29.08.2012 - (idw) Ruhr-Universitt Bochum

First place in an EU competitive call on Unconventional Computing was awarded to a collaborative proposal coordinated by Prof. John McCaskill from the RUB Faculty of Chemistry and Biochemistry. The project MICREAgents plans to build autonomous self-assembling electronic microreagents that are almost as small as cells. They will exchange chemical and electronic information to jointly direct complex chemical reactions and analyses in the solutions they are poured into. The EU supports the project within the FP7 programme with 3.4 million Euros for three years. Turning chemistry inside-out Self-assembling smart microscopic reagents to pioneer pourable electronics 3.4 million Euros from EU programme for international research project

First place in an EU competitive call on Unconventional Computing was awarded to a collaborative proposal coordinated by Prof. John McCaskill from the RUB Faculty of Chemistry and Biochemistry. The project MICREAgents plans to build autonomous self-assembling electronic microreagents that are almost as small as cells. They will exchange chemical and electronic information to jointly direct complex chemical reactions and analyses in the solutions they are poured into. This is a form of embedded computation to compute is to construct in which for example the output is a particular catalyst or coating needed in the (input) local chemical environment. The EU supports the project within the FP7 programme with 3.4 million Euros for three years. Four research groups at RUB will join forces with top teams across Europe, from Israel and New Zealand.

Self-assembling electronic agents

In order to create this programmable microscale electronic chemistry, MICREAgents (Microscopic Chemically Reactive Electronic Agents) will contain electronic circuits on 3D microchips, called lablets. The lablets have a diameter of less than 100 m and self-assemble in pairs or like dominos to enclose transient reaction compartments. They can selectively concentrate, process, and release chemicals into the surrounding solution, under local electronic control, in a similar way to which the genetic information in cells controls local chemical processes. The reversible pairwise association allows the lablets to transfer information from one to another.

Translating electronic signals into chemical processes

The lablet devices will integrate transistors, supercapacitors, energy transducers, sensors and actuators, and will translate electronic signals into constructive chemical processing as well as record the results of this processing. Instead of making chemical reactors to contain chemicals, the smart MICREAgents will be poured into chemical mixtures, to organize the chemistry from within. Ultimately, such microreactors, like cells in the bloodstream, will open up the possibility of controlling complex chemistry from the inside out.

The self-assembling smart micro reactors can be programmed for molecular amplification and other chemical processing pathways that start from complex mixtures, concentrate and purify chemicals, perform reactions in programmed cascades, sense reaction completion, and transport and release products to defined locations. MICREAgents represent a novel form of computation intertwined with construction. By embracing self-assembly and evolution, they are a step towards a robust and evolvable realization of John von Neumanns universal construction machine vision. Although these nanoscale structures will soon be sufficiently complex to allow self-replication of their chemical and electronic information, they will not present a proliferative threat to the environment, because they depend for their function on the electronic circuit layer that is fabricated as part of their substrate.

RUB collaborators

For the project, Prof. Dr. John S. McCaskill (Microsystems Chemistry and Biological Information Technology) collaborates with Prof. Dr. Gnter von Kiedrowski (Bioorganic Chemistry), Prof. Dr. Jrgen Oehm (Analog Integrated Circuits) and Dr. Pierre Mayr (Integrated Digital Circuits). McCaskills and von Kiedrowskis labs at RUB have already joined forces in previous European Projects forging a path towards artificial cells. The ECCell project, for example, that finished in February this year, has laid the foundation for an electronic chemical cell. There, the electronics and microfluidics were exterior to the chemistry: in MICREAgents this is being turned inside out.

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Project MICREAgents: self-assembling smart microscopic reagents to pioneer pourable electronics

ScienceDaily (Aug. 28, 2012) Researchers from the University of Bonn and the Max Planck Institute of Biochemistry in Martinsried have decoded a signal path that could boost the burning of body fat. Mice that are missing a signal switch called VASP are clearly leaner and have more of the coveted brown and beige-colored fat cells that convert energy into heat. This might point the way to a new method for fighting obesity.

The researchers presented their results in the current issue of the journal Science Signaling.

The numbers of obese people are climbing steeply all over the world-with obvious major consequences for their health. Due to excess food intake and a lack of physical activity, but also due to genetic factors, the risk for overweight people dying from diseases like coronary heart disease, diabetes and atherosclerosis increases. "The body's fat reserves are actually used as a place to store energy that allows surviving lean times," says Prof. Dr. Alexander Pfeifer, Director of the Institute of Pharmacology and Toxicology of the University of Bonn. "But nowadays, hardly anyone in the industrialized nations is exposed to such hunger phases anymore."

A signal path boosts the burning of fat in the body

Since many people ingest more energy in their diet than they can burn, many harbor dreams of a magic pill that will simply make fat melt away. Now, scientists working with Prof. Pfeifer in collaboration with colleagues from Epileptology and from the PharmaCenter Bonn, together with the Max Planck Institute of Biochemistry in Martinsried -- have discovered a signal path in the metabolism of mice that is indeed able to greatly boost combustion inside the rodents' bodies.

