Results from independent cross-checks of last month's FTL neutrino findings wont start rolling in for at least a few more months. In the meantime, however, physicists at the OPERA lab who made the initial observations will be running their experiment yet again — only this time they'll be measuring things a little differently.

In the original experiments, physicists fired off protons from CERN in extended streams that lasted on the order of 10 millionths of a second. That might not seem like a long time, but it's long enough to release so many subatomic particles that it becomes impossible to look at the flight time of any discrete group of particles, let alone a single neutrino.

So in the researchers' revised experimental design, protons will be fired in a series of abbreviated bursts that are thousands of times shorter in duration that those of the original experiments. This new method should, in theory, give the OPERA researchers a more detailed look at what's going on with these particles on their 732-kilometer trip from Switzerland to Italy.

"It's like sending a series of loud and isolated clicks instead of a long blast on a horn," explains Rutgers University physicist Matt Strassler, one of the scientists who has taken issue with the OPERA team's original methods. "In the latter case you have to figure out exactly when the horn starts and stops, but in the former you just hear each click and then it's already over."

The results of the revised experiment should be in by December. OPERA researchers hope to include their new measurements in the manuscript that they'll be submitting for peer review and publication in the coming months.

[Via BBC]

Results from independent cross-checks of last month's FTL neutrino findings wont start rolling in for at least a few more months. In the meantime, however, physicists at the OPERA lab who made the initial observations will be running their experiment yet again — only this time they'll be measuring things a little differently.

In the original experiments, physicists fired off protons from CERN in extended streams that lasted on the order of 10 millionths of a second. That might not seem like a long time, but it's long enough to release so many subatomic particles that it becomes impossible to look at the flight time of any discrete group of particles, let alone a single neutrino.

So in the researchers' revised experimental design, protons will be fired in a series of abbreviated bursts that are thousands of times shorter in duration that those of the original experiments. This new method should, in theory, give the OPERA researchers a more detailed look at what's going on with these particles on their 732-kilometer trip from Switzerland to Italy.

"It's like sending a series of loud and isolated clicks instead of a long blast on a horn," explains Rutgers University physicist Matt Strassler, one of the scientists who has taken issue with the OPERA team's original methods. "In the latter case you have to figure out exactly when the horn starts and stops, but in the former you just hear each click and then it's already over."

The results of the revised experiment should be in by December. OPERA researchers hope to include their new measurements in the manuscript that they'll be submitting for peer review and publication in the coming months.

[Via BBC]

The world's first vaccine designed to prevent cancer was not developed by a pharmaceutical company. Instead, its development was funded by public institutions on two continents, including three universities, and the U.S. National Cancer Institute. The vaccine prevents human papillomavirus (HPV), an ailment that can lead to deadly cervical cancer. HPV is spread through sexual contact, and 80% of males and females become infected during their lifetimes. But, thanks the to HPV vaccine, it doesn't have to be that way anymore.

How the HPV vaccine works

The HPV vaccine relies on virus-like particles (VLPs). The VLPs in the HPV vaccine share the same outer protein coat (L1) as human papillomavirus, however, the VLPs do lack the genetic material in HPV necessary to infect a human. The outer protein coat is the key to how the vaccine works. Thanks to the protein coat, the VLPs can assemble in the same way as HPV, and this structural similarity allows the components of the vaccine to produce an immune response without subjecting the patient to the virus in any way. It's not a neutered or dead form of the virus as in the influenza vaccine - it's no virus at all.

3 schools, 4 research groups, & (at least) 4 patents

The creation of the HPV vaccine was an effort two decades in the making. Researchers at Georgetown University are credited with the dominant patent for the the HPV vaccine due to their initial background research, however, the Georgetown team never worked with the virus-like particles. The Georgetown University group showed that the native conformation (the normal form) of L1 protein coat was needed to allow virus-like particles to form.

The U.S. Patent Office also recognizes patent claims from the U.S. National Cancer Institute, the University of Queensland, and the University of Rochester. Researchers at the University of Queensland published data with two different types of protein coats, L1 and L2, and noted that these coats allowed the assembly of virus like particles, but these virus like particles were small and not correctly assembled. This finding pre-dated the Georgetown University publication, and has spurred some controversy concerning the dominant patent.

Researchers at the National Cancer Institute, a branch of the NIH separate and apart from universities, were the first to produce an active virus-like particle that produced an immune response in animals. The NCI researchers also determined that other researchers had been using a mutant of the major HPV L1 capsid, causing slight changes in the manner in which the VLPs formed, thus refining the process.

The University of Rochester team was responsible for the first studies showing an immune response in humans. The University of Queensland research was pioneered by Dr. Ian Frazer in Australia, and sold partial patents to Merck and an Australian company CSL Limited to finance their research and clinical trials. The teams at Georgetown University and the University of Rochester were funded through grants from the National Cancer Institute.

These four groups may not have worked jointly, however, their work (and possible academic rivalry) combined with public funding allowed for quick and efficient discovery and optimization of the VLPs, as most of the major research findings paving the way for the HPV vaccine occurred between 1991 and 1993.

