Vandals spoke with Big Sky, but only about non-football programs

Published: Jul 17, 2012 at 8:57 PM MDT Last Updated: Jul 17, 2012 at 11:06 PM MDT MOSCOW, Idaho (KBOI) - We've been talking about the possibility of the Vandals heading to the Big Sky Conference for months, and the Big Sky has made it clear they'd be interested in adding Idaho.

Athletic Director Rob Spear says the Vandals have spoken with the Big Sky, but before things go any further he wanted to clear things up.

Spear made an announcement on his Twitter account that said, "Despite reports at this point in time the only conversations with the Big Sky have centered around a home for our non football sports."

That shouldn't come as a surprise to Idaho sports fans, as the Vandals have been trying to figure out any way to keep their football program at the FBS level ever since it became clear football was not in the Western Athletic Conference's future.

In conversations with KBOI 2 Sports, the Big Sky Conference Assistant Commissioner of Media Relations Jon Kasper said they'd be open to adding Idaho without their pigskin program, if the Vandals were interested in trying to make it as a football independent.

Source: http://www.kboi2.com/sports/college/Idaho-Vandals-Big-Sky-non-football-programs-162817376.html

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Video: Team uses X-ray imaging to observe running batteries in action

Thursday, July 19, 2012

Most electric cars, from the Tesla Model S to the Nissan Leaf, run on rechargeable lithium-ion batteries ? a pricey technology that accounts for more than half of the vehicle's total cost. One promising alternative is the lithium-sulfur battery, which can theoretically store five times more energy at a much lower cost.

But lithium-sulfur technology has a major drawback: After a few dozen cycles of charging and discharging, the battery stops working.

"The cycle life of lithium-sulfur batteries is very short," said Johanna Nelson, a postdoctoral scholar at the SLAC National Accelerator Laboratory at Stanford University. "Typically, after a few tens of cycles the battery will die, so it isn't viable for electric vehicles, which require many thousands of cycles over a 10- or 20-year lifetime."

A typical lithium-sulfur battery consists of two electrodes ? a lithium metal anode and a sulfur-carbon cathode ? surrounded by a conductive fluid, or electrolyte. Several studies have attributed the battery's short cycle life to chemical reactions that deplete the cathode of sulfur.

But a recent study by Nelson and her colleagues is raising doubts about the validity of previous experiments. Using high-power X-ray imaging of an actual working battery, the Stanford-SLAC team discovered that sulfur particles in the cathode largely remain intact during discharge. Their results, published in the Journal of the American Chemical Society (JACS), could help scientists find new ways to develop commercially viable lithium-sulfur batteries for electric vehicles.

"Based on previous experiments, we expected sulfur particles to completely disappear from the cathode when the battery discharges," said Nelson, the lead author of the JACS study. "Instead, we saw only negligible changes in the size of the particles, the exact opposite of what earlier studies found."

Nelson and her co-workers conducted their experiments at SLAC using two powerful imaging techniques: X-ray diffraction and transmission X-ray microscopy. The X-ray microscope enabled the researchers to take nanosize snapshots of individual sulfur particles before, during and after discharge ? the first real-time imaging of a lithium-sulfur battery in operation.

"The standard way to do high-resolution imaging is with electron microscopes after the battery has partially discharged," Nelson said. "But electrons don't penetrate metal and plastic very well. With SLAC's X-ray microscope, we can actually see changes that are happening while the battery is running."

Pesky polysulfides

In lithium-sulfur batteries, an electric current is generated when lithium ions in the anode react with sulfur particles at the cathode during discharge. The byproducts of this chemical reaction are compounds known as lithium polysulfides.

Problems can arise when the polysulfides leak into the electrolyte and permanently bond with the lithium metal anode. "When that happens, all of the sulfur material in the polysulfides is lost," Nelson said. "It will never recycle. You don't want to lose active sulfur material every time the battery discharges. You want a battery that can be cycled multiple times."

Previous experiments also showed the formation of dilithium sulfide (Li2S) crystals during the discharge phase. "Crystalline Li2S and polysulfides can form a thin film that prevents the conduction of electrons and lithium ions," Nelson said. "The film acts as an insulating layer that can cause the battery to die."