"Science distinguishes between three different types of fat," reports Prof. Pfeifer. White fat is used to store energy and is found in the "problem zones" of overweight people. "Brown fat cells, however, are used as a kind of heating unit," says the pharmacologist. "In babies, they make sure that they do not lose too much heat." Unfortunately, adults have hardly any brown fat cells left-except for small areas at the back of their necks and along their spines. The third category-the so-called "beige fat cells"-are the ones the researchers are betting on. "Just like brown fat cells, they are efficient at converting energy from food into heat, and they can form from the undesirable white fat cells," explains Prof. Pfeifer.

How can white fat cells be converted into brown or beige ones?

Consequently, the team's research focused on how to turn the white fat cells into as many beige ones as possible. "The issue was finding a way to brown white fat -- of course, not in a skillet, but directly inside the body," the University of Bonn pharmacologist summarized the problem. In a study published in 2009, the team around Prof. Pfeifer found that brown fat needs the neurotransmitter "cGMP." And according to the new findings, this is also true for beige fat. The researchers now studied in mice where cGMP comes from and how it is regulated.

These studies showed that vasodilator-stimulated phosphoprotein (VASP) plays an essential role as a switch on a signal path that slows down the formation of brown and beige fat cells. "This is why mice in which the gene for forming VASP was switched off have the more active brown and beige fat," Prof. Pfeifer summarizes the study results. "These animals are lean and dissipate more energy." In developing a regulator for the VASP/cGMP signaling pathway, the researchers see a potential starting point for promoting the energy- and fat-burning brown fat cells.

Hope for new obesity therapies

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How 'beige' fat makes the pounds melt away

ScienceDaily (Aug. 27, 2012) Some RNA molecules spend time in a restful state akin to hibernation rather than automatically carrying out their established job of delivering protein-building instructions in cells, new research suggests.

And instead of being a fluke or a mistake, the research suggests that this restful period appears to be a programmed step for RNA produced by certain types of genes, including some that control cell division and decide where proteins will work in a cell to sustain the cell's life.

This could mean that protein production in cells is not as clear-cut as biology textbooks suggest, scientists say.

"This could mean there are more variations to the proteins in our bodies than we realize; it means that RNAs can be stored and reactivated and we don't know what biological process that affects -- it could influence embryonic development, or neurological activity, or even cancer," said Daniel Schoenberg, professor of molecular and cellular biochemistry at Ohio State University and lead author of the study.

Schoenberg and colleagues discovered this phenomenon by tracing the origins of a cap-like structure on messenger RNA (mRNA) that is known to coordinate most of this RNA molecule's short life. Messenger RNA is manufactured in a cell's nucleus and each mRNA contains the instructions needed to produce a specific protein that a cell needs to live.

Until now, scientists have believed that once an mRNA is no longer needed to make protein, the cap comes off and the molecule is degraded, its job complete. But Schoenberg's lab discovered in 2009 that some mRNAs that were thought to be degraded were instead still present in the cell, but they were missing part of their sequence and had caps placed back on the newly formed ends. Because these mRNAs were in the cytoplasm, the changes had to happen there rather than inside the nucleus.

In this new study, the researchers were looking for further evidence of these apparent rogue mRNAs, but instead they found that a completely unexpected biological process occurs before some proteins are even a glimmer in a gene's eye: The uncapping and recapping of mRNAs outside the nucleus results from a cap recycling operation in the cell cytoplasm. This process appeared to enable certain RNAs to pause, without being degraded, before launching protein production.

"What this discovery tells us is a complete fundamental reworking of the relationship between a gene, messenger RNA and a protein. It's more complicated than we realize," Schoenberg said.

The research is published online in the open-access journal Cell Reports.

That fragments of mRNA could exist at all in the cell's main body was first reported by other scientists in 1992. Years later, Schoenberg asked a postdoctoral researcher in his lab to revisit these unexpected RNA fragments and confirm they exist. The postdoc's experiments showed that these mRNA, thought to be the dregs left over from their degradation, had caps on them -- suggesting they still had the potential to function in protein production. Schoenberg, also director of Ohio State's Center for RNA Biology, has been investigating this cytoplasmic capping operation ever since.

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To cap or not to cap: Scientists find new RNA phenomenon that challenges dogma

Alireza "Ray" Rezaie spends his days in a lab manipulating molecules to make some of their functions work better while turning off others that can cause unwanted side effects.

His work could one day help prevent and treat health conditions ranging from heart disease to blood poisoning.

In July, the National Institutes of Health awarded Rezaie, professor of biochemistry and molecular biology at St. Louis University, a four-year, $1.52 million grant to study how antithrombin, the key blood-clotting inhibitor produced by the liver, can be improved to prevent premature death from heart disease.

Two years ago, the NIH gave him $1.5 million to study activated Protein C. In its activated form it helps regulate inflammation, blood clotting and cell death. It also helps maintain the permeability of blood vessel walls.

Rezaie has been studying ways to ramp up activated Protein C's ability to prevent organ failure while reducing its anti-clotting activity, to prevent hemorrhaging.

The antithrombin study is still in its infancy, but Rezaie recently discovered that it also blocks inflammation in the blood vessel wall, which can lead to heart disease and acute sepsis. The later is a violent, life-threatening reaction to blood infections.

He's moved from the petri dish stage of the study to looking at its effects in mice. It could be years before a drug is developed for clinical trials and even longer before FDA approval.

