OXFORD, England (AP) ? Roger Bannister returned to the track where he broke the 4-minute barrier for the mile 58 years ago, walking slowly but smiling broadly as he carried the Olympic torch across the finish line Tuesday just 17 days before the start of the London Games.
The 83-year-old Bannister walked 30 yards along the track, holding the Olympic torch aloft in his left hand as hundreds cheered for a man who is an embodiment of sporting achievement in Britain.
"In a way, I'm back in the sport that I belong to," he said. "I spent 10 years training before I broke the 4-minute mile."
Bannister ? who shattered an ankle in a car accident in 1975 and didn't run again ? put his walking cane aside and leaned on a young man to descend three stairs from the podium where the Olympic torch was lit to start the day's relay.
He walked down the track before handing the torch to an Oxford doctoral student Nicola Byrom, who ran a full lap wearing the white torchbearer uniform.
Bannister declined to wear the uniform, fueling speculation that the Oxford-educated neurologist may put on the outfit to light the cauldron at the opening ceremony in London on July 27.
Bannister is among those considered a candidate to light the cauldron.
He refused to speculate, saying he was fully focused on Tuesday's torch relay event.
Bannister said he felt "right at home" on the track where he ran the mile in 3 minutes, 59.4 seconds on May 6, 1954. The Iffley Road track is now called the Roger Bannister track.
"It's an honor to be included in a list of torch carriers, which has included injured soldiers back from Afghanistan and other places," Bannister said.
The strong winds on a chilly, rainy Tuesday reminded him of that historic day when "the weather was so bad that I nearly decided not to attempt it."
"In retrospect, I'm glad because if I hadn't attempted it that day I might not have had another chance," Bannister said.
Also in attendance Tuesday was Sebastian Coe, the former two-time Olympic 1,500-meter gold medalist and mile record-holder who chairs the organizing committee for the London Games.
He called Bannister one of Britain's "national treasures of sport."
"Breaking the four-minute mile as a mark of athletic achievement is central in the history of our sport," Coe said. "He paved the way for what we did in the late '70s and early '80s."
Despite attending eight Olympics ? one as an athlete and seven as a spectator ? Bannister never won an Olympic medal. He finished fourth in the 1,500 meters at the 1952 Helsinki Games.
Had Bannister won the Olympic gold in Helsinki, he probably would have retired and the first sub-4-minute mile would have been achieved by someone else. Instead, he competed for another two years and attacked the mile landmark.
Australia's John Landy and American Wes Santee ran times of 4:02, and it was a question of who would get there first.
Bannister scheduled his attempt for May 6, 1954, during a meet between Oxford University and the Amateur Athletic Union. The weather was miserable ? rainy, cool and windy. He only decided to make the attempt when he saw the English flag from a neighboring church start to flutter more gently as the race time approached.
He was paced by English runners Chris Brasher and Chris Chataway. Brasher ran the first lap in 58 seconds and the first half-mile in 1:58. Chataway moved to the front and took them through three laps in 3:01. Bannister had to run the final lap in 59 seconds and did.
The record didn't stand for long. Six weeks later, Landy ran 3:57.9 in Turku, Finland.
Bannister settled the score with Landy in August 1954 at the Empire Games, now called the Commonwealth Games, in Vancouver in what was dubbed the "Mile of the Century" or the "Miracle Mile." Bannister won in 3:58.8, with Landy second in 3:59.
The current record stands at 3:43.13, held by Morocco's Hicham El Guerrouj since 1999.
Bannister had a distinguished 40-year medical career since retiring after the 1954 Empire Games. He was knighted in 1975.
He was among number of sporting celebrities carrying the Olympic flame on Tuesday. At Henley-on-Thames, five-time Olympic rowing gold medalist Steve Redgrave carried the torch in his left and an oar in his right as he helped steer a boat to the Leander rowing club.
"To have my hands on the torch is pretty special," he said.
It may not be the last time. Redgrave is the British bookmakers' favorite to light the cauldron at the opening ceremony.
The flame stops included the Royal Ascot race course, where Italian jockey Frankie Dettori climbed aboard the retired Monsignor to carry the torch around the parade ring.
Dettori was initially forced to jump off the horse after the 18-year-old gelding appeared unnerved by the huge noise from spectators and later by the sight of the flame.
But after calming Monsignor, the Italian jockey rode the horse with the torch in his hand before jumping off again in his trademark leaping dismount.
