'It is in everyone's best interest for Reebok to end its partnership with Mr. Ross,' sneaker giant says in a statement to MTV News.
Rick Ross
Photo: Alexander Tamargo
Source: http://www.mtv.com/news/articles/1705463/rick-ross-reebok-controversy.jhtml
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SAN FRANCISCO (AP) ? The U.S. Navy's Blue Angels says the rest of its season is canceled because of federal budget cuts.
The aerobatic team's lead pilot and team commander Tom Frosch made the announcement Tuesday at the team's headquarters. He says it is the first time since the Korean War that the team would not make the air show rounds.
The San Francisco Chronicle reports (http://bit.ly/1498cmj) that the cancellation means the team won't be flying over San Francisco during this fall's Fleet Week, and the future of the city's annual Fleet Week could be in doubt with the air show canceled.
Fleet Week organizer J. Michael Myatt says there probably would be no air show without the Blue Angels and the Parade of Ships also could be in jeopardy because of budget cuts.
___
Information from: San Francisco Chronicle, http://www.sfgate.com
Source: http://news.yahoo.com/blue-angels-cancel-air-shows-over-budget-cuts-033848352.html
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Those red pins look almost like little hearts, revealing which countries have been showered with the affection of Google's crowdsourced map improvement tool and those -- like the UK -- that have so far been left out. We can now safely ignore the chart, however, as the UK has just received its dose of Map Maker love, taking its rightful place among nations like the US, France, India and even North Korea. Instead of just reporting problems, which has long been possible, Brits can use the browser-based service to contribute additional local knowledge about everything from bus stations to cycle routes, as well as natural features like parks and even bits of shrubbery. (Hopefully, only really amazing bits of shrubbery.) You can watch folks adding these sorts of things, almost in real-time, at the Google link below -- and it's weirdly addictive.
Filed under: Internet
Via: BBC News
Source: Google Map Maker
Source: http://www.engadget.com/2013/04/11/google-map-maker-comes-to-the-uk/
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Fifty years ago, a young Soviet Cosmonaut called Yuri Gagarin was blasted into space and into the history books. His may be a well-known story but ITV's Lawrence McGinty, has some fascinating facts that have stayed secret for all those years.
By Miriam Kramer
Space.com
This week, space geeks around the world will celebrate the historic flight that made Yuri Gagarin the first person to leave the confines of Earth 52 years ago.
"Yuri's Night" (celebrated annually the week of April 12) commemorates Soviet cosmonaut Yuri Gagarin's first flight with parties and special events honoring more than five decades of human spaceflight. This year, festivities will take place on Friday, with some lasting into the weekend and next week.
Gagarin launched into space on April 12, 1961 aboard his Vostok space capsule, ushering in the age of human spaceflight. Exactly 20 years after Gagarin's historic flight, NASA launched the first space shuttle mission on April 12, 1981 to kick of reusable spacecraft program that would last three decades. Yuri's Night celebrations are aimed at marking both space anniversaries, as well as toasting the spirit of space exploration. [Yuri Gagarin: First Man in Space (Photos)]
"Yuri's Night is the world space party," the project's spokesman Brice Russ told Space.com. "(It's a) global celebration of space."
So far, 255 parties in 42 countries have been registered through Yuri's Night's official website, Russ said. Groups of space fans on six continents are planning celebrations, and Russ is in negotiations with a possible party host in Antarctica to get the last continent added to the list.?
ESA
Cosmonaut Yuri Gagarin was the first human to travel into space.
"We have 75 events officially registered on our website for the United States, with more coming in each day," Russ wrote Space.com in an email. "If people are interested in participating in Yuri's Night but don't have an event nearby (and don't want to start one up themselves), they can join Yuri's Night online via webcasts or virtual events."