Nevertheless, Rezaie is excited about the promising findings.

"What's interesting is antithrombin is involved in normal circulation to prevent clot formation," he says. "After a clot is formed, at the site of a cut or bruise, antithrombin is the molecule that comes and stops the clotting. You have to stop it at one point when it's finished."

Patients with coronary artery disease, embolisms, strokes and heart attacks are typically treated with blood thinners such as Heparin and Coumadin, which inhibit antithrombin and put patients at risk of hemorrhaging. Rezaie's antithrombin could potentially be used in lieu of those drugs.

Originally posted here:
In the lab: Manipulating molecules for better health

Oak Hill High staff is commended

I would like to commend the staff at Oak Hill High School for the excellent education you provided our children. Our son returned to Marshall University as a senior and graduate with a biochemistry degree, then will move on to graduate or medical school. Our daughter moved in on Aug. 22 with 25 credit hours achieved through the hard work and dedication of those professionals at Oak Hill High School. She will begin her journey towards receiving her biochemistry degree and becoming a pediatric oncologist.

I am writing this article not only to commend educators who strive to make a difference, but also to help young people realize that dreams are not impossible. Sometimes they are hard to achieve because of the dedication and hard work that is needed to accomplish the goal, but if its worth the effort to make Gods world a better place, then do it.

My question to all of the wonderful students I have been blessed by is simply this: Why did God create you and what is your purpose in life? If you cant answer this question, then our world has no future.

Cathy Broughman

Oak Hill

Avoid buying puppies from roadside peddlers

If you have been to the Fayette Town Center more than a few times, you have surely seen people in the median selling pure-bred or designer breed puppies from their vehicles with a handmade sign. I would like to encourage readers not to walk, but run away from these people.

The plaza tried to solve the problem with signage, but the signs soon disappeared and the puppy peddlers returned. A puppy mill or a backyard breeder is an extremely common business that often operates underground, and right here in Fayette County.

The operator chooses a breed of the current fad (often a toy breed) and forces dogs of that breed or breeds to reproduce at an unhealthy frequency in deplorable conditions. The mothers do not receive adequate care, socialization, recreation or affection in order to keep operating costs at a minimum. Some spend most of their lives in a cage the size of your dishwasher.

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Tribune Readers’ Views for Thursday, Aug. 23

Public release date: 23-Aug-2012 [ | E-mail | Share ]

Contact: Steve Graff stephen.graff@jefferson.edu 215-955-5291 Thomas Jefferson University

PHILADELPHIAIt's widely accepted that molecular mechanisms mediating epigenetics include DNA methylation and histone modifications, but a team from Thomas Jefferson University has evidence to the contrary regarding the role of histone modifications.

A study of Drosophila embryos from Jefferson's Department of Biochemistry and Molecular Biology published ahead of print in Cell August 23 found that parental methylated histones are not transferred to daughter DNA. Rather, after DNA replication, new nucleosomes are assembled from newly synthesized unmodified histones.

"Essentially, all histones are going away during DNA replication and new histones, which are not modified, are coming in," said Alexander M. Mazo, Ph.D., professor of Biochemistry and Molecular Biology at Jefferson, and a member of Jefferson's Kimmel Cancer Center. "In other words, what we found is that histone modifying proteins are hiding on the way over replicating DNA, instead of histones 'jumping' over as currently thought."

"What this paper tells us," he continues, "is that these histone modifying proteins somehow are able to withstand the passage of the DNA replication machinery. They remained seated on their responsive binding sites, and in all likelihood they will re-establish histone modification and finalize the chromatin structure that allows either activation or repression of the target gene."

The team suggests that since it appears these histone modifying proteinsthe Trithorax-group (TrxG), which maintain gene expression, and the Polycomb-group (PcG), which plays a role in epigenetic silencing of genesre-establish the histone code on newly assembled unmethylated histones, they may act as epigenetic marks.

Epigenetics is the study of heritable changes in gene expression caused by mechanisms other than changes in the underlying DNA sequence. Epigenetic marks have become an important focus in recent years because they are thought to have the potential to explain mechanisms of aging, human development, and the origins of diseases, like cancer, heart disease, and mental illness.

According to widely-accepted models applied today, the tails of methylated histones turn genes in DNA "on" or "off" by loosening or tightening nucleosome structure, thus changing the accessibility of transcription factors and other proteins to DNA.

"People believe that everything gets worked off of DNA during the replication process and that these methylated histones act as epigenetic marks, since they are believed to rapidly jump from parental to daughter DNA" said Dr. Mazo. "But there is no experimental evidence to back this up."

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Histone-modifying proteins, not histones, remain associated with DNA through replication

Public release date: 22-Aug-2012 [ | E-mail | Share ]

Contact: Garth Hogan ghogan@asmusa.org American Society for Microbiology

Andrew Lee Lovering, Ph.D., School of Biosciences, University of Birmingham, has received a 2012 ICAAC Young Investigator Award for his seminal work on the structural biology and biochemistry of the proteins that synthesize and modify cell walls in bacteria. Natalie Strynadka, University of British Columbia, describes the significance of Lovering's work: "his spectacular abilities in structural biology clearly paved the way for our understanding of these important antibacterial targets which are also membrane-anchored, a hurdle that has thwarted literally decades of attempts at previous characterization by many groups worldwide." "His protein structure work has shown how Gram positive bacteria synthesize teichoic acids, how bacterial cell walls are transglycosylated, and how enzymes of predatory bacteria partially degrade bacterial cell walls as they invade prey bacteria," explained nominator Liz Sockett, University of Nottingham.