Two versions of the vaccine

Gardisil, the first HPV vaccine on the market, is manufactured by Merck and protects against four different strains of HPV. This protection covers HPV-16 and HPV-18, with these causing 70% of cervical cancer cases, cases which kill as many as 300,000 women annually. HPV-16 has also been linked to oropharyngeal cancer. Gardisil also protects against HPV-6 and HPV-11, guarding against 90% of genital warts. Protection against general warts and a recent FDA statement showing Gardisil to prevent anal and oropharyngeal cancer has increased demand amongst both males and females.

Cervarix, produced by GlaxosmithKline and approved for use in the United States in 2009 after several years of use in other areas of the world, protects only against HPV-16 and HPV-18, and thus lacks protection against genital warts. Despite this lack of protection against the physical attributes of sexually transmitted disease, one recent National Cancer Institute study showed that two of the mandated three shots of Cervarix may be sufficient for protection. This is quite the finding, as the third dose is taken six months after the initial injection, and likely to be skipped by the patient. Additionally, Cevarix has been shown to be effective over 7 years after administration.

Arguing against the HPV Vaccine

The suggestion that boys and young men receive the HPV vaccine has been met with controversy. Dr. William Schaffner, chairman of the Department of Preventive Medicine at Vanderbilt University School of Medicine, recently stated his support for administering the vaccine to boys and young men, emphasizing how far basic research has come:

This is cancer, for Pete's sake […] A vaccine against cancer was the dream of our youth.

You might not like shots, but it's hard to argue against getting the HPV vaccine. There is no dead or neutered virus involved - there is no genetic material in the vaccine at all. The HPV vaccine a great example of public funding and several universities putting the parts together quickly and saving many lives in the process.

Images courtesy of the World Health Organization, Medscape, and GlaxoSmithKline. Sources linked within article.

The world's first vaccine designed to prevent cancer was not developed by a pharmaceutical company. Instead, its development was funded by public institutions on two continents, including three universities, and the U.S. National Cancer Institute. The vaccine prevents human papillomavirus (HPV), an ailment that can lead to deadly cervical cancer. HPV is spread through sexual contact, and 80% of males and females become infected during their lifetimes. But, thanks the to HPV vaccine, it doesn't have to be that way anymore.

How the HPV vaccine works

The HPV vaccine relies on virus-like particles (VLPs). The VLPs in the HPV vaccine share the same outer protein coat (L1) as human papillomavirus, however, the VLPs do lack the genetic material in HPV necessary to infect a human. The outer protein coat is the key to how the vaccine works. Thanks to the protein coat, the VLPs can assemble in the same way as HPV, and this structural similarity allows the components of the vaccine to produce an immune response without subjecting the patient to the virus in any way. It's not a neutered or dead form of the virus as in the influenza vaccine - it's no virus at all.

3 schools, 4 research groups, & (at least) 4 patents

The creation of the HPV vaccine was an effort two decades in the making. Researchers at Georgetown University are credited with the dominant patent for the the HPV vaccine due to their initial background research, however, the Georgetown team never worked with the virus-like particles. The Georgetown University group showed that the native conformation (the normal form) of L1 protein coat was needed to allow virus-like particles to form.

The U.S. Patent Office also recognizes patent claims from the U.S. National Cancer Institute, the University of Queensland, and the University of Rochester. Researchers at the University of Queensland published data with two different types of protein coats, L1 and L2, and noted that these coats allowed the assembly of virus like particles, but these virus like particles were small and not correctly assembled. This finding pre-dated the Georgetown University publication, and has spurred some controversy concerning the dominant patent.

Researchers at the National Cancer Institute, a branch of the NIH separate and apart from universities, were the first to produce an active virus-like particle that produced an immune response in animals. The NCI researchers also determined that other researchers had been using a mutant of the major HPV L1 capsid, causing slight changes in the manner in which the VLPs formed, thus refining the process.

The University of Rochester team was responsible for the first studies showing an immune response in humans. The University of Queensland research was pioneered by Dr. Ian Frazer in Australia, and sold partial patents to Merck and an Australian company CSL Limited to finance their research and clinical trials. The teams at Georgetown University and the University of Rochester were funded through grants from the National Cancer Institute.

These four groups may not have worked jointly, however, their work (and possible academic rivalry) combined with public funding allowed for quick and efficient discovery and optimization of the VLPs, as most of the major research findings paving the way for the HPV vaccine occurred between 1991 and 1993.

Two versions of the vaccine

Gardisil, the first HPV vaccine on the market, is manufactured by Merck and protects against four different strains of HPV. This protection covers HPV-16 and HPV-18, with these causing 70% of cervical cancer cases, cases which kill as many as 300,000 women annually. HPV-16 has also been linked to oropharyngeal cancer. Gardisil also protects against HPV-6 and HPV-11, guarding against 90% of genital warts. Protection against general warts and a recent FDA statement showing Gardisil to prevent anal and oropharyngeal cancer has increased demand amongst both males and females.