Launched in 2001, Yuri's Night began with 64 events around the world. Ten years later ? on the 50-year anniversary of human spaceflight in 2011 ? people in 74 different countries hosted 550 events making it the largest Yuri's Night in the event's history. This year is shaping up to be the second-largest, Russ added.
?
"Everyone is welcome to come to celebrate Yuri's night with us," Russ added. "There is something at Yuri's night for everyone."
It is not too late to register and host your own Yuri's Night party. Simply sign up online through YurisNight.netto make your party searchable in the "party list." There is no party too big or too small to be a part of the celebration, Russ said.
If you'd like to find a party near you, visit the "Find a Party" page and use the Google Map to search for a convenient location.
Follow Miriam Kramer @mirikramer and Google+. Follow us @Spacedotcom, Facebook?and Google+. Original article on Space.com.
Copyright 2013 Space.com, a TechMediaNetwork company. All rights reserved. This material may not be published, broadcast, rewritten or redistributed.
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![[ Back to EurekAlert! ]](http://www.eurekalert.org/images/back2e.gif){kind=small}
Public release date: 9-Apr-2013
Share ] Contact: Jan Grabowski
jan.grabowski@helmholtz-hzi.de
49-531-618-11407
Helmholtz Centre for Infection Research
This press release is available in German.
In the search for new antibiotics, researchers are taking an unusual approach: They are developing peptides, short chains of protein building blocks that effectively inhibit a key enzyme of bacterial metabolism. Now, scientists at the Helmholtz Institute for Pharmaceutical Research Saarland (HIPS) in Saarbrcken, a branch of the Helmholtz Center for Infection Research (HZI), have published their findings and the implications for potential medical application in the scientific journal ACS Chemical Biology.
The road from gene to protein has an important stop along the way: ribonucleic acid, or RNA. This molecule is essentially a "negative copy" of DNA, the cell's hereditary material, and serves as a blueprint for the cell to make proteins, the basic building blocks of life. This "template" is assembled by the enzyme RNA polymerase, whose job it is to read off the information that is stored within the DNA molecule.
Bacterial RNA polymerase consists of several subunits. The core enzyme has to first bind a certain protein molecule called "sigma factor" which essentially allows the enzyme to begin production of the RNA molecule. The sigma factor locates the starting point of the gene to be copied - as soon as its job is done, it once again detaches from the enzyme complex. The next time, the sigma factor and the core enzyme have to bind to each other again. If this is no longer possible, new RNA cannot be synthesized and no more proteins will be made by the cell. Cellular processes come to a complete standstill, and the bacterium dies.
Which is exactly the reason why the point of contact between the sigma factor and the core enzyme represents a potential target for new therapies against bacterial infections. Another feature makes this a particularly attractive target: "Sigma factors are unique to bacteria and are not found in mammalian cells," explains Kristina Hsecken, Ph.D. student at the HIPS and the publication's first author. "This way, we are able to specifically target the bacteria without putting the body's own cells at risk." Which also means potential side effects are not to be expected.
The drug researchers from Saarbrcken have looked at a range of peptides, short chains of amino acids, capable of inhibiting the polymerase. Their structure corresponds to areas from the binding site of one of the enzyme parts: A perfect fit, the peptides dock either to the core enzyme or to the sigma factor, specifically at the exact location where the counterpart would normally attach to. This way, the components are prevented from combining to form a functional enzyme since the binding site is already occupied. Of the 16 total peptides the researchers examined, one in particular proved especially effective. The peptide called P07 was able to show in further tests that it actually does prevent transcription of DNA to RNA in bacterial cells by interfering with the interaction between sigma and core enzyme.
A number of current antibiotics target bacterial RNA polymerase, among them rifampicin, which was first introduced in the late 1960s. Yet these classic drugs are quickly losing their efficacy, as germs are evolving resistance to them. "Since we're looking at a new mode of action, it won't come to cross resistance, which is a much-feared issue with new antibiotics," says Dr. Jrg Haupenthal, the study's principal investigator. This could be the case with any new substance whose mode of action is similar to that of an antibiotic the bacteria have already evolved resistance to.