Lovering obtained his B.Sc. in Biochemistry from Birmingham University, where he also earned his Ph.D. in Biosciences. There he used x-ray crystallography to detail the mechanism of action of two enzymes involved in cancer therapies; one a bacterial nitroreductase used in gene therapy of solid tumors, and the other a target for a cell differentiation approach tackling acute myeloid leukemia.

After graduating from Birmingham University, a postdoctoral position in Strynadka's laboratory at the University of British Columbia introduced Lovering to the subject of antibacterial research. This led to determination of the structures of two monotopic membrane proteins involved in bacterial cell wall synthesis. One of these, S. aureus PBP2, represented the first detailed view of how bacteria catalyze the essential step of peptidoglycan polymerisation, a potentially excellent drug target. The other, S. epidermidis TagF, revealed how the Gram-positive wall polymer teichoic acid is synthesized and may form the basis for the development of antivirulents. The PBP2 publication was chosen as one of the highlights of the year by Science and C&E News.

Since establishing his own research group in 2010, Lovering's focus has shifted to deciphering the molecular basis of bacterial predation by Bdellovibrio bacteriovorus, a phenomenon that may lead to its exploitation as a "living antibiotic". In collaboration with Sockett at the University of Nottingham, this approach has already begun to detail how the invading bacterium modifies the prey cell wall for purposes of niche formation, and also how Bdellovibrio and other bacteria hydrolyze the ubiquitous bacterial second messenger cyclic-di-GMP. "As invited speaker of the 2012 Gordon Conference on Bacterial Sensory Transduction, he described the first ever crystal structure of an HD-GYP bacterial signaling protein," says Sockett.

"Lovering's enthusiasm and fascination with the microbial world is always palpable. His level of insight, profound knowledge of fundamental biochemistry, and ability to see connections that others would have missed never fail to amaze me," summarizes Klaus Ftterer, University of Birmingham. "As he builds his research group it is clear that his work will enlighten our understanding of an unusual microorganism, and his enthusiasm will inspire junior researchers in both the structural biology and microbiology communities."

Strynadka agrees, "he is highly collegial, modest, and a natural teacher. His love of and interest in science is truly infectiousknowledge he loves to share with others. Collectively, I believe him to be a truly exceptional rising star who will continue to make fundamental advances to structural microbiology."

###

The ICAAC Young Investigator Award will be presented during ASM's 52nd Interscience Conference on Antimicrobial Agents and Chemotherapy (ICAAC), September 9-12, 2012 in San Francisco, CA. ASM is the world's oldest and largest life science organization and has more than 40,000 members worldwide. ASM's mission is to advance the microbiological sciences and promote the use of scientific knowledge for improved health, economic, and environmental well-being.

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The American Society for Microbiology honors Andrew Lovering

Anton Iliuk never expected to be an entrepreneur.

Now, the former Purdue University biochemistry students doctoral project to develop new technology that can help pinpoint potential targets for cancer therapy has transformed into a growing startup in Purdue Research Park.

Iliuks former adviser, biochemistry associate professor W. Andy Tao, is his business partner.

Most science majors have two paths, Iliuk said. One is academia. One is industry. This is the path less traveled. Im not a business guy.

But the companys first product, PolyMAC, still managed to generate sales of nearly $50,000 in five months for his company, Tymora Analytical Operations LLC.

Id like to turn this into a multimillion-dollar company, Iliuk said. If you dont believe, nobody else will.

Iliuk, the companys president and chief technology officer, said a realistic goal for next year would be to double the sales of PolyMAC, which analyzes tissue modification on a cellular level.

You send in a fishing net, you try to pick up everything there is, sort through it and see what has changed from normal tissue to cancer tissue, Iliuk said.

The next step for Tymora is to get its next product, pIMAGO, to market. Iliuk said the goal of pIMAGO is to cut the cost associated with the early stages of drug development by showing which drugs will be more effective.

Its sort of a launch pad, Iliuk said. Were trying to improve the way people do lab research.

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Purdue grad hopes to grow Tymora startup into 'multimillion-dollar company'

Newswise Sivaguru (Siva) Jayaraman, Ph.D., associate professor of chemistry and biochemistry at North Dakota State University, Fargo, has received a three-year, $429,500 award from the National Science Foundation (NSF) to conduct research outlined in his proposal titled Light Induced Enantiospecific Chiral Transfer in Solution. The funding also provides research opportunities to graduate and undergraduate students to develop environmentally benign, green strategies to perform chemical reactions.

The research program in Dr. Sivas group focuses on using light to transfer molecular chirality in photochemical reactions (reactions initiated by light) to produce molecules that are chiral (have two non-superimposable mirror images) and make only one of the two possible forms (a single enantiomer).

