WASHINGTON (Reuters) - A bipartisan fiscal commission offered a plan to reduce U.S. government deficit spending by $2.4 trillion over 10 years on Tuesday and do so with a combination of spending cuts, a healthcare overhaul and tax reform.
The proposal by Democrat Erskine Bowles and Republican Alan Simpson, co-chairmen of a fiscal commission that President Barack Obama appointed early in his first term, added to the Washington debate over how to get a handle on $1 trillion annual deficits and a $16 trillion national debt.
The Simpson-Bowles plan would aim to achieve $2.4 trillion in deficit reduction over 10 years. About one-fourth of that reduction would come from health care reforms and another fourth from tax reform.
The remaining reduction would come from a combination of mandatory spending cuts, stronger caps on U.S. discretionary spending, using the Consumer Price Index for inflation-indexed provisions in the budget, and lower interest payments.
"The proposal also calls for a parallel process to make Social Security sustainably solvent and further actions to bring transportation spending and revenues in line and limit per capita cost growth in federal budgetary commitment to health care to about the growth rate of the economy," according to a summary of the plan.
(Reporting By Steve Holland; Editing by Doina Chiacu)
NEW YORK (AP) ? The parent company of Reader's Digest has filed for Chapter 11 bankruptcy protection for the second time in less than four years, saying it needs to cut its debt so it can keep restructuring.
RDA Holding Co. says it will keep publishing the magazine during the bankruptcy, and aims to be out of Chapter 11 within six months.
The New York company said late Sunday that it plans to cut its debt load by 80 percent during the restructuring, leaving it with about $100 million in debt. It said it has already reached agreements with its secured lender and more than 70 percent of its secured noteholders. A group of its creditors have supplied $45 million in new financing to help Reader's Digest go through the process as part of a $105 million loan to repay existing bank debt.
Reader's Digest has also been selling off some of its assets. It sold its food website Allrecipes.com for $175 million last year, and it sold its Every Day with Rachael Ray cooking magazine in late 2011. Both went to Meredith Corp., publisher of the Better Homes and Gardens magazine.
Reader's Digest paid circulation fell 0.6 percent to 5.5 million at the end of last year, according to the Alliance for Audited Media. That was about where it stood after cutting its guaranteed circulation in 2009. The circulation-tracking company said Reader's Digest is the fifth-biggest U.S. consumer magazine by circulation, behind two AARP publications, Game Informer Magazine, and Better Homes and Gardens.
RDA's Reader's Digest Association Inc. filed for Chapter 11 protection in 2009 in the midst of a recession and a drop in advertising and circulation. The company emerged from bankruptcy in early 2010 with less debt, but has still struggled.
Robert E. Guth, RDA's president and CEO, said a "complex transformation" begun 18 months ago under new senior managers "has resulted in a more streamlined, more focused, and more profitable business, but we have unfortunately been unable to align our debt levels correspondingly."
Besides Reader's Digest, the company publishes a food publication, Taste of Home, and has 21 brands globally.
The bankruptcy filing in the Southern District of New York covers the company's U.S. businesses. It said its international operations are not part of the filing. It said it is still looking for agreements to sell and license its international businesses, and expects to finalize some deals in coming weeks.
The dreaded day is upon us, as Twitter has followed through with its plan to increase the maximum length of t.co wrapped links. So, from now on, you've got a few less characters to play with if you want to share an URL with the world: links of the http kind now take up 22 characters instead of 20, and https links hog 23 characters instead of 21. Forget the "t.co wrapped" part -- the reduction comes into force when any URL is included in a tweet, and you can't trick it with shortened links from sites like Bit.ly, so u'll jus need 2b a lil more concise. Even Neo can't mess with the laws of the Twitter.
BOSTON ? A subatomic particle discovered last year that may be the long-sought Higgs boson might doom our universe to an unfortunate end, researchers say.
The mass of the particle, which was uncovered at the world's largest particle accelerator ? the Large Hadron Collider (LHC) in Geneva ? is a key ingredient in a calculation that portends the future of space and time.
"This calculation tells you that many tens of billions of years from now there'll be a catastrophe," Joseph Lykken, a theoretical physicist at the Fermi National Accelerator Laboratory in Batavia, Ill., said Monday (Feb. 18) here at the annual meeting of the American Association for the Advancement of Science.