Whether or not P07 will be developed into a market-ready drug is something Haupenthal and his colleagues cannot predict. "Even though our research points the way to new and effective antibiotics, actually developing them into full-blown drugs for clinical use requires much additional research," says Haupenthal. As such, the researchers are working at optimizing P07 while also looking for other molecules capable of binding to the same spot on the polymerase enzyme.
###
Original publication:
K. Hsecken, M. Negri, M. Fruth, S. Boettcher, R.W. Hartmann, J. Haupenthal
Peptide-Based Investigation of Escherichia coli RNA Polmerase ?(70):Core Interface As Target Site
ACS Chemical Biology, 2013, DOI: 10.1021/cb3005758 dx.doi.org/10.1021/cb3005758
The Helmholtz Centre for Infection Research
At the Helmholtz Centre for Infection Research (HZI) in Braunschweig, scientists are studying microbial virulence factors, host-pathogen interactions and immunity. The goal is to develop strategies for the diagnosis, prevention and therapy of human infectious diseases. http://www.helmholtz-hzi.de/en
The Helmholtz Insititute for Pharmaceutical Research Saarland
The Helmholtz Institute for Pharmaceutical Research Saarland (HIPS) is a branch of the Helmholtz Centre for Infection Research (HZI) in Braunschweig and was founded together with the Saarland University in 2009. Where do new compounds against widespread infections come from, how can they be optimised for the application to humans and how are they delivered efficiently to the target site? The scientists at HIPS are searching for answers to these questions by deploying highly modern methods of pharmaceutical sciences. http://www.helmholtz-hzi.de/HIPS
[ | 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.
Public release date: 9-Apr-2013 Share ] Contact: Jan Grabowski
jan.grabowski@helmholtz-hzi.de
49-531-618-11407
Helmholtz Centre for Infection Research
This press release is available in German.
In the search for new antibiotics, researchers are taking an unusual approach: They are developing peptides, short chains of protein building blocks that effectively inhibit a key enzyme of bacterial metabolism. Now, scientists at the Helmholtz Institute for Pharmaceutical Research Saarland (HIPS) in Saarbrcken, a branch of the Helmholtz Center for Infection Research (HZI), have published their findings and the implications for potential medical application in the scientific journal ACS Chemical Biology.
The road from gene to protein has an important stop along the way: ribonucleic acid, or RNA. This molecule is essentially a "negative copy" of DNA, the cell's hereditary material, and serves as a blueprint for the cell to make proteins, the basic building blocks of life. This "template" is assembled by the enzyme RNA polymerase, whose job it is to read off the information that is stored within the DNA molecule.
Bacterial RNA polymerase consists of several subunits. The core enzyme has to first bind a certain protein molecule called "sigma factor" which essentially allows the enzyme to begin production of the RNA molecule. The sigma factor locates the starting point of the gene to be copied - as soon as its job is done, it once again detaches from the enzyme complex. The next time, the sigma factor and the core enzyme have to bind to each other again. If this is no longer possible, new RNA cannot be synthesized and no more proteins will be made by the cell. Cellular processes come to a complete standstill, and the bacterium dies.
Which is exactly the reason why the point of contact between the sigma factor and the core enzyme represents a potential target for new therapies against bacterial infections. Another feature makes this a particularly attractive target: "Sigma factors are unique to bacteria and are not found in mammalian cells," explains Kristina Hsecken, Ph.D. student at the HIPS and the publication's first author. "This way, we are able to specifically target the bacteria without putting the body's own cells at risk." Which also means potential side effects are not to be expected.