Based on the funding from the National Science Foundation, his research group will study light-induced enantiospecific chiral transfer in solution. One of the research goals is to gain a fundamental understanding of interaction of light with photoreactive substrates, coupled with an intricate control over molecular reactivity, dynamics and non-bonding interactions to enhance stereoselectivity in the photoproducts.

Synthesizing chiral compounds with high stereoselectivity during light-induced transformations provides an opportunity to develop sustainable strategies with minimal impact on the environment, said Dr. Jayaraman.

Students learn how modern chemical methods can be used for synthesizing compounds with minimal environmental impact. With this most recent NSF funding, students involved in the proposed investigations will learn both traditional techniques to characterize and evaluate asymmetric induction during enantiospecific phototransformations and modern spectroscopic methods and characterization techniques to assess excited state reactivity.

The award is a renewal grant of Dr. Jayaramans CAREER award, which includes research opportunities for NDSU students. His research also provides opportunities to area high school students through a program called PICNICS (Parents Involvement with Children, Nurturing Intellectual Curiosity in Science).

As part of the PICNICS program, top area high school students conduct a variety of research each summer alongside graduate students and postdoctoral fellows at the Department of Chemistry and Biochemistry, NDSU, Fargo. The PICNICS program was developed by Dr. Jayaraman as an outreach component in his NSF CAREER award to engage high school students and their parents about recent science and technology advancements and to encourage high school juniors and seniors to consider science as a career path.

Dr. Sivaguru (Siva) Jayaraman joined the faculty at NDSU in 2006. He was promoted to associate professor in 2011. He previously received an NSF CAREER award in 2008, a Grammaticakis-Neumann Prize from the Swiss Chemical Society in 2010, a Young-investigator award from the Inter-American Photochemical Society (I-APS) in 2011, and a Young-investigator award from Sigma Xi in 2012.

At NDSU, Dr. Jayaraman received the 2010 Excellence in Research Award, 2011 Excellence in Teaching award and 2012 Peltier Award for Innovation in Teaching. He completed a post-doctoral fellowship at Columbia University, New York, N.Y., after receiving his Ph.D. from Tulane University, New Orleans, La. He received a masters degree in chemistry from the Indian Institute of Technology, Madras, India, and completed a bachelors degree in chemistry from St. Josephs College, Bharathidasan University, Trichy, India.

For more info regarding Dr. Sivaguru Jayaramans research, teaching and outreach visit http://sivagroup.chem.ndsu.nodak.edu/

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NDSU Faculty Receives NSF Funding for Chemistry Research

ASHBURN, Va. (AP) -- Lorenzo Alexander has quite a collection of white bottles, labeled with words straight from a biochemistry class. Beta Alanine Supreme. Carnitine Synergy. Uber C. Some 19 containers, big and small, in his Washington Redskins locker.

''I have a lot of supplements,'' he said.

The consummate self-made NFL player, Alexander has always been conscious about his diet. Like many players, he also gets advice on the right mix of tablets to maximize his endurance and energy output. Or, as he puts it, ''to help balance your body out.''

This year, it's been more of a challenge to find that balance. Alexander, who once was a 300-pound lineman, arrived at training camp weighing 245, having dropped some 30 pounds from this time last season so that he can hold his own in his new role as the team's primary backup at inside linebacker.

''Being 265,'' he said, ''is not ideal for covering tight ends and fast wide receivers down the middle of the field.''

No one would expect anything different from the player who arrived as a practice squad nobody in 2006 and soon became an indispensable utility man, working his way up to his current role as a team captain who now gets annual support from his teammates as an ought-to-be Pro Bowl player.

''I'd say he's one of, if not the biggest influence I've had since I've been here,'' said linebacker Ryan Kerrigan, a first-round draft pick last year. ''He seems to me what really embodies a professional. Not just a professional athlete, but a professional human being. He shows you what hard work can do.''

Alexander was a novelty his rookie season, a three-way player who saw game action on the offensive line, defensive line and special teams. He made his name with hard work, smarts and big special teams hits.

In 2010, the Redskins (No. 25 in the AP Pro32) moved him to outside linebacker. Last year, he started learning the inside linebacker position. This year, it's his main focus on the only experienced alternative to starters London Fletcher and Perry Riley in the 3-4 scheme.

Alexander's weight loss has been noticeable during training camp. He broke up a pass over the middle to Santana Moss during Wednesday's practice, the type of play he couldn't have made when he was a lot heavier.

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Redskins' Alexander shrinks to play linebacker

Public release date: 14-Aug-2012 [ | E-mail | Share ]

Contact: David Ruth david@rice.edu 713-348-6327 Rice University

A Rice University researcher and his colleagues have received a National Institutes of Health grant to see how delays in gene transcription life's most basic messaging system affect cellular processes.

Matthew Bennett, an assistant professor of biochemistry and cell biology, will receive more than a million dollars over five years to gather and combine data from computer simulations and live cells. The goal is to create techniques to generate and analyze models of gene networks that incorporate delay as part of their process.

"Delay in transcriptional signaling is an unavoidable consequence of the way biochemistry works," said Bennett, a theoretical physicist by training who turned to synthetic biology as a postdoctoral researcher before joining Rice in 2009. "Once a gene is activated, often as a response to a molecule being introduced into the cell, it takes time for the results to come to fruition. Eventually the DNA must be transcribed into RNA, and the RNA must be translated into protein. Then, sometimes, the protein has to be modified or has to fold."