"It may be the universe we live in is inherently unstable, and at some point billions of years from now it's all going to get wiped out," added Lykken, a collaborator on one of the LHC's experiments. [Gallery: Search for the Higgs Boson]
The Higgs boson particle is a manifestation of an energy field pervading the universe called the Higgs field, which is thought to explain why particles have mass. After searching for decades for proof that this field and particle existed, physicists at the LHC announced in July 2012 that they'd discovered a new particle whose properties strongly suggest it is the Higgs boson.
To confirm the particle's identity for sure, more data are needed. But many scientists say they're betting it's the Higgs.
"This discovery to me was personally astounding," said I. Joseph Kroll, a University of Pennsylvania physicist who also works at the LHC. "To me, the Higgs was sort of, it might be there, it might not. The fact that it's there is really a tremendous accomplishment."
And finding the Higgs, if it's truly been found, not only confirms the theory about how particles get mass, but it allows scientists to make new calculations that weren't possible before the particle's properties were known.
For example, the mass of the new particle is about 126 billion electron volts, or about 126 times the mass of the proton. If that particle really is the Higgs, its mass turns out to be just about what's needed to make the universe fundamentally unstable, in a way that would cause it to end catastrophically in the far future.
That's because the Higgs field is thought to be everywhere, so it affects the vacuum of empty space-time in the universe.
"The mass of the Higgs is related to how stable the vacuum is," explained Christopher Hill, a theoretical physicist at the Fermi National Accelerator Laboratory. "It's right along the critical line. That could either be a cosmic coincidence, or it could be that there's some physics that's causing that. That's something new, which we didn't know before."
Strikingly, if the Higgs mass were just a few percent different, the universe wouldn't be doomed, the scientists said.
But even if the universe is in for an unfortunate end, there is at least one reason for consolation.
"You won't actually see it, because it will come at you at the speed of light," Lykken said. "So in that sense don't worry."
Follow Clara Moskowitz on Twitter?@ClaraMoskowitz?or LiveScience?@livescience. We're also on Facebook?&?Google+.
Copyright 2013 LiveScience, a TechMediaNetwork company. All rights reserved. This material may not be published, broadcast, rewritten or redistributed.
Contact: Ivan Coluzza ivan.coluzza@univie.ac.at 43-142-775-1176 University of Vienna
This press release is available in German.
Physicists of the University of Vienna together with researchers from the University of Natural Resources and Life Sciences Vienna developed nano-machines which recreate principal activities of proteins. They present the first versatile and modular example of a fully artificial protein-mimetic model system, thanks to the Vienna Scientific Cluster (VSC), a high performance computing infrastructure. These "bionic proteins" could play an important role in innovating pharmaceutical research. The results have now been published in the renowned journal "Physical Review Letters".
Proteins are the fundamental building blocks of all living organism we currently know. Because of the large number and complexity of bio-molecular processes they are capable of, proteins are often referred to as "molecular machines". Take for instance the proteins in your muscles: At each contraction stimulated by the brain, an uncountable number of proteins change their structures to create the collective motion of the contraction. This extraordinary process is performed by molecules which have a size of only about a nanometer, a billionth of a meter. Muscle contraction is just one of the numerous activities of proteins: There are proteins that transport cargo in the cells, proteins that construct other proteins, there are even cages in which proteins that "mis-behave" can be trapped for correction, and the list goes on and on. "Imitating these astonishing bio-mechanical properties of proteins and transferring them to a fully artificial system is our long term objective", says Ivan Coluzza from the Faculty of Physics of the University of Vienna, who works on this project together with colleagues of the University of Natural Resources and Life Sciences Vienna.
Simulations thanks to Vienna Scientific Cluster (VSC)
In a recent paper in Physical Review Letters, the team presented the first example of a fully artificial bio-mimetic model system capable of spontaneously self-knotting into a target structure. Using computer simulations, they reverse engineered proteins by focusing on the key elements that give them the ability to execute the program written in the genetic code. The computationally very intensive simulations have been made possible by access to the powerful Vienna Scientific Cluster (VSC), a high performance computing infrastructure operated jointly by the University of Vienna, the Vienna University of Technology and the University of Natural Resources and Life Sciences Vienna.
