JOHANNESBURG (AP) ? Nelson Mandela's grandson says he will contest a court order for him to move the remains of three family members to their original gravesite.
The family feud comes as Mandela, 94, remains in critical condition Sunday in a Pretoria hospital.
The grandson, Mandla Mandela, issued a statement Sunday saying he was compelled to take action against 16 other family members who had pressed the case.
The court orders that the remains of Nelson Mandela's three deceased children should be moved back to the family gravesite in Qunu from the nearby village of Mvezo, according to South Africa's Sunday Times newspaper.
The Mandela family feud over the gravesite is apparently a prelude to a disagreement over where Nelson Mandela's remains will stay.
The Department of Computer Science is proud to congratulate our
students Dor Arad,
Noa Korner
and Mira Shalah, recipients
of the
2013
Anita Borg scholarships, among 39 scholars from Europe, The Middle East and North Africa.
All finalists will receive 7,000 Euro
and will be invited to visit Google?s Engineering Centre in Zurich for a
networking retreat.
Google established the Anita Borg Memorial Scholarship in 2003 to encourage
undergraduate and graduate women completing degrees in computer science and
related fields to excel in computing and technology and become active role
models and leaders in the field.
CAIRO (AP) ? Hundreds of thousands of Egyptians took to the streets Sunday, some in support of Islamist President Mohammed Morsi and others to call for his ouster. Here is a look at Egypt's current political standoff, what it means and where it could lead:
___
WHO IS LEADING THE CAMPAIGN AGAINST MORSI AND HIS MUSLIM BROTHERHOOD?
A new youth movement called Tamarod, or Rebel, is spearheading the latest campaign aimed at forcing Morsi from office. The group launched a petition drive around three months ago to collect signatures from Egyptians who want the president to step down. Tapping into growing discontent with Morsi over what his critics allege is his failure to effectively tackle the country's pressing problems, Tamarod claims it has collected more than 22 million signatures. The petitions have no legal weight and have not been independently authenticated, but the tally would be ? if verified ? nearly twice the number of votes Morsi received a year ago when he narrowly won the presidency. The main collection of opposition groups, the National Salvation Front, has endorsed Tamarod, and parties under the NSF umbrella helped collect signatures.
CAN THE OPPOSITION REALLY FORCE MORSI TO STEP DOWN?
Morsi, who has three years left in his four-year term, says he has no intention of resigning. The Tamarod organizers and opposition figures say protesters will not leave the streets until he does. If both sides stick to their guns, then the standoff could last for days, maybe even weeks. There are other factors at play, however. If the large numbers in Sunday's mass protests are repeated for days, and are later reinforced by strikes and a civil disobedience campaign, the country would grind to a standstill and significantly ratchet up the pressure on Morsi.
Still, the Muslim Brotherhood, the fundamentalist group that propelled Morsi to power, has shown little sign of backing down. The group points to Morsi's election victory in a vote that is widely recognized to have been free and fair, and says that forcing Morsi from office will set a dangerous precedent for his successors, an argument Morsi cited in an interview with The Guardian published on Sunday. The only way to challenge Morsi, his supporters say, is through the ballot box.
WHAT ABOUT THE ARMY?
The army chief, Gen. Abdel-Fattah el-Sissi, called on Morsi and the opposition a week ago to reach an understanding and warned that the military would intervene if the country plunges into civil strife. The remarks were the strongest from the military on the nation's political turmoil since Morsi appointed el-Sissi last August. Since those comments, the army has dispatched reinforcements to bases outside cities across the nation and deployed troops backed by armored vehicles outside vital facilities.
A secretive institution by nature, the army has not tipped its hand on Egypt's current political standoff. It is considered unlikely that the military will stage a coup to depose Morsi. One possible scenario, however, could see troops coming to the defense of opposition protesters if violence breaks out. Such a move would provide a boost to the anti-Morsi camp and likely embolden many more Egyptians to take to the streets confident they would be protected by the military.
On the other hand, the military may see the wave of mass protests as a golden opportunity to get rid of Morsi and the Brotherhood. El-Sissi has not publicly clashed with Morsi, although there have been signs of tension between the two powerful institutions they represent. Some observers say the army has never been comfortable with the president's close ties with Hamas, the Brotherhood's Palestinian chapter that the military has long seen as a threat to stability in Egypt's Sinai Peninsula that borders Israel and the Hamas-ruled Gaza Strip.