Several studies using electron microscopes produced images of electrodes coated with polysulfides and crystalline Li2S, and cathodes depleted of sulfur. Those images led researchers to conclude that much of the sulfur had been chemically transformed into Li2S-polysulfide sheets that prevented the battery from operating.

Flawed findings

But according to Nelson and her colleagues, some of the previous studies were flawed. "The approach they were using was mistaken," Nelson said. "Typically, they would cycle the battery, disassemble it, wash away the electrolyte and then analyze it with X-ray diffraction or an electron microscope. But when you do that, you also wash away all of the polysulfides that are loosely trapped on the cathode. So when you image the cathode, you don't see any sulfur species at all."

The Stanford-SLAC team took a different approach. Researchers used the transmission X-ray microscope at SLAC to take multiple images of tiny sulfur particles every five minutes while the battery discharged. Each particle was a fraction of the size of a grain of sand. The results were clear: Every particle retained its basic shape and size throughout the discharge cycle.

"We expected the sulfur to completely disappear and form polysulfides in the electrolyte," Nelson said. "Instead we found that, for the most part, the particles stayed where they were and lost very little mass. They did form polysulfides, but most of those were trapped near the carbon-sulfur cathode. We didn't have to disassemble the battery or even stop it, because we could image the sulfur content while the device was operating."

X-ray diffraction yielded an additional surprise. "Based on previous experiments, we expected that crystalline Li2S would form at the end of the discharge cycle," she said. "But we did a very deep discharge and never saw any Li2S in its crystalline state."

Future research

The Stanford-SLAC study could open new avenues of research that could improve the performance of lithium-sulfur batteries, said co-author Michael Toney, head of the Materials Sciences Division at SLAC's Stanford Synchrotron Radiation Lightsource.

"Our study demonstrates the importance of using high-power X-ray technologies to study batteries while they are operating," Toney said. "From an engineering standpoint, it's valuable to know that relying on standard electron microscopy to test the fidelity of materials may give you deceptive results."

Several research labs are looking for new ways to trap polysulfides on the cathode. A variety of techniques have shown promise, including novel electrolytes and carbon nanotubes coated with sulfur.

But the polysulfide problem might not be as daunting as previous studies suggest.

"We found that very few of the polysulfides went into the electrolyte," Nelson said. "The carbon-sulfur cathode actually trapped them better than expected. But even a small amount of polysulfides will cause the battery to fail within 10 cycles. If scientists want to improve the cycle life of the battery, they need to prevent virtually all of the polysulfides from leaking into the electrolyte. If they really want to know what's going on inside the battery, they can't just use standard analysis. They need a technology that tells the whole story."

###

Stanford University: http://news.stanford.edu

Thanks to Stanford University for this article.

This press release was posted to serve as a topic for discussion. Please comment below. We try our best to only post press releases that are associated with peer reviewed scientific literature. Critical discussions of the research are appreciated. If you need help finding a link to the original article, please contact us on twitter or via e-mail.

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Source: http://www.labspaces.net/121832/Video__Team_uses_X_ray_imaging_to_observe_running_batteries_in_action

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Eating Right to Improve your Personal Life | Reference and Education