Artificial proteins in the laboratory
The team now works on realizing such artificial proteins in the laboratory using specially functionalized nanoparticles. The particles will then be connected into chains following the sequence determined by the computer simulations, such that the artificial proteins fold into the desired shapes. Such knotted nanostructures could be used as new stable drug delivery vehicles and as enzyme-like, but more stable, catalysts.
###
This project was supported by the Austrian Science Fund (FWF) within the SFB "Vienna Computational Materials Laboratory" (ViCoM).
Publication in Physical Review Letters
Sequence Controlled Self-Knotting Colloidal Patchy Polymers: Ivan Coluzza, Peter D. J. van Oostrum, Barbara Capone, Erik Reimhult, and Christoph Dellago. February 11, 2013.
http://prl.aps.org/abstract/PRL/v110/i7/e075501
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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.
Contact: Ivan Coluzza ivan.coluzza@univie.ac.at 43-142-775-1176 University of Vienna
This press release is available in German.
Physicists of the University of Vienna together with researchers from the University of Natural Resources and Life Sciences Vienna developed nano-machines which recreate principal activities of proteins. They present the first versatile and modular example of a fully artificial protein-mimetic model system, thanks to the Vienna Scientific Cluster (VSC), a high performance computing infrastructure. These "bionic proteins" could play an important role in innovating pharmaceutical research. The results have now been published in the renowned journal "Physical Review Letters".
Proteins are the fundamental building blocks of all living organism we currently know. Because of the large number and complexity of bio-molecular processes they are capable of, proteins are often referred to as "molecular machines". Take for instance the proteins in your muscles: At each contraction stimulated by the brain, an uncountable number of proteins change their structures to create the collective motion of the contraction. This extraordinary process is performed by molecules which have a size of only about a nanometer, a billionth of a meter. Muscle contraction is just one of the numerous activities of proteins: There are proteins that transport cargo in the cells, proteins that construct other proteins, there are even cages in which proteins that "mis-behave" can be trapped for correction, and the list goes on and on. "Imitating these astonishing bio-mechanical properties of proteins and transferring them to a fully artificial system is our long term objective", says Ivan Coluzza from the Faculty of Physics of the University of Vienna, who works on this project together with colleagues of the University of Natural Resources and Life Sciences Vienna.
Simulations thanks to Vienna Scientific Cluster (VSC)
In a recent paper in Physical Review Letters, the team presented the first example of a fully artificial bio-mimetic model system capable of spontaneously self-knotting into a target structure. Using computer simulations, they reverse engineered proteins by focusing on the key elements that give them the ability to execute the program written in the genetic code. The computationally very intensive simulations have been made possible by access to the powerful Vienna Scientific Cluster (VSC), a high performance computing infrastructure operated jointly by the University of Vienna, the Vienna University of Technology and the University of Natural Resources and Life Sciences Vienna.
Artificial proteins in the laboratory
The team now works on realizing such artificial proteins in the laboratory using specially functionalized nanoparticles. The particles will then be connected into chains following the sequence determined by the computer simulations, such that the artificial proteins fold into the desired shapes. Such knotted nanostructures could be used as new stable drug delivery vehicles and as enzyme-like, but more stable, catalysts.
###
This project was supported by the Austrian Science Fund (FWF) within the SFB "Vienna Computational Materials Laboratory" (ViCoM).
Publication in Physical Review Letters
Sequence Controlled Self-Knotting Colloidal Patchy Polymers: Ivan Coluzza, Peter D. J. van Oostrum, Barbara Capone, Erik Reimhult, and Christoph Dellago. February 11, 2013.
http://prl.aps.org/abstract/PRL/v110/i7/e075501
[ | 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.
The New York Department of Taxation and Finance has announced that it will provide relief to farmers and fishermen who are unable to file and pay their 2012 personal income tax and metropolitan commuter transportation mobility tax (MCTMT) by the March 1 deadline. Generally, if an estimated tax payment is not made on January 15 for personal income tax purposes, or on January 31 for MCTMT purposes, such taxpayers are not subject to a penalty if they file their return and pay the full amount of tax due by March 1. However, under the penalty relief, such taxpayers will not be subject to the underpayment of estimated tax penalty if they file and pay their tax due by April 15, 2013, for personal income tax purposes, or by April 30, 2013, for MCTMT purposes.