Bennett and his team want to know precisely what happens and why in that cascade of events, which can take minutes. "We want to be able to create accurate mathematical models of gene networks in order to predict how they function and how they fail, so we can design new synthetic networks and know what they're going to do before we build them," he said.

Synthetic biology has become an increasingly hot topic as researchers create biological systems not found in nature. (A leader in the field, J. Craig Venter, will speak at Rice on Oct. 10 as part of the university's Centennial Celebration.)

Bennett sees the process as similar to sophisticated electronic design, in which the genetic equivalent of logic gates can be used to program circuit-like behavior in living things. The resulting genomes can be used in cells for information processing, materials fabrication, chemical sensing, the production of energy and even food.

"We've learned that delays can have a significant impact on the function of genetic networks, and the discoveries have changed our fundamental understanding of how genes talk to one another," Bennett said. "There are many processes in cells that require specific timing in order to operate: Stress responses, circadian oscillations, cellular growth and division. We've found the dynamics of these networks are important to their function, and delay can have a profound effect. Understanding that delay and being able to model is critical for accurate computational simulations."

While simple models are able to help build simple cellular "circuits," Bennett felt a more sophisticated model will expand the possibilities for synthetic biology and lower the cost of engineering new synthetic microbes.

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NIH backs Rice University study of delay in gene transcription networks

Public release date: 13-Aug-2012 [ | E-mail | Share ]

Contact: Angela Hopp ahopp@asbmb.org 240-283-6614 American Society for Biochemistry and Molecular Biology

A research team at the University of California, Davis, has found that important and resourceful bacteria in the baby microbiome can ferret out nourishment from a previously unknown source, possibly helping at-risk infants break down components of breast milk.

Breast milk is amazingly intricate, providing all of the nutrients necessary to sustain and strengthen infants in the first months of life. Moreover, this natural source of nutrition provides protection from infections, allergies and many other illnesses.

Breast milk also promotes the growth of protective bacteria in an infant's intestine. Because breast milk contains glycans (complex sugars) that infants cannot breakdown, it promotes the growth a specific type of bacteria, called bifidobacteria, that can process these glycans. While it is known that bifidobacteria avail themselves of the free glycans in breast milk, it was not known whether these bacteria could also obtain glycans that were linked to proteins. Such proteins are called glycoproteins, and they are abundant in breast milk.

The research team led by David A. Mills at the UC-Davis investigated the ability of bifidobacteria to remove glycans from milk glycoproteins. Their work was recently published in the journal Molecular & Cellular Proteomics.

Mills' group found that specific strains of bifidobacteria possessed enzymes capable of removing glycan groups from glycoproteins, enabling them to use these glycans as an additional food source. Surprisingly, one of the enzymes, EndoBI-1, was able to remove any type of N-linked glycan (glycans attached to proteins by the amino acid asparagine). This is unique among enzymes of this type and may provide a growth advantage for bifidobacteria in the infant intestine because the glycoproteins in breast milk have complex glycans attached.

Mills explains that the ability of EndBI-1 to remove a variety of complex N-linked glycans combined with its unusual heat stability make "this potentially a very useful tool in both food processing and proteomics/pharmaceutical research."

The team's work suggests that bifidobacteria do not primarily feed on the glycans from milk glycoproteins. However, the study did show that under the proper conditions bidfidobacteria can grow when protein-linked glycans are the only energy source.

"One obvious goal of this research is to find ways to translate the benefits provided by milk and bifidobacteria to at risk populations such as premature infants, malnourished children, among many others," Mills says.

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Protective bacteria in the infant gut have resourceful way of helping babies break down breast milk

The American Society of Biochemistry and Molecular Biology (ASBMB) named Caltech chemistry professor Shu-ou Shan a recipient of the 2013 Young Investigator Award. The award will be presented at the ASBMB annual meeting in Boston next April.

Shan was recognized for her research that addresses how "a novel class of nucleotide hydrolases drives the efficient and accurate delivery of newly synthesized proteins to their correct destinations."

"This award would not have been possible without the support from my subgroup and division and all the wonderful Caltech students and postdocs who work so hard," says Shan.

"We are extremely happy that ASBMB has selected Shu-ou Shan for the Young Investigators Award," said Jacqueline Barton, Arthur and Marian Hanisch Memorial Professor, professor of chemistry, and chair of the Division of Chemistry and Chemical Engineering at Caltech. "It is a testament to the hard work and dedication of Shan and her team here at Caltech."

Shan's research interfaces between chemistry and biology to understand fundamental cellular processes at the level of chemical and physical principles. More information about Shan's research group at Caltech can be found at http://shangroup.caltech.edu.

The ASBMB Young Investigator Award recognizes outstanding research contributions to biochemistry and molecular biology. The recipient must have no more than 15 years postdoctoral experience. Nominations for these awards are made by ASBMB members, but nominees need not be members. The award consists of a plaque, $5,000, transportation, and expenses to present a lecture at the 2013 ASBMB annual meeting.

