Archive for the ‘Nobel Prize WInners’ Category

The History, Uses, and Future of the Nobel Prize, 1:00pm – 6:00pm, Thursday, October 4, 2018, Harvard Medical School

Reporter in Real Time: Aviva Lev-Ari, PhD, RN


Center for the History of Medicine

Francis A. Countway Library of Medicine

invites you to register for

 The History, Uses, and Future of the Nobel Prize

1:00pm – 6:00pm, Thursday, October 4, 2018

A half-day symposium bringing together an international group of historians and Nobel laureates to consider the history of the Nobel Prize and its enduring social, political, and scientific roles


Panel I: Scientific Credit and the History of the Nobel Prize

Chair: Allan Brandt (Harvard Medical School and Harvard University) /

Jacalyn M. Duffin (Queen’s University): Commemorating Excellence: the Nobel Prize and the Historical Sociology of Science /

Nils Hansson, Thorsten Halling,  and

Heiner Fangerau (Heinrich Heine-University): The First US-American Nobel Prize Nominees in Medicine (and why they failed) /

Jeffrey Flier (Harvard Medical School): The Past, Present, and Future of Scientific Credit in Biomedicine


Panel II: The Nobel – and Ig Nobel – Prize in Practice

Chair: David S. Jones (Harvard Medical School and Harvard University) /

David Kaiser (Massachusetts Institute of Technology): But Does it Scale? Awarding Nobel Prizes in Physics amid Exponential Growth /

Marc Abrahams (Annals of Improbable Research/Ig Nobel Prizes): Ig Nobel: Research that Makes You Laugh, then Makes You Think


Panel III: The Uses and Future of the Nobel Prize

Chair: Scott H. Podolsky (Harvard Medical School) /

Eric Chivian, Ira Helfand,

Bernard Lown,

James Muller, and

John Pastore (leadership of IPPNW, recipient of the Nobel Peace Prize, 1985): Decreasing the Nuclear Threat to Humanity – Nobel Peace Prizes to IPPNW in 1985 and ICAN in 2017 /

Torsten Wiesel (recipient, Nobel Prize in Physiology or Medicine, 1981): Nobel – Excellence Forever /

Jack Szostak (recipient, Nobel Prize in Physiology or Medicine, 2009): Opportunities and Responsibilities that Come with Winning the Nobel Prize



From: Center for the History of Medicine <chm=hms.harvard.edu@mail45.sea31.mcsv.net> on behalf of Center for the History of Medicine <chm@hms.harvard.edu>

Reply-To: Center for the History of Medicine <chm@hms.harvard.edu>

Date: Monday, September 24, 2018 at 3:14 PM

To: Aviva Lev-Ari <AvivaLev-Ari@alum.berkeley.edu>

Subject: Only 9 days away! Register for The History, Uses, and Future of the Nobel Prize on 10/4

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2017 Nobel prize in chemistry given to Jacques Dubochet, Joachim Frank, and Richard Henderson  for developing cryo-electron microscopy


Reporter: Aviva Lev-Ari, PhD, RN


Here’s what the images that just won the Nobel prize in chemistry look like and why they’re so transformative

Over the last few years, researchers have published atomic structures of numerous complicated protein complexes. a. A protein complex that governs the circadian rhythm. b. A sensor of the type that reads pressure changes in the ear and allows us to hear. c. The Zika virus.
The Royal Swedish Academy of Sciences

The Nobel Prize in Chemistry 2017

4 October 2017

The Royal Swedish Academy of Sciences has decided to award the Nobel Prize in Chemistry 2017 to

Jacques Dubochet
University of Lausanne, Switzerland

Joachim Frank
Columbia University, New York, USA


Richard Henderson
MRC Laboratory of Molecular Biology, Cambridge, UK

“for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution”


Cool microscope technology revolutionises biochemistry

We may soon have detailed images of life’s complex machineries in atomic resolution. The Nobel Prize in Chemistry 2017 is awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for the development of cryo-electron microscopy, which both simplifies and improves the imaging of biomolecules. This method has moved biochemistry into a new era.

A picture is a key to understanding. Scientific breakthroughs often build upon the successful visualisation of objects invisible to the human eye. However, biochemical maps have long been filled with blank spaces because the available technology has had difficulty generating images of much of life’s molecular machinery. Cryo-electron microscopy changes all of this. Researchers can now freeze biomolecules mid-movement and visualise processes they have never previously seen, which is decisive for both the basic understanding of life’s chemistry and for the development of pharmaceuticals.

Electron microscopes were long believed to only be suitable for imaging dead matter, because the powerful electron beam destroys biological material. But in 1990, Richard Henderson succeeded in using an electron microscope to generate a three-dimensional image of a protein at atomic resolution. This breakthrough proved the technology’s potential.

Joachim Frank made the technology generally applicable. Between 1975 and 1986 he developed an image processing method in which the electron microscope’s fuzzy twodimensional images are analysed and merged to reveal a sharp three-dimensional structure.

Jacques Dubochet added water to electron microscopy. Liquid water evaporates in the electron microscope’s vacuum, which makes the biomolecules collapse. In the early 1980s, Dubochet succeeded in vitrifying water – he cooled water so rapidly that it solidified in its liquid form around a biological sample, allowing the biomolecules to retain their natural shape even in a vacuum.

Following these discoveries, the electron microscope’s every nut and bolt have been optimised. The desired atomic resolution was reached in 2013, and researchers can now routinely produce three-dimensional structures of biomolecules. In the past few years, scientific literature has been filled with images of everything from proteins that cause antibiotic resistance, to the surface of the Zika virus. Biochemistry is now facing an explosive development and is all set for an exciting future.

Read more about this year’s prize

Popular Information
Pdf 2.7 MB

Scientific Background
Pdf 837 Kb

To read the text you need Acrobat Reader.

Image – 3D structures (pdf 1.4 MB)
© Johan Jarnestad/The Royal Swedish Academy of Sciences

Image – Blobology (pdf 8.5 MB)
© Martin Högbom/The Royal Swedish Academy of Sciences

Image – Dubochet’s preparation method (948 kB)
© Johan Jarnestad/The Royal Swedish Academy of Sciences

Image – Frank’s image analysis (pdf 1 MB)
© Johan Jarnestad/The Royal Swedish Academy of Sciences


Jacques Dubochet, born 1942 in Aigle, Switzerland. Ph.D. 1973, University of Geneva and University of Basel, Switzerland. Honorary Professor of Biophysics, University of Lausanne, Switzerland.

Joachim Frank, born 1940 in Siegen, Germany. Ph.D. 1970, Technical University of Munich, Germany. Professor of Biochemistry and Molecular Biophysics and of Biological Sciences, Columbia University, New York, USA.

