Hauppauge is taking its considerable video-recording prowess mobile with the HD PVR Rocket. Its 4.3-ounce frame is smaller than the HD PVR 2's and instead of using a computer to store recorded video, it uses USB media. The company estimates that you'll fill a 16GB thumb drive with about four hours ...
Apple seems to be promoting its built-in software within iOS App Store search results. Search terms such as "browser", "SMS", or "messages" will yield a card showing one of Apple's built-in apps as the first result, with a link at the bottom of the card that will take you to Apple's web page about the feature. Frederico Viticci of MacStories:
This morning, I noticed a tweet by Lukas Burgstaller with a screenshot of Apple’s Safari browser showing up in App Store search results for the “browser” search query. I did some tests, and I’ve discovered other search results advertising built-in iOS system apps and features with banners and links to open an app or read more information about it. I’m not sure when Apple started displaying their own built-in apps in the App Store search results, but it’s an interesting (and, I believe, good) idea worth discussing.
Viticci does note, however, that this could push developers and third party apps further down the search chain, and if Apple starts taking over too much of the results, could cause them problems. Check out his article for the full story and let me know what you think.
Source: MacStories
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Just when we thought we'd seen every musical incarnation of our favorite Disney characters imaginable comes the latest production from the creative brain of Todrick Hall. (Have you see the former American Idol contestant/YouTube hit-maker's take on Cinderella?!) Hall has been known for his lavish videos in the past, but now he is taking on his biggest challenge yet: Disney's villains!
Source: http://www.ivillage.com/video-disney-villains-get-their-spell-block-tango-revenge-chicago-spoof/1-a-551364?dst=iv%3AiVillage%3Avideo-disney-villains-get-their-spell-block-tango-revenge-chicago-spoof-551364
In the months since information about the NSA's bulk surveillance efforts began to leak, many of the tech companies named in documents have been unable to even discuss their involvement. Those blinds have been pried back a little with the release of a few transparency reports, but today Google, ...![[ Back to EurekAlert! ]](http://www.eurekalert.org/images/back2e.gif){kind=small}
PUBLIC RELEASE DATE: 31-Oct-2013
ShareContact: Ryouhei Nishigaya
rnishiga@hosp.ncgm.go.jp
Public Library of Science
Malaria is one of the major infectious diseases transmitted by mosquitos, with enormous impact on quality of life. According to World Health Organization figures, as of 2010 there were over 219 million reported cases of malaria with an estimated 660,000 deaths. Plasmodium vivax, which is the second most prevalent species of the human malaria parasite, is widely distributed around the world especially in Asia, Melanesia, the Middle East, South and Central America. 2.85 billion people worldwide live at risk of the infection in 2009.
Vivax malaria was once endemic in Japan including the mainland (Honshu) and the northern island (Hokkaido), but it has been eliminated from these areas as of 1959. In the same way as Japan, the Republic of Korea (South Korea) is another country where vivax malaria had been successfully eliminated by the late 1970s. However, re-emergence of vivax malaria in South Korea was reported in 1993. The first patient was a South Korean soldier who served in the demilitarized zone (a border region between South and North Korea) and had never been abroad. In spite of continuous malaria control measures implemented by the South Korean government, there was a steady increase in the number of reported vivax malaria cases until 2000 (4,183 cases), then a gradual decrease until 2004 (864 cases), when the number of infected civilians who lived in or near the area increased gradually. The number of reported cases fluctuated between 838 and 2,227 per year from 2005 to 2011.
Similarities in the ecology (i.e., climate, vegetation, species of mosquito vector) of Japan and South Korea mean that the Japanese environment is particularly suited to the establishment of Korean strains of vivax malaria. For example, the main vector species of vivax malaria in South Korea is Anopheles sinensis, which in the past has also been the main vector species of vivax malaria in the mainland of Japan, and which remains distributed throughout Japan. In addition, mosquitoes on the mainland of Japan are highly prevalent from June to September (the rainy season and the summer season), which is the same period in which vivax malaria is most prevalent in South Korea.
For these reasons, it is very important not only for South Korea, but also for Japan, to understand the characteristics of vivax malaria in South Korea and to provide a possible explanation as to why, in spite of a continuous malaria control program spanning two decades, efforts to eliminate vivax malaria have been unsuccessful. To answer this question, Dr. Moritoshi Iwagami, et al. conducted a 15-year-long longitudinal study on P. vivax population genetics in South Korea using highly polymorphic neutral markers of the parasites.