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Caltech Chemist Wins ASBMB Young Investigator Award

10.08.2012 - (idw) Max-Planck-Institut fr Biochemie

The European Research Council (ERC) encourages excellent basic research in Europe in order to promote visionary projects and open up new interdisciplinary science areas. Three young group leaders of the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich succeeded in obtaining one of the coveted ERC Starting Grants. Spread over a period of five years, Esben Lorentzen, Andreas Pichlmair and Frank Schnorrer will receive 1.5 million each for their research projects. Due to their scientific achievements until now they were the winners against several thousand competitors. Delivery Service for Cilia Tiny hair-like structures (cilia) are found on the surface of most cells in the body, where they serve to move the cell, process external signals and coordinate the correct arrangement of the inner organs during development of the organism. To do this, cilia have to be supplied with the right building blocks. This is taken over by a complex transport system which is called intraflagellar transport (IFT). Defects in the IFT can lead to severe physical and mental disorders. Together with his research group Structural Biology of Cilia, Esben Lorentzen investigates how the system works. Using X-ray crystallography, the scientists could already decipher the structure of a subunit of the IFT complex, and others shall follow. These results could help avoid mistakes in the composition of the cilia and thus prevent the development of diseases.

Targeting Viruses When viruses enter our body across our mucosa, the immune system reacts promptly. Immune cells recognize the pathogens via signal molecules on the cells surface and initiate the appropriate maneuver. These molecular sensors for viruses are the research focus of Andreas Pichlmair and his research group Innate Immunity. If the viruses are successful and enter the cell, the pathogens take command and make the cellular metabolism work for them. It is still not known in detail how viruses alter the genetic activity and the protein production of the infected cells. To identify modified proteins and elucidate their importance for viral replication, Andreas Pichlmair and his colleagues utilize mass spectrometry among other methods.

Flying Power Packs The fruit fly Drosophila melanogaster possesses different kinds of muscles and therefore can perform various behaviors such as crawling, running and, of course, flying. With the help of targeted gene modifications, the scientists in Frank Schnorrers research group Muscle Dynamics investigate how muscles of the fruit fly develop at the right place in the body and how the contractile machinery within the muscles is assembled properly. By performing more than 25,000 flight tests, the scientists identified the essential switch gene Spalt, which enables Drosophila to fly. It initiates the development of the special flight muscles, which can contract 200 times per second. Spalt and its related genes are not only important for the development of the flight muscles in insects, but probably also for the proper functioning of human heart muscles. In the future, Frank Schnorrer wants to understand how flight muscles achieve their special properties through the influence of Spalt.

Contact Dr. Esben Lorentzen Structural Biology of Cilia Max Planck Institute of Biochemistry Am Klopferspitz 18 82152 Martinsried E-Mail: lorentze@biochem.mpg.de http://www.biochem.mpg.de/lorentzen

Dr. Andreas Pichlmair Innate Immunity Max Planck Institute of Biochemistry Am Klopferspitz 18 82152 Martinsried E-Mail: apichl@biochem.mpg.de http://www.biochem.mpg.de/pichlmair

Dr. Frank Schnorrer Muscle Dynamics Max Planck Institute of Biochemistry Am Klopferspitz 18 82152 Martinsried E-Mail: schnorrer@biochem.mpg.de http://www.biochem.mpg.de/schnorrer

Anja Konschak Public Relations Max Planck Institute of Biochemistry Am Klopferspitz 18 82152 Martinsried Tel. +49 89 8578-2824 E-Mail: konschak@biochem.mpg.de http://www.biochem.mpg.de function fbs_click() {u=location.href;t=document.title;window.open('http://www.facebook.com/sharer.php?u='+encodeURIComponent(u)+'&t='+encodeURIComponent(t),'sharer','toolbar=0,status=0,width=626,height=436');return false;} html .fb_share_link { padding:2px 0 0 20px; height:16px; background:url(http://www.eugenesis.com/wp-content/uploads/2012/08/29c1d78260e_icon.gif.gif?6:26981) no-repeat top left; } Share on Facebook Weitere Informationen: http://www.biochem.mpg.de/en/news - New Press Releases of the MPI of Biochemistry http://erc.europa.eu/ - Website of the European Research Council (ERC) Anhang Press Release (PDF)

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About 4.5 Million Funding for Group Leaders at the MPIB

NASA-JPl / Reuters

This artist's concept depicts the moment that NASA's Curiosity rover touches down onto the Martian surface

Barreling in from space at 13,000 mph before stopping a mere 25 feet above the ground would make anyone want to catch their breath, and NASAs Curiosity rover is no exception. Now that the Seven Minutes of Terror is over, the compact-car-sized biochemistry lab is spending its first two weeks doing the same thing you might do after stepping off a hair-raising roller coaster: making sure its parts are where theyre supposed to be and functioning correctly.

That means daily surprises, as technicians at the Jet Propulsion Laboratory in La Canada Flintridge, Calif., raise antennas, activate cameras, and gradually bring systems on line. Among the early treats: 297 black-and-white thumbnail pictures, which NASA processed into a low-quality video showing the final two-and-a-half minutes of Curiositys stomach-churning plunge through the Martian atmosphere. The thumbnails, though grainy, show the protective heat shield dropping away, the bumps from the rovers parachute descent, and dust kicking up as cables lowered the rover to the Martian surface. Scientists expect to have a full-resolution video from Curiositys descent imager in a few days.