Cervarix, produced by GlaxosmithKline and approved for use in the United States in 2009 after several years of use in other areas of the world, protects only against HPV-16 and HPV-18, and thus lacks protection against genital warts. Despite this lack of protection against the physical attributes of sexually transmitted disease, one recent National Cancer Institute study showed that two of the mandated three shots of Cervarix may be sufficient for protection. This is quite the finding, as the third dose is taken six months after the initial injection, and likely to be skipped by the patient. Additionally, Cevarix has been shown to be effective over 7 years after administration.

Arguing against the HPV Vaccine

The suggestion that boys and young men receive the HPV vaccine has been met with controversy. Dr. William Schaffner, chairman of the Department of Preventive Medicine at Vanderbilt University School of Medicine, recently stated his support for administering the vaccine to boys and young men, emphasizing how far basic research has come:

This is cancer, for Pete's sake […] A vaccine against cancer was the dream of our youth.

You might not like shots, but it's hard to argue against getting the HPV vaccine. There is no dead or neutered virus involved - there is no genetic material in the vaccine at all. The HPV vaccine a great example of public funding and several universities putting the parts together quickly and saving many lives in the process.

Images courtesy of the World Health Organization, Medscape, and GlaxoSmithKline. Sources linked within article.

Drinking can wreak havoc on your insides, and not just the relatively short-lived brand of havoc brought on by a one-night drinking spree. We're talking long-term damage to the mucous membrane of your stomach that can give rise to all manner of gastrointestinal disorders, including ulcers, colorectal cancer, and inflammatory bowel disease.

Now a team of European scientists has found that strawberries can help mitigate the stomach-punishing effects of alcohol consumption, and could even help improve the treatment of stomach ulcers.

Sara Tulipani, researcher at the University of Barcelona and co-author of the study, explains that "the positive effects of strawberries are not only linked to their antioxidant capacity and high content of phenolic compounds, but also to the fact that they activate the antioxidant defenses and enzymes of the body."

Translation? Gastrointestinal diseases like stomach ulcers are caused in part by what are known as free radicals, which are atoms and molecules with unpaired electrons. The fact that these chemicals have unpaired electrons makes them unstable and highly reactive. In an attempt to regain stability, these free radicals will react with and try to nab electrons from other, normal molecules, giving rise to damaging chain reactions in your cells that accumulate over time.

Free radicals are the byproducts of oxidation reactions that go on inside your body; so when when Tulipani talks about the "antioxidant capacity" of strawberries, or their ability to activate the antioxidant defenses of the body, she's talking about their ability to inhibit the oxidation of other molecules, and, by extension, the production of harmful free radicals.

Finally, the phenolic compounds Tulipani is referring to are called anthocyanins (the same class of molecules that causes leaves to appear red during autumn), which are described by the researchers as having a "high radical-scavenging activity."

To verify the protective effects of strawberries and anthocyanins, Tulipani and her colleagues gave absolute ethanol to laboratory rats for a period of one hour, after which their stomachs were examined for injury in the form of ulceration.

Those rats that had been fed anthocyanin-containing strawberry extracts in the days leading up to ingestion of alcohol suffered significantly less gastric damage. What's more, the researchers found that rats that had consumed strawberry extract with a higher total anthocyanin content sustained significantly less gastric injury than those that had eaten less anthocyanin-rich extract.

The rats in the study were fed strawberry extract in quantities of 40 milligrams per day per kilogram of body weight, starting as much as 10 days before they were given alcohol. But according to Maurizio Batino, coordinator of the research group at the Marche Polytechnic University in Italy, "the consumption of strawberries during or after pathology could lessen stomach mucous membrane damage" as well.

So there you have it. Not that we'd ever be ones to condone heavy drinking, but remember: if you are planning on punishing your stomach lining this weekend, be sure to load up on strawberries in the days ahead. Just make sure to ask for the ones with extra anthocyanins.

The researchers' findings are published in the latest issue of PLoS ONE.

Drinking can wreak havoc on your insides, and not just the relatively short-lived brand of havoc brought on by a one-night drinking spree. We're talking long-term damage to the mucous membrane of your stomach that can give rise to all manner of gastrointestinal disorders, including ulcers, colorectal cancer, and inflammatory bowel disease.

Now a team of European scientists has found that strawberries can help mitigate the stomach-punishing effects of alcohol consumption, and could even help improve the treatment of stomach ulcers.

Sara Tulipani, researcher at the University of Barcelona and co-author of the study, explains that "the positive effects of strawberries are not only linked to their antioxidant capacity and high content of phenolic compounds, but also to the fact that they activate the antioxidant defenses and enzymes of the body."

Translation? Gastrointestinal diseases like stomach ulcers are caused in part by what are known as free radicals, which are atoms and molecules with unpaired electrons. The fact that these chemicals have unpaired electrons makes them unstable and highly reactive. In an attempt to regain stability, these free radicals will react with and try to nab electrons from other, normal molecules, giving rise to damaging chain reactions in your cells that accumulate over time.

Free radicals are the byproducts of oxidation reactions that go on inside your body; so when when Tulipani talks about the "antioxidant capacity" of strawberries, or their ability to activate the antioxidant defenses of the body, she's talking about their ability to inhibit the oxidation of other molecules, and, by extension, the production of harmful free radicals.

