual complexity display the emergence of an organic aesthetics from geometric elements and inspire a more holistic view of life than that provided by reductionist science alone. 2 Introduction There are a number of common themes weaving through the fabric of my sculptural work. -
Channel Hoppers Land Chemistry Nobel Jim Giles Two Structural Biologists Credited With
news Channel hoppers land chemistry Nobel Jim Giles Two structural biologists credited with A. ABBOTT transforming our understanding of how cells work have been awarded the 2003 R. BOREA/AP Nobel Prize in Chemistry. Peter Agre of Johns Hopkins University in Baltimore and Roderick MacKinnon of the Rockefeller University in New York share the prize for experiments that revealed the intri- cate workings of the channels that allow ions and water to enter and leave cells. MacKinnon is perhaps the most widely tipped Nobel winner of recent years.In a land- mark 1998 paper (D. A. Doyle et al. Science 280, 69–77; 1998), he and his colleagues pro- vided the first detailed three-dimensional Roderick MacKinnon (left) and Peter Agre’s work on cell-membrane proteins has won them recognition. picture of a protein that acts as a channel to control the flow of potassium ions across cell deserved a Nobel.“His work is a tour de force,” Kuhajda and P. Agre J. Biol. Chem. 263, membranes. This channel is immensely says John Walker, a structural biologist at the 15634–15642; 1988). “No one had seen it important to neuroscientists, as the flow of University of Cambridge, UK. “The award is before,but we found that it was the fifth most potassium ions helps to generate the voltage absolutely spot on and richly deserved.” abundant protein in the cell,” says Agre. pulses that brain cells use to communicate. MacKinnon was on holiday when the “That’s like coming across a big town that’s Before MacKinnon’s paper, many biolo- prize was announced, and couldn’t be not on the map.It gets your attention.” gists had questioned whether the technique informed directly by the Nobel prize com- The protein, now known as aquaporin 1, he used — X-ray crystallography — could be mittee. -
Nobel Laureates Endorse Joe Biden
Nobel Laureates endorse Joe Biden 81 American Nobel Laureates in Physics, Chemistry, and Medicine have signed this letter to express their support for former Vice President Joe Biden in the 2020 election for President of the United States. At no time in our nation’s history has there been a greater need for our leaders to appreciate the value of science in formulating public policy. During his long record of public service, Joe Biden has consistently demonstrated his willingness to listen to experts, his understanding of the value of international collaboration in research, and his respect for the contribution that immigrants make to the intellectual life of our country. As American citizens and as scientists, we wholeheartedly endorse Joe Biden for President. Name Category Prize Year Peter Agre Chemistry 2003 Sidney Altman Chemistry 1989 Frances H. Arnold Chemistry 2018 Paul Berg Chemistry 1980 Thomas R. Cech Chemistry 1989 Martin Chalfie Chemistry 2008 Elias James Corey Chemistry 1990 Joachim Frank Chemistry 2017 Walter Gilbert Chemistry 1980 John B. Goodenough Chemistry 2019 Alan Heeger Chemistry 2000 Dudley R. Herschbach Chemistry 1986 Roald Hoffmann Chemistry 1981 Brian K. Kobilka Chemistry 2012 Roger D. Kornberg Chemistry 2006 Robert J. Lefkowitz Chemistry 2012 Roderick MacKinnon Chemistry 2003 Paul L. Modrich Chemistry 2015 William E. Moerner Chemistry 2014 Mario J. Molina Chemistry 1995 Richard R. Schrock Chemistry 2005 K. Barry Sharpless Chemistry 2001 Sir James Fraser Stoddart Chemistry 2016 M. Stanley Whittingham Chemistry 2019 James P. Allison Medicine 2018 Richard Axel Medicine 2004 David Baltimore Medicine 1975 J. Michael Bishop Medicine 1989 Elizabeth H. Blackburn Medicine 2009 Michael S. -
October 2017 Current Affairs