Intervening would likely leave the military effectively in charge of the country again, much as it was after the 2011 uprising that toppled Hosni Mubarak. The military has been sharply criticized for its record running the country over that nearly 17-month period. Critics have blamed it for mismanaging the transition, and accuse it of committing large scale human rights violations, including torturing detainees and conducting virginity tests on women protesters.
WHAT IF THE MILITARY DOES NOT INTERVENE, MORSI REFUSES TO LEAVE OFFICE AND PROTESTS CONTINUE?
The hundreds of thousands who have taken to the streets on Sunday chanting "leave!" have dealt a serious blow to Morsi's claim of holding a popular mandate, and it is difficult to see him riding this out without it taking a toll on his authority. The path Morsi chooses, however, may be heavily influenced by his experience as a longtime member of the Muslim Brotherhood, a secretive group that spent much of the more than 80 years since its creation underground to avoid government crackdowns. The Brotherhood waited eight decades to rule Egypt, and the prospect of relinquishing power now that they have it after so many years of persecution ? including the execution of some of its most revered leaders ? clearly isn't something the group relishes. Already, Morsi and his Brotherhood supporters have allowed radical Islamist groups with a violent past to take the lead in the campaign to defend the president. They have publicly spoken about "wiping" the protesters and routinely refer to them as "infidels" or paid Mubarak loyalists. But it would be a very risky gamble to unleash them on the opposition, a course of action that could drive Egypt to the brink of civil war, as many have already warned.
But there is the potential for violence on the opposition side as well, particularly if the protests drag on and Morsi holds his ground. Some anti-government protests in the past have devolved into clashes. Over just the past week, anti-Morsi protesters have stormed and ransacked several offices of the Muslim Brotherhood and its political arm, the Freedom and Justice party, while clashes in a string of Nile Delta cities and the coastal port city of Alexandria killed at least seven people and wounded hundreds.
IS THERE ROOM FOR COMPROMISE?
So far, neither side appears willing to make concessions. Tamarod and the opposition parties insist that early presidential elections are their bottom line. Morsi has insisted, most recently in an interview published Sunday, that he will not step down.
Raising girls in the Middle East is not for the faint of heart. That was the consensus yesterday of three extraordinary women whose fearless commitment to empowering and educating girls in Afghanistan, Pakistan, and Yemen has inspired millions across the globe and brought them to speak at this year's Aspen Ideas Festival.
Shabana Basij-Rasikh, Nadia Al-Sakkaf, and Farahnaz Ispahani are social innovators who, despite incredible risks, continue to work tirelessly to advance the proposition that education for girls matters and that neither bombs nor bullets will keep them from sending girls to school.
But the risks for girls who don't receive education are even higher -- without education girls in so many countries are sucked into an enduring cycle of poverty, forced marriage, violence, and are never given their rightful place in their respective societies.
On the other hand, the critical link between education and economic development, health, and social mobility is crystal clear. A woman who receives an education will bring in more money for her family and for her community, she will raise healthier children, and she will have far greater social mobility. Investing in girls delivers a proven return on investment.
While that link is painfully clear, there are plenty of challenges in Muslim majority countries that inhibit girls' education, cutting the economic potential for them, their families, their communities, and their countries.
I sat down with Shabana, Nadia, and Farahnaz to discuss these challenges and the opportunities that exist to overcome them. The big takeaways of our conversation were the following:
Education needs to be approached from an inclusive perspective -- winning the support of the men in these girls' lives is critical. Whether they are fathers, brothers, or husbands, men can help stand up to social pressure, if it exists, against educating women. Shabana shared an incredible story of a girl whose father proudly defied the Taliban, ready to sacrifice his life, in order to send his daughter back to school in Kabul.
The legal framework guaranteeing education for girls is indispensible. From the perspective of a Pakistani parliamentarian, Farahnaz spoke passionately about the importance of building the legal framework for universal access to education. Hard-fought gains are far more secure when the law is on their side.
Content matters. Access to education is invaluable, but it is the content of that education that will determine whether it creates strong and knowledgeable women. As Editor-in-Chief of the Yemen Times, Nadia knows the value of producing honest content. She also underscored the challenge facing Yemen in reforming curriculum to foster creativity and encourage even-handed thinking on political, religious, and cultural issues facing Yemen and the Arab world.