"It is an honor and a privilege to be invited to carry the Olympic flame, especially at a track that holds such happy memories for me," Dettori said. "I've been round this paddock thousands of times, I've seen the queen here at Royal Ascot, but I've never seen a reception like it."
______
AP Sports Writer Stephen Wilson in London contributed to this report.
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Being related to that considerably powerful Ascend D Quad could spark some sort of a double-edged sword effect on Huawei's lesser-specced D1, but if all those cores the former has to offer mean nothing to those in China, the latter wouldn't be such a bad choice. In case you've forgotten -- unlike its beefier, quad-core-loaded brother -- this 4.5-inch (1280 x 720) Ascend D1's only sporting a dual-core, 1.5GHz TI OMAP CPU, which is paired next to 1GB of RAM and a tasty bite of Google's 4.0 treat. According to Huawei, the device is set to hit online shelves throughout the Great Wall starting today, with Russia being its next stop come August and "other markets to follow" sometime after. Be sure to pay the source below a visit if you're planning on grabbing one of these for yourself.
Penn engineers convert a natural plant protein into drug-delivery vehiclesPublic release date: 3-Jul-2012 [ | E-mail | Share ]
Contact: Evan Lerner elerner@upenn.edu 215-573-6604 University of Pennsylvania
PHILADELPHIA Finding biocompatible carriers that can get drugs to their targets in the body involves significant challenges. Beyond practical concerns of manufacturing and loading these vehicles, the carriers must work effectively with the drug and be safe to consume. Vesicles, hollow capsules shaped like double-walled bubbles, are ideal candidates, as the body naturally produces similar structures to move chemicals from one place to another. Finding the right molecules to assemble into capsules, however, remains difficult.
Researchers from the University of Pennsylvania have now shown a new approach for making vesicles and fine-tuning their shapes. By starting with a protein that is found in sunflower seeds, they used genetic engineering to make a variety of protein molecules that assemble into vesicles and other useful structures.
Daniel A. Hammer, Alfred G. and Meta A. Ennis Professor of Bioengineering, graduate student Kevin Vargo and research scientist Ranganath Parthasarathy of the Department of Chemical and Biomolecular Engineering in Penn's School of Engineering and Applied Science conducted the research.
Their work was published in the Proceedings of the National Academy of Sciences.
"To our knowledge, this is the first time a vesicle has been made from a recombinant protein," Hammer said.
Recombinant proteins are the products of a well-established technique that involves introducing a designed gene sequence into a host organism in most cases, the bacterium E. coli in order to get that organism to make a protein it would not normally produce.
Hammer's group worked for nearly a decade to find a protein that was biocompatible, could be produced through recombinant methods and, most important, could be induced to form vesicles.
"The molecule we identified is called oleosin," Hammer said. "It's a surfactant protein found in sunflower and sesame seeds."
Surfactants are soap-like chemicals that have two distinct sides; one side is attracted to water and the other is repelled by it. They can make many structures in solution but making vesicles is rare. Most often, surfactants make micelles, in which a single layer of molecules aggregates with the water-loving part on the outside and the water-hating part on the inside. Micelles have a limited ability to carry drugs. Vesicles, in contrast, have two walls aligned so the two water-hating sides face each other. The water-loving interior cavity allows the transport of a large payload of water-soluble molecules that are suspended in water. Since many drugs are water soluble, vesicles offer significant advantages for drug delivery.
The team systematically modified oleosin to find variants of the molecule that could form vesicles. Getting oleosin to take this complex shape meant selectively removing and changing parts of oleosin's gene sequence so that the corresponding protein would fold the way the researchers wanted after it was produced by the E.coli.
"We started by truncating the sequence that codes for the hydrophobic part, shortening the protein itself," Hammer said. "We did more complex truncations at the ends for separation and to control the shape of the assembly."
"There are simple ways to correlate the gene sequence to the geometry you get in the protein," Vargo said. "For example, getting the right amount of curvature to make a spherical vesicle means the chains should be sufficiently large that they do not pack tightly."
In the process of finding the right protein for this task, the researchers came up with several other useful protein variants that form different shapes, including sheets and fibers, when grown in the appropriate salt solutions.
Materials made by recombinant methods offer an additional advantage in that the precise sequence of amino acids can be controlled for targeting to specific receptors and other biological targets. For proteins of this size, this level of control is not attainable by any other method.