The team of researchers from the Japanese National Center for Global Health and Medicine, Inje University and the University of Tokyo analyzed 163 South Korean P. vivax isolates collected from South Korean soldiers who served in the demilitarized zone from 1994 to 2008, using 14 microsatellite DNA loci of the parasite genome. Based on this data, they performed population genetic analysis, with a focus on the differences of the parasite populations between successive years. Through this, they aimed to provide a detailed and precise estimate of the characteristics of the vivax malaria population structure and the temporal dynamics of its transmission.
Their population genetic analyses show that two genotypes coexisted from 1994 to 2001, while three different genotypes coexisted from 2002 to 2008. This result suggested that a drastic genetic change occurred in the South Korean population during 2002 and 2003.
This data suggests that vivax parasites were introduced from another population, most probably from North Korea, especially during 2002 and 2003, and explains why South Korea was not able to eliminate vivax malaria for 20 years. The finding is an example that malaria parasites were transmitted by Anopheles mosquitos between two countries where traveling is basically prohibited. This evidence demonstrates the difficulty of malaria elimination by one country and the need for collaboration between two (or more) adjacent countries for effective malaria elimination.
In the (near) future, a distribution of Anopheles mosquitoes might expand in Japan due to global warming or climate change. Should a certain numbers of vivax malaria patients (and/or carriers of vivax malaria hypnozoites) come to Japan from South Korea and stay in or near A. sinensis breeding sites during summer season, indigenous vivax malaria transmission might occur by locally infected mosquitoes in Japan. Therefore, careful monitoring of all travelers coming from endemic areas of South Korea is required, as is collaboration between both nations in order to prevent the introduction of the malaria parasite into Japan.
###
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: 31-Oct-2013
ShareContact: Ryouhei Nishigaya
rnishiga@hosp.ncgm.go.jp
Public Library of Science
Malaria is one of the major infectious diseases transmitted by mosquitos, with enormous impact on quality of life. According to World Health Organization figures, as of 2010 there were over 219 million reported cases of malaria with an estimated 660,000 deaths. Plasmodium vivax, which is the second most prevalent species of the human malaria parasite, is widely distributed around the world especially in Asia, Melanesia, the Middle East, South and Central America. 2.85 billion people worldwide live at risk of the infection in 2009.
Vivax malaria was once endemic in Japan including the mainland (Honshu) and the northern island (Hokkaido), but it has been eliminated from these areas as of 1959. In the same way as Japan, the Republic of Korea (South Korea) is another country where vivax malaria had been successfully eliminated by the late 1970s. However, re-emergence of vivax malaria in South Korea was reported in 1993. The first patient was a South Korean soldier who served in the demilitarized zone (a border region between South and North Korea) and had never been abroad. In spite of continuous malaria control measures implemented by the South Korean government, there was a steady increase in the number of reported vivax malaria cases until 2000 (4,183 cases), then a gradual decrease until 2004 (864 cases), when the number of infected civilians who lived in or near the area increased gradually. The number of reported cases fluctuated between 838 and 2,227 per year from 2005 to 2011.
Similarities in the ecology (i.e., climate, vegetation, species of mosquito vector) of Japan and South Korea mean that the Japanese environment is particularly suited to the establishment of Korean strains of vivax malaria. For example, the main vector species of vivax malaria in South Korea is Anopheles sinensis, which in the past has also been the main vector species of vivax malaria in the mainland of Japan, and which remains distributed throughout Japan. In addition, mosquitoes on the mainland of Japan are highly prevalent from June to September (the rainy season and the summer season), which is the same period in which vivax malaria is most prevalent in South Korea.
For these reasons, it is very important not only for South Korea, but also for Japan, to understand the characteristics of vivax malaria in South Korea and to provide a possible explanation as to why, in spite of a continuous malaria control program spanning two decades, efforts to eliminate vivax malaria have been unsuccessful. To answer this question, Dr. Moritoshi Iwagami, et al. conducted a 15-year-long longitudinal study on P. vivax population genetics in South Korea using highly polymorphic neutral markers of the parasites.
The team of researchers from the Japanese National Center for Global Health and Medicine, Inje University and the University of Tokyo analyzed 163 South Korean P. vivax isolates collected from South Korean soldiers who served in the demilitarized zone from 1994 to 2008, using 14 microsatellite DNA loci of the parasite genome. Based on this data, they performed population genetic analysis, with a focus on the differences of the parasite populations between successive years. Through this, they aimed to provide a detailed and precise estimate of the characteristics of the vivax malaria population structure and the temporal dynamics of its transmission.