Culture is not a monolith. It's a common refrain that the 'culture' in Muslim-majority countries is hostile to educating young girls. That's an analytical crutch that encourages unproductive thinking. In reality, the barriers are far more complicated than 'culture.' History, family, socio-economic status, access, parental education, and misconceptions all play a role in determining whether a girl will receive an education.
While studying these issues and speaking to these visionary young women, I couldn't help but reflect on the prescient Arab Human Development Report, published in 2002 by UNDP. It listed the barriers to development in the Arab world as stemming principally from three deficits: freedom, empowerment of women, and knowledge.
These deficits are the underpinnings for the transformational change that we are seeing across the region. And, the historical disempowerment of women in the Middle East positions them to play an even more important role as change agents and stakeholders in their respective societies. Education is a fundamental part of women's empowerment -- without it, women will not be stakeholders in their respective societies.
Shabana, Nadia, and Farahnaz embody the effort to drive development through women's empowerment and education. They are the change agents. Their voices are being heard, they are reclaiming their place, and they will not retreat. As brave as they are, however, they can't do it alone, so let's help to share their big Idea.
COLLEGE STATION -- Scientists using sophisticated imaging techniques have observed a molecular protein folding process that may help medical researchers understand and treat diseases such as Alzheimer's, Lou Gehrig's and cancer.
The study, reported this month in the journal Cell, verifies a process that scientists knew existed but with a mechanism they had never been able to observe, according to Dr. Hays Rye, Texas A&M AgriLife Research biochemist.
"This is a step in the direction of understanding how to modulate systems to prevent diseases like Alzheimer's. We needed to understand the cell's folding machines and how they interact with each other in a complicated network," said Rye, who also is associate professor of biochemistry and biophysics at Texas A&M.
Rye explained that individual amino acids get linked together like beads on a string as a protein is made in the cell.
"But that linear sequence of amino acids is not functional," he explained. "It's like an origami structure that has to fold up into a three-dimensional shape to do what it has to do."
Rye said researchers have been trying to understand this process for more than 50 years, but in a living cell the process is complicated by the presence of many proteins in a concentrated environment.
"The constraints on getting that protein to fold up into a good 'origami' structure are a lot more demanding," he said. "So, there are special protein machines, known as molecular chaperones, in the cell that help proteins fold."
But how the molecular chaperones help protein fold when it isn't folding well by itself has been the nagging question for researchers.
"Molecular chaperones are like little machines, because they have levers and gears and power sources. They go through turning over cycles and just sort of buzz along inside a cell, driving a protein folding reaction every few seconds," Rye said.
The many chemical reactions that are essential to life rely on the exact three-dimensional shape of folded proteins, he said. In the cell, enzymes, for example, are specialized proteins that help speed biological processes along by binding molecules and bringing them together in just the right way.
"They are bound together like a three-dimensional jigsaw puzzle," Rye explained. "And the proteins -- those little beads on the string that are designed to fold up like origami -- are folded to position all these beads in three-dimensional space to perfectly wrap around those molecules and do those chemical reactions.
"If that doesn't happen -- if the protein doesn't get folded up right -- the chemical reaction can't be done. And if it's essential, the cell dies because it can't convert food into power needed to build the other structures in the cell that are needed. Chemical reactions are the structural underpinning of how cells are put together, and all of that depends on the proteins being folded in the right way."
When a protein doesn't fold or folds incorrectly it turns into an "aggregate," which Rye described as "white goo that looks kind of like a mayonnaise, like crud in the test tube.
"You're dead; the cell dies," he said.
Over the past 20 years, he said, researchers have linked that aggregation process "pretty convincingly" to the development of diseases -- Alzheimer's disease, Lou Gehrig's disease, Huntington's disease, to name a few. There's evidence that diabetes and cancer also are linked to protein folding disorders.
"One of the main roles for the molecular chaperones is preventing those protein misfolding events that lead to aggregation and not letting a cell get poisoned by badly folded or aggregated proteins," he said.
Rye's team focused on a key molecular chaperone -- the HSP60.
"They're called HSP for 'heat shock protein' because when the cell is stressed with heat, the proteins get unstable and start to fall apart and unfold," Rye said. "The cell is built to respond by making more of the chaperones to try and fix the problem.
"This particular chaperone takes unfolded protein and goes through a chemical reaction to bind the unfolded protein and literally puts it inside a little 'box,'" Rye said.