Richard Henderson, born 1945 in Edinburgh, Scotland. Ph.D. 1969, Cambridge University, UK. Programme Leader, MRC Laboratory of Molecular Biology, Cambridge, UK.

Prize amount: 9 million Swedish krona, to be shared equally between the Laureates.
Further information: http://www.kva.se and http://nobelprize.org



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2017 Nobel Prize in Physiology or Medicine jointly to Jeffrey C. Hall (ex-Brandeis, University of Maine), Michael Rosbash (Brandeis University) and Michael W. Young (Rockefeller University in New York) for their discoveries of molecular mechanisms controlling the circadian rhythm


Curator: Aviva Lev-Ari, PhD, RN


Press Release


The Nobel Assembly at Karolinska Institutet has today decided to award

the 2017 Nobel Prize in Physiology or Medicine

jointly to

Jeffrey C. Hall, Michael Rosbash and Michael W. Young

for their discoveries of molecular mechanisms controlling the circadian rhythm

READ the Summary



Jeffrey C. Hall was born 1945 in New York, USA. He received his doctoral degree in 1971 at the University of Washington in Seattle and was a postdoctoral fellow at the California Institute of Technology in Pasadena from 1971 to 1973. He joined the faculty at Brandeis University in Waltham in 1974. In 2002, he became associated with University of Maine.

Michael Rosbash was born in 1944 in Kansas City, USA. He received his doctoral degree in 1970 at the Massachusetts Institute of Technology in Cambridge. During the following three years, he was a postdoctoral fellow at the University of Edinburgh in Scotland. Since 1974, he has been on faculty at Brandeis University in Waltham, USA.

Michael W. Young was born in 1949 in Miami, USA. He received his doctoral degree at the University of Texas in Austin in 1975. Between 1975 and 1977, he was a postdoctoral fellow at Stanford University in Palo Alto. From 1978, he has been on faculty at the Rockefeller University in New York.


Key publications

Zehring, W.A., Wheeler, D.A., Reddy, P., Konopka, R.J., Kyriacou, C.P., Rosbash, M., and Hall, J.C. (1984). P-element transformation with period locus DNA restores rhythmicity to mutant, arrhythmic Drosophila melanogaster. Cell 39, 369–376.

Bargiello, T.A., Jackson, F.R., and Young, M.W. (1984). Restoration of circadian behavioural rhythms by gene transfer in Drosophila. Nature 312, 752–754.

Siwicki, K.K., Eastman, C., Petersen, G., Rosbash, M., and Hall, J.C. (1988). Antibodies to the period gene product of Drosophila reveal diverse tissue distribution and rhythmic changes in the visual system. Neuron 1, 141–150.

Hardin, P.E., Hall, J.C., and Rosbash, M. (1990). Feedback of the Drosophila period gene product on circadian cycling of its messenger RNA levels. Nature 343, 536–540.

Liu, X., Zwiebel, L.J., Hinton, D., Benzer, S., Hall, J.C., and Rosbash, M. (1992). The period gene encodes a predominantly nuclear protein in adult Drosophila. J Neurosci 12, 2735–2744.

Vosshall, L.B., Price, J.L., Sehgal, A., Saez, L., and Young, M.W. (1994). Block in nuclear localization of period protein by a second clock mutation, timeless. Science 263, 1606–1609.

Price, J.L., Blau, J., Rothenfluh, A., Abodeely, M., Kloss, B., and Young, M.W. (1998). double-time is a novel Drosophila clock gene that regulates PERIOD protein accumulation. Cell 94, 83–95.

Keeping time on our human physiology

The biological clock is involved in many aspects of our complex physiology. We now know that all multicellular organisms, including humans, utilize a similar mechanism to control circadian rhythms. A large proportion of our genes are regulated by the biological clock and, consequently, a carefully calibrated circadian rhythm adapts our physiology to the different phases of the day (Figure 3). Since the seminal discoveries by the three laureates, circadian biology has developed into a vast and highly dynamic research field, with implications for our health and wellbeing.

The circadian clock

Figure 3. The circadian clock anticipates and adapts our physiology to the different phases of the day. Our biological clock helps to regulate sleep patterns, feeding behavior, hormone release, blood pressure, and body temperature.




Medicine Nobel awarded for work on circadian clocks, Jeffrey Hall, Michael Rosbash and Michael Young unpicked molecular workings of cells’ daily rhythms.

Ewen CallawayHeidi Ledford

02 October 2017


Other Related Research 

Charles Weitz, Ph.D., M.D.
Robert Henry Pfeiffer Professor of Neurobiology

Mammalian Circadian Clocks

Circadian clocks are molecular oscillators with ~24-hour periods that drive daily biological rhythms.  Such clocks are found in all of the major branches of life, and they likely represent ancient timekeeping systems important for predicting daily environmental cycles on our rotating planet.  In mammals, circadian clocks are present in most if not all cells. These distributed clocks control a myriad of processes, in aggregate creating coherent 24-hour programs of physiology and behavior.

A picture of how circadian clocks are built has emerged in the last two decades.  The core mechanism is a transcriptional feedback loop, wherein the protein products of several clock genes build the molecular machinery to inhibit the transcription factor responsible for their own production.  The molecular components of circadian clocks are conserved from insects to humans.

The Weitz lab uses molecular biology, biochemistry, genetics, and structural biology to investigate the mammalian circadian clock.  The focus of our efforts at present is to understand the circadian clock in terms of the integrated functions of its several multi-protein machines.  This effort is principally based on the purification of endogenous circadian clock protein complexes from mouse tissues and their biochemical analysis and structural study by cryo-electron microscopy.

Fig. 1.  Class-average electron microscopy images of the mouse nuclear PER complex, a core circadian clock machine.  It is a 1.9-MDa assembly of about thirty proteins that appears as a quasi-spherical, beaded particle of 40-nm diameter. Our current work provides an initial low-resolution view of the structural organization of endogenous clock machinery from a eukaryote.  We aim to obtain high-resolution structures.

Selected papers:

Duong HA, Robles MS, Knutti K, Weitz CJ.  A molecular mechanism for circadian clock negative feedback. Science  332, 1436-1439 (2011).

Padmanabhan K, Robles MS, Westerling T, Weitz CJ.  Feedback regulation of transcriptional termination by the mammalian circadian clock PERIOD complex. Science  337, 599-602 (2012).

Kim JY, Kwak PB, Weitz CJ. Specificity in circadian clock feedback from targeted reconstitution of the NuRD co-repressor.  Mol. Cell  56, 738-748 (2014).

Aryal RA, Kwak PB, Tamayo AG, Chiu PL, Walz T, Weitz CJ.  Macromolecular assemblies of the mammalian circadian clock.  Mol. Cell  (2017, in press).