Finally, the phenolic compounds Tulipani is referring to are called anthocyanins (the same class of molecules that causes leaves to appear red during autumn), which are described by the researchers as having a "high radical-scavenging activity."

To verify the protective effects of strawberries and anthocyanins, Tulipani and her colleagues gave absolute ethanol to laboratory rats for a period of one hour, after which their stomachs were examined for injury in the form of ulceration.

Those rats that had been fed anthocyanin-containing strawberry extracts in the days leading up to ingestion of alcohol suffered significantly less gastric damage. What's more, the researchers found that rats that had consumed strawberry extract with a higher total anthocyanin content sustained significantly less gastric injury than those that had eaten less anthocyanin-rich extract.

The rats in the study were fed strawberry extract in quantities of 40 milligrams per day per kilogram of body weight, starting as much as 10 days before they were given alcohol. But according to Maurizio Batino, coordinator of the research group at the Marche Polytechnic University in Italy, "the consumption of strawberries during or after pathology could lessen stomach mucous membrane damage" as well.

So there you have it. Not that we'd ever be ones to condone heavy drinking, but remember: if you are planning on punishing your stomach lining this weekend, be sure to load up on strawberries in the days ahead. Just make sure to ask for the ones with extra anthocyanins.

The researchers' findings are published in the latest issue of PLoS ONE.

Miraculin is a special protein that makes people perceive sour tastes as sweetness instead. At least, for a limited time. Now we know why it works.

Taste adventurers will be interested in a little chemical named miraculin. It was used in West Africa as a way of making some meals more palatable. A small red berry contained trace amounts of the chemical, and before chowing down on something that was certain to be too sour, or stale, people chewed a berry or two, letting the chemical coat their mouths. In 1968 miraculin was first isolated and extracted deliberately from the berry. Since then it's been sold in small tablets that people let dissolve in their mouth.

Recently, scientists have proved exactly how it works. We perceive foods as sweet when they bind to certain receptors on our tongue. Sugar, aspartame, and other sweeteners all bind to the same proteins. Sour foods bind to other receptors. Some thought that miraculin modified the sour food enough for them to bind to the sweetness receptors. In fact, it's the miraculin itself that binds to the receptors itself. It can only do that, however, in a sour environment. Outside of a bath of the acids that make food sour, it doesn't bind to any receptor at all, transforming itself into something completely tasteless.

It's also likely that miraculin blocks the receptor for sourness, at least partially. The combined effect is to turn any hint of sourness in any food sweet. There are any number of foods that would have their tastes significantly altered. It might be interesting to grab some miraculin before a buffet. Not appetizing, but interesting.

Image: Foodaholic

Via Scientific American.

The recent announcement that neutrinos had been observed seemingly going faster than the speed of light sent shockwaves through the physics community. But there's one possible explanation that could keep Einstein's relativity intact and open up a whole new cosmos.

It should be stressed that we're still far from a confirmed result for these faster-than-light neutrinos. The findings from Italy's OPERA detector have stood up decently well to initial scrutiny, and a lot of the more obvious objections have been answered, at least for the time being. But there's still every chance this is some sort of systematic error, and we won't be able to declare this an actual discovery until the results can be replicated elsewhere, with many other teams already beginning their own experiments. This is still a crazy result, and our first, second, and third reactions should all be deeply skeptical.

Still, while it shouldn't yet be considered the most likely possibility, let's imagine for a moment that these results stand up and it turns out the neutrinos really did arrive at their destination 60 nanoseconds faster than the speed of light would allow. What then? While it might seem that such a discovery would invalidate Albert Einstein's theory of special relativity - which takes it as a given that the speed of light is the absolute limit - there may be a way to reconcile the theory with the results.

The idea is that the speed of light does remain the fastest possible speed in the three spatial dimensions we're familiar with - but that the neutrinos aren't just traveling in those dimensions. Instead, they could take a shortcut through a theoretical fourth spatial dimension, which would provide a shorter distance between two points than would be possible in the normal three dimensions. The neutrinos still aren't exceeding the speed of light in this scenario. And yes, that is basically the particle physics equivalent of doing the Kessel Run in twelve parsecs.

Anyway, the larger idea here is that the three spatial dimensions and one temporal dimension we're familiar with are what make up a four-dimensional membrane, known as the brane. However, this brane "floats" in a larger reality known as the bulk. While in the ordinary course of things it would be impossible to leave the universe - to leave the brane - at incredibly high energies it might be possible for particles to temporarily break free and zip through the bulk.

This may be all getting a bit metaphysical, but a lot of these ideas are crucial to string theory, which takes extra hidden dimensions as one of its central features. Until now, string theory has remained an elegant theory that is completely beyond the bounds of experimentation. If - and, again, this is one gargantuan if - the OPERA results hold up, that could represent the first tangible evidence for string theory.

Basically, it's possible for Einstein to still be right and the speed of light to remain inviolate even if this result turns out to be a genuine discovery - his theory might just prove to be somewhat incomplete. And, if that's the case, then we're on the verge of some seriously exotic new realms of physics. It's a little too early for that much optimism...but it's still an extremely intriguing thought.

Read more at New Scientist. Image of OPERA detector via.

