Tag: Lindquist Lab

Image: Diagrams of protein fibers

Unweaving amyloid fibers to solve prion puzzles

June 8, 2005

Amyloid fibers are best known as the plaque that gunks up neurons in people with neurodegenerative illnesses such as Alzheimer’s and Creutzfeldt-Jacob disease—the human analog of mad cow disease. But even though amyloids are common and implicated in a host of conditions, researchers haven’t been able to identify their precise molecular structures.

Prions act as stepping stones in evolution

August 18, 2004

When a protein misfolds, the results can be disastrous. An incorrect change in the molecule’s shape can lead to diseases including Alzheimer’s and Huntington’s. But scientists have discovered that misfolded proteins can have a positive side in yeast.

Susan Lindquist elected to Germany’s top scientific academy

July 28, 2004

Whitehead Institute Director Susan Lindquist has been elected a member of Deutsche Akademie Der Naturforscher Leopoldina, the oldest scientific academy in Germany.

Amyloid fibers exposed to Hsp104

Researchers discover protein that dissolves amyloid fibers

May 20, 2004

Amyloid fibers, those clumps of plaque-like proteins that clog up the brains of Alzheimer’s patients, have perplexed scientists with their robust structures. In laboratory experiments, they are able to withstand extreme heat and cold and powerful detergents that cripple most other proteins.

Whitehead Director elected to Johnson & Johnson Board of Directors

February 5, 2004

Susan Lindquist, director of Whitehead Institute for Biomedical Research and a professor of biology at Massachusetts Institute of Technology, has been elected to the Board of Directors of Johnson & Johnson.

“Mad Cow” Mechanism May Be Integral to Storing Memory

December 24, 2003

Scientists have discovered a new process for how memories might be stored, a finding that could help explain one of the least-understood activities of the brain.

Yeast Helps Researchers Better Understand Parkinson's Mystery

December 4, 2003

Scientists know that in patients with Parkinson’s disease, certain proteins in the brain form clusters that somehow contribute to cell death and, eventually, lead to the onset of the disease’s debilitating symptoms. Whitehead scientists have succeeded in duplicating the disease’s most critical features in the most readily manipulated model organism in existence.

"Photogram" Exhibit Shows Science and Art in Silhouette

October 2, 2003

Showcasing the similarities between science and art is one motivation behind a special photography exhibit in New York that features Whitehead Institute scientists Susan Lindquist and Eric Lander.

Lindquist Receives 2003 Dickson Prize in Medicine

September 25, 2003

Whitehead Director Susan L. Lindquist received the 2003 Dickson Prize in Medicine Sept. 24 during Science 2003: Improving the Human Condition, a three-day showcase of research held at the University of Pittsburgh.

Whitehead Director, Former Director Elected to American Philosophical Society

May 8, 2003

Whitehead Institute for Biomedical Research Director Susan Lindquist and Whitehead Founding Member and former director Gerald Fink have been elected to the American Philosophical Society, the oldest learned society in the United States devoted to the advancement of scientific and scholarly inquiry.

Ursinus to Bestow Honorary Degree on Director Susan Lindquist

November 5, 2002

Known for groundbreaking work in the study of the stress response and protein folding, Susan L. Lindquist, the Director of the Whitehead Institute for Biomedical Research, will receive an honorary degree from Ursinus College on Nov. 12, 2002.

Lindquist Lab Sheds Light on How Prion Proteins Kill Neurons

October 17, 2002

Prion diseases—such as mad cow disease in cattle and Creutzfeldt-Jakob disease (CJD) in humans—have stumped scientists for decades with a complex "whodunit" complete with many suspects and a missing murder weapon. Unlike other infectious diseases that are linked to pathogens such as bacteria and viruses, these diseases have a unique and mysterious connection to a misfolded protein.

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