Although 'Plans' do not materialize but sudden thoughts do!! The scene is: some of us are sitting in fac lounge and having tea, time is around 12:30hrs and we are all dying to have good cake (certainly not from ShopC if the condition of "good" is attached).
Suddenly somebody floats the idea of going to Globus again on the same evening!! Some other, floats another "fundoo" idea of making it "right now". Well RIGHT NOW!!! LUNCH and CAKE!!
And the rare thingy is "we all are ready". Ready to leave our quotidians for a day!! Out here!! In Kanpur!! Really a Rare Phenomena it is, believe me :)
We hired a 'Vikram'!!
More later, have some work right now!!! :))
Saturday, February 17, 2007
Tuesday, January 2, 2007
Woo Suk Hwang
The South Korean stem-cell researcher Woo Suk Hwang has been at the centre of one of the largest investigations of scientific fraud in living memory.
In January 2006, Hwang's home research institution, Seoul National University, delivered a damning report about Hwang's work on cloned human embryos, concluding it was all based on fraudulent data. The revelation has destroyed the best evidence so far that stem cells can be extracted from a clone matched to a specific patient. With Hwang discredited, both the field of therapeutic cloning and the public's trust in science have suffered a serious setback.
Read more at: http://en.wikipedia.org/wiki/Hwang_Woo-Suk
Thursday, December 28, 2006
A Scientist's Nightmare: Software Problem Leads to Five Retractions
Until recently, Geoffrey Chang's career was on a trajectory most young scientists only dream about. In 1999, at the age of 28, the protein crystallographer landed a faculty position at the prestigious Scripps Research Institute in San Diego, California. The next year, in a ceremony at the White House, Chang received a Presidential Early Career Award for Scientists and Engineers, the country's highest honor for young researchers. His lab generated a stream of high-profile papers detailing the molecular structures of important proteins embedded in cell membranes.
Then the dream turned into a nightmare. In September, Swiss researchers published a paper in Nature that cast serious doubt on a protein structure Chang's group had described in a 2001 Science paper. When he investigated, Chang was horrified to discover that a homemade data-analysis program had flipped two columns of data, inverting the electron-density map from which his team had derived the final protein structure. Unfortunately, his group had used the program to analyze data for other proteins. As a result, on page 1875, Chang and his colleagues retract three Science papers and report that two papers in other journals also contain erroneous structures.
"I've been devastated," Chang says. "I hope people will understand that it was a mistake, and I'm very sorry for it." Other researchers don't doubt that the error was unintentional, and although some say it has cost them time and effort, many praise Chang for setting the record straight promptly and forthrightly. "I'm very pleased he's done this because there has been some confusion" about the original structures, says Christopher Higgins, a biochemist at Imperial College London. "Now the field can really move forward."
The most influential of Chang's retracted publications, other researchers say, was the 2001 Science paper, which described the structure of a protein called MsbA, isolated from the bacterium Escherichia coli. MsbA belongs to a huge and ancient family of molecules that use energy from adenosine triphosphate to transport molecules across cell membranes. These so-called ABC transporters perform many essential biological duties and are of great clinical interest because of their roles in drug resistance. Some pump antibiotics out of bacterial cells, for example; others clear chemotherapy drugs from cancer cells. Chang's MsbA structure was the first molecular portrait of an entire ABC transporter, and many researchers saw it as a major contribution toward figuring out how these crucial proteins do their jobs. That paper alone has been cited by 364 publications, according to Google Scholar.
Read more about this at: http://www.sciencemag.org/cgi/content/full/314/5807/1856
Then the dream turned into a nightmare. In September, Swiss researchers published a paper in Nature that cast serious doubt on a protein structure Chang's group had described in a 2001 Science paper. When he investigated, Chang was horrified to discover that a homemade data-analysis program had flipped two columns of data, inverting the electron-density map from which his team had derived the final protein structure. Unfortunately, his group had used the program to analyze data for other proteins. As a result, on page 1875, Chang and his colleagues retract three Science papers and report that two papers in other journals also contain erroneous structures.
"I've been devastated," Chang says. "I hope people will understand that it was a mistake, and I'm very sorry for it." Other researchers don't doubt that the error was unintentional, and although some say it has cost them time and effort, many praise Chang for setting the record straight promptly and forthrightly. "I'm very pleased he's done this because there has been some confusion" about the original structures, says Christopher Higgins, a biochemist at Imperial College London. "Now the field can really move forward."
The most influential of Chang's retracted publications, other researchers say, was the 2001 Science paper, which described the structure of a protein called MsbA, isolated from the bacterium Escherichia coli. MsbA belongs to a huge and ancient family of molecules that use energy from adenosine triphosphate to transport molecules across cell membranes. These so-called ABC transporters perform many essential biological duties and are of great clinical interest because of their roles in drug resistance. Some pump antibiotics out of bacterial cells, for example; others clear chemotherapy drugs from cancer cells. Chang's MsbA structure was the first molecular portrait of an entire ABC transporter, and many researchers saw it as a major contribution toward figuring out how these crucial proteins do their jobs. That paper alone has been cited by 364 publications, according to Google Scholar.
Read more about this at: http://www.sciencemag.org/cgi/content/full/314/5807/1856
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