Circadian Clock’s Inner Gears


Other related articles Published in this Open Access Online Scientific Journal included the following: 

Search Keyword “Sleep” – 161 Scientific Articles


Search Keyword “Circadian” Rhythm

Ultra-Pure Melatonin Product Helps Maintain Sleep for Up to 7 Hours

Curator: Gail S. Thornton, M.A.



Alteration in Reduced Glutathione level in Red Blood Cells: Role of Melatonin

Author: Shilpa Chakrabarti, PhD



Melatonin and its effect on acetylcholinesterase activity in erythrocytes

Author: S. Chakravarty, PhD



Day and Night Variation in Melatonin Level affects Plasma Membrane Redox System in Red Blood Cells

Author: Shilpa Chakravarty, PhD



Prolonged Wakefulness: Lack of Sufficient Duration of Sleep as a Risk Factor for Cardiovascular Diseases – – Indications for Cardiovascular Chrono-therapeutics

Curator: Aviva Lev-Ari, PhD, RN


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Program for 2/16/2018 – ELA’s 36th Birthday Party

Curator: Aviva Lev-Ari, PhD, RN 


Eight Iconic Photos Of Bob Dylan, Newly Anointed Nobel Laureate



Top 10 Bob Dylan Songs – YouTube



My seection

  • Blowing In The Wind (Live On TV, March 1963) – YouTube


  • Bob Dylan – Just Like A Woman Lyrics | Genius Lyrics


  • Sad-Eyed Lady of The Lowlands


  • Bob Dylan 2016 Nobel Prize – A Hard Rain’s A Gonna Fall live – YouTube



2018 – NOBEL OFFICIAL WEBSITE: Bob Dylan – Nobel Lecture 

The 114 Nobel laureates in Literature from 1901 to 2017 have come from the following countries:

Country Number
France 16
United Kingdom 12
United States 11
Germany 8
Sweden 8
Italy 6
Spain 6
Ireland 3
Poland 4
Russia/USSR 4
Denmark 3
Norway 3
Chile 2
China 2
Greece 2
Japan 2
South Africa 2
Switzerland 2
Austria 1
Australia 1
Belarus 1
Belgium 1
Bulgaria 1
Canada 1
Colombia 1
Czechoslovakia 1
Egypt 1
Finland 1
Guatemala 1
Hungary 1
Iceland 1
India 1
Israel 1
Mauritius 1
Mexico 1
Nigeria 1
Peru 1
Portugal 1
Saint Lucia 1
Turkey 1
Yugoslavia 1


  • Bob Dylan – Nobel Lecture





  • Why Bob Dylan Matters – Richard F. Thomas – Hardcover



  • Bob Dylan “EYES ON THE PRIZE” Documentary Fantastic insightful. – YouTube



  • Al Kooper: The Making of Bob Dylan’s Blonde on Blonde / The Record That Changed Nashville – YouTubE



  • Bob Dylan Documentary Interviews Performances and Pretentious Cravats. – YouTube



  • The Bob Dylan Documentary 2017. Great insight into the greatest singer/songwriter – YouTube





Neighborhood Bully — SONG ON ISRAEL >>>> Barry Shrage on Bob Dylan¹s Long-Lost Israel Song | JewishBoston



Top 25 Bob Dylan Studio Albums – YouTube



UPDATED on Jun 5, 2017

Acceptance Speech – Bob Dylan – 2016 Nobel Prize Gala

Reporter: Aviva Lev-Ari, PhD, RN


Published on Jun 5, 2017

Bob Dylan received the 2016 Nobel Prize in Literature “for having created new poetic expressions within the great American song tradition”.

UPDATED on 6/15/2017

Bob Dylan – Nobel Lecture

The Nobel Foundation has not obtained the right to assign any usage right to the Nobel Lecture to any third party, and any such rights may thus not be granted. All rights to the Nobel Lecture by Bob Dylan are reserved and the Nobel Lecture may not be published or otherwise used by third parties with one exception: the audio file containing the Nobel Lecture, as published at Nobelprize.org, the official website of the Nobel Prize, may be embedded on other websites.



Listen to Bob Dylan’s Nobel Lecture on SoundCloud

Nobel Lecture

5 June 2017



UPDATED on 2/12/2017

Bob Dylan speech at the 2016 Nobel Banquet

Published on Dec 15, 2016

Bob Dylan’s speech at the 2016 Nobel Banquet as read by American Ambassador to Sweden Azita Raji.
© Nobel Media AB / Production SVT




Bob Dylan to Provide Nobel Prize Speech, Patti Smith to Perform

Smith to cover “A Hard Rain’s A-Gonna Fall” at Nobel gala




By Patti Smith

December 14, 2016


Patti Smith singing the song “A Hard Rain’s A-Gonna Fall” at Nobel gala



Patti Smith sings A Hard Rain’s A-Gonna Fall




Bob Dylan sings A Hard Rain’s A-Gonna Fall




The Nobel Prize in Literature 2016
Bob Dylan

Bob Dylan – Banquet Speech

Banquet speech by Bob Dylan given by the United States Ambassador to Sweden Azita Raji, at the Nobel Banquet, 10 December 2016.

Ambassador Azita Raji gives the banquet speech.
Copyright © Nobel Media AB 2016
Photo: Alexander Mahmoud



But, like Shakespeare, I too am often occupied with the pursuit of my creative endeavors and dealing with all aspects of life’s mundane matters. “Who are the best musicians for these songs?” “Am I recording in the right studio?” “Is this song in the right key?” Some things never change, even in 400 years.

Not once have I ever had the time to ask myself, “Are my songs literature?”

So, I do thank the Swedish Academy, both for taking the time to consider that very question, and, ultimately, for providing such a wonderful answer.

My best wishes to you all,

Bob Dylan

Copyright © The Nobel Foundation 2016






Bob Dylan Awarded Nobel Prize in Literature, Scientists cited his Verses in Scientific Article Titles

Reporter: Aviva Lev-Ari, PhD, RN


In 1964, I was in the 9th grade in High School in Haifa, Israel, our very gifted English teacher, brought to class Bob Dylan and explained in class how important it is to expose high school students to his very creative poetic expressions and lyrics which had an influence on her as a Literature Critique.

Our English teacher, Tamara has immigrated to Israel from the UK. Tamara Sachs, who Chaired the Committee for Curriculum Development for the English Language Arts Subject Matter at Ministry of Education in Israel, was also the Editor of the Textbook used for English Subject matter in Israeli high Schools for the 9th and 10th grades. She created Textbooks that had Contemporary Literature contents beside the Classic English Text taught in high School in Israel and part of the National Standardized Matriculation Exam at the end of the 12th grade.

