Discoveries in subatomic physics wins Nobel

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Discoveries in subatomic physics wins Nobel
Tuesday, 07 Oct, 2008


2008 Nobel Prize winners for Physics: Yoichiro Nambu, Makoto Kobayashi and Toshihide Maskawa respctively.–AFP

STOCKHOLM: Two Japanese and an American have won the 2008 Nobel Prize for discoveries in the world of subatomic physics, the Royal Swedish Academy of Sciences announced on Tuesday.

American Yoichiro Nambu of the University of Chicago won half of the prize for the discovery of a mechanism called spontaneous broken symmetry in subatomic physics.

'Spontaneous broken symmetry conceals nature's order under an apparently jumbled surface,’ the academy said in its citation. ‘Nambu's theories permeate the standard model of elementary particle physics'. He developed a ‘standard model of elementary particle physics (which) unifies the smallest building blocks of all matter and three of nature's four forces in one single theory’ according to the Nobel jury.

Makoto Kobayashi and Toshihide Maskawa of Japan shared the other half of the prize for discovering ‘of the origin of the broken symmetry that predicts the existence of at least three families of quarks in nature.’

Kobayashi and Maskawa ‘explained broken symmetry within the framework of the standard model but required that the model be extended to three families of quarks.’ The academy added that it was only in recent years that scientists have been able to confirm the explanations that Kobayashi and Maskawa proffered in 1972. The results of various current physics experiments were exactly as Kobayashi and Maskawa had predicted almost three decades earlier

The trio will share the 10 million kronor (US$1.4 million) purse, a diploma and an invitation to the prize ceremonies in Stockholm on Dec. 10.

The prize, awarded by the Nobel Committee for Physics at the Royal Swedish Academy of Sciences, was the second of this year's crop of Nobel prizes.
The prizes are handed out annually for achievements in science, peace, literature and economics. The prizes bearing the name of Alfred Nobel were first awarded in 1901 in accordance with the 1895 will of the Swedish dynamite millionaire.

‘I am happy that Mr. Nambu has won it. I thought there was a bigger chance this year,’ Maskawa said, as quoted by Jiji Press

Kobayashi said the news came as a shock. ‘It is my great honour and I can't believe this,’ he said, in a phone interview broadcast at a news conference.

 

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A Guiding Glow to Track What Was Once Invisible
By KENNETH CHANG

Looking at a cell through an optical microscope is like a satellite view of New York City. You can see Central Park, buildings, streets and even cars, but understanding the cultural and economic life of the city from the distance of Earth orbit is difficult, maybe impossible.

Tissues of a mouse embryo tagged with green and red fluorescent proteins, which can be used to follow where proteins are moving in a cell.

Likewise, biologists can easily see large structures inside a cell like the nucleus with its folded-up chromosomes and the energy factories of the mitochondria. But most of the details of how a cell functions — the locations of specific proteins, the mechanisms used by the cell to send messages back and forth, the transportation system that moves proteins from place to place — were too small to be seen.

Nowadays, using the same optical microscopes, biologists can see what was once invisible with the help of a fluorescent protein that is the focus of this year’s Nobel Prize in chemistry. The prize was awarded to Osamu Shimomura of the Marine Biological Laboratory in Massachusetts and Boston University, Martin Chalfie of Columbia University and Roger Y. Tsien of the University of California, San Diego.

The protein, known as the green fluorescent protein, or G.F.P., was for years just a biological curiosity from a glowing jellyfish.

It was found in the summer of 1961 when Dr. Shimomura, then a researcher at Princeton, and Frank Johnson, a Princeton biology professor, collected 10,000 Aequorea victoria jellyfish in the waters off Friday Harbor in Washington State. They were looking for what made the jellyfish glow at its edges, and from the 10,000 jellyfish they extracted aequorin, a bioluminescent protein that flashes blue when it interacts with calcium.