Their population genetic analyses show that two genotypes coexisted from 1994 to 2001, while three different genotypes coexisted from 2002 to 2008. This result suggested that a drastic genetic change occurred in the South Korean population during 2002 and 2003.
This data suggests that vivax parasites were introduced from another population, most probably from North Korea, especially during 2002 and 2003, and explains why South Korea was not able to eliminate vivax malaria for 20 years. The finding is an example that malaria parasites were transmitted by Anopheles mosquitos between two countries where traveling is basically prohibited. This evidence demonstrates the difficulty of malaria elimination by one country and the need for collaboration between two (or more) adjacent countries for effective malaria elimination.
In the (near) future, a distribution of Anopheles mosquitoes might expand in Japan due to global warming or climate change. Should a certain numbers of vivax malaria patients (and/or carriers of vivax malaria hypnozoites) come to Japan from South Korea and stay in or near A. sinensis breeding sites during summer season, indigenous vivax malaria transmission might occur by locally infected mosquitoes in Japan. Therefore, careful monitoring of all travelers coming from endemic areas of South Korea is required, as is collaboration between both nations in order to prevent the introduction of the malaria parasite into Japan.
###
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: 31-Oct-2013
ShareContact: Sarah Smith
sas2072@med.cornell.edu
646-317-7401
Weill Cornell Medical College
NEW YORK (October 31, 2013) -- Collaborating scientists at The Scripps Research Institute (TSRI) and Weill Cornell Medical College have determined the first atomic-level structure of the tripartite HIV envelope protein -- long considered one of the most difficult targets in structural biology and of great value for medical science.
The new data provide the most detailed picture yet of the AIDS-causing virus's complex envelope, including sites that future vaccines will try to mimic to elicit a protective immune response.
"Most of the prior structural studies of this envelope complex focused on individual subunits, but we've needed the structure of the full complex to properly define the sites of vulnerability that could be targeted, for example with a vaccine," said Dr. Ian A. Wilson, the Hansen Professor of Structural Biology at TSRI and a senior author of the new research with biologists Drs. Andrew Ward and Bridget Carragher of TSRI and virologist and immunologist Dr. John Moore of Weill Cornell.
The findings were published in two papers in Science Express, the early online edition of the journal Science, on October 31, 2013.
A Difficult Target
HIV, the human immunodeficiency virus, infects about 34 million people globally, 10 percent of whom are children, according to World Health Organization estimates. Although antiviral drugs are now used to manage many HIV infections, especially in developed countries, scientists have long sought a vaccine that can prevent new infections and would help perhaps to ultimately eradicate the virus from the human population.
However, none of the HIV vaccines tested so far has come close to providing adequate protection. This failure is due largely to the challenges posed by HIV's envelope protein, known to virologists as Env.
HIV's Env is not a single, simple protein but rather a "trimer" made of three identical, loosely connected structures with a stalk-like subunit, gp41, and a cap-like region, gp120. Each trimer resembles a mushroom and about 15 of these Env trimers sprout from the membrane of a typical virus particle, ready to latch onto susceptible human cells and facilitate viral entry.
Although Env in principle is exposed to the immune system, in practice it has evolved highly effective strategies for evading immune attack. It frequently mutates its outermost "variable loop" regions, for example, and also coats its surfaces with hard-to-grip sugar molecules called glycans.
Even so, HIV vaccine designers might have succeeded by now had they been able to study the structure of the entire Env protein at atomic-scale--in particular, to fully characterize the sites where the most effective virus-neutralizing antibodies bind. But Env's structure is so complex and delicate that scientists have had great difficulty obtaining the protein in a form that is suitable for atomic-resolution imaging.
"It tends to fall apart, for example, even when it's on the surface of the virus, so to study it we have to engineer it to be more stable," said Dr. Ward, who is an assistant professor in TSRI's Department of Integrative Structural and Computational Biology.
The key goal in this area has been to engineer a version of the Env trimer that has the stability and other properties needed for atomic-resolution imaging, yet retains virtually all of the complex structural characteristics of native Env.
Imaging Env
After many years in pursuit of this goal, Drs. Moore, Rogier W. Sanders and their colleagues at Weill Cornell, working with Drs. Wilson, Ward and others at TSRI, recently managed to produce a version of the Env trimer (called BG505 SOSIP.664 gp140) that is suitable for atomic-level imaging work--and includes all of the trimer structure that normally sits outside the viral membrane. The TSRI researchers then evaluated the new Env trimer using advanced versions of two imaging methods, X-ray crystallography and electron microscopy. The X-ray crystallography study was the first ever of an Env trimer, and both methods resolved the trimer structure to a finer level of detail than has been reported before.