Unique IAS Academy – October 2017 Current Affairs 1. Which state to host the 36th edition of National Games of India in 2018? [A] Goa [B] Assam [C] Kerala [D] Jharkhand Correct 2. Which Indian entrepreneur has won the prestigious International Business Person of the Year award in London for innovative IT solutions? [A] Birendra Sasmal [B] Uday Lanje [C] Madhira Srinivasu [D] Ranjan Kumar 3. The United Nations‟ (UN) International Day of Non-Violence is observed on which date? [A] October 4 [B] October 1 [C] October 2 [D] October 3 4. Which country to host the 6th edition of World Government Summit (WGS)? 0422 4204182, 9884267599 1st Street, Gandhipuram Coimbatore Page 1 Unique IAS Academy – October 2017 Current Affairs [A] Israel [B] United States [C] India [D] UAE 5. Who of the following has/have won the Nobel Prize in Physiology or Medicine 2017? [A] Jeffrey C. Hall [B] Michael Rosbash [C] Michael W. Young [D] All of the above 6. Which state government has launched a state-wide campaign against child marriage and dowry on the occasion of Mahatma Gandhi‟s birth anniversary? [A] Odisha [B] Bihar [C] Uttar Pradesh [D] Rajasthan 7. The 8th Conference of Association of SAARC Speakers and Parliamentarians to be held in which country? [A] China [B] India [C] Sri Lanka [D] Nepal Correct 8. Which committee has drafted the 3rd National Wildlife Action Plan (NWAP) for 2017- 2031? [A] Krishna Murthy committee [B] JC Kala committee 0422 4204182, 9884267599 1st Street, Gandhipuram Coimbatore Page 2 Unique IAS Academy – October 2017 Current Affairs [C] Prabhakar Reddy committee [D] K C Patan committee 9. -
Quantifying Nucleation in Vivo Reveals the Physical Basis of Prion-Like Phase Behavior
bioRxiv preprint doi: https://doi.org/10.1101/205690; this version posted March 2, 2018. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Quantifying nucleation in vivo reveals the physical basis of prion-like phase behavior 1,3 1,3 1,2,3 1,3 1,3 Tarique Khan , Tejbir S. Kandola , Jianzheng Wu , Shriram Venkatesan , Ellen Ketter , 1 1 1 1 1 Jeffrey J. Lange , Alejandro Rodríguez Gama , Andrew Box , Jay R. Unruh , Malcolm Cook , 1,2, and Randal Halfmann * 1 Stowers Institute for Medical Research, 1000 East 50th Street, Kansas City, MO 64110 2 Department of Molecular and Integrative Physiology, University of Kansas Medical Center, 3901 Rainbow Boulevard, Kansas City, KS 66160, USA 3 These authors contributed equally *Corresponding author: [email protected] Highlights ● Distributed Amphifluoric FRET (DAmFRET) quantifies nucleation in living cells ● DAmFRET rapidly distinguishes prion-like from non-prion phase transitions ● Nucleation barriers allow switch-like temporal control of protein activity ● Sequence-intrinsic features determine the concentration-dependence of nucleation barriers Summary Protein self-assemblies modulate protein activities over biological time scales that can exceed the lifetimes of the proteins or even the cells that harbor them. We hypothesized that these time scales relate to kinetic barriers inherent to the nucleation of ordered phases. To investigate nucleation barriers in living cells, we developed Distributed Amphifluoric FRET (DAmFRET). DAmFRET exploits a photoconvertible fluorophore, heterogeneous expression, and large cell numbers to quantify via flow cytometry the extent of a protein’s self-assembly as a function of cellular concentration. -
Molecular Chaperones & Stress Responses
Abstracts of papers presented at the 2010 meeting on MOLECULAR CHAPERONES & STRESS RESPONSES May 4–May 8, 2010 CORE Metadata, citation and similar papers at core.ac.uk Provided by Cold Spring Harbor Laboratory Institutional Repository Cold Spring Harbor Laboratory Cold Spring Harbor, New York Abstracts of papers presented at the 2010 meeting on MOLECULAR CHAPERONES & STRESS RESPONSES May 4–May 8, 2010 Arranged by F. Ulrich Hartl, Max Planck Institute for Biochemistry, Germany David Ron, New York University School of Medicine Jonathan Weissman, HHMI/University of California, San Francisco Cold Spring Harbor Laboratory Cold Spring Harbor, New York This meeting was funded