I enjoyed Bob Dylan songs ever since, 1964 to Present.

I took my family to attend his performance in the Berkshires, MA on JUL 2016 SATURDAY, 7:00 PM

Bob Dylan with Mavis Staples

Tanglewood – Koussevitzky Music Shed – Lenox, MA 

View Map

Tanglewood welcomes Bob Dylan with special guest Mavis Staples to the Koussevitzky Music Shed on Saturday, July 2 at 7 p.m. Legendary singer-songwriter Bob Dylan has performed twice at Tanglewood first in 1991 and again during the 1997 season. Gates open at 4PM.

UPDATED on 12/15/2016

Patti Smith covers, bungles Bob Dylan’s song upon accepting his Nobel Prize at ceremony in Stockholm, 12/10/2016



Bob Dylan Awarded Nobel Prize in Literature

BMJ 2015; 351 doi: http://dx.doi.org/10.1136/bmj.h6505 (Published 14 December 2015)Cite this as: BMJ 2015;351:h6505

  1. Carl Gornitzki, librarian1,
  2. Agne Larsson, statistician1,
  3. Bengt Fadeel, professor2

Author affiliations

  1. Correspondence to: C Gornitzki carl.gornitzki@ki.se

Carl Gornitzki and colleagues examine how far medical scientists are under his spell

In September 2014 it emerged that a group of scientists at the Karolinska Institute in Sweden had been sneaking the lyrics of Bob Dylan into their papers as part of a long running bet. The story, originally published in the house magazine KI-Bladet, quickly went viral—spreading from the local Swedish press to international media such as theGuardian and Washington Post.1 2 It all started in 1997 with a review in Nature Medicine entitled “Nitric oxide and inflammation: the answer is blowing in the wind.”3 A local phenomenon was thus revealed, but was this Dylan citing unique to the Karolinska Institute? We decided to investigate how Dylan’s lyrics are cited in the biomedical literature.

Knockin’ on pollen’s door

We used a list of all Dylan’s song and album titles downloaded from bobdylan.com to do a search using Medline in May 2015. In addition, we searched for truncated versions of a selection of the most popular Dylan songs to find modified titles,4 such as “Knockin’ on pollen’s door: live cell …


Citing Dylan. Bob Dylan has won this year’s Nobel Prize for Literature. In 2015, inspired by researchers at the Karolinska Institute in Sweden who had been sneaking Dylan lyrics into their papers, a team writing in the BMJ reported that Dylan citations were “uncommon before 1990 but [have] increased exponentially since then”. They note: “Some journals have more Dylan citing articles than others; for instance, we found six articles citing Dylan songs in Nature.”

For more daily science news, check in at www.nature.com/news; @NatureNews on Twitter; or on our Facebook page.

This newsletter is new and evolving — tell us what you think! Please send feedback to daily@nature.com.




Editorial Reactions to Bob Dylan’s Nobel Prize in Literature


How Dylan Became Dylan

By THE EDITORIAL BOARD OCT. 13, 2016, New York Times



Why Bob Dylan Shouldn’t Have Gotten a Nobel

By ANNA NORTH OCT. 13, 2016, New York Times



Bob Dylan, Master of Change

By GREIL MARCUS OCT. 13, 2016, New York Times



Don’t think twice, it’s all right

Nobel Prize in Literature for Bob Dylan gets no argument from Harvard scholars

October 13, 2016 | Editor’s Pick Popular

By Jill Radsken and Colleen Walsh, Harvard Staff Writers

Harvard Gazette



The right and Rightful Choice: The decision to award Bob Dylan the Nobel Prize in Literature was a long time coming

Rachel Shukert in Tablemag


Bob Dylan, the Musician: America’s Great One-Man Songbook

By JON PARELES OCT. 13, 2016 in New York Times



Expanding the Nobel Pantheon to Include Bob Dylan

OCT. 14, 2016


New York

The writer is the author of “1968 in America.”


San Francisco

The writer is a poet.




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2016 Nobel Prize in Chemistry awarded for development of molecular machines, the world’s smallest mechanical devices, the winners: Jean-Pierre Sauvage, J. Fraser Stoddart and Bernard L. Feringa

Reporter: Aviva Lev-Ari, PhD, RN


3 Makers of World’s Smallest Machines Awarded Nobel Prize in Chemistry



■ Jean-Pierre Sauvage, J. Fraser Stoddart and Bernard L. Feringa shared the Nobel Prize in Chemistry on Wednesday for development of molecular machines, the world’s smallest mechanical devices.

Who are the winners?

Dr. Sauvage, 71, was born in Paris and received his Ph.D. in 1971 from the University of Strasbourg in France, where he is a professor emeritus. He is also director of research emeritus at the National Center for Scientific Research in France.

Dr. Stoddart, 74, was born in Edinburgh, received his Ph.D. in 1966 from Edinburgh University, and is a professor of chemistry at Northwestern University in Evanston, Ill. He previously taught at U.C.L.A. and was knighted by Queen Elizabeth II for his services to science.

Dr. Feringa, 64, was born in Barger-Compascuum, the Netherlands, and received his Ph.D. in 1978 from the University of Groningen, where he is a professor of organic chemistry.


Three pioneers in the development of nanomachines, made of moving molecules, were awarded the Nobel Prize in Chemistry on Wednesday.

Molecular machines, the world’s smallest mechanical devices, may eventually be used to create new materials, sensors and energy storage systems, the Royal Swedish Academy of Sciences said in announcing the prize.

“In terms of development, the molecular motor is at the same stage as the electric motor was in the 1830s, when scientists displayed various spinning cranks and wheels, unaware that they would lead to electric trains, washing machines, fans and food processors,” the academy said.

The three scientists — Jean-Pierre Sauvage, J. Fraser Stoddart and Bernard L. Feringa — will share equally in the prize of 8 million Swedish kronor, or about $930,000.

Why did they win?

Nanotechnology — the creation of structures on the scale of a nanometer, or a billionth of a meter — has been a field of fruitful research for a couple of decades. Now, scientists are learning how to construct tiny moving machines about one-thousandth the width of a strand of human hair.

Why is the work important?

The three men invigorated the field of topological chemistry, the academy said on Wednesday. They were pioneers in the second wave of nanotechnology, a field that the physicist Richard P. Feynman, also a Nobel laureate, foresaw as early as 1959. He gave a seminal lecture in 1984, toward the end of his life, on design and engineering at the molecular scale.

In living organisms, nature has produced a slew of molecular machines that ferry materials around cells, construct proteins and divide cells. Artificial molecular machines are still primitive by comparison, but scientists can already envision applications in the future.