"The new data are consistent with the findings on Env subunits over the last 15 years, but also have enabled us to explain many prior observations about HIV in structural terms for the first time," said Dr. Jean-Philippe Julien, a senior research associate in the Wilson laboratory at TSRI, who was first author of the X-ray crystallography study.
The data illuminated the complex process by which the Env trimer assembles and later undergoes radical shape changes during infection and clarified how it compares to envelope proteins on other dangerous viruses, such as flu and Ebola.
Arguably the most important implications of the new findings are for HIV vaccine design. In both of the new studies, Env trimers were imaged while bound to broadly neutralizing antibodies against HIV. Such antibodies, isolated from naturally infected patients, are the very rare ones that somehow bind to Env in a way that blocks the infectivity of a high proportion of HIV strains.
Ideally an HIV vaccine would elicit large numbers of such antibodies from patients, and to achieve that, vaccine designers would like to know the precise structural details of the sites where these antibodies bind to the virus--so that they can mimic those viral "epitopes" with the vaccine.
"It's been a privilege for us to work with the Scripps' team on this project," said Dr. Moore, a professor of microbiology and immunology at Weill Cornell. "Now we all need to harness this new knowledge to design and test next-generation trimers and see if we can induce the broadly active neutralizing antibodies that an effective vaccine is going to need."
"One surprise from this study was the revelation of the complexity and the relative inaccessibility of these neutralizing epitopes," Dr. Julien added. "It helps to know this for future vaccine design, but it also makes it clear why previous structure-based HIV vaccines have had so little success."
"We found that these neutralizing epitopes encompass features such as the variable loop regions and glycans that were excluded from previous studies of individual Env subunits," said Dmitry Lyumkis, first author of the electron microscopy study, who is a graduate student at TSRI participating in the NIH-funded National Resource for Automated Molecular Microscopy. "We observed, too, that neutralizing antibody binding to gp120 can be influenced by the neighboring gp120 structure within the trimer--another complication that was not apparent when we were not studying the whole trimer."
Having provided these valuable structural insights, the new Env trimer is now being put to work in vaccine development. "We and others are already injecting the trimer into animals to elicit antibodies," Dr. Ward said. "We can look at the antibodies that are generated and if necessary modify the Env trimer structure and try again. In this iterative way, we aim to refine and increase the antibody response in the animals and eventually, humans."
###
Other contributors to the studies, "Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 Env trimer," and "Crystal structure of a soluble cleaved HIV-1 envelope trimer in complex with a glycan-dependent broadly neutralizing antibody," included TSRI's Natalia de Val, Devin Sok, Drs. Robyn L. Stanfield and Marc C. Deller; and Weill Cornell Medical College's Albert Cupo and Dr. Per-Johan Klasse. In addition to Drs. Wilson, Ward and Carragher, senior participants at TSRI included Drs. Clinton S. Potter and Dennis Burton.
The research was supported in part by the National Institutes of Health (HIVRAD P01 AI82362, R01 AI36082, R01 AI084817, R37 AI36082, R01 AI33292), the NIH's National Institute of General Medical Sciences (GM103310) and the International AIDS Vaccine Initiative Neutralizing Antibody Consortium. IAVI has filed a patent that includes WCMC and TSRI authors on the development of the BG505 SOSIP.664 trimers as vaccine antigens.
Weill Cornell Medical College
Weill Cornell Medical College, Cornell University's medical school located in New York City, is committed to excellence in research, teaching, patient care and the advancement of the art and science of medicine, locally, nationally and globally. Physicians and scientists of Weill Cornell Medical College are engaged in cutting-edge research from bench to bedside, aimed at unlocking mysteries of the human body in health and sickness and toward developing new treatments and prevention strategies. In its commitment to global health and education, Weill Cornell has a strong presence in places such as Qatar, Tanzania, Haiti, Brazil, Austria and Turkey. Through the historic Weill Cornell Medical College in Qatar, the Medical College is the first in the U.S. to offer its M.D. degree overseas. Weill Cornell is the birthplace of many medical advances -- including the development of the Pap test for cervical cancer, the synthesis of penicillin, the first successful embryo-biopsy pregnancy and birth in the U.S., the first clinical trial of gene therapy for Parkinson's disease, and most recently, the world's first successful use of deep brain stimulation to treat a minimally conscious brain-injured patient. Weill Cornell Medical College is affiliated with NewYork-Presbyterian Hospital, where its faculty provides comprehensive patient care at NewYork-Presbyterian Hospital/Weill Cornell Medical Center. The Medical College is also affiliated with Houston Methodist. For more information, visit weill.cornell.edu.
