Senate unanimously passes legislation declaring Israel "major strategic partner," sets stage for enhanced cooperation across range of issues


The Senate late Thursday unanimously passed bipartisan legislation establishing Israel as a "major strategic partner" of the United States, establishing a basis for expanded cooperation across areas as diverse as security, energy, and trade. The bill had been authored by Sens. Barbara Boxer (D-CA) and Roy Blunt (R-MO) and had gained 81 co-sponsors before it went to the floor. The House had already passed parallel legislation in March, and the pro-Israel lobby AIPAC called on Congress "to move quickly to reconcile the two versions of the legislation and send it to the President for his signature." Broad aspects of the bill will see Israel's trade status upgraded and new mechanisms created to facilitate technological cooperation in corporate and academic contexts. The Times of Israel specifically focused on aspects of the legislation that will - per the outlet's description - increase "the frequency and detail of US government reporting on Israel's qualitative military edge" and "expand the authority for forward-deployed US weapons stockpiles in Israel." The value of those stockpiles, which the Israelis have tapped into during their recent wars with Hamas, will now be increased by $200 million to a total of $1.8 billion. The Times of Israel also picked out provisions of the bill requiring the president to "study the feasibility of expanding US-Israel cooperation on cyber security." A recently leaked top-secret memo detailed previously unknown dimensions of US-Israeli intelligence cooperation, revealing that Washington and Jerusalem coordinate on cyber issues to an unprecedented degree. There are also provisions in the legislation to broaden energy cooperation, just a few weeks after the Houston Chronicle reported on broad efforts being made to establish links between Israel and Texas-based energy companies on issues ranging from regulatory advice to resource co-production. The vote itself came less than a month after a bipartisan Congressional delegation visited Israel to among other things push back against swirling reports of strain between Washington and Jerusalem. American support for Israel and sympathy for Israel remain near all time highs, and Congressional legislation expressing Washington's backing for the Jewish state routinely cruises through the Senate without dissent. Scholar and journalist Walter Russell Mead, the James Clarke Chace Professor of Foreign Affairs and Humanities at Bard College, has described public American support for Israel as "one of the most potent political forces in U.S. foreign policy."

Kitty might be the purrfect pet but according to a new Technion-Israel Institute of Technology study, she could also hold the clue to new anti-HIV drugs. The feline virus FIV that causes the disease in cats looks a lot like HIV. Both FIV and HIV rely on a protein called integrase that inserts the virus’ DNA into an infected cell’s DNA. Faculty of Biology Assistant Professor Akram Alian and graduate student Meytal Galilee say they may have found a new weak point in the protein that drug designers may be able to target in the future. In an article recently published in Cell Structure, the two researchers offer up a detailed, 3-D molecular map of FIV integrase that could help scientists also understand how this protein works in HIV. The researchers have pinpointed a single amino acid change that seems to be critical in highlighting how the protein assembles itself from simpler building blocks. Anti-HIV drug designers are eager to find ways to derail this assembly process. “Designing drugs which target such specific hot spots,” Alian says, “may be easier than targeting the entire protein-protein interacting interface.” Scientists have been able to determine the 3-D structure of the complicated molecular core of HIV integrase. But in FIV, Alian and Galilee were able to solve the structure in a more simple form. The researchers determined that a mutation in a single amino acid can convert the integrase from the more complex to the simpler form in FIV. And that single amino acid may act as a crucial “hinge” point that connects two molecular subunits and allows them to pivot about in the protein’s fully active core, says the scientists. “Highlighting the hinge… is an important observation that should be considered in the future design of integrase drugs,” says Alian. (via Israel21c)

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