In the jellyfish, Dr. Johnson and Dr. Shimomura also discovered a smaller protein, the green fluorescent protein, which is fluorescent rather than luminescent. Bioluminescent proteins require other molecules to provide energy in order to light up. Fluorescent proteins do not. The G.F.P. proteins absorb the energy of ultraviolet or blue light and re-emit the energy as green light.

For biologists, that is an important advantage, because cells with G.F.P.-tagged proteins do not have to be swathed in additional chemicals to make them shine.

G.F.P. remained largely a curiosity until 1992, when Dr. Chalfie used it to make E. coli bacteria glow. He then made individual cells inside C. elegans roundworms glow.

The key to the use of G.F.P. is that biologists now know the gene that produces it. When they want to track the activity of a particular protein in a cell they first must identify the gene that produces it. Then, they can splice in the gene for G.F.P. next to the new gene. The result is that the protein is produced with a slight modification, an attached fluorescent snippet.

All that remains is to shine ultraviolet light on the cells. The tagged proteins glow, revealing their locations.

That is like sticking a GPS tag on every police officer or every delivery truck or every Wall Street trader in New York City. Suddenly, scientists could track the movements of groups of proteins in real time, and a hubbub of activity came into view.

For example, Jennifer Lippincott-Schwartz, a researcher at the National Institute of Child Health and Human Development, has used G.F.P. to follow not only where proteins are moving in a cell, but also where a given protein is present in the largest numbers. Brightness indicates how many protein molecules there are.

Her observations on the traffic patterns of proteins contradicted some long-standing ideas about how some newly made proteins make their way through a structure known as the Golgi complex en route to being secreted out of the cell. Many biologists thought of it as a conveyor belt system carrying the proteins in an orderly fashion. “With this type of imaging approach, we could show that was wrong,” Dr. Lippincott-Schwartz said.

Instead, a newly made protein moves through a series of compartments. When it enters one, it bounces around with other proteins already there; periodically, by chance, one of the proteins is bounced to the next compartment. Thus, the movement was more akin to the diffusion of a gas than a conveyor belt.

Before the advent of the G.F.P. technique, the primary method for pinpointing proteins was to synthesize an antibody that would hook onto a protein and attach fluorescent snippets to the antibodies. The antibodies, injected into a cell, would attach to the proteins, and the biologists could see where they were.

Designing the antibodies was not easy, and each protein required a different antibody. A larger limitation was that that the cells had to be immobilized and “fixed” — killed, in other words.

“Even though it was great,” Dr. Lippincott-Schwartz said, “it certainly was not optimal.”

Other scientists including Dr. Tsien worked out clever ways to study some proteins in living cells. Dr. Tsien and his collaborators were able to extract the proteins they wanted, attach fluorescent molecules to them in the laboratory and then inject the modified proteins back into the cells, taking care not to damage the proteins or kill the cells.

This technique was limited and arduous, leading Dr. Tsien to seek alternatives. By mutating the G.F.P. gene, Dr. Tsien’s lab was the first to make a gene that produced a blue fluorescent protein. Fluorescent proteins now span the spectrum from violet-blue to red and even infrared.

In one study, Dr. Tsien and his collaborators tagged two different proteins that attach to calcium, an important messenger within cells, with two different fluorescent colors. In the presence of calcium, the two proteins stick together, and the colors change noticeably.

A variation of the idea has been used for a sensor of glutamate, an amino acid that is the most common neurotransmitter for exciting neighboring neurons in the human brain. One of the students in Dr. Tsien’s laboratory took a bacterial protein and engineered it with a cyan tag at one end and a yellow tag at the other. When the engineered bacterial protein attaches to glutamate, it changes shape, and again the color changes.

http://www.nytimes.com/2008/10/14/science/14gree.html

 

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Krugman Wins Nobel Prize for Economics
By THE ASSOCIATED PRESS

STOCKHOLM, Sweden — The American economist Paul R. Krugman won the Nobel economics prize on Monday for his analysis of trade patterns and location of economic activity.