Office of External Affairs
Weill Cornell Medical College
tel: 646.317.7401
email: pr@med.cornell.edu
Follow WCMC on Twitter and Facebook
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: 31-Oct-2013
ShareContact: Sarah Smith
sas2072@med.cornell.edu
646-317-7401
Weill Cornell Medical College
NEW YORK (October 31, 2013) -- Collaborating scientists at The Scripps Research Institute (TSRI) and Weill Cornell Medical College have determined the first atomic-level structure of the tripartite HIV envelope protein -- long considered one of the most difficult targets in structural biology and of great value for medical science.
The new data provide the most detailed picture yet of the AIDS-causing virus's complex envelope, including sites that future vaccines will try to mimic to elicit a protective immune response.
"Most of the prior structural studies of this envelope complex focused on individual subunits, but we've needed the structure of the full complex to properly define the sites of vulnerability that could be targeted, for example with a vaccine," said Dr. Ian A. Wilson, the Hansen Professor of Structural Biology at TSRI and a senior author of the new research with biologists Drs. Andrew Ward and Bridget Carragher of TSRI and virologist and immunologist Dr. John Moore of Weill Cornell.
The findings were published in two papers in Science Express, the early online edition of the journal Science, on October 31, 2013.
A Difficult Target
HIV, the human immunodeficiency virus, infects about 34 million people globally, 10 percent of whom are children, according to World Health Organization estimates. Although antiviral drugs are now used to manage many HIV infections, especially in developed countries, scientists have long sought a vaccine that can prevent new infections and would help perhaps to ultimately eradicate the virus from the human population.
However, none of the HIV vaccines tested so far has come close to providing adequate protection. This failure is due largely to the challenges posed by HIV's envelope protein, known to virologists as Env.
HIV's Env is not a single, simple protein but rather a "trimer" made of three identical, loosely connected structures with a stalk-like subunit, gp41, and a cap-like region, gp120. Each trimer resembles a mushroom and about 15 of these Env trimers sprout from the membrane of a typical virus particle, ready to latch onto susceptible human cells and facilitate viral entry.
Although Env in principle is exposed to the immune system, in practice it has evolved highly effective strategies for evading immune attack. It frequently mutates its outermost "variable loop" regions, for example, and also coats its surfaces with hard-to-grip sugar molecules called glycans.
Even so, HIV vaccine designers might have succeeded by now had they been able to study the structure of the entire Env protein at atomic-scale--in particular, to fully characterize the sites where the most effective virus-neutralizing antibodies bind. But Env's structure is so complex and delicate that scientists have had great difficulty obtaining the protein in a form that is suitable for atomic-resolution imaging.
"It tends to fall apart, for example, even when it's on the surface of the virus, so to study it we have to engineer it to be more stable," said Dr. Ward, who is an assistant professor in TSRI's Department of Integrative Structural and Computational Biology.
The key goal in this area has been to engineer a version of the Env trimer that has the stability and other properties needed for atomic-resolution imaging, yet retains virtually all of the complex structural characteristics of native Env.
Imaging Env
After many years in pursuit of this goal, Drs. Moore, Rogier W. Sanders and their colleagues at Weill Cornell, working with Drs. Wilson, Ward and others at TSRI, recently managed to produce a version of the Env trimer (called BG505 SOSIP.664 gp140) that is suitable for atomic-level imaging work--and includes all of the trimer structure that normally sits outside the viral membrane. The TSRI researchers then evaluated the new Env trimer using advanced versions of two imaging methods, X-ray crystallography and electron microscopy. The X-ray crystallography study was the first ever of an Env trimer, and both methods resolved the trimer structure to a finer level of detail than has been reported before.
"The new data are consistent with the findings on Env subunits over the last 15 years, but also have enabled us to explain many prior observations about HIV in structural terms for the first time," said Dr. Jean-Philippe Julien, a senior research associate in the Wilson laboratory at TSRI, who was first author of the X-ray crystallography study.
The data illuminated the complex process by which the Env trimer assembles and later undergoes radical shape changes during infection and clarified how it compares to envelope proteins on other dangerous viruses, such as flu and Ebola.