He added that the mystery had long been how the folding worked because, while researchers could see evidence of that happening, no one had ever seen precisely how it happened.
Rye and the team zeroed in on a chemically modified mutant that in other experiments had seemed to stall at an important step in the process that the "machine" goes through to start the folding action. This clued the researchers that this stalling might make it easier to watch.
They then used cryo-electron microscopy to capture hundreds of thousands of images of the process at very high resolutions which allowed them to reconstruct from two-dimensional flat images a three-dimensional model. A highly sophisticated computer algorithm aligns the images and classifies them in subcategories.
"If you have enough of them you can actually reconstruct and view a structure as a three-dimensional model," Rye said.
What the team saw was this: The HSP60 chaperone is designed to recognize proteins that are not folded from the ones that are. It binds them and then has a separate co-chaperone that puts a "lid" on top of the box to keep the folding intermediate in the box. They could see the box move, and parts of the molecule moved to peel the chaperone box away from the bound protein or "gift" in the box. But the bound protein was kept inside the package where it could then initiate a folding reaction. They saw tiny tentacles, "like a little octopus in the bottom of the box rising up and grabbing hold of the substrate protein and helping hold it inside the cavity."
"The first thing we saw was a large amount of an unfolded protein inside of this cavity," he said. "Even though we knew from lots and lots of other studies that it had to go in there, nobody had ever seen it like this before. We can also see the non-native protein interacting with parts of the box that no one had ever seen before. It was exciting to see all of this for the first time. I think we got a glimpse of a protein in the process of folding, which we actually can compare to other structures."
"By understanding the mechanism of these machines, the hope is that one of the things we can learn to do is turn them up or turn them off when we need to, like for a patient who has one of the protein folding diseases," he said.
Rye collaborated on the research with Dong-Hua Chen and Wah Chiu at the Baylor College of Medicine in Houston, Damian Madan and Zohn Lin at Princeton University, Jeremy Weaver at Texas A&M and Gunnar Schrder at the Institute of Complex Systems in Germany.
###
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Scientists view 'protein origami' to help understand, prevent certain diseasesPublic release date: 28-Jun-2013 [ | E-mail | Share ]
COLLEGE STATION -- Scientists using sophisticated imaging techniques have observed a molecular protein folding process that may help medical researchers understand and treat diseases such as Alzheimer's, Lou Gehrig's and cancer.
The study, reported this month in the journal Cell, verifies a process that scientists knew existed but with a mechanism they had never been able to observe, according to Dr. Hays Rye, Texas A&M AgriLife Research biochemist.
"This is a step in the direction of understanding how to modulate systems to prevent diseases like Alzheimer's. We needed to understand the cell's folding machines and how they interact with each other in a complicated network," said Rye, who also is associate professor of biochemistry and biophysics at Texas A&M.
Rye explained that individual amino acids get linked together like beads on a string as a protein is made in the cell.
"But that linear sequence of amino acids is not functional," he explained. "It's like an origami structure that has to fold up into a three-dimensional shape to do what it has to do."
Rye said researchers have been trying to understand this process for more than 50 years, but in a living cell the process is complicated by the presence of many proteins in a concentrated environment.
"The constraints on getting that protein to fold up into a good 'origami' structure are a lot more demanding," he said. "So, there are special protein machines, known as molecular chaperones, in the cell that help proteins fold."
But how the molecular chaperones help protein fold when it isn't folding well by itself has been the nagging question for researchers.
"Molecular chaperones are like little machines, because they have levers and gears and power sources. They go through turning over cycles and just sort of buzz along inside a cell, driving a protein folding reaction every few seconds," Rye said.
The many chemical reactions that are essential to life rely on the exact three-dimensional shape of folded proteins, he said. In the cell, enzymes, for example, are specialized proteins that help speed biological processes along by binding molecules and bringing them together in just the right way.
"They are bound together like a three-dimensional jigsaw puzzle," Rye explained. "And the proteins -- those little beads on the string that are designed to fold up like origami -- are folded to position all these beads in three-dimensional space to perfectly wrap around those molecules and do those chemical reactions.
"If that doesn't happen -- if the protein doesn't get folded up right -- the chemical reaction can't be done. And if it's essential, the cell dies because it can't convert food into power needed to build the other structures in the cell that are needed. Chemical reactions are the structural underpinning of how cells are put together, and all of that depends on the proteins being folded in the right way."
