Bruce Frankel

Author of the new book "What Should I Do with the Rest of My Life? True Stories of Finding Success, Passion, and New Meaning in the Second Half of Life."

Dancing Deep Into Matter: Choreographer Liz Lerman Questions The Particles Of Life

September 15, 2010

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“Liz Lerman really brought this whole piece together so well, and we, the dancers, are feeling quite happy performing in it,” dancer Thomas Dwyer told me, following the premiere last week of “The Matter of Origins,” the dance-theater meditation on physics and life inspired by the choreographer’s visit to the particle-accelerating Large Hadron Collider at the CERN laboratory near Geneva.

After three years of work developing the piece, Lerman, Dwyer, and the rest of members of her Dance Exchange company should be feeling pretty good about the way things turned out.

In her Sept. 13 review in the Washington Post, dance critic Sarah Kaufman raved, “This hour-long contemplation of the universe is a work of expansive range, emotional depth and singular beauty,” Washington Post dance critic Sara Kaufman of “The Matter of Origins.” The headline cheered, “Liz Lerman Achieves Sublime Fusion of Art and Physics.”

The seventy-six-year old Dwyer, who took up dance in his 50s and is profiled in What Should I Do With The Rest Of My Life?, was particularly delighted with his duet with Martha Wittman, an elegant dancer who has been teaching, performing and choreographing for more than 50 years and was a long-time member of the Bennington College dance faculty. Together they illustrate the emotional equivalent of sub-atomic action and reaction. “Somehow she’s able to move with me in a way that makes it work,” said Dwyer, still a little astonished by what he has come to do with his life.

Here’s Liz Lerman, a MacArthur “Genius Grant” Fellow, in conversation with Bill Dorland discussing the weighty questions her considerations of the atom-smashing meant to simulate the Big Bang provoked.

” title=“Lerman on Matter of Origins”>Liz Lerman talks to Bill Dorland


The company will perform “Matters of Origin” on Oct. 1 & 2 at Wesleyan University in Middletown, CT.

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Still Working: Morris Wilkinson, Sally Gordon, And Increasing Numbers Of Elderly

September 7, 2010

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“The preparation before work each morning starts in a methodical fashion. By 6 a.m., Morris Wilkinson, a 91-year-old letter carrier, irons his postal worker uniform—a crisp, collared shirt and gray slacks—a habit he formed while in the Marines during World War II.

He enjoys a hearty breakfast of eggs or pancakes with his wife. He shines his black shoes. And he’s off to work,” arriving at a Birmingham, Alabama post office by 7 a.m. as he has for six decades.

“I’d rather work than be idle,” he said one morning before heading off on his route to deliver mail to 550 families in his white mail truck.


So began CNN’s story today taking note of the fact that across the nation, more men and women—even in their 90s and 100s—are choosing to forgo retirement and staying at their jobs longer and seeking new employment later in life. The reasons, of course, are not always voluntary.

“It’s a combination of economics and just seeing they bring a lot of value to the workplace in terms of skills and ability,” says Deborah Russell, director of workforce issues with AARP, told the network.

By 2012, nearly one-fifth of the U.S. work force will be older than 55, the AARP reported. As they prepare to retire, baby boomers likely will continue to work well beyond the traditional retirement age of 65, Russell said.

While a daily job can provide older individuals with a schedule, alleviate boredom and sometimes improve their physical health, many older people also are continuing to work to supplement their retirement savings or help provide extra money for their families.

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For some, like Sally Gordon, 101, of Lincoln, Nebraska, it’s a preference. Gordon, assistant sergeant at arms for the Nebraska Legislature, was recognized in August by Experience Works as America’s Outstanding Oldest Worker for 2010. She says she likes the extra income. Besides she’s had a steady job since the 1920s and as long as the state wants to pay her to continue to work, she’ll be happy to oblige.

“I used to be a model, and now I’m a Model T,” Gordon jokes. “I hope there’s a lot of mileage left.”

See the entire CNN story @ http://www.cnn.com/2010/LIVING/09/07/older.workers.100s.90s/index.html?hpt=C1

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Nobel Winner Paul Greengard, 84, Identifies Potential Key To Halting Alzheimer’s.