How to live healthier
The main thing to a healthier you, is to eat right exercise and visit your family doctor regularly. This is all part of a healthier you and if your healthier you will feel better about your self. One of the biggest problems we have today is that most people do not eat right. While the world is wising up, they still fall short of proper eating habits, since we are rushed by a face paced world.?
What do I have to do to eat right?Eating right is a hard thing to do for some of us and for others it is easier to do. Eating healthy is a big problem these days. For some of us it is hard to buy healthier food due to the fact it cost more to fix meals the right way. There are a lot of people that are just making it in the real word with out having to buy a loaf of bread that cost $2.50 a loaf when they can get a loaf for $.50 so what do they do get the $.50 loaf and knowing that its bad for them but that?s all they can afford. So eating right can be hard for you too. We have options. You can grow your own home garden; bake your own bread for a fraction of the cost and so on.?
What are some of the things I can eat?Some of the things you can eat right are vegetables, dairy products, high-protein dishes and so on. You need a certain amount of fat, carbs, etc, which helps to keep you healthy. ?You can get a list from your family doctor or you can go to the library to get information on the basic four food groups. If you cannot afford to eat right then maybe you should not eat as much. In addition, do some excising; excising is always good for you. Exercise will increase your health, even if you cannot afford the four basic groups of nutritious foods. In addition, you have many services available to you, which can offer you food supplies. ?
How do I learn how to eat right?If you want to learn how eat right you can read about it in books from the local library or maybe you will want to talk to your doctor. Your doctor might be able to tell you how to go about doing this and the right way for your body. You cannot just jump in and change everything about you overnight. You have to take time to start and to learn. For some of us that have been eating wrong all of our life, this would be hard to do over night. Then again, others may not have any problems with it. You want to consider your position and move forward.?
Will I feel better if I eat right?You will feel a lot better if you eat right. Eating right has a lot to do with how we feel. If we lack nutrients, it can make one feel depressed, ill, etc. Since, we get vitamins from our foods, you may want to include natural regimens of vitamins in your daily schedule also.?
The right vitamins we need every day to make us feel good about our self. We get many vitamins from what we eat. Vitamins are what make us feel like a person. So if you eat right and get the right vitamins daily that your body needs to function you will feel a lot better about your self and that will help you to improve your personal life.

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Source: http://phrenesia.com/eating-right-to-improve-your-personal-life/

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BoE's King tells how Bob Diamond took a bullet

LONDON (Reuters) - Barclays was in such denial about the scandal over its interest rate manipulation that the Bank chief Mervyn King said he had to tell it that regulators had lost confidence in Bob Diamond as chief executive days before he resigned.

King, governor of the central bank since 2003, dismissed accusations on Tuesday that he was asleep at the helm while Barclays traders tried to skew a benchmark interest rate that underpins transactions worth trillions of dollars worldwide between 2005 and 2009.

He gave an insight into the flurry of meetings and telephone calls that sealed Diamond's fate on the weekend before the July 3 resignation, but dismissed the suggestion from Treasury Select Committee Chairman Andrew Tyrie that his intervention was akin to handing someone a revolver to shoot the Barclays CEO.

"I don't like these firearm analogies, and they are false," King told the parliamentary committee.

After the hearing Tyrie said he was still concerned that there were insufficient checks on the BoE's ability to use "arbitrary pressure" to force out senior bank executives.

King said he had consulted Chancellor George Osborne before informing Barclays that regulators had lost confidence in the bank's executive management, shorthand for Diamond.

"The board of Barclays had been in something of a state of denial about the concerns of the regulators," said King, who appeared composed during his testimony and even smiled at times.

Barclays was fined $453 million last month by U.S. and UK authorities for manipulating the London Interbank Offered Rate (Libor), the short-term interest rate that is supposed to show the price at which major banks are willing to lend to each other.

In testament to the seriousness of the scandal, lawmakers' regular discussion of financial stability with Britain's top financial regulators - including King, his deputy Paul Tucker and Financial Services Authority (FSA) chairman Adair Turner - turned almost entirely into a grilling over Libor.

ERA OF GREED?

U.S.-born Diamond fought to save his career for several days, but swiftly changed tack after the most powerful men in the City of London decided he must go to save Barclays from further turmoil.

Once the darling of the City of London, Diamond's aggressive leadership and 17-million-pound earnings appeared at odds with an era of European austerity, with bankers cast as the villains who staked the world economy for their bonuses.

"All of us involved had built up genuine concern that it is possible to sail close to the wind once. You can sail close twice or maybe even three times," King said.

"But when it gets to four or five times it becomes a regular pattern of behaviour (and you) ... have to ask questions about the navigational skills of the captain."

Osborne said the Libor scandal showed a culture of greed and irresponsibility in the City of London and on Wall Street.

King dismissed accusations that he failed to pick up on the manipulation of Libor, saying he only found out about the malpractice two weeks ago and shooting back at implied criticism from U.S. authorities that London had been too slow to act.

"The first I knew of Libor wrongdoing was when FSA reports came out two weeks ago," King said.