(PHOTOS: An Inside Look at the Mars Curiosity Rover)

The rover also sent a new postcard: the first full-color landscape image of Curiositys Gale Crater home, taken as part of a focus test to check one of the cameras mounted on the rovers mast. Until this week the camera, called the Mars Hand Lens Imager (MAHLI),hadnt moved its focal components since July 2011four months before Curiosity launched. Even now, with the mast still tucked horizontally atop the rovers front left shoulder, the cameras initial focus test offers a tempting glimpse of the north wall of the rim at Gale Crater.

But thats just a small taste of what this particular camera, one of 17 aboard Curiosity, will provide once the mast is lifted and extended, especially once the cameras clear dust covers lift away. Its so awesome because we can put this camera anywhere, says Ken Edgett of Malin Space Science Systems in San Diego, which operates the camera. Up, down, within an inch of the soil, underneath the rover, anywhere. Itll extend up above the mast to give us the giraffes-eye view, or give us the oblique, dogs-eye view across the Martian surface. This camera can look wherever we want.

Many of this weeks most captivating images havent come from Curiosity but a high-resolution camera aboard the Mars Reconnaissance Orbiter, another player on NASAs robotic exploration team. One day after capturing a stunning shot of Curiosity parachuting towards Martian surface, the Orbiter executed an unusual 41-degree roll to deliver a fascinating crime scene image taken by a high-resolution camera aboard the Mars Reconnaissance Orbiter some 186 miles above the surface. The view offers a look at the pimple-sized rover in relation to the locations where Curiositys heat shield, parachute, back shell, and ballyhooed sky crane crash-landed after dropping away from the rover during its descent.

(Cover Story: Live From Mars)

Simply put, theyre all in the same Gale Crater neighborhood. The heat shield is farthest from Curiosity, about three-quarters of a mile away. Both the back shell and sky crane wound up about four-tenths of a mile from the rover. Of particular visual interest is a jagged pattern in the Martian soil to one side of the downed sky crane. Those dark areas downrange are the disturbed dust, says Sarah Milkovich, a JPL scientist. Its the same pattern we see when we have meteorites forming impact craters on the surface of a planetary body. Since the impacts from the spacecrafts components kicked up plenty of dust as well, Milkovich says future images should have even greater resolution. The Orbiter will again aim its cameras at Gale Crater in a few days, possibly for color photos.

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After the Descent: Mars Rover Preps for Thrilling Expedition

Biochemistry and the self-reinforcing upward spiral of success.

The past century of science has demonstrated the pivotal role of biochemistry in such human phenomena as love, attraction, and lust. But to consider that individual neurobiology might impact things as rational and complex as, say, stock markets seems rather radical. Yet that's precisely what trader-turned-neuroscientist John Coates explores in The Hour Between Dog and Wolf: Risk Taking, Gut Feelings and the Biology of Boom and Bust (public library) -- an ambitious look at how body chemistry affects high-stakes financial trading, in which Coates sets out to construct -- and deconstruct -- a "universal biology of risk-taking."

One particularly fascinating aspect of risk-taking has to do with what is known as "the winner effect," a self-reinforcing osmosis of the two key hormones driving the biochemistry of success and failure -- testosterone, which Coates calls "the hormone of economic bubbles," and cortisol, "the hormone of economic busts." In traders -- as in athletes, and in the rest of us mere mortals when faced with analogous circumstances -- testosterone rises sharply and durably during financial booms, inducing a state of risk-seeking euphoria and providing a positive feedback loop in which success itself provides a competitive advantage. By contrast, the stress hormone cortisol spikes during financial downturns; traders with sustained high levels of cortisol become more risk-averse and timid, ultimately being less competitive.

Coates explains:

The euphoria, overconfidence and heightened appetite for risk that grip traders during a bull market may result from a phenomenon known in biology as the 'winner effect.'

[...]

Biologists studying animals in the field had noticed that an animal winning a fight or a competition for turf was more likely to win its next fight. This phenomenon had been observed in a large number of species. Such a finding raised the possibility that the mere act of winning contributes to further wins. But before biologists could draw such a conclusion they had to consider a number of alternative explanations. For example, maybe an animal keeps winning simply because it is physically larger than its rivals. To rule out possibilities such as this, biologists constructed controlled experiments in which they pitted animals that were equally matched in size, or rather that were equally matched in what is called 'resource holding potential,' in other words the total physical resources -- muscular, metabolic, cardiovascular -- an animal can draw on in an all-out fight. They also controlled for motivations, because a small, hungry animal eating a carcass can successfully chase off a larger, well-fed animal. Yet even when animals were evenly matched for size (or resources) and motivation, a pure winner effect nonetheless emerged.

An intriguing correlation, certainly, but what is the causal mechanism at work? Scientists have suggested that there are several elements at play: First, testosterone levels rise when animals face off, producing anabolic effects on muscle mass and hemoglobin, quickening reactions, improving visual acuity, and increasing the animal's persistence and fearlessness. Then, once the fight is over, the winning animal emerges with even higher levels of testosterone, and the loser with lower ones. Coates sums it up thusly:

Life for the winner is more glorious. It enters the next round of competition with already elevated testosterone levels, and this androgenic priming gives it an edge that increases its