Microsoft's big coming out day for Windows 8 is finally upon us. In celebration, Redmond's throwing a launch party for its newest OS update on New York City's Pier 57. You may not be able to join in on the fun in person, but we've got this handy stream beyond the break should you wish to play along virtually, and it's starting any minute.
Update: Some folks are having issues with the primary stream, and if you're one of those folks, you may wanna redirect your browser here for an alternative feed.
Update 2: The stream is back, this time with a focus on the Surface RT. Follow along below!
Structure discovered for promising tuberculosis drug targetPublic release date: 25-Oct-2012 [ | E-mail | Share ]
Contact: Catherine Kolf ckolf@jhmi.edu 443-287-2251 Johns Hopkins Medicine
M. tuberculosis cell wall could soon be breached
Researchers at Johns Hopkins have figured out the three-dimensional shape of the protein responsible for creating unique bonds within the cell wall of the bacteria that cause tuberculosis. The bonds make the bacteria resistant to currently available drug therapies, contributing to the alarming rise of these super-bacteria throughout the world.
With the protein structure in hand, the scientists say, drug designers have a clear way forward for weakening the cell wall and killing these deadly bacteria. Their results are reported in a paper published online Oct. 25 in Structure.
"We've known for a while that this protein would make a good drug target, but without a structural model, drug discovery is like blindly choosing random objects to fit into a small hole of unknown shape and size. The results of our study have removed the blindfold," says L. Mario Amzel, Ph.D., professor and director of the Department of Biophysics and Biophysical Chemistry at The Johns Hopkins University School of Medicine.
The Johns Hopkins team used a technique called X-ray crystallography to scatter radiation off a specially prepared portion of the enzyme that forms the unique molecular bonds within the cell wall of Mycobacterium tuberculosis. They then used information about the direction and intensity of the radiation scattered to build a 3-D model of the arrangement of atoms in the enzyme.
Mario A. Bianchet, Ph.D., assistant professor of neurology at Johns Hopkins and a member of the research team, says the challenge of TB infection is that most of the long and costly standard drug treatment is just to get rid of the roughly 1 percent of bacteria that persist after the first week of a patient's treatment. "The 'persisters' resist in part because of unique bonds within their cell walls. Their cell walls form a thick, three-layered boundary between the bacteria and the outside world, including a middle layer of interlocking molecules, called peptidoglycans, that form a network resembling a chain-link fence," says Bianchet.
Peptidoglycans are long chains of individual sugar molecules with short protein branches extending from every other sugar on alternating sides of the chain. Specific enzymes bond the protein branches to each other to create a meshwork. In most species of bacteria, Amzel says, the majority of the bonds between these branches are created between position 4 on one branch and position 3 on an opposing branch. In M. tuberculosis, however, the majority of the bonds are created between positions 3 on both branches. The most common antibiotics interfere with the enzyme that creates the 4-3 bonds, which is enough to destabilize the cell wall and kill most of the TB bacteria.
The bacteria that persist have a particularly high level of 3-3 bonds between the peptidoglycan chains in their cell walls. These 3-3 bonds are created by a different enzyme, the one that Amzel and Bianchet studied, which is not specifically targeted by any current drugs. In addition to showing the structure of the enzyme, the team also showed a peptidoglycan molecule inside the action site where the 3-3 bonds are made, giving drug designers even more details about the way the protein works.
Amzel adds that "beyond fighting TB, the structure of this enzyme may help us fight other disease-causing bacteria that have similar enzymes, such as Enterococcus faecium and the spore-forming, drug-resistant Clostridium difficile."
###
Other authors on the paper include Sabri Erdemli, Radhika Gupta, William Bishai and Gyanu Lamichhane from The Johns Hopkins University.
This work was supported by grants from the National Institutes of Health Office of the Director (DP2OD008459) and the National Institute of Allergy and Infectious Diseases (1R56AI087749).
On the Web:
Link to article: http://dx.doi.org/10.1016/j.str.2012.09.016
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.
Structure discovered for promising tuberculosis drug targetPublic release date: 25-Oct-2012 [ | E-mail | Share ]
Contact: Catherine Kolf ckolf@jhmi.edu 443-287-2251 Johns Hopkins Medicine
M. tuberculosis cell wall could soon be breached
Researchers at Johns Hopkins have figured out the three-dimensional shape of the protein responsible for creating unique bonds within the cell wall of the bacteria that cause tuberculosis. The bonds make the bacteria resistant to currently available drug therapies, contributing to the alarming rise of these super-bacteria throughout the world.