Diamond has apologised for the actions of his traders but has criticised regulators and central banks for failing to heed warnings over Libor.

BOE IN DENIAL?

When questioned over a 2008 email sent by Timothy Geithner, then president of the New York Fed, to King about recommendations to enhance the credibility of Libor, King said the Fed did not raise any evidence of wrongdoing.

In emails released by the Bank, Geithner's proposals, dated May 27, 2008, included a section on how to eliminate the incentive to misreport banks' lending rates.

John Mann, a Labour MP on the Treasury Select Committee, bluntly told King that it appeared he, too, was in denial about the wrongdoing over Libor.

"If it was so obvious and it was all in the newspapers and everyone was talking about it, one might ask the question why everyone didn't say this is wrong?" King replied.

"The reason was because it wasn't wrongdoing; it was in a market that was dysfunctional and not operating in any effective way," King said.

While King appeared confident and composed throughout the three hours of questioning, his deputy Paul Tucker was defensive when pressed on why he did not suspect Libor manipulation in 2008 after a New York Fed note talking about steps to prevent "deliberate misreporting" in Libor.

"It didn't set off dishonesty alarm bells," Tucker said.

Tucker was the favourite to get King's job next year until a 2008 memo from Diamond appeared to suggest that Tucker had condoned the rate-rigging. An earlier hearing brought no evidence of this, though Tucker's prospects to succeed King have still been hurt.

Emails between Tucker and Diamond revealed by Mann during Tuesday's hearing showed the chumminess in the relationship between the regulator and the bank boss.

"Congratulations. Well done, man. I am really, really proud of you," Diamond said in an email after Tucker was promoted to deputy governor in December 2008. Tucker replied: "Thanks so much Bob. You've been an absolute brick through this."

More than a dozen banks are being investigated for their roles in setting Libor, including Citigroup, JPMorgan Chase & Co, Deutsche Bank, HSBC Holdings Plc, UBS and Royal Bank of Scotland.

Morgan Stanley analysts have calculated the litigation risk to each of the 16 banks involved in setting Libor at between $60 million and $1.1 billion.

Libor rates submitted by banks are compiled by Thomson Reuters, parent company of Reuters, on behalf of the British Bankers' Association.

(Writing by Guy Faulconbridge; Additional reporting by David Milliken, Huw Jones and Venetia Rainey, Maria Golovnina; editing by Alex Smith and Will Waterman)

Source: http://news.yahoo.com/boes-king-faces-likely-scrutiny-over-barclays-000629111--business.html

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What earnings reports have revealed about ads

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Source: http://news.yahoo.com/earnings-reports-revealed-ads-230629505.html

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Romney appears in final stages of running-mate decision

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Source: http://news.yahoo.com/romney-appears-final-stages-running-mate-decision-232628141.html

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New tools facilitate matching cancer drugs with gene targets

ScienceDaily (July 16, 2012) ? A new study details how a suite of web-based tools provides the research community with greatly improved capacity to compare data derived from large collections of genomic information against thousands of drugs. By comparing drugs and genetic targets, researchers can more easily identify pharmaceuticals that could be effective against different forms of cancer.

The newly updated software, called CellMiner, was built for use with the NCI-60, one of the most widely utilized collections of cancer cell samples employed in the testing of potential anti-cancer drugs. The tools, available free, provide rapid access to data from 22,379 genes catalogued in the NCI-60 and from 20,503 previously analyzed chemical compounds, including 102 U.S. Food and Drug Administration-approved drugs.

The study, written by the scientists that developed the tools at the National Cancer Institute (NCI), part of the National Institutes of Health, appeared in the July 16, 2012, issue of Cancer Research.

"Previously you would have to hire a bioinformatics team to sort through all of the data, but these tools put the entire database at the fingertips of any researcher," explained Yves Pommier, M.D., Ph.D., of the NCI's Center for Cancer Research. "These tools allow researchers to analyze drug responses as well as make comparisons from drug to drug and gene to gene."