Paul Krugman

Mr. Krugman, 55, a professor at Princeton University in New Jersey and a columnist for The New York Times, formulated a new theory to answer questions about free trade, the Royal Swedish Academy of Sciences said.

“What are the effects of free trade and globalization? What are the driving forces behind worldwide urbanization? Paul Krugman has formulated a new theory to answer these questions,” the academy said in its citation.

“He has thereby integrated the previously disparate research fields of international trade and economic geography,” it said.

Mr. Krugman was the lone of winner of the 10 million kronor ($1.4 million) award, the latest in a string of American researchers to be honored.

The award, known as the Nobel Memorial Prize in Economic Sciences, is the last of the six Nobel prizes announced this year and is not one of the original Nobels. It was created in 1968 by the Swedish central bank in Nobel’s memory.

http://www.nytimes.com/2008/10/14/business/14nobel.html

 

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Discoverers of AIDS and Cancer Viruses Win Nobel

The $1.4 million award will be shared by, from left, Dr. Harald zur Hausen, 72, of Germany, and French virologists Dr. Françoise Barré-Sinoussi, 61, and Dr. Luc Montagnier, 76.

By LAWRENCE K. ALTMAN

The Nobel Prize in Medicine was awarded Monday to three European scientists who had discovered viruses behind two devastating illnesses, AIDS and cervical cancer.

Half of the award will be shared by two French virologists, Françoise Barré-Sinoussi, 61, and Luc A. Montagnier, 76, for discovering H.I.V., the virus that causes AIDS. Conspicuously omitted was Dr. Robert C. Gallo, an American virologist who vied with the French team in a long, often acrimonious dispute over credit for the discovery of H.I.V.

The other half of the $1.4 million award will go to a German physician-scientist, Dr. Harald zur Hausen, 72, for his discovery of H.P.V., or the human papilloma virus. Dr. zur Hausen of the German Cancer Research Center in Heidelberg “went against current dogma” by postulating that the virus caused cervical cancer, said the Karolinska Institute in Stockholm, which selects the medical winners of the prize, formally called the Nobel Prize in Physiology or Medicine.

His discovery led to the development of two vaccines against cervical cancer, the second most common cancer among women. An estimated 250,000 women die of cervical cancer each year, mostly in poor countries.

This year’s Nobel Prize-winning research focused on two viruses that take many years to cause damage. Much of the research was carried out a quarter of a century or more ago.

Since its discovery in 1981, AIDS has rivaled the worst epidemics in history. An estimated 25 million people have died, and 33 million more are living with H.I.V.

In 1983, Dr. Montagnier and Dr. Barré-Sinoussi, a member of his lab at the Pasteur Institute in Paris, published their report of a newly identified virus. The Karolinska Institute said that discovery led to blood tests to detect the infection and to anti-retroviral drugs that can prolong the lives of patients. The tests are now used to screen blood donations, making the blood supply safer for transfusions and blood products.

The viral discovery has also led to an understanding of the natural history of H.I.V. infection in people, which ultimately leads to AIDS and death unless treated.

H.I.V. is a member of the lentivirus family of viruses. The French scientists were cited for identifying a virus they called L.A.V. (now known as H.I.V.) in lymph nodes from early and late stages of the infection.

“Never before has science and medicine been so quick to discover, identify the origin and provide treatment for a new disease entity,” the Karolinska Institute said.

Reached by the Nobel committee in Abidjan, Ivory Coast, where he is attending an international AIDS conference, Dr. Montagnier said, “The fight is not finished” and he was now working on a way to eradicate H.I.V. in those already infected. Dr. Montagnier now works at the World Foundation for AIDS Research and Prevention in Paris. For a brief time in the late 1990s, he worked at Queens College in New York City.

Nobel Foundation rules limit the number of recipients of its medical prizes to a maximum of three each year, and omissions often create controversy.

The dispute between Dr. Gallo and the French team spanned years and sprawled from the lab into the highest levels of government. Dr. Gallo, 71, now at the University of Maryland in Baltimore, worked for many years at the National Cancer Institute in Bethesda, Md.