The drug researchers from Saarbrcken have looked at a range of peptides, short chains of amino acids, capable of inhibiting the polymerase. Their structure corresponds to areas from the binding site of one of the enzyme parts: A perfect fit, the peptides dock either to the core enzyme or to the sigma factor, specifically at the exact location where the counterpart would normally attach to. This way, the components are prevented from combining to form a functional enzyme since the binding site is already occupied. Of the 16 total peptides the researchers examined, one in particular proved especially effective. The peptide called P07 was able to show in further tests that it actually does prevent transcription of DNA to RNA in bacterial cells by interfering with the interaction between sigma and core enzyme.
A number of current antibiotics target bacterial RNA polymerase, among them rifampicin, which was first introduced in the late 1960s. Yet these classic drugs are quickly losing their efficacy, as germs are evolving resistance to them. "Since we're looking at a new mode of action, it won't come to cross resistance, which is a much-feared issue with new antibiotics," says Dr. Jrg Haupenthal, the study's principal investigator. This could be the case with any new substance whose mode of action is similar to that of an antibiotic the bacteria have already evolved resistance to.
Whether or not P07 will be developed into a market-ready drug is something Haupenthal and his colleagues cannot predict. "Even though our research points the way to new and effective antibiotics, actually developing them into full-blown drugs for clinical use requires much additional research," says Haupenthal. As such, the researchers are working at optimizing P07 while also looking for other molecules capable of binding to the same spot on the polymerase enzyme.
###
Original publication:
K. Hsecken, M. Negri, M. Fruth, S. Boettcher, R.W. Hartmann, J. Haupenthal
Peptide-Based Investigation of Escherichia coli RNA Polmerase ?(70):Core Interface As Target Site
ACS Chemical Biology, 2013, DOI: 10.1021/cb3005758 dx.doi.org/10.1021/cb3005758
The Helmholtz Centre for Infection Research
At the Helmholtz Centre for Infection Research (HZI) in Braunschweig, scientists are studying microbial virulence factors, host-pathogen interactions and immunity. The goal is to develop strategies for the diagnosis, prevention and therapy of human infectious diseases. http://www.helmholtz-hzi.de/en
The Helmholtz Insititute for Pharmaceutical Research Saarland
The Helmholtz Institute for Pharmaceutical Research Saarland (HIPS) is a branch of the Helmholtz Centre for Infection Research (HZI) in Braunschweig and was founded together with the Saarland University in 2009. Where do new compounds against widespread infections come from, how can they be optimised for the application to humans and how are they delivered efficiently to the target site? The scientists at HIPS are searching for answers to these questions by deploying highly modern methods of pharmaceutical sciences. http://www.helmholtz-hzi.de/HIPS
[ | 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.
Source: http://www.eurekalert.org/pub_releases/2013-04/hcfi-bop040913.php
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Perhaps the last-minute opponent change was exactly what Gegard Mousasi needed. The former Strikeforce light heavyweight champion made his debut on Saturday and pulled out a decision over Ilir Latifi, a late replacement after Alexander Gustafsson was not cleared for the fight because of a cut. Mousasi pulled out the unanimous decision win, but shared afterwards that he was dealing with a knee injury.
"I don't want to talk a lot about my injury, but I can tell that this injury, I'm pretty sure 95 percent wouldn't fight, from other fighters," Mousasi said in the postfight press conference.
"You know, I stepped up, I didn't cancel the show, you know, I don't know, we go from here, you know."
In other action, Ross Pearson notched a second-round TKO over Ryan Couture. Matt Mitrione stopped his losing streak with a 19-second KO of Philip de Fries. Brad Pickett won a split decision over Mike Easton in a bout that won Fight of the Night honors. Diego Brandao submitted Pablo Garza in the third round with an arm-triangle choke.
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Apr. 8, 2013 ? More powerful batteries could help electric cars achieve a considerably larger range and thus a breakthrough on the market. A new nanomaterial for lithium ion batteries developed in the labs of chemists at ETH Zurich and Empa could come into play here.