Genomic sequencing and analysis have become increasingly important in biomedicine, but they are yielding data sets so vast that researchers may find it difficult to access and compare them. As new technologies emerge and more data are generated, tools to facilitate the comparative study of genes and potentially promising drugs will be of even greater importance. With the new tools, available at http://discover.nci.nih.gov/cellminer, researchers can compare patterns of drug activity and gene expression, not only to each other but also to other patterns of interest. CellMiner allows the input of large quantities of genomic and drug data, calculates correlations between genes and drug activity profiles, and identifies correlations that are statistically significant. Its data integration capacities are easier, faster, and more flexible than other available methods, and these tools can be adapted for use with other collections of data.

Researchers looking at a particular drug can use the tools to access data from previous experiments done on that drug and analyze how the drug relates to other drugs and various gene profiles. As a case example for this study, the researchers compared drug activity levels and gene expression patterns from previous research to identify an investigational compound, called NSC732298, which is not currently being studied for colon cancer, but could be a potential therapy for the disease based on a CellMiner gene-drug match. In the same exercise, the researchers were able to identify that a second investigational drug that is being tested for colon cancer, called selumetinib, might also be effective against melanoma.

"We're looking forward to seeing how other people are going to use this tool to look at gene co-regulation, regulation of gene expression, and the relationship between gene expression and cancer," said Pommier.

This work was supported by NCI's Center for Cancer Research and Division of Cancer Treatment and Diagnosis under intramural project number ZIA BC 006150.

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The above story is reprinted from materials provided by NIH/National Cancer Institute.

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Journal Reference:

  1. Reinhold WC, Sunshine M, Liu H, Varma S, Kohn KW, Morris J, Doroshow J, and Pommier Y. Web-based genomic and pharmacologic tools for gene and microRNA transcript levels, drug activities, and their pattern comparisons across the NCI-60. Cancer Research, July 16, 2012

Note: If no author is given, the source is cited instead.

Disclaimer: This article is not intended to provide medical advice, diagnosis or treatment. Views expressed here do not necessarily reflect those of ScienceDaily or its staff.

Source: http://www.sciencedaily.com/releases/2012/07/120716090426.htm

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Microsoft All Set To Unveil Office 15

This July 16, you will be treated to a new version of Microsoft's productivity suite, Microsoft Office 15. The suite which is being unveiled in San Francisco has been available to a select group of users since January.

Reports published in the PCWorld?indicate that Windows XP and Windows Vista may not be able to run Office 15. This is in line with the overall organization strategy to discontinue support for Microsoft XP in 2014 and Vista support in 2017.

It is yet to be ascertained if the Monday launch will showcase the beta version or if it will be unveiled in summer. If Microsoft Office 15 runs only on Windows 7 and Windows 8, then many users may not upgrade to the latest version of the productivity suite.

Metro, the main design language for Windows 8 and Windows phone, is tipped to play a major role in the Office 15 build as well. The new version of Office also integrates with Cloud services such as Facebook, Flickr, Hotmail and Skydrive.

Identified as "the most ambitious undertaking yet for the Office Division," by P J Hough, Vice President - Development, Microsoft Office, the program suit is likely to come in bold, basic colors and square edges.

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Details are awaited on how Microsoft will customize the new program suite for tablets, including the iPad. In late 2011, Microsoft released OneNote for the iPad. Also, word is awaited on whether the program suite will feature a touch-only Metro version on Windows 8, the next version of operating system scheduled for release in October.

Source: http://www.ibtimes.com/articles/363113/20120715/microsoft-microsoftoffice15-microsoftprogramsuite-office15-microsoftoffice15launch-microsoftwindows8.htm

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How Barley Protects Against Invasion

Unlike animals, plants do not have a circulating blood system containing cell?capable?of fighting off bacterial invasion. Instead, they have to rely on various other techniques, which I covered in detail way back on my old Field of Science blog. One method they use is to kill off cells that are close to a bacterial or fungi infection in order to starve the oncoming infection and prevent it spreading.

This technique can work very well, killing off approaching pathogens before they cause too much damage and then just growing more leaves or branches to replace the ones left. It?s an?intriguing?technique and so is completely alien to anything a human body would think of doing! I was fascinated the first time I wrote about it, which was why I was particularly interested to?find an article in the latest PLoS Pathogens exploring the death proteins in barley.