When a protein doesn't fold or folds incorrectly it turns into an "aggregate," which Rye described as "white goo that looks kind of like a mayonnaise, like crud in the test tube.
"You're dead; the cell dies," he said.
Over the past 20 years, he said, researchers have linked that aggregation process "pretty convincingly" to the development of diseases -- Alzheimer's disease, Lou Gehrig's disease, Huntington's disease, to name a few. There's evidence that diabetes and cancer also are linked to protein folding disorders.
"One of the main roles for the molecular chaperones is preventing those protein misfolding events that lead to aggregation and not letting a cell get poisoned by badly folded or aggregated proteins," he said.
Rye's team focused on a key molecular chaperone -- the HSP60.
"They're called HSP for 'heat shock protein' because when the cell is stressed with heat, the proteins get unstable and start to fall apart and unfold," Rye said. "The cell is built to respond by making more of the chaperones to try and fix the problem.
"This particular chaperone takes unfolded protein and goes through a chemical reaction to bind the unfolded protein and literally puts it inside a little 'box,'" Rye said.
He added that the mystery had long been how the folding worked because, while researchers could see evidence of that happening, no one had ever seen precisely how it happened.
Rye and the team zeroed in on a chemically modified mutant that in other experiments had seemed to stall at an important step in the process that the "machine" goes through to start the folding action. This clued the researchers that this stalling might make it easier to watch.
They then used cryo-electron microscopy to capture hundreds of thousands of images of the process at very high resolutions which allowed them to reconstruct from two-dimensional flat images a three-dimensional model. A highly sophisticated computer algorithm aligns the images and classifies them in subcategories.
"If you have enough of them you can actually reconstruct and view a structure as a three-dimensional model," Rye said.
What the team saw was this: The HSP60 chaperone is designed to recognize proteins that are not folded from the ones that are. It binds them and then has a separate co-chaperone that puts a "lid" on top of the box to keep the folding intermediate in the box. They could see the box move, and parts of the molecule moved to peel the chaperone box away from the bound protein or "gift" in the box. But the bound protein was kept inside the package where it could then initiate a folding reaction. They saw tiny tentacles, "like a little octopus in the bottom of the box rising up and grabbing hold of the substrate protein and helping hold it inside the cavity."
"The first thing we saw was a large amount of an unfolded protein inside of this cavity," he said. "Even though we knew from lots and lots of other studies that it had to go in there, nobody had ever seen it like this before. We can also see the non-native protein interacting with parts of the box that no one had ever seen before. It was exciting to see all of this for the first time. I think we got a glimpse of a protein in the process of folding, which we actually can compare to other structures."
"By understanding the mechanism of these machines, the hope is that one of the things we can learn to do is turn them up or turn them off when we need to, like for a patient who has one of the protein folding diseases," he said.
Rye collaborated on the research with Dong-Hua Chen and Wah Chiu at the Baylor College of Medicine in Houston, Damian Madan and Zohn Lin at Princeton University, Jeremy Weaver at Texas A&M and Gunnar Schrder at the Institute of Complex Systems in Germany.
###
[ | 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.
Being a Netflix subscriber is almost like being cursed -- sure, you have access to untold troves of streaming TV shows and films, but how do you choose what to watch? The burden of choice weighs heavily on the indecisive Netflix user, trapping them in a labyrinth of enticing categories, familiar recommendations and episode backlogs. Admit it, you don't know jack about picking out a good flick, which is exactly why Netflix created Max, a comedic recommendation engine that gamifies movie night with quick choices, mini games and quirky humor.
Netflix Vice President of Product Innovation Todd Yellin caught up with us at E3 earlier this month to give us a brief demo of the upcoming feature. Yellin parked us in front of a PS3 to demonstrate, pointing out that our screen's topmost category had been replaced by a larger banner. "My mother wanted me to be a lawyer," the Play Max prompt reads. "But my dream is to help you find great stuff to watch." Quirky. Yellin tells us that this is one of several boiler plates the streaming menu provides to lure users into trying Max. A cheeky button beneath the dialogue encourage us to "live our dreams" and give the content recommendation game a spin. Sure, why not?
The Department of Computer Science is proud to congratulate our
students Dor Arad,
Noa Korner
and Mira Shalah, recipients
of the
2013
Anita Borg scholarships![[ Back to EurekAlert! ]](http://www.eurekalert.org/images/back2e.gif){kind=small}
Public release date: 28-Jun-2013
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