in part by the National Institute on Aging; the National Heart, Lung and Blood Institute; and the National Institute of General Medical Sciences; branches of the National Institutes of Health; and Enzo Life Sciences, Inc. Contributions from the following companies provide core support for the Cold Spring Harbor meetings program. Corporate Sponsors Agilent Technologies Life Technologies (Invitrogen & AstraZeneca Applied Biosystems) BioVentures, Inc. Merck (Schering-Plough) Research Bristol-Myers Squibb Company Laboratories Genentech, Inc. New England BioLabs, Inc. GlaxoSmithKline OSI Pharmaceuticals, Inc. Hoffmann-La Roche Inc. Sanofi-Aventis Plant Corporate Associates Monsanto Company Pioneer Hi-Bred International, Inc. Foundations Hudson-Alpha Institute for Biotechnology Front cover, top: HSP90, a regulator of cell survival. Inhibition of HSP90 activity by drugs like geldanamycin (GA) destabilizes client proteins which ultimately lead to the onset of apoptosis. Dana Haley-Vicente, Assay Designs (an Enzo Life Sciences company). Front cover, bottom: C. elegans expressing a proteotoxic polyglutamine- expansion protein. Richard Morimoto, Northwestern University. -
2017 Nobel Prize in Chemistry Awarded to Prof. Joachim Frank
2017 Nobel Prize in Chemistry Awarded to Prof. Joachim Frank October 4, 2017 Columbia University congratulates Joachim Frank, PhD, professor of biochemistry and molecular biophysics and of biological sciences, a winner of the Nobel Prize in Chemistry 2017, shared with Richard Henderson and Jacques Dubochet “for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution.” Joachim Frank's Bio Joachim Frank, PhD, is a professor of biochemistry and molecular biophysics at Columbia University Medical Center and biological sciences at Columbia University. Dr. Frank helped pioneer the development of cryo-electron microscopy, a technique used to reveal the structures of large organic molecules at high resolution. Dr. Frank developed the necessary computational methods for reconstructing the three- dimensional shape of biological molecules from thousands of two-dimensional images of molecules, methods employed today by most structural biologists who use electron microscopy. Cryo-electron microscopy is commonly used by structural biologists to study the molecular processes inside cells that drives protein synthesis. Using this technique, Dr. Frank has made important discoveries about the interactions between ribosomes (complex molecules that serve as the ‘factories’ of the cell) and other proteins in the cell. In a 2013 paper in Nature, Dr. Frank uncovered unique details about ribosomes from the parasite that causes African sleeping sickness that could lead to the development of new drugs for this disease. In another Nature paper later that year, he revealed how viral RNA commandeers the ribosome of the virus’s host to produce new viruses. Dr. Frank was born in Germany during World War II. -
11/05/09 Agenda Attachment 6
Bioinformatics @ UCSF: Faculty Multidisciplinary graduate study in biological composition, structure, David Agard function and evolution at the [email protected] molecular and systems levels Professor, Biochemistry & Biophysics Apply Now Structure, function, and folding of proteins, chromosomes, and About the Program centrosomes Training Program: Program Overview Core Curriculum Nadav Ahituv Electives [email protected] Seminars & Journal Club Assistant Professor, Bioengineering and Therapeutic Sciences Academic Progression & Procedures Deciphering the role of gene regulatory sequences in human People: biology and disease Students Faculty Alumni Patricia Babbitt Current Events [email protected] Admission Information Professor, Bioengineering and Therapeutic Sciences and Links Pharmaceutical Chemistry Contact Computational and experimental analysis of protein NEWS: UCSF wins HHMI Award for its superfamilies for functional inference and enzyme design Integrative Program in Complex Biological Systems Bruce Conklin [email protected] Associate Professor, Gladstone Institute of Cardiovascular Disease, Medicine & Pharmacology Combining the tools of molecular biology, genetics, bioinformatics, and physiology to answer fundamental issues in pharmacology. Joe DeRisi [email protected] Hughes Investigator, Associate Professor, Biochemistry & Biophysics Malaria gene expression profiling, functional genomics, microarrays Ken Dill [email protected] Professor, Pharmaceutical Chemistry Statistical mechanics of biomolecules, protein -