“Think about nanomachines, microrobots,” said Dr. Feringa, who spoke by telephone with journalists assembled in Stockholm at the prize announcement. “Think about tiny robots that the doctor in the future will inject in your blood veins, and they go search for cancer cells or going to deliver drugs, for instance.”

The technology could also lead to the creation of “smart materials” that change properties based on external signals, Dr. Feringa said.



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2016 Nobel Prize in Physics for their research into the bizarre properties of matter in extreme states, the winners: David J. Thouless, F. Duncan M. Haldane and J. Michael Kosterlitz

Reporter: Aviva Lev-Ari, PhD, RN

3 Who Studied Unusual States of Matter Win 2016 Nobel Prize in Physics


David J. Thouless, F. Duncan M. Haldane and J. Michael Kosterlitz shared the Nobel Prize in Physics last Tuesday for their research into the bizarre properties of matter in extreme states.

Who are the winners?

Dr. Thouless, 82, was born in Bearsden, Scotland, was an undergraduate at Cambridge University and received a Ph.D. in 1958 from Cornell. From 1965 to 1978, he taught mathematical physics at the University of Birmingham in England, where he collaborated with Dr. Kosterlitz. In 1980, he joined the University of Washington in Seattle, where he is now an emeritus professor.

Dr. Haldane, 65, was born in London. He received his Ph.D. from Cambridge, where he was also an undergraduate, in 1978. He worked at the Institut Laue-Langevin in Grenoble, France; the University of Southern California; Bell Laboratories; and the University of California, San Diego, before joining the Princeton faculty in 1990.

Dr. Kosterlitz, 73, was born in Aberdeen, Scotland, and received his doctorate in high-energy physics from Oxford University in 1969. He has worked at the University of Birmingham; the Institute of Theoretical Physics in Turin, Italy; and Cornell, Princeton, Bell Laboratories and Harvard.

Three physicists born in Britain but now working in the United States were awarded the Nobel Prize in Physics on Tuesday for research into the bizarre properties of matter in extreme states, including superconductors, superfluids and thin magnetic films.

David J. Thouless of the University of Washington was awarded half of the prize of 8 million Swedish kronor, or about $930,000, while F. Duncan M. Haldane of Princeton University and J. Michael Kosterlitz of Brown University shared the other half.

The scientists relied on advanced mathematical models to study “theoretical discoveries of topological phase transitions and topological phases of matter,” in the words of the Royal Swedish Academy of Sciences in Stockholm.

Their studies may have major applications in electronics, materials science and computing. In an email, Michael S. Turner, a physicist at the University of Chicago, described the work as “truly transformational, with long-term consequences both practical and fundamental.”

Why did they win?

The three laureates sought to understand matter that is so cold or so thin that weird quantum effects overpower the random atomic jostling that dominates ordinary existence. Superconductivity, in which all electrical resistance vanishes in matter, is one example of such an effect.

Dr. Thouless and Dr. Kosterlitz worked together at the University of Birmingham in the 1970s to investigate what happens when two-dimensional films of matter shift from one exotic phase, like superconductivity, to another.





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2016 Nobel in Economics for Work on The Theory of Contracts to winners: Oliver Hart and Bengt Holmstrom


Reporter: Aviva Lev-Ari, PhD, RN


Oliver Hart and Bengt Holmstrom Win 2016 Nobel in Economics for Work on Contracts



About the Winners

Dr. Holmstrom, 67, was born in Helsinki, Finland, and speaks Swedish well enough to answer questions in that language at Monday’s news conference.

In the early 1970s, he was working for a Finnish company that wanted to use computers to improve productivity. Dr. Holmstrom, sent to Stanford on a one-year fellowship, concluded that the real challenge was not programming but providing employees with proper incentives.

He stayed to earn a Ph.D., and has been an professor at M.I.T. since 1994.

Dr. Hart, 68, was born in London and came to the United States to earn his Ph.D. in 1974 from Princeton. He has been a professor of economics at Harvard since 1993.

“He will not let go until he’s understood what you have to say,” Dr. Bolton said. “And most of the time, your argument fails. Which is an unpleasant experience as a student. But when you succeed, it gives you an incredible confidence.”


Why They Won

Dr. Holmstrom’s work has focused on employment contracts. Companies would like managers to behave as if they owned the place: working hard and minding costs while taking smart risks. Employees, on the other hand, would like to be paid as much as possible while working no harder than necessary. And performance is difficult to assess.

Economists since Adam Smith have grappled with the conflicts inherent in the relationship between owners and employees. Dr. Holmstrom’s work, beginning in the late 1970s, presented evidence that companies should tie pay to the broadest possible evaluation of an employee’s performance. In later work, he focused on the benefits of simple contracts that mixed base pay with limited incentives.

Dr. Hart’s work begins from the observation that contracts are incomplete instruction manuals. They cannot specify what to do in every case. Instead, they must stipulate how decisions should be made.

“His research provides us with theoretical tools for studying questions such as which kinds of companies should merge, the proper mix of debt and equity financing, and which institutions such as schools or prisons ought to be privately or publicly owned,” the academy said in a summary of his work.

Dr. Holmstrom, speaking via an audio connection to a news conference hosted by the academy, said he had been “very surprised and very happy” to get the news. Asked how his day was going, he said there was “a sense of things being surreal.”

Dr. Hart said he had hugged his wife, roused his son from sleep and spoken by phone with Dr. Holmstrom, a close friend whom he has known for years.

“I woke at about 4:40 and was wondering whether it was getting too late for it to be this year, but then fortunately the phone rang,” Dr. Hart said.

Why the Work Is Important

One implication of Dr. Holmstrom’s work is that it makes sense to withhold some compensation for a time, to evaluate the results of a manager’s work.

Companies have turned increasingly to this kind of deferred compensation, particularly for senior executives.

But his influence on compensation practices is limited. He has argued, for example, that companies should tie such evaluations to the stock market performance of their industry rather than focusing solely on the company’s own stock price. It makes little sense to reward an executive for gains that reflect a broader change in the industry’s fortunes, or to punish executives for setbacks beyond their control. But such advice has not become common practice.



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The Nobel Prize in Physiology or Medicine 2016 – awarded to Yoshinori Ohsumi “for his discoveries of mechanisms for autophagy”.

Curator: Aviva Lev-Ari, PhD, RN


“The Nobel Prize in Physiology or Medicine 2016”. Nobelprize.org. Nobel Media AB 2014. Web. 4 Oct 2016. 