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Taxpayers do not need to take any special action with New York to be eligible for the penalty relief. This relief is being provided in response to the Internal Revenue Service?s announcement that it will provide relief from its estimated tax penalty for farmers and fishermen unable to file and pay their 2012 taxes by the March 1 deadline due to the delayed start for filing tax returns.
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Important Notice N-13-2 , New York Department of Taxation and Finance, February 2013 , ?407-777
Fresno State has absorbed several tough lessons this season under second-year coach Rodney Terry.
Wednesday night was one of the toughest. After leading No. 19 New Mexico by 11 points at halftime, the Bulldogs scored just 17 in the second half and lost 54-48 to the Mountain West Conference leaders.
Fresno State shot 26.9 percent after halftime and missed a chance for its first victory over a Top 25 team since 2002.
"In this league you have to play for 40 minutes; you can't play for 38 or leave 3 extra minutes out there without finishing it out," Terry said. "At the end of the day you have to make shots, too. I said to our guys a little while ago, we've learned some really tough lessons this year."
Kendall Williams scored 13 points, capped by an emphatic dunk just before the final buzzer, and Alex Kirk added 10 points, nine rebounds and six blocks for the Lobos (21-4, 8-2 Mountain West).
Tony Snell also scored 10, and his 18-foot leaner with 20 seconds left sealed the victory as New Mexico remained a half-game ahead of second-place Colorado State in the conference standings.
"When you're down 11 at the half on the road and you play the way we played in the second half, it was outstanding," Lobos coach Steve Alford said. "These guys, they just find a way. You shoot 37 percent and still get a road win."
Kevin Olekaibe led Fresno State (8-15, 2-8) with 11 points, while Kevin Foster had 10 points and 10 rebounds. Foster scored all of his points in the first half.
The Bulldogs scored only three points, on Olekaibe's 3-pointer, in the final 10:08.
"We knew that their coach was going to get on them at halftime, and they were going to come out with fire," Olekaibe said. "We just have to try and master our intensity in the second half."
After Olekaibe's shot put Fresno State ahead 48-45 with 3:46 remaining, the Lobos pulled within one on a layup by Cameron Bairstow.
Kirk then blocked a shot on the other end, which led to a 3-point attempt by Hugh Greenwood. The shot missed, but Greenwood grabbed the offensive rebound and threaded a bounce pass to Bairstow for a dunk with 1:28 left that put the Lobos ahead for good.
"It was a loose ball, so I knew something was going to be open," Greenwood said. "I just knew he was there and I threw it under him."
Alford was more complimentary of Greenwood's pass, which skipped past several defenders.
"A lot of guys just dribble back out," Alford said. "But he saw Cam and made a great pass."
Greenwood made one of two free throws with 53 seconds to go for a two-point New Mexico lead, and the Lobos maintained possession when the miss went off a Fresno State player out of bounds.
New Mexico then milked most of the 35-second shot clock before Snell's jumper made it a four-point game.
"It's bagging road wins," Alford said. "We're sitting at the top of the league not just in wins but in most road wins. We're plus-three now, 3-2 on the road with three road games to go, and that's huge."
New Mexico used the first 9 minutes of the first half to whittle away at an 11-point halftime deficit. The Lobos finally went ahead 41-40 with 11:02 remaining when Snell found Williams along the baseline for a dunk.
Fresno State answered right back, regaining the lead on Marvelle Harris' drive. But the Bulldogs, who average the fewest points in the MWC, didn't score for the next 6:59.
Fresno State led 31-20 at halftime after limiting the Lobos to 25.9 percent shooting. Those 31 points represented the Bulldogs' highest-scoring first half during conference play. Fresno State scored 22 of those points in the final 7:30.
"It was really, really, really quiet (at halftime)," Kirk said. "We had to come in, come together as a team and focus a little bit. That's what we did. It was a lot better second half."
New Mexico led by as many as eight before Fresno State went on a 14-0 run sparked by two jumpers from Harris and capped by Olekaibe's 3-pointer.
After Kirk made two free throws to stop New Mexico's 4:46 scoring drought, Olekaibe and Foster extended the Bulldogs' lead to double digits at halftime.
The Lobos lost key reserve Demetrius Walker late in the first half to a knee injury after he crashed into two defenders under the basket. He did not return and will be evaluated by team doctors, Alford said.
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Public release date: 15-Feb-2013
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