Vita-202106.Pdf
Curriculum Vitae (major activities) Christoffer Eric Petersen (he/him) Education • Bachelor of Science in History (summa cum laude), Oregon State University, 1999. • Bachelor of Science in Sociology (summa cum laude), Oregon State University, 1999. Employment • Senior Faculty Research Assistant 2, Oregon State University Libraries and Press, Special Collections and Archives Research Center, July 2019 to present • Senior Faculty Research Assistant 1, Oregon State University Libraries and Press, Special Collections and Archives Research Center, July 2013 to June 2019. • Faculty Research Assistant, Oregon State University Libraries and Press, Special Collections/Special Collections and Archives Research Center, October 1999 to June 2013. • Temporary Library Technician 3, Oregon State University Libraries Special Collections, June- October 1999. I. Linus Pauling and the Pauling Legacy Pauling: Arrangement and Description The physical processing, arrangement, description and provision of access to the Ava Helen and Linus Pauling Papers was the central focus of my work from 1999-2006. I led all aspects of this undertaking. The completed Pauling Catalogue was self-published as a six-volume set, and widely reviewed. Pauling: Digital Projects The Pauling Blog – http://paulingblog.wordpress.com I am the founder, editor and publisher of this resource, which has been releasing new content about once per week since its creation in 2008. Consisting primarily of original research, The Pauling Blog is a major resource for the study of Linus Pauling’s life and work, and a project with few peers in the world of archives and special collections. Digital Exhibits - http://scarc.library.oregonstate.edu/digitalresources/pauling/ Six Documentary History sites were created and released by Special Collections/SCARC from 2003-2013, each following a similar format. -
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HUMBOLDT No. 108 / 2018 No. KOSMOSResearch – Diplomacy – Internationality DEUTSCHE VERSION: BITTE WENDEN Coming to change Ten years of Alexander von Humboldt Professorships ALL LOVE EACH OTHER THERE’S SOMETHING WRONG HERE The advantages of polygamy and How social media can make science better why it so seldom works Ten years of Alexander von Humboldt Professorships With a value of five million euros, the Alexander von Humboldt Professorship is the most highly-endowed research award in Germany and draws top international researchers to German universities. It is financed by the Federal Ministry of Education and Research. David Ausserhofer David / www.humboldt-professur.de/en Photo: Humboldt Foundation Humboldt Photo: Photo: Fati Aziz, Fotolia / preto_perola HUMBOLDTIANS IN PRIVATE MY (NON-)SELFIE WITH THE GERMAN PRESIDENT Hello, can you see the guy at the back of the pic with the engaging smile? That’s me. I’m surrounded by hundreds of Humboldtians at the Humboldt Foundation’s Annual Meeting in the beautiful grounds of Schloss Bellevue, the main residence of the German head of state in Berlin. Federal President Frank-Walter Steinmeier just held a speech welcoming his guests. And now we are all waiting to meet him per- sonally and – best case – get a photo taken together. Of course, not everyone will be so lucky. After all, the President doesn’t have all day. Well, in the end, I at least, was not successful – or that’s what I orig- inally thought. After shaking countless hands and posing for as many selfies, the President took his leave without having a photo taken with me.