They provide power for electric cars, electric bicycles, smartphones and laptops; nowadays, rechargeable lithium ion batteries are the storage media of choice when it comes to supplying a large amount of energy in a small space and light weight. All over the world, scientists are currently researching a new generation of such batteries with an improved performance. Scientists headed by Maksym Kovalenko from the Laboratory of Inorganic Chemistry at ETH Zurich and Empa have now developed a nanomaterial which enables considerably more power to be stored in lithium ion batteries.
The nanomaterial is composed of tiny tin crystals, which are to be deployed at the minus pole of the batteries (anode). When charging the batteries, lithium ions are absorbed at this electrode; while discharging, they are released again (see box). "The more lithium ions the electrodes can absorb and release -- the better they can breathe, as it were -- the more energy can be stored in a battery," explains Kovalenko.
Uniform crystals
The element tin is ideal for this: every tin atom can absorb at least four lithium ions. However, the challenge is to deal with the volume change of tin electrodes: tin crystal becomes up to three times bigger if it absorbs a lot of lithium ions and shrinks again when it releases them back. The scientists thus resorted to nanotechnology: they produced the tiniest tin nanocrystals and embedded a large number of them in a porous, conductive permeable carbon matrix. Much like how a sponge can suck up water and release it again, an electrode constructed in this way can absorb lithium ions while charging and release them when discharging. If the electrode were made of a compact tin block, this would practically be impossible.
During the development of the nanomaterial, the issue of the ideal size for the nanocrystals arose, which also carries the challenge of producing uniform crystals. "The trick here was to separate the two basic steps in the formation of the crystals -- the formation of as small as a crystal nucleus as possible on the one hand and its subsequent growth on the other," explains Kovalenko. By influencing the time and temperature of the growth phase, the scientists were able to control the size of the crystals. "We are the first to produce such small tin crystals with such precision," says the scientist.
Larger cycle stability
Using uniform tin nanocrystals, carbon, and binding agents, the scientists produced different test electrodes for batteries. "This enables twice as much power to be stored compared to conventional electrodes," says Kovalenko. The size of the nanocrystals did not affect the storage capacity during the initial charging and discharging cycle. After a few charging and discharging cycles, however, differences caused by the crystal size became apparent: batteries with ten-nanometre crystals in the electrodes were able to store considerably more energy than ones with twice the diameter. The scientists assume that the smaller crystals perform better because they can absorb and release lithium ions more effectively. "Ten-nanometre tin crystals thus seem to be just the ticket for lithium ion batteries," says Kovalenko.
As the scientists now know the ideal size for the tin nanocrystals, they would like to turn their attention to the remaining challenges of producing optimum tin electrodes in further research projects. These include the choice of the best possible carbon matrix and binding agent for the electrodes, and the electrodes' ideal microscopic structure. Moreover, an optimal and stable electrolyte liquid in which the lithium ions can travel back and forth between the two poles in the battery also needs to be selected. Ultimately, the production costs are also an issue, which the researchers are looking to reduce by testing which cost-effective base materials are suitable for electrode production. The aim is to prepare batteries with an increased energy storage capacity and lifespan for the market, in collaboration with a Swiss industrial partner.
How lithium ion batteries work
In lithium ion batteries, the energy is stored in the form of positively charged lithium atoms (ions) that are found at the minus pole in a charged battery. If energy is taken from the battery, negatively charged electrons flow from the minus pole to the plus pole via the external circuit. To balance the charge, positively charged lithium ions also flow from the minus pole to the plus pole. However, these travel in the electrolyte fluid inside the battery. The process is reversible: lithium ion batteries can be recharged with electricity. In most lithium ion batteries these days, the plus pole is composed of the transition metal oxides cobalt, nickel, and manganese, the minus pole of graphite. In more powerful lithium ion batteries of the next generation, however, elements such as tin or silicon may well be used at the minus pole.
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The above story is reprinted from materials provided by ETH Zurich. The original article was written by Fabio Bergamin.
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