While in Bethesda in 1984, a year after the French team’s report, Dr. Gallo reported finding a virus that he called H.T.L.V.-3 and that was later shown to be nearly identical to the French L.A.V. After additional studies, Dr. Gallo said cultures in his laboratory had accidentally become contaminated with the French virus.

In 1986, Dr. Gallo and Dr. Montagnier shared a prestigious Lasker award, given in the United States; Dr. Montagnier was cited for discovering the virus and Dr. Gallo for determining that it caused AIDS.

In 1987, President Reagan and Prime Minister Jacques Chirac of France signed an agreement to share royalties and credit for the discovery.

But Maria Masucci, a member of the Nobel Assembly, told Reuters on Monday that “there was no doubt as to who made the fundamental discoveries.”

Dr. Gallo told The Associated Press on Monday that it was “a disappointment” not to have been honored with the French team. Later, Dr. Gallo issued a statement congratulating this year’s Nobel Prize winners and said he “was gratified to read Dr. Montagnier’s kind statement this morning expressing that I was equally deserving.”

Dr. John E. Niederhuber, the director of the National Cancer Institute, said Monday that Dr. Gallo “was instrumental in every major aspect of the discovery of the AIDS virus. Dr. Gallo discovered interleukein-2 (Il-2), an immune system signaling molecule, which was necessary for the discovery of the AIDS virus, serving as a co-culture factor that allowed the virus to grow. Numerous scientific journal articles, many co-authored by Dr. Gallo and Dr. Montagnier, cite the two scientists as co-discoverers of the AIDS virus.”

Dr. Anthony S. Fauci, a virologist and immunologist who directs the National Institute of Allergy and Infectious Diseases, said in an interview, “The committee has a long history of awarding the prize to the person or group that makes the first seminal observation or discovery, and they did that in this case.” He added, “Nobel Prizes are always associated with great joy and great sadness, depending on who wins and who you are.”

The link between human papilloma virus and cervical cancer took years to gain acceptance. When Dr. zur Hausen proposed the connection in the 1970s, infection with papilloma virus was thought to cause nothing more serious than common warts, and the prevailing scientific view was that herpes type 2 virus caused cervical cancer. But Dr. zur Hausen consistently failed to find herpes type 2 DNA in cervical cancer cells using the newer molecular biology laboratory techniques.

In the 1980s, an American researcher said that financing agencies in the United States had rejected as unpromising his grant proposals to study links between papilloma viruses and cancer. The National Institutes of Health did not reply on Monday to questions about such proposals.

In 1983, Dr. zur Hausen discovered the first H.P.V., type 16, among biopsies of women who had cervical cancer. He went on to show that more than one H.P.V. type could lead to cervical cancer, in part by cloning H.P.V. 16 and another type, 18. Further research has shown that the two H.P.V. types are consistently found in about 70 percent of cervical cancer biopsies throughout the world, the institute said.

Of the more than 100 human papilloma viruses now known, about 40 infect the genital tract and 15 of them put women at high risk for cervical cancer. But in a vast majority of cases, the body’s immune system clears H.P.V. before the viruses cause harm. It is chronic infection that is dangerous.

H.P.V. viruses account for more than 5 percent of all cancers worldwide. Some types of H.P.V. are found in cancers of the vulva, penis, mouth and other areas. Other H.P.V. viruses cause warts on the foot and elsewhere.

Dr. zur Hausen’s research has led to development of vaccines that protect against strains of H.P.V. that cause most cases of cervical cancers. However, controversy has arisen over who should get the vaccines.

The United States Food and Drug Administration has approved one papilloma virus vaccine, Gardasil, for girls and women ages 9 to 26 and with advice that they get immunized before sexual activity begins. Because the vaccine was developed recently, doctors do not know for how long it will last.

The Nobel Prizes were created in the will of Alfred Nobel, the Swedish explosives inventor and manufacturer, who died in 1896. The first prizes were awarded in 1901.

 

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