Science yields many rewards. There's the awed hush at nerd cocktail parties when you mention what you do, the sweet smell of urea in the morning, and the ability to name, or nickname, the things that you discover. Plenty of people name things after themselves. Some name them after their personal heroes, or their nations. And then there are a few who just can't resist a cheap joke.

There are a ton of funny names for chemical elements. They are sometimes in-jokes, sometimes references to celebrities, but a disturbing amount of them are butt-obsessed. Today, we will look at the third category.

Arsole is only the beginning. The derivation of its nickname is obvious. Entirely separate from arsole, there's a pair of completely separate ringed structures called miazole and urazole. These are nitrogen rings that have other atoms hanging off of them. The chemistry joke that goes with these is, "What's the difference between miazole and urazole? The size of the ring. Yours is bigger." Urazole is pictured below. (Don't snicker. I expect more from io9 readers.)

But chemists aren't content with the merely human. There is also the molecule cristane. This is a folded molecule is named after a crissum, the anus of a bird. It doesn't look like one. (I would be even more disturbed by the thought that random chemists knew what bird anuses look like.) It just got its name from the pigeon that flew in through a window and shat all over the lab during the molecule's discovery. Rounding out the anatomical names, there's BUM, tertiary-Butyloxymethyl group, a useless molecule that hangs off the back of a peptide.

There are also molecules named after the products of various human apertures. Diurea is a molecule used for improving flow in greases and paints. There's also cacodyl. It comes from the Greek word "kakodes," which means "stinking." Reportedly actually does smell of manure. And just to finish it off, is skatole, the white powder that turns brown as it ages.

This list just touches the surface of funny names like vaginatin, uranates, and constipatic acid, but those get their names from actual unfortunate chemical combinations or weird base words (vaginatin gets its name from Selinum Vaginatum, the plant that the chemical comes from). These are just the chemicals that sent the high-minded scientist's imaginations straight into the - well. Nevermind where their minds went. We all know.

Via Silly Molecules.

You've gotta give it up for creative taxonomists — the scientists responsible for naming, and thereby classifying, newly discovered species. Without them, we'd never have species with names like the ant pictured above, who is named after a science fiction institution. (See if you can guess who it is — it's very subtle.)

Over at Deep Sea News, Miriam Goldstein is asking for people to list some of their other favorite scientific names:

Sure, the purpose of scientific names is to provide taxonomic clarity, but some of them just sound awesome. This post was inspired by the Australian crayfish, Cherax destructor, which sounds like a comic supervillian...Crepidula fornicata is simply descriptive at what those slipper shells of loose moral fiber spend their WHOLE LIVES doing, while Thetys vagina was clearly named by someone who'd spent a looooong time at sea. And I have a weakness for terrible puns – it was a sad day when the clam Abra cadabra was put into the genus Theora.

Tracking down punny scientific names is something of a time-honored tradition among the ranks of science geeks, so show us what you've got! Goldstein provides links to a few resources to get you started, so be sure to show her some love — in the meantime, here are a few of our favorites:

Ytu brutus (a beetle)
Ba humbugi (a snail)
Lalapa lusa (a wasp)
Vampiroteuthis infernalis (the vampire squid)
Leonardo davinci (a moth)
Orizabus subaziro (palindromic name for a spp of scarab beetle)
Abra cadabra (a clam)
Gelae baen, Gelae belae, Gelae donut, Gelae fish, and Gelae rol (all types of fungus beetle)

Top image via

Coffee! Is there anything it can't do? We've already seen it linked to dropped rates of breast and prostate cancer, and now it seems to guard against skin cancer too.

Okay, to be fair, it's caffeine that's the cause this time. Red Bull, tea, black black gum, you're all in on this one.

We've actually known for a little while that ingesting caffeine can help prevent squamous cell carcinoma, but it hasn't really been understood how — until now. Caffeine, it seems, inhibits ataxia telangiectasia and Rad3-related enzyme — better known as ATR. When this enzyme is out of the way, DNA-damaged cells are far more likely to die.

Rather than slathering mice in caffeine in order to pick apart if this was the reason, researchers bred a mouse with significantly diminished ATR function in their skin, and put them in an intense UV environment. Compared to their normal cousins, they remained tumor-free for significantly longer, and had fewer tumors when they did develop.

The benefit is prophylactic; researchers believe the ATR inhibition is useful for preventing cancer from forming.

The researchers suggest a topical caffeine sunscreen could be used — it would serve double duty, both in limiting ATR and directly absorbing the UV radiation. I'm betting ThinkGeek already has this covered...

Photo by Umberto Shtanzman via Shutterstock

Microcredit institutes like Kiva claim to help small business in the developing world by offering small loans to people who aren't able to get them through the normal channels. Their claim is that these tiny loans help the people who are the most impoverished grow their businesses, and substantially improve their lot. Microfinance expert Dean Karlan has just published a study of the effects of microcredit, and while there are some advantages, they're definitely not what we originally thought.

Microloans have been a contentious issue for quite some time — a status exacerbated by the recent surge in interest thanks to online donations. Criticisms have been leveled at microcredit institutes for problems like high interest rates (getting up to 60% per year) and causing the borrowers to become dependent on repeat loans — which sound remarkably similar to the complaints against payday loans.