Arguably the most important implications of the new findings are for HIV vaccine design. In both of the new studies, Env trimers were imaged while bound to broadly neutralizing antibodies against HIV. Such antibodies, isolated from naturally infected patients, are the very rare ones that somehow bind to Env in a way that blocks the infectivity of a high proportion of HIV strains.
Ideally an HIV vaccine would elicit large numbers of such antibodies from patients, and to achieve that, vaccine designers would like to know the precise structural details of the sites where these antibodies bind to the virus--so that they can mimic those viral "epitopes" with the vaccine.
"It's been a privilege for us to work with the Scripps' team on this project," said Dr. Moore, a professor of microbiology and immunology at Weill Cornell. "Now we all need to harness this new knowledge to design and test next-generation trimers and see if we can induce the broadly active neutralizing antibodies that an effective vaccine is going to need."
"One surprise from this study was the revelation of the complexity and the relative inaccessibility of these neutralizing epitopes," Dr. Julien added. "It helps to know this for future vaccine design, but it also makes it clear why previous structure-based HIV vaccines have had so little success."
"We found that these neutralizing epitopes encompass features such as the variable loop regions and glycans that were excluded from previous studies of individual Env subunits," said Dmitry Lyumkis, first author of the electron microscopy study, who is a graduate student at TSRI participating in the NIH-funded National Resource for Automated Molecular Microscopy. "We observed, too, that neutralizing antibody binding to gp120 can be influenced by the neighboring gp120 structure within the trimer--another complication that was not apparent when we were not studying the whole trimer."
Having provided these valuable structural insights, the new Env trimer is now being put to work in vaccine development. "We and others are already injecting the trimer into animals to elicit antibodies," Dr. Ward said. "We can look at the antibodies that are generated and if necessary modify the Env trimer structure and try again. In this iterative way, we aim to refine and increase the antibody response in the animals and eventually, humans."
###
Other contributors to the studies, "Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 Env trimer," and "Crystal structure of a soluble cleaved HIV-1 envelope trimer in complex with a glycan-dependent broadly neutralizing antibody," included TSRI's Natalia de Val, Devin Sok, Drs. Robyn L. Stanfield and Marc C. Deller; and Weill Cornell Medical College's Albert Cupo and Dr. Per-Johan Klasse. In addition to Drs. Wilson, Ward and Carragher, senior participants at TSRI included Drs. Clinton S. Potter and Dennis Burton.
The research was supported in part by the National Institutes of Health (HIVRAD P01 AI82362, R01 AI36082, R01 AI084817, R37 AI36082, R01 AI33292), the NIH's National Institute of General Medical Sciences (GM103310) and the International AIDS Vaccine Initiative Neutralizing Antibody Consortium. IAVI has filed a patent that includes WCMC and TSRI authors on the development of the BG505 SOSIP.664 trimers as vaccine antigens.
Weill Cornell Medical College
Weill Cornell Medical College, Cornell University's medical school located in New York City, is committed to excellence in research, teaching, patient care and the advancement of the art and science of medicine, locally, nationally and globally. Physicians and scientists of Weill Cornell Medical College are engaged in cutting-edge research from bench to bedside, aimed at unlocking mysteries of the human body in health and sickness and toward developing new treatments and prevention strategies. In its commitment to global health and education, Weill Cornell has a strong presence in places such as Qatar, Tanzania, Haiti, Brazil, Austria and Turkey. Through the historic Weill Cornell Medical College in Qatar, the Medical College is the first in the U.S. to offer its M.D. degree overseas. Weill Cornell is the birthplace of many medical advances -- including the development of the Pap test for cervical cancer, the synthesis of penicillin, the first successful embryo-biopsy pregnancy and birth in the U.S., the first clinical trial of gene therapy for Parkinson's disease, and most recently, the world's first successful use of deep brain stimulation to treat a minimally conscious brain-injured patient. Weill Cornell Medical College is affiliated with NewYork-Presbyterian Hospital, where its faculty provides comprehensive patient care at NewYork-Presbyterian Hospital/Weill Cornell Medical Center. The Medical College is also affiliated with Houston Methodist. For more information, visit weill.cornell.edu.
Office of External Affairs
Weill Cornell Medical College
tel: 646.317.7401
email: pr@med.cornell.edu
Follow WCMC on Twitter and Facebook
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.
Join Peter, Richard, and me for the live version of our iPad Air and iPad mini buyers guide! We'll be talking through upgrading, which models to get, how they compare, choosing the right capacity, color, and carrier, and more!
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