Yoshinori Ohsumi

Born: 1945, Fukuoka, Japan

Affiliation at the time of the award: Tokyo Institute of Technology, Tokyo, Japan

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Deciphering cell’s recycling machinery earns 2016 Nobel in Physiology and Medicine – Yoshinori Ohsumi honored for studies of autophagy

2:45PM, OCTOBER 3, 2016

Ohsumi‘s discoveries helped reveal the mechanism and significance of a fundamental physiological process, biologist Maria Masucci of the Karolinska Institute in Sweden said in a news briefing October 3. “There is growing hope that this knowledge will lead to the development of new strategies for the treatment of many human diseases.”

Scientists got their first glimpse of autophagy in the 1960s, not long after the discovery of the lysosome, a pouch within cells that acts as a garbage disposal, grinding fats and proteins and sugars into their basic building blocks. (That discovery won Belgian scientist Christian de Duve a share of the Nobel Prize in 1974.) Researchers had observed lysosomes stuffed with big chunks of cellular material — like the bulk waste of the cellular world — as well as another, mysterious pouch that carried the waste to the lysosome.


What do autophagy’s leading scientists have to say about this year’s Nobel Prize and its recipient?


Initial Contribution Article for 2016 Nobel in Physiology and Medicine – Yoshinori Ohsumi honored for studies of autophagy

Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction.

K Takeshige, M Baba, S Tsuboi, T Noda, Y Ohsumi

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Reporter: Aviva Lev-Ari, PhD, RN

Each year the recipient(s) of the Warren Alpert Foundation Prize are recognized at a scientific symposium hosted by Harvard Medical School.

OCTOBER 6, 2016 –

1:30PM TO 5:30PM


The CRISPR/Cas9 Revolution and Gene Editing

In honor of Rodolphe Barrangou, Emmanuelle Charpentier,  Jennifer Doudna, Philippe Horvath, Viginijus Siksnys for remarkable contributions to the understanding of the CRISPR bacterial defense system and the revolutionary discovery that it can be adapted for genome editing.

Harvard Medical School
The Joseph B.Martin Conference Center
77 Avenue Louis Pasteur
Boston, MA 02115

RSVP: HMS_events@hms.harvard.edu
Seating available on a first-come first served basis

Opening Remarks

Barbara J McNeil, MD, PhD, Acting Dean, HMS

Warren Alpert a very prestiguos Prize for advancements in Medicine, Treatment of disease and alleviation of suffering

Clifford Tabin, MD, Prof. of Genetics at HMS

  • CRISPR as regulatory system

Featured Speakers include:

Rodolphe Barrangou, PhD
Todd R. Klaenhammer Distinguished Scholar in Probiotics Research
North Carolina State University
CRISPR-mediated immunity in bacteria: discovery and applications


Philippe Horvath, PhD
Senior Scientist
CRISPR-mediated immunity in bacteria: discovery and applications

  • CRISPR-Cas: basics, history, applications, future
  • cas1 (larger number of spacers) and Cas 2 almost universal
  • DNA repeate in preKariotes, 2002 Milk coagulation, dairy industry – lactic acid, bacteriaphaging – failure of fermentation


  • 2005 outstanding spacer polymorphism
  • CRISPR genotype – phase sensitivity & resistance correlation
  • CRISPR – Mechanism of Action
  • 8/2005 Patent of bacteriaphage – Eureka:comercialization in 1990 200 sequence resistance to phage – Anti Phaging Hypothesis
  • certain spacers in genome cross immunity against the phage –
  • Spacers: engineeringCRISPR-encoded immunity resistence against phaging: ad spacer gain resistence
  • cas9 disruption >> loss of phage resistence in dairy bacteria
  • csn2 disruption -.. no subsequence acquisition of spacers
  • no phenotypic resistance loss
  • RNSi – A putative RNA-interference-based immune system
  • Science 2007
  • Discovery of the CRISPR motif (PAM): resistence in Streptococcus Thermophilus
  • Immunity is mediated by small CRISPR RNAs (crRNAs)
  • CRISPR Immunity – DNA encoded in bacteria
  • CRISPR/Cas bacterial immune system cleaves bacteriaphage and plasmid DNA, Nature 11/2010
  1. Immunization
  2. Interference with expression of immunity – with invading nucleus by viral DNA infection

Applications for CRISPR

  1. Bacterial strain typing
  2. natural vaccination against phages: CRISPerization (cultivation, plating)
  3. Natural genetc tagging
  • signature in the genome – genetic tag
  • strain identification
  • Patent for phage genome editing in 2009
  • Lethal self-targegting in bacteria programmable antimicrobial is death
  • genotype of interest selected
  • Agriculture applications: contamination in food, starters probiotics

Perspective on last Decade  

  • phage resistance phenotype
  • In silico & predictions in vitro
  • success in Crops, Food, Animals
  • Matters: IP (file for Patent, convert, publish), PR, Reg

Emmanuelle Charpentier, PhD
Prof. Dr.; Scientific Member of the Max Planck Society, Max Planck Director
Professor, Umeå University
The transformative genome engineering CRISPR-Cas9 technology: lessons learned from bacteria

  • Non-infectious Disease: Cancer, Heart Genetic, Brain
  • Infectious Diseases: Transmiable & Comnunicative
  1. Bacteria
  2. Viruses
  3. funcgi
  4. parasites
  • Enzyme Cas9 S. Pyogenes: Group A Strep
  • spacer acquisition – crRNA expression and maturationng CRISPR-CAS evolved into 6 types
  • Human Bacterial host
  • An mRNA : Type II CRISPR -Cas locus: TracrRNA – pre-crRNA
  • Cas9 requires tracrRNA:crRNA to cleave DNA
  • Genome editing with sequence specific nucleatease
  • RNA -programmable CRISPR -Cas9
  • Applications of CRISPR-Cas9 in human medicine: sequencing of Human genome – gene therapy to an organ, genetic predisposition of diseases
  • trcrRNA is associated to Type II CRISPR-Cas
  • Interchangeability among dual-RNA-Cas9 orthologs
  • Cpf1 – Type V-A
  • Adaptive Immune system
  • Mechnism of maturation of CRISPR-RNA

Jennifer Doudna, PhD
Li Ka Shing Chancellor’s Chair in Biomedical and Health Sciences/HHMI Investigator
University of California, Berkeley
The Future of Genome Engineering: Biology, Technology and Ethics

  • Biology
  • Technology  – Gene Editing
  • Ethics


  • Adaptation – acquire and maintain genetic memory Prokaryotic cells
  • crRNA Biogenesis
  • Interference
  • Supercoiled plasmid target helps for the integration reaction
  • Integration preceeds via a 3′-OH nucleophilic attack, 3′ – PO4
  • What directs Cas1-Cas2 to the leader side of CRISPR Loci
  • Integration Host Factor (IHF): alpha and beta
  • IHF is required for spacer acquisition in vivo
  • mechanism of spacer integration for DNA repair and repeat replication
  • Harness integrase for genomic tagging