Dean Karlan and his colleague Jonathan Zinman undertook a large study of 1600 individuals in the Philippines, randomly giving half of them small loans and tracking the progress of all of them over the next 11-22 months. Rather than seeing the businesses grow, most of them stayed the same size or even shrunk. The microloans didn't generate higher income, and the recipients wound up feeling less confident.

The benefit the researchers did find was that the people they funded had stronger risk management, and their families were better able to weather fluctuations in personal finance and unexpected expenses. They were then able to better rely on informal lending from other sources, and the ties between the individuals and their communities were strengthened.

While this is only one study in one country, it does paint a picture remarkably different from the one that the creators of these programs want us to see, where microfinance leads to small businesses growing stronger and more wealthy. Instead we see businesses stay the same size or even shrink, but cement their places in the community.

When in a cardiac emergency, your body turns your own worst fears against you. The more acutely you feel fear, the worse your heart problem gets. It's like the plot of IT, but without the bad special effects.

One of first books to really scare me was a children's story called Ronia, The Robber's Daughter. It was set in a magical wood, and that wood was populated by various magical creatures. One group of those creatures was called The Gray Dwarves. They would be harmless, and run away from anyone who even shouted at them, as long as that person was not afraid. If they were afraid, the creatures would get vicious, and claw, bite, and pick-axe the person to death. That trope has been picked up in a lot of horror stories. IT involved a creature that would take the form of anyone's worst fears. A Dollhouse episode featured a creature that would come after people in a computer program if they felt too much fear. But of course, that doesn't work in the real world.

Oh, but it does.

Over two years, hospital employees conducted a study that measured the fear of death of a group of people coming into the hospital with a temporarily blocked coronary artery. They also measured the level of each patient's tumour necrosis factor alpha (TNF) molecule. This molecule increases system-wide inflamation, which has been shown to damage the heart. They found that the people who reported high levels of fear had four-fold increase in inflammatory response independent of the actual severity of their condition. This worsened the episode, and not just for the moment. Three weeks later, people with high levels of fear showed low cortisol levels and low heart rate variability. Cortisol is a stress hormone. Low levels of it show that bodily inflammation is still high, making things harder on the heart. Heart rate variability serves as a measure of heart function. When the heart can't adjust well to different circumstances, heart rate variability is low. Both of these factors are bad signs.

The orchestrators of the study at St. George's Hospital in London aren't sure whether the treating the inflammation itself would have effect, or whether they would need to treat the patient's emotional response as well. For the time being they encourage doctors to reassure their patients, and encourage them to talk about their emotional state. They also want people to know that major strides in medicine make coronary artery blockage a treatable phenomenon. Although it should be treated as an emergency, it is not a harbinger of doom.

The lesson I'm taking from this is the same thing I took from the book: Fearing something makes it happen. Be afraid.

Read the full scientific article via European Heart Journal

Most radioactive isotopes of the lighter elements decay in minutes or less. But one particular isotope of carbon takes 6000 years to decay, and that fact has revolutionized archaeology. But why it does that has long been a complete mystery.

This isn't really a small problem - the isotpe in question, carbon-14, takes roughly three billion times longer than its comparable isotopes to decay. That fact has baffled physicists for decades, but that ignorance hasn't stopped researchers from using carbon-14 to estimate the ages of various artifacts with tremendous precision, transforming forever our understanding of history and archaeology.

Now researchers Pieter Maris and James Vary, both from Iowa State University, have figured out what makes carbon-14 special, and why it's taken so long to figure this out. It all comes down to the three-way interactions between particles in the nucleus. While it's fairly easy to calculate how two particles - since this is the atomic nucleus, we could be talking about either neutrons or protons - might interact, but when you add a third into the mix the whole thing becomes fiendishly complex to simulate.

Basically, under normal circumstances, the forces that govern the normal decay of radioactive isotopes is always pairwise, meaning it involves interactions between only two particles. But the structure of the carbon-14 nucleus means that those two-particle interactions constantly turn into three-particle interactions, and that cancels out the effects that, in any other similar isotope, would cause it to decay in about a minute or so.

All it took to figure this out was a billion-by-billion matrix, a computer capable of handling 30 trillion different elements, and about three months of processing time. But, as Vary explains, now that they've figured out this answer, an even more complicated question arises:

"The whole story doesn't come together until you include the three-particle forces. The elusive three-nucleon forces contribute in a major way to this fact of life that carbon-14 lives so long...Everybody now knows about these three-nucleon forces. But what about four-nucleon forces? This does open the door for more study."

Via Physical Review Letters. Image via.

If you suffer frequent migraines, you probably already know that tinted lenses are your friend - but now we have scientific proof. Precision tinted lenses have been known for years to provide relief for migraine sufferers and people hit with certain reading difficulties, and now we have the fMRI scans to prove it.

For some people, viewing striped patterns like this one can be enough to trigger a migraine, and for others it can even trigger a seizure due to the illusions of shifting color and motion. When you go in for precision tinted lenses, doctors test your eyes to find the perfect hue and saturation that can counteract this effect, reducing the eye-melting optical illusion to something you can handle, and hopefully reducing your chances of getting an excruciating headache too. It's also thought that some people's dyslexia is caused by a similar problem, so tinted lenses can help them too.