"Other groups have synthesized polypeptide vesicles, but they have a hard time controlling the sequences in individual sections of their molecules," Vargo said. "We can go in a change a single amino acid in the protein by modifying the corresponding part of the gene."
"Recombinant methods mean we can make polymers that are all of a defined length and dictate the chemical composition at each location along that length," Hammer said. "You get the exact length and sequence every time."
According to Hammer's team, the hardest part of the research was confirming that these sequences did indeed fold into vesicles. This was only possible with specialized equipment available to the researchers through their association with Penn's Materials Research Science and Engineering Center and made possible by a grant written by professor Karen Winey from Materials Science and Engineering.
"The vast majority of our time in this project was doing the imaging; making the protein was relatively easy," Hammer said.
The imaging technique used is known as cyro-transmission electron microscopy, or cryoTEM
"With cryoTEM," Vargo said, "we create a thin layer of solution, then plunge it into ethane, freezing it fast enough that the water doesn't crystallize. Ice crystals would also destroy the vesicles, so this technique leaves you with your particles and structures intact."
As their protein is already routinely eaten, the researchers are confident that their oleosin vesicles will be of great interest in drug-delivery applications, particularly oral-drug delivery. Future work will entail adding genes for functional groups to allow the vesicles to target certain tissues, as well as determining whether the proteins can be induced to change shape once they reach their targets.
"This research opens up the possibility of using switchable motifs to allow us to release high concentrations of drugs on different cues, such as a change in acidity," Hammer said. "Tumor microenvironments and the interior of tumors are known to be acidic, so a vesicle that falls apart in acidic environments would be extremely valuable."
###
The work was supported by the National Science Foundation through the Penn MRSEC and the U.S. Department of Energy, Office of Basic Energy Sciences, Division of Materials Sciences and Engineering.
[ | E-mail | Share ]
?
AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
Penn engineers convert a natural plant protein into drug-delivery vehiclesPublic release date: 3-Jul-2012 [ | E-mail | Share ]
Contact: Evan Lerner elerner@upenn.edu 215-573-6604 University of Pennsylvania
PHILADELPHIA Finding biocompatible carriers that can get drugs to their targets in the body involves significant challenges. Beyond practical concerns of manufacturing and loading these vehicles, the carriers must work effectively with the drug and be safe to consume. Vesicles, hollow capsules shaped like double-walled bubbles, are ideal candidates, as the body naturally produces similar structures to move chemicals from one place to another. Finding the right molecules to assemble into capsules, however, remains difficult.
Researchers from the University of Pennsylvania have now shown a new approach for making vesicles and fine-tuning their shapes. By starting with a protein that is found in sunflower seeds, they used genetic engineering to make a variety of protein molecules that assemble into vesicles and other useful structures.
Daniel A. Hammer, Alfred G. and Meta A. Ennis Professor of Bioengineering, graduate student Kevin Vargo and research scientist Ranganath Parthasarathy of the Department of Chemical and Biomolecular Engineering in Penn's School of Engineering and Applied Science conducted the research.
Their work was published in the Proceedings of the National Academy of Sciences.
"To our knowledge, this is the first time a vesicle has been made from a recombinant protein," Hammer said.
Recombinant proteins are the products of a well-established technique that involves introducing a designed gene sequence into a host organism in most cases, the bacterium E. coli in order to get that organism to make a protein it would not normally produce.
Hammer's group worked for nearly a decade to find a protein that was biocompatible, could be produced through recombinant methods and, most important, could be induced to form vesicles.
"The molecule we identified is called oleosin," Hammer said. "It's a surfactant protein found in sunflower and sesame seeds."
Surfactants are soap-like chemicals that have two distinct sides; one side is attracted to water and the other is repelled by it. They can make many structures in solution but making vesicles is rare. Most often, surfactants make micelles, in which a single layer of molecules aggregates with the water-loving part on the outside and the water-hating part on the inside. Micelles have a limited ability to carry drugs. Vesicles, in contrast, have two walls aligned so the two water-hating sides face each other. The water-loving interior cavity allows the transport of a large payload of water-soluble molecules that are suspended in water. Since many drugs are water soluble, vesicles offer significant advantages for drug delivery.