  • CAS9 is a dual-RNA guided DNA Endonuclease
  • Cas9 programmed by single chimeric RNA
  • Most CISPR systems target dsDNA
  • PAM binding drives DNA target recognition: protospacer — PAM– dsDNA
  • C2c2 is an RNA-activated RNase: cis Cleavage vs trans Cleavage – used to detect specific RNA


  • Chromatin search
  • DNA repair
  • RNA targeting


  • CRISPR based white mushrooms programmed to resist browning
  • human gene modification


Virginijus Siksnys, PhD
Professor and Chief Scientist/Department Head, Institute of Biotechnology
Vilnius University
From mechanisms of microbial immunity to novel genome editing tools

  • bacteria can absorb interference
  • superinfection survival
  • defense islands in genomes
  • CCGG-family: specificity of restriction enzymes that recognize different nucleotides
  • meganucleases: ZFN, TALEN
  • CRISPR-Cas are transportable: CRISPR3 was transferred to e-Coli and plasmid
  • isolate Cas9 protein – RNA-guided endonuclease – adaptive immunity in bacteria
  • generate Cas9 variants
  • Cas9 – restriction enzyme – targeting 2 sites on a pUC18 plasmid
  • Cas9 specificityis encoded by crRNA: REases
  • Cas9- versatilegenome editing tool: induce DNA breaks, gene editing of Human cells, animals plants
  • Cas target is composite – >1000 Cas9 orthologues are known: 20 nt protospacer PAM sequence PAM Assay: PAM depends on Cas9 concentration
  • RNP assembly Cas9
  • Type II-CCRISPR-Cas for B. laterosporus
  • PAM preference for Blat Cas9
  • Maze genome
  • Off-target cleavage: role of PAM, PAM contribute to cleavage at off-target site: Stringent PAM restriction on Cas9



Invited Speakers:

Luhan Yang, PhD
Chief Scientific Officer
Rewriting the pig genome to transform Xenotransplantation

  • Organ transplantation unmet needs
  • natural bioreactor for organ transplants manufacturing

Obstacles for Xenotransplantation

viral transmission

  • immunological Incompatibility
  • New tools: CRISPR-Cas9 multiplexible genome engineering
  • Infectivity of virus  – Infectivity is real: gRNA to destroy catalytic PERVs
  • Eridicate of PERVs activates in PK15 cells
  • generate viable PERV free embryo
  • Genotyping of Clone 40
  • viral transmission

immunological Incompatibility

  • a disruptive technology across tissue and organ types
  • therapeutic applications


  • write the Genome
  • Next Generation of Gene Editing Tools


Austin Burt, PhD
Professor of Evolutionary Genetics
Imperial College London
Developing CRISPR-based gene drive for malaria control

  • Genetically MODIFICATION of the mosquito strains that brings Malaria to Humans
  • Driving Y chromosom – convert all population of mosquitos to MALE: don’t bite, don’t transmit and do not contribute to next generation
  • Homing: natural process endonuclease genes in many microbes
  • Find Gene needed for female fertility: Ovary  expression : sterile non-sterile
  • gene needed for vector competence
  • target gene validation: number of Larvae
  • CRISPR-based homing at target gene – Frequency
  • Issues arising form this approach: Resistance, ecological and biodiversity, Governance and acceptance, step by step development pathway


Warren Alpert Foundation Prize Recipients


For remarkable contributions to the understanding of the CRISPR bacterial defense system and the revolutionary discovery that it can be adapted for genome editing.


For their pioneering discoveries in chemistry and parasitology, and personal commitments to translate these into effective chemotherapeutic and vaccine-based approaches to control malaria – their collective work will impact millions of lives globally particularly in the developing countries.


For seminal contributions to our understanding of neurotransmission and neurodegeneration.


For their seminal contributions to concepts and methods of creating a genetic map in the human, and of positional cloning, leading to the identification of thousands of human disease genes and ushering in the era of human genetics.


For the discovery, preclinical and clinical development of bortezomib to FDA approval and front line therapy for the treatment of patients with multiple myeloma.


In recognition of their extraordinary contributions to medicine and innovations in bioengineering.


For the expansion and differentiation of human keratinocyte stem cells for permanent skin restoration in victims of extensive burns.


For the discovery, characterization and implementation of laser panretinal photo-coagulation, which is used to treat proliferative diabetic retinopathy.


For work leading to the development of a vaccine against human papillomavirus.


For their contribution to the development of the breast cancer therapy Herceptin, the first target-directed cancer treatment for solid tumors.


For discovering angiogenesis and its relationship to disease, and for championing the concept of anti-angiogenic therapies.


For her seminal contributions to the understanding of how the antitumor agent Taxol kills cancer cells.


For their pioneering work on the purification, characterization, and cloning of human interferon-alpha.


For his pioneering work in understanding the role of vitamin A supplementation in preventing blindness and life-threatening infections in children in the developing world.


For their pioneering work in cardiovascular research which has dramatically reduced the mortality rate for heart attacks.


For their research that contributed to the development of a drug that effectively treats chronic megelogenous leukemia and other forms of cancer.


For their research in the development of statins which lower the level of cholesterol in the heart.


For elucidating the pathway forming the leukotrienes and their role in bronchial asthma.


For their discovery of human immune deficiency virus (HIV).


For their discoveries of molecules that regulate the growth and differentiation of bone marrow cells in health and disease.


For the development of the lung surfactant used for treating pulmonary hyaline membrane disease.


For identifying Helicobacter pylori as the organism that causes gastric and duodenal ulcers.


For developing a complete description of thalassemia at the molecular level.


For discovering the enzymatic basis of Gaucher’s disease leading to its effective treatment.


For designing a powerful new approach to the treatment of high blood pressure and congestive heart failure.


For pioneering the use of DNA in the diagnosis of congenital anemias.


For defining the genetic basis of muscular dystrophy.

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Nobel Laureate Roger Tsien Dies at 64  – Distinguished Howard Hughes Medical Institute investigator and UC San Diego Professor who helped develop glowing proteins, illuminating life

Reporter: Aviva Lev- Ari, PhD, RN 

Nobel Laureate Roger Tsien Dies

Roger Tsien, who shared the 2008 Nobel Prize in chemistry, has died, the University of California, San Diego, has announced. He was 64. His cause of death has not been determined, though the Los Angeles Times says he died while on a bike trail in Eugene, Ore.

Tsien was awarded the Nobel along with Woods Hole’s Osamu Shimomura and Columbia University’s Martin Chalfie for their discovery and development of green fluorescent protein (GFP) from a jellyfish protein into a laboratory tool.