A ladybird on barley - image by T. Voekler, credit below

The?proteins?the paper looks at are called R-proteins, short for ?disease resistant proteins?. When the barley recognises an approaching pathogen, such as a mildew fungi, it activates the R-proteins in the cells closest to the fungi. The idea is that faced with a barren landscape of dead cells the fungi will simply die from starvation. From the plant?s point of view the trick is to coordinate these R-proteins, quickly and efficiently killing off the required cells without causing any damage to the rest of the plant.

In barley the?relevant?R-proteins are called the MLA proteins, and numbered 1-10. These proteins can either hang out in the nucleus (where the DNA is) or in the cytoplasm (the rest of the cell) It had been previously shown that a pool of MLA10 in the nucleus was required for resistance against a certain strain of fungi. In this paper the researchers wanted to examine this further. What the found was that while MLA10 in the nucleus was important for disease resistance, it alone was not enough to cause cell-death. In order for the plants cells to successfully die, MLA10 had to be present in the cytoplasm. Not only that but cytoplasmic MLA10 alone was enough to cause cell death.

The structure of the protein domains in MLA10. Each domain has a separate purpose within the protein (pathologists/immunologists might recognise the LRR domain!) Image done by me but copied from the reference

In order to get a better understanding of how MLA10 works, the researchers created various proteins that were fragments of the MLA10, containing different combinations of the domains shown in the diagram above. For example they created a protein that was just the CC domain (the turquoise box), or the CC-NB domain. They then tested for cell-death by using a blue stain. One of the first things they found was that the CC domain is vital for cell death. Using any fragments that did not contain a CC domain completely removed the death response.?They also rather interestingly found that the fragment that produced the strongest death response was the CC-NB fragment. This produced a stronger death than the CC-NB-ARC fragment which suggests that the ARC may have a negative regulatory effect.

To take a closer look at the importance of the CC fragment they created proteins with mutations in the CC part. Each of the 17 mutants had just one amino-acid changed. All except 1 of these mutants decreased the cell-death ability of the protein, some very significantly. The image below is taken from the paper, and shows the areas of the leaves with the different mutations stained for cell-death activity. There?s one strong blue blob for the wild type (labelled CC in the top left) and one other mutant also showing cell-death ability down at the bottom.

Reference below

When they looked at the location of the different fragment mutants, it was found that rather than different fragments locating to different places, the CC-NB fragment was found both in the nucleus and the cytoplasm. This was a little surprising as the LRR section of the protein is the part that carries out the binding to the DNA. However forcing the CC-NB fragment to stay only in the nucleus blocked the death response completely. Forcing it to stay in the cytoplasm increased the death response. The same results were seen with the full length wild-type MLA10.

In order to fit in with earlier research showing high localisation of MLA10 in the nucleus (and to explain what the hell the LRR domain is doing if it?s floating around in the cytoplasm) the researchers propose an integrated model. They suggest that MLA10 in the cytoplasm is needed in order to initiate and amplify the death-signal, while MLA10 in the nucleus helps to trigger further disease resistance. They also imply that looking at ?nuclear localisation? might be a bit simplistic, as responses can differ depending on exactly where in the nucleus the MLA10 hangs out. Around the edges of the nuclear envelope might allow one portion of the MLA10 to maintain sneakily cytoplasmic while the rest is inside the nucleus.

This research builds up a picture of an incredibly sophisticated plant defence system which, while it might not seem as complex as the human immune system, nevertheless depends on organised and structured intracellular behaviour. As the human population keeps expanding finding ways of protecting our crop species against disease, and to maximise the yield of what we can get out of the ground, will become more and more vital.

?

Credit link for T. Voekler

Reference:? Bai S, Liu J, Chang C, Zhang L, Maekawa T, et al. (2012) Structure-Function Analysis of Barley NLR Immune Receptor MLA10 Reveals Its Cell Compartment Specific Activity in Cell Death and Disease Resistance. PLoS Pathog 8(6): e1002752. doi:10.1371/journal.ppat.1002752

Source: http://rss.sciam.com/click.phdo?i=aaf42c80d39883cb1068fc173016fa68

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