The team systematically modified oleosin to find variants of the molecule that could form vesicles. Getting oleosin to take this complex shape meant selectively removing and changing parts of oleosin's gene sequence so that the corresponding protein would fold the way the researchers wanted after it was produced by the E.coli.
"We started by truncating the sequence that codes for the hydrophobic part, shortening the protein itself," Hammer said. "We did more complex truncations at the ends for separation and to control the shape of the assembly."
"There are simple ways to correlate the gene sequence to the geometry you get in the protein," Vargo said. "For example, getting the right amount of curvature to make a spherical vesicle means the chains should be sufficiently large that they do not pack tightly."
In the process of finding the right protein for this task, the researchers came up with several other useful protein variants that form different shapes, including sheets and fibers, when grown in the appropriate salt solutions.
Materials made by recombinant methods offer an additional advantage in that the precise sequence of amino acids can be controlled for targeting to specific receptors and other biological targets. For proteins of this size, this level of control is not attainable by any other method.
"Other groups have synthesized polypeptide vesicles, but they have a hard time controlling the sequences in individual sections of their molecules," Vargo said. "We can go in a change a single amino acid in the protein by modifying the corresponding part of the gene."
"Recombinant methods mean we can make polymers that are all of a defined length and dictate the chemical composition at each location along that length," Hammer said. "You get the exact length and sequence every time."
According to Hammer's team, the hardest part of the research was confirming that these sequences did indeed fold into vesicles. This was only possible with specialized equipment available to the researchers through their association with Penn's Materials Research Science and Engineering Center and made possible by a grant written by professor Karen Winey from Materials Science and Engineering.
"The vast majority of our time in this project was doing the imaging; making the protein was relatively easy," Hammer said.
The imaging technique used is known as cyro-transmission electron microscopy, or cryoTEM
"With cryoTEM," Vargo said, "we create a thin layer of solution, then plunge it into ethane, freezing it fast enough that the water doesn't crystallize. Ice crystals would also destroy the vesicles, so this technique leaves you with your particles and structures intact."
As their protein is already routinely eaten, the researchers are confident that their oleosin vesicles will be of great interest in drug-delivery applications, particularly oral-drug delivery. Future work will entail adding genes for functional groups to allow the vesicles to target certain tissues, as well as determining whether the proteins can be induced to change shape once they reach their targets.
"This research opens up the possibility of using switchable motifs to allow us to release high concentrations of drugs on different cues, such as a change in acidity," Hammer said. "Tumor microenvironments and the interior of tumors are known to be acidic, so a vesicle that falls apart in acidic environments would be extremely valuable."
###
The work was supported by the National Science Foundation through the Penn MRSEC and the U.S. Department of Energy, Office of Basic Energy Sciences, Division of Materials Sciences and Engineering.
[ | E-mail | Share ]
?
AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert! system.
Face detection is a common sight in still photography, but it's a rarity in video outside of certain research projects. Google may be keen to take some of the mystery out of those clips through a just-published patent application: its technique uses video frames to generate clusters of face representations that are attached to a given person. By knowing what a subject looks like from various angles, Google could then attach a name to a face whenever it shows up in a clip, even at different angles and in strange lighting conditions. The most obvious purpose would be to give YouTube viewers a Flickr-like option to tag people in videos, but it could also be used to spot people in augmented reality apps and get their details -- imagine never being at a loss for information about a new friend as long as you're wearing Project Glass. As a patent, it's not a definitive roadmap for where Google is going with any of its properties, but it could be a clue as to the search giant's thinking. Don't be surprised if YouTube can eventually prove that a Google+ friend really did streak across the stage at a concert.
It's rare, to say the least, for a competitive-eating injury to rate coverage on CNN and ESPN. Eating-related maladies tend to be chuckled over by newscasters and DJs, who see eating contests as fodder for light human-interest stories, and exploited by op-ed jeremiahs, who see competitive eating as the apotheosis of a litany of American sins: gluttony, obesity, our love of dumb spectacles. Honestly, most eating injuries are pretty unsurprising, arising from health conditions you'd expect to find among the professionally hungry (obesity, diabetes) or from the poor choices of inexperienced eaters who get in over their heads. But Kobayashi's sore jaw deserves all the attention it's getting and more. It is something new to competitive eating: a true athletic injury. By introducing a tragic dimension to a phenomenon that has always gorged on irony and slapstick comedy, the man they call "Tsunami" is doing competitive eating a great and useful service.
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