“Our work is often described as building and training molecular spies,” Tsien once said, according to UCSD. “Molecules that will enter a cell or organism and report back to us what the conditions are, what’s going on with the biochemistry, while the cell is still alive.”

UCSD adds that Tsien became interested in chemistry at a young age — his first Boy Scout merit badge was in chemistry. He also won the Westinghouse Talent Search at 16 before studying chemistry and physics as an undergraduate at Harvard University. He then earned a doctorate in physiology from the University of Cambridge, where he was a research fellow for a few years before joining UC-Berkeley and then UCSD.

“Rarely are the smartest people the most creative too, but Roger was both,” Barry Sharpless, a Nobel laureate from the Scripps Research Institute, tells the Los Angeles Times.

Tsien also once stood off with another laureate, James Watson, over Watson’s comments about oxidants and antioxidants in cancer research. After the verbal sparring, Tsien told the San Diego Union-Tribune, “You should take all elderly scientists with a grain of salt — including me.”



Nobel Laureate Roger Tsien Dies, Age 64 – UC San Diego professor helped develop glowing proteins, illuminating life




Nobel Laureate Roger Tsien, PhD, UC San Diego School of Medicine professor and Howard Hughes Medical Institute investigator, died August 24, 2016.

Roger Tsien, PhD, co-winner of the 2008 Nobel Prize in chemistry and professor of pharmacology, chemistry and biochemistry at University of California San Diego School of Medicine for 27 years, died August 24 in Eugene, Ore. He was 64.

Tsien’s work literally illuminated science. With Osamu Shimomura, PhD, an emeritus professor at the Marine Biological Laboratory in Woods Hole, Mass. and Martin Chalfie, PhD, a professor of biological sciences at Columbia University, Tsien helped scientists peer within living cells and organisms as never before, earning not just the 2008 Nobel Prize but scores of subsequent  awards and accolades.

“Every honor was justly deserved, and always received with humility,” said Pradeep Khosla, chancellor of UC San Diego. “Roger was an extraordinary man: kind, generous, gracious, and always the consummate scientist pushing the limits of his work to expand the possibilities of science. He was a rare talent we cannot replace.”

Tsien, Shimomura and Chalfie collaborated to discover and develop green fluorescent protein (GFP), derived from the jellyfish Aequorea victoria, as a new and soon-indispensable research tool.

Shimomura identified the crucial jellyfish protein and revealed that it glowed bright green under ultraviolet light. Chalfie showed how it could be used as a biological marker. Combining his deep skills in chemistry and biology, Tsien found ways to make GFP glow more brightly and consistently; then he created a full palette of fluorescent proteins that scientists could use to track different cellular processes at the same time.

“I’ve always been attracted to colors,” Tsien told the San Diego Union-Tribune in 2008. “Color helps make the work more interesting and endurable. It helps when things aren’t going well. If I had been born color-blind, I probably never would have gone into this.”

GFPs have become a fundamental fixture in life sciences labs around the world, allowing researchers to look into cells or whole animals, to watch molecules interact in real-time and ask questions once thought impossible.

Cultured HeLa cancer cellsCultured HeLa cancer cells depicted using fluorescent proteins to illustrate Golgi apparatus (orange) and microtubules (green), with DNA-carrying nuclei counterstained blue. Image courtesy of National Institutes of Health.

“Our work is often described as building and training molecular spies,” Tsien once said, “molecules that will enter a cell or organism and report back to us what the conditions are, what’s going on with the biochemistry, while the cell is still alive.”

Tsien was never content to rest upon his Nobel laurels. He wanted his research to be clinically relevant. Working with colleagues like Quyen T. Nguyen, MD, PhD, research collaborator and head and neck surgeon at UC San Diego Health, Tsien helped develop experimental injectable fluorescent peptides that cause hard-to-see peripheral nerves to glow, allowing surgeons to avoid them when removing damaged or cancerous tissues.

“The analogy I use is that when construction workers are excavating, they need a map showing where the existing underground cables are actually buried, not just old plans of questionable accuracy,” Tsien said. “Likewise when surgeons are taking out tumors, they need a live map showing where the nerves are actually located, not just a static diagram of where they usually lie in the average patient.”

As a distinguished Howard Hughes Medical Institute investigator, Tsien sought to better visualize cancer in other ways — or maybe treat it. He and colleagues have designed U-shaped peptides able to carry either imaging molecules or chemotherapy drugs to targeted cancer cells.

His lab created a new generation of fast-acting fluorescent dyes that optically highlight electrical activity in neuronal membranes, deciphering how brain cells function and interact. And using a modified plant protein, he and colleagues created a new type of genetic tag visible under an electron microscope (EM), allowing researchers to see life in unprecedented detail.

“The big advantage of EM is that it has always had much higher spatial resolution than light microscopy,” Tsien said. You can get up to a hundred-fold higher useful magnification from EM than from light microscopy.” The result is extraordinarily refined, three-dimensional images of microscopic objects at resolutions measuring in the tens of nanometers, tiny enough to meticulously render the internal anatomy of individual cells.

“Roger’s vision was vast and yet incredibly precise,” said David A. Brenner, MD, vice chancellor, UC San Diego Health Sciences and dean of UC San Diego School of Medicine. “He saw both the big picture, but also the incredible need to see and understand — in glorious color — all of the infinitesimal details that make it up, that make up life.”

“He was ahead of us all,” said Tsien’s wife, Wendy. “He was ever the adventurer, the pathfinder, the free and soaring spirit. Courage, determination, creativity and resourcefulness were hallmarks of his character. He accomplished much. He will not be forgotten.”

Biography in brief

Roger Yonchien Tsien was born February 1, 1952 in New York City, the third son of immigrant parents. He was a scientist from early childhood, sketching out chemistry experiments as an 8-year-old in a notebook now kept in the Nobel Museum in Stockholm, Sweden. His first Boy Scout merit badge was in chemistry.

In 1968 at the age of 16, he took first prize in the prestigious Westinghouse Science Talent Search for high school seniors. He attended Harvard College, graduating summa cum laude in chemistry and physics in 1972, then earned his doctorate in physiology in 1977 at the University of Cambridge in England.

Before coming to UC San Diego in 1989, he worked as a research assistant in Cambridge and then as a junior professor at UC Berkeley.

Tsien was a member of the Institute of Medicine, the American Academy of Arts and Sciences, the U.S. National Academy of Sciences and the Royal Society of London. Among his awards: the Gairdner Foundation International Award, the American Chemical Society Award for Creative Invention, the Heineken Prize for Biochemistry and Biophysics, the Max Delbruck Medal in Molecular Medicine, the Wolf Prize and the Keio Medical Science Prize.

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