New research has finally put these theories to the test, providing solid evidence that this improvement exists in the real world. The study compared the fMRI scans of migraine sufferers both with and without the colored lenses. When they had the spectacles on, there was reduced cortical activation in the visual area of the occipital cortex of the brain, which is associated with the onset of migraine.

If you have trouble reading because of visual distortion or get horrible migraines from looking at certain patterns, it might be time to swing by your optometrist and get some sweet looking sunglasses.

The atomic clocks we've already got are marvels of precision timekeeping, but their successors could be something else altogether, losing less than a second every 80 billion years. That could allow us to probe some of physics's most fundamental questions.

Anyone who has ever had to wind a watch knows that, over time, clocks will stop keeping entirely accurate time. The most precise atomic clocks currently in operation rely on the movement of electrons between energy orbits in a single aluminum ion. Because the electrons in such an ion will move from the higher energy orbit to the lower orbit at an extremely precise frequency, we can use that movement to keep time, allowing for clocks that will remain accurate for roughly 3 billion years before they lose even a second.

Now, that's pretty good, certainly for anyone who wants to use those clocks to simply keep time. But the problem is that, over time, background photons will cause the energy levels in the aluminum ions to shift around a bit, which makes the frequency shift around a bit. Since physicists can't adjust for that variance, they can't maintain the accuracy of the clock, which is why a second is lost every three billion years. Building even more accurate atomic clocks will require finding a way around that issue.

That's where the University of Delaware's Marianna Safronova enters the picture. She and her team have found a way through the so-called "heat haze" created by these photons, and they can combine a pair of mathematical approaches to figure out how the energy gap will vary over time.

If this new approach holds up, it would allow us to build atomic clocks that would only lose a second every 80 billion years or so, and possibly even better than that. We're getting close to the point that we would be able to build clocks that would keep accurate time for as long as the universe is around (or at the very least, until the universe expands into nothingness).

Even more excitingly, such clocks could monitor incredibly subtle changes over far shorter time periods. The most intriguing possibility is that we might be able to test whether the fundamental constants of the universe are really constant, or if they are in fact changing. Any changes would be exceptionally minute, beyond even the level of precision that our current atomic clocks could muster - but this new generation might be able to do it.

Via New Scientist.

The Pioneer 10 and 11 probes are currently heading out of the solar system, but they're not quite doing it quickly enough. This physics-defying anomaly has stubbornly defied explanation, but an old computer graphics technique has finally solved the conundrum.

The Pioneer probes are both on escape trajectories that will eventually take them out of the solar system. They're travelling fast, but both are slightly decelerating because the Sun's gravity is pulling them back. The so-called Pioneer Anomaly comes from the fact that both probes are slowing down slightly more than they ought to. It's less than an extra billionth of a meter per second squared, but that's still enough to fall outside our understanding of physics.

There was much speculation on the sorts strange and bizarre hidden effects that could be causing this, including the exotic idea that gravity itself somehow becomes stronger over the distances separating the Sun from the Pioneer probes. These by and large fell by the wayside when physicists realized the heat produced by the probes might be able to account for the extra deceleration. But even then, calculations revealed thermal effects could only account for about two-thirds of the anomaly, still leaving the basic mystery unsolved.

That's where researchers at Portugal's Institute for Plasmas and Nuclear Fusion enter the picture. They realized that all the previous calculations had only looked at the heat emitted, ignoring any heat reflected back at the probes. They used a computer modeling technique first developed in the 1970s known as Phong shading to figure out how the heat would reflect off the spacecraft and in which direction it would then travel.

Phong shading, which is often used to render the reflection of light off of 3D objects, proved just as adept at working out the various heat reflections on the Pioneer craft. The technique revealed that heat emitted from the main equipment compartment bounces off the back of the probes' antennae. These antennae are of course pointed back towards Earth to allow information to be relayed, which means they're also pointed at the Sun. In turn, any heat reflected off the back of these antennae will create a force in the direction of the Sun.

With this secondary effect taken into account, the Portuguese researchers are able to completely able to remove the pesky anomaly, as they explain in their paper:

"With the results presented here it becomes increasingly apparent that, unless new data arises, the puzzle of the anomalous acceleration of the Pioneer probes can ?nally be put to rest."

Of course, this won't be considered generally accepted until other groups are able to confirm and replicate these results. But this is a convincing result, and it seems far, far more likely for this to be the case than some otherwise undiscovered property of physics. Hopefully, the Pioneer Anomaly can soon be put to rest, and we can get back to what's really amazing about all this - that both these probes, sooner or later, will actually leave our solar system behind and become, along with the Voyager probes, humanity's first interstellar travelers.

arXiv via Technology Review. Artist's conception of Pioneer 10 via ETSU.

The io9 Book Club meets once per month to discuss a book, then chat with the author. In March, we're meeting on the 29th to discuss God's War by Kameron Hurley. We also have free epub copies of the book for you!