September 2, 2010

Scientist Paul Greengard first became interested in Alzheimer’s twenty-five years ago when his father-in-law developed the disease. Now, the 84-year-old researcher, awarded a Noble Prize in 2000 for his work on how brain cells communicate, may have found a target for drugs that could slow or stop the progress of the now untreatable disease.

Greengard, who still works seven days a week in his Rockefeller University laboratory in New York City, recently identified a new protein that is key to the development of beta amyloid, the destructive plaque that builds up in the brains of people with Alzheimer’s and is a hallmark of the disorder, according to a study published today in Nature.


“This really is a new approach,” said Dr. Paul Aisen, of the University of California, San Diego, told Gina Kolata of The New York Times. “The work is very strong, and it is very convincing.” Dr. Aisen directs a program financed by the National Institute on Aging to conduct clinical trials of treatments for Alzheimer’s disease.

In Greengard’s lab, when scientists knocked out a gene that produces the new protein, called γ-secretase activating protein (GSAP), mice used in the experiment developed fewer amyloid plaques.  GSAP works through a mechanism involving its interactions with γ-secretase, an enzyme that chops up the amyloid precursor protein, a large molecule produced naturally in the body and found in many different types of cells.

“Alzheimer’s disease is a devastating disorder for which there are no satisfactory treatments,” says Greengard, Vincent Astor Professor and director of the Fisher Center for Alzheimer’s Research at Rockefeller. “Our findings reveal that γ-secretase activating protein is a potential target for a new class of anti-amyloid therapies.”

While the discovery is exciting researchers recently deflated by setbacks in the research of anti-Alzheimer’s drugs, that the finding comes out of his lab will surprise few who know Greengard, who walks to work each day with his Bermese mountain dog, Alpha.

Born in New York City in 1925, Greengard’s Jewish mother, Pearl Meister, died in childbirth. After his father’s remarriage, Greengard was raised as an Episcopalian and denied awareness of his mother’ family or his Jewish heritage, which he discovered later in life.

He used his Nobel Prize money to create the Pearl Meister Greengard Prize, to honor women scientists and combat discrimination against women in science. Self-depricating, at the time he announced the prize, he said before the Nobel Prize his greatest previous prize came from winning a Boy Scout potato sack race.

During World War II, he served in the United States Navy as an electronics technician at the Massachusetts Institute of Technology working on an early warning system against Japanese kamikaze planes. He graduated from Hamilton College in 1948 with a bachelor’s degree in mathematics and physics, but chose to pursue biophysics in graduate school because post-war physics research was focusing on nuclear weapons.

While studying for his Ph.D. at Johns Hopkins University, a lecture by Alan Hodgkin, a Nobel Prize winner in 1963, inspired him to begin work on the molecular and cellular function of neurons.

Until now, scientists have been searching for ways to reduce amyloid-β production in Alzheimer’s patients by blocking γ-secretase, but most γ-secretase inhibitors also block the cleavage of an important immune system molecule called Notch. Notch plays a pivotal role in the development of blood-forming organs and the immune system. Earlier research by Greengard and his colleagues showed that Gleevec, a drug used to treat leukemia and gastrointestinal stromal tumors, successfully inhibited the ability of γ-secretase to form amyloid-β without affecting the Notch pathway.

In the new study, led by Gen He, a research associate in Greengard’s lab, the researchers showed that GSAP stimulates production of amyloid-β in cell lines, and that reducing GSAP reduces amyloid-β.

Unfortunately, the Gleevec molecule does not cross the blood-brain barrier, the gatekeeper that prevents some substances in the blood from entering the brain. Greengard, however, believes that it will be possible to design drugs that target GSAP but do not have this limitation.

“Anti-amyloid therapeutic drugs represent a valid approach to treating Alzheimer’s disease, but their inability to accumulate in the brain has limited their usefulness,” says Greengard, who is head of the Laboratory of Molecular and Cellular Neuroscience. “The development of compounds that work like Gleevec, but have the ability to pass the blood-brain barrier and target GSAP, could revolutionize the treatment of this disease.”

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