With the protein structure in hand, the scientists say, drug designers have a clear way forward for weakening the cell wall and killing these deadly bacteria. Their results are reported in a paper published online Oct. 25 in Structure.
"We've known for a while that this protein would make a good drug target, but without a structural model, drug discovery is like blindly choosing random objects to fit into a small hole of unknown shape and size. The results of our study have removed the blindfold," says L. Mario Amzel, Ph.D., professor and director of the Department of Biophysics and Biophysical Chemistry at The Johns Hopkins University School of Medicine.
The Johns Hopkins team used a technique called X-ray crystallography to scatter radiation off a specially prepared portion of the enzyme that forms the unique molecular bonds within the cell wall of Mycobacterium tuberculosis. They then used information about the direction and intensity of the radiation scattered to build a 3-D model of the arrangement of atoms in the enzyme.
Mario A. Bianchet, Ph.D., assistant professor of neurology at Johns Hopkins and a member of the research team, says the challenge of TB infection is that most of the long and costly standard drug treatment is just to get rid of the roughly 1 percent of bacteria that persist after the first week of a patient's treatment. "The 'persisters' resist in part because of unique bonds within their cell walls. Their cell walls form a thick, three-layered boundary between the bacteria and the outside world, including a middle layer of interlocking molecules, called peptidoglycans, that form a network resembling a chain-link fence," says Bianchet.
Peptidoglycans are long chains of individual sugar molecules with short protein branches extending from every other sugar on alternating sides of the chain. Specific enzymes bond the protein branches to each other to create a meshwork. In most species of bacteria, Amzel says, the majority of the bonds between these branches are created between position 4 on one branch and position 3 on an opposing branch. In M. tuberculosis, however, the majority of the bonds are created between positions 3 on both branches. The most common antibiotics interfere with the enzyme that creates the 4-3 bonds, which is enough to destabilize the cell wall and kill most of the TB bacteria.
The bacteria that persist have a particularly high level of 3-3 bonds between the peptidoglycan chains in their cell walls. These 3-3 bonds are created by a different enzyme, the one that Amzel and Bianchet studied, which is not specifically targeted by any current drugs. In addition to showing the structure of the enzyme, the team also showed a peptidoglycan molecule inside the action site where the 3-3 bonds are made, giving drug designers even more details about the way the protein works.
Amzel adds that "beyond fighting TB, the structure of this enzyme may help us fight other disease-causing bacteria that have similar enzymes, such as Enterococcus faecium and the spore-forming, drug-resistant Clostridium difficile."
###
Other authors on the paper include Sabri Erdemli, Radhika Gupta, William Bishai and Gyanu Lamichhane from The Johns Hopkins University.
This work was supported by grants from the National Institutes of Health Office of the Director (DP2OD008459) and the National Institute of Allergy and Infectious Diseases (1R56AI087749).
On the Web:
Link to article: http://dx.doi.org/10.1016/j.str.2012.09.016
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.
Remember back in August when Acers JT Wang suggested that if Microsoft priced the Surface with Windows RT at $199 that it would negatively impact its partners and vendors? So now that the Apple event is over and we heard Apple announce the iPad Mini at $329, heres where the Microsoft Surface with Windows RT stands in terms of price:
Since its the more expensive option at this point, doesnt include the full type cover as initially thought (without additional charges), and only includes Office 2013 Home and Student Edition, does the Surface still stand a chance in the marketplace? Im curious to know how others feel about this.
Despite everything, Im still interested in the Microsoft Surface and Windows 8 application developer. For enterprise users, Windows 8 seems to be the best of both worlds, something that arguably Apple still cant capture. During Apples press conference today, they mentioned that they have 125 million documents in the cloud. They also announced that theyve sold over 100 million iPads. This means that theres just over 1 document in the cloud per person. Thats not too impressive. The other thing they mentioned is that developers made over $6.5 billion (with a b) on applications in the App Store. However, they failed to mention that this also translates to $2.79 billion that Apple themselves have pocketed for developers hard earned dollars. Microsoft is changing the game, slightly, for developers by offering an 80/20 split after the application has made $25,000 in the Microsoft Store.