Watch for a post on the 29th announcing the book club, and jump into comments for discussion! There's still time to read the book, too. It's a fast read, and our pals at Night Shade Books are offering a free epub version of the book to anyone who would like to participate in this month's io9 Book Club.

Night Shade publisher Jeremy Lassen says:

Please send an email to io9GodsWarGiveAway@nightshadebooks.com to receive your free copy electronic copy of God's War. It will be available until March 29, 2011.

The file will be an industry standard DRM free epub format. This electronic file will be provided as is, with no warranty or support. If you can't get it to work on your device/software combination, please try a different combination.

This is free, and we don't have the resources to trouble shoot your specific platform. If you want technical support (or want to support the author monetarily), please consider buying a copy at one of our partner ebook vendors.

We're hoping Kameron Hurley will join us later in the week of March 29 for a discussion.

If you're wondering what this whole io9 Book Club thing is all about, you can visit our past meetings here.

Today, clocks throughout the United States jump forward an hour to mark the beginning of Daylight Saving Time. The economic and energy benefits of DST have been hotly debated for nearly a century, but does it pose a health risk?

All our American readers (except those in Hawaii, Arizona, and various territories) skipped the hour between 2 and 3 A.M. this morning, creating the much dreaded 23 hour day, which somehow the promise of a 25 hour day in November never quite makes up for. The practice was first instituted in the United States back in 1918 to help the war effort, as adding more daylight to the afternoon was thought to conserve fuel and improve efficiency.

The practice was unpopular, and it was abolished shortly after the war. President Franklin Roosevelt restored the practice in 1942 as a year-round practice known as "War Time", and this lasted until September 1945. By that time, the concept of Daylight Saving Time had caught on, and it became national policy by the mid-sixties.

The actual benefits of Daylight Saving Time remain controversial. People's livelihoods can be dramatically affected by DST, both positively and negatively - retail and sports events both benefit from extra daylight, while farming and forms of evening entertainment that need night to help set the mood are more adversely affected, not to mention things that rely on precise synchronized timekeeping, which can include everything from business meetings to travel and medical devices. The impact of DST on energy consumption is very difficult to figure out based on the available data, which tends to be either woefully incomplete or entirely contradictory.

But does DST actually affect people's health? Can losing one hour in March and gaining one back in November really matter to a person's general wellness? According to Yale researcher Dr. Xiaoyong Yang, the answer is actually yes, under certain circumstances:

"Most people don't have much of a problem - they can adjust their body clock quickly. Eventually, after a couple of days, they already can adapt to the new schedule. But for some groups of people - people who have depression or a heart problem - there's some research that suggests that [they] have a higher risk of suicide and heart attack."

There's some evidence to back up that assertion. A 2008 Australian study found that men are more likely to commit suicide in the first few weeks after Daylight Saving Time begins than any other time in the year, and in the same year Swedish researchers found that serious heart attacks jump 6% to 10% during the first three workdays after DST. It's a subtle effect, but even this slight disruption to people's normal body clocks can have serious effects on those who are already dealing with serious medical conditions.

Dr. Yang suspects the shifts in biological rhythms brought on by DST can actually trigger inflammatory or metabolic reactions in the body's cells. For most people, these events are of little consequence, but individuals with depression or serious heart problems are at more of a risk.

This might not be enough to simply do away with Daylight Saving Time, but it's certainly a reminder of just how finely-tuned our biological rhythms are and how important a good night's sleep really can be. Now, if you'll excuse me, I'm going to completely disregard that lesson and stay up until 4:00 in the morning...or is it 3:00?

Via Time. Image via National Geographic.

Purple is hot. Rhodopsin, or visual purple, doesn't just let you know when Prince is performing or when the Joker is about to gun you down. Recently, scientists discovered it's also a heat sensor.

Rhodopsin is one of the pigments in the eyeball which lets us see the world around us in glorious technicolor. It's a chromophere - a compound that responds to light - attached to a protein nestled in the retina at the back of the eyeball. When light hits the chromophere, it changes shape. This nudges the protein, which nudges others and gets a certain signal to the brain. The chromophere lets people see red-blue light, which gives it the name 'visual purple'. Rhodopsin is also very helpful when it comes to nightvision, and lets many animals see at night. It bleaches under bright light, but returns to form after some time in the dark.

When a pigment is used to show visual light, it's not good for it to respond to heat. It's hard to admire, for example, the Mona Lisa if the body heat from all the other art lovers in the room is causing you to see a wave of purple that overcomes the painting's details. Accurate color sensors have to be triggered by only very specific things.

So scientists were surprised when they found out fruit fly larvae without rhodopsin did not try to seek out the temperature that they preferred. These larvae were happy to stay where they would be mildly frozen or fried, while their rhodopsin-possessing counterparts tried to get to the sweet spot of 18 degrees celsius. Once they were injected with mouse-derived rhodopsin they started their quest for the perfect temperature once again.

Scientists don't know how exactly the rhodopsin managed to be a heat sensor as well as a color sensor, without confusing the two of them. Right now they're just wondering what other strange senses other pigments in the eye might have. Perhaps the part of the eye that senses the color red can also tell when there's a ghost nearby.

Via Science News and the Encyclopedia Britannica.