To begin to learn how to develop for Windows 8, download Visual Studio Express here and visit Generation App, a 30-day training plan for developing a Windows 8 application.
DELHI, NY (10/24/2012)(readMedia)-- SUNY Delhi students will show their appreciation to the community that founded their college by volunteering locally through the O'Connor Center for Community Engagement for Community Service Day on Saturday, October 27.
Students will assist various area organizations in celebration of Delhi's 100th birthday. "This year our annual Community Service Day not only celebrates the college's centennial by helping the town and village of Delhi, but it also celebrates National 'Make A Difference Day,'" said Elizabeth Sova, SUNY Delhi Coordinator of the O'Connor Center for Community Engagement. "The day will be jam-packed with activities right here on campus as well as many of our traditional volunteer sites."
Delhi students will be volunteering at the following non-profit agencies and organizations: Saturday's Bread in Oneonta, Roberto's Kids, Merchants on Main (Village of Delhi), Delaware County Community Action Network (DCCAN), The ARC of Delaware County, area churches, Delaware Opportunities Big Buddies, Delaware County Office for the Aging, Delhi Senior Housing, Delhi Outdoor Education Center, WSKG, Oneonta World of Learning (OWL) and Woodland Cemetery.
Also on October 27, SUNY Delhi will host the Spooky Science Event, co-sponsored by the O'Connor Center for Community Engagement (OCCE), WSKG and OWL. Approximately 500 elementary and middle school students and their families from Delhi, South Kortright, Charlotte Valley, Stamford, Walton and Oneonta schools will participate. New PBS SciGirls Spooky Science episodes will be shown from 11 a.m. to 2 p.m. in The Okun Theatre. A science dance workshop will be held in the college's dance studio and 21 stations of take-home activities will be led by OWL volunteers and SUNY Delhi students. SUNY Delhi's Patisserie Club will also offer cupcake decorating.
The O'Connor Center for Community Engagement began in 1999 with grant support from the O'Connor Foundation and other local organizations. The Center matches individual students, clubs, classes, and faculty and staff volunteers with non-profit agencies and organizations within the greater Delhi community that need a helping hand. It serves as a clearinghouse for these community organizations, and facilitates volunteerism by arranging for transportation, orientation and training, and feedback on completed community service projects. The O'Connor Center has been named to the
President's National Honor Roll for Community Service for the last six years. Delhi students complete over 24,000 hours of service annually with over 70 percent involved in some type of service activity through clubs and organizations.
For more information about Community Service Day or the Spooky Science Event, contact Elizabeth Sova at 607-746-4781.
__________________ You don't have to know everything, if you know where to find it. When you do ask questions, you may look stupid. When you do NOT ask questions, you will STAY stupid.
It would be nice to have the Timezone ( GMT +/- x ) in the location field in the profile. (User CP -> Edit Your Details)
Gowrings Motobility will be bringing its roadshow to the RAF Museum in London on 1-3 November 2012.?Located approximately?6 miles from central London, the RAF Museum houses a world-class collection of aircraft, aviation artefacts and memorabilia. Visitors can get close to flying machines from an early airship gondola, a Bl?riot from 1909 and the most up to date aircraft, the Eurofighter Typhoon.
About the Roadshow
The aim of the roadshow,?which is now in its third year,?is to inspire people with disabilities to experience attractions and places of interest they may not have otherwise considered.? It is hoped that it will show people what they can do and that they can take the attitude that you really can ?go where you want to go?.
Visitors will be able to experience a taste of flying first hand as Aerobility will be bringing their fully wheelchair accessible flight simulator.??Also on hand will be a number of local charities to offer news, information and advice.
Discounts for wheelchair users
Wheelchair users and their carers can take advantage of free parking and 10% off at the gift shop.? To?take advantage of the offer during the Roadshow, visitors should request an invitation in advance from Gowrings Mobility by calling 0845 608 8020.? This offer is only valid during the Roadshow dates on the following dates:
Thursday 1 November
Friday 2 November and
Saturday 3 November 2012.
The Roadshow is open between 10 AM and 4 PM each day.
More details can be found here
?
Address:
Royal Air Force Museum London, Grahame Park Way London NW9 5LL
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Public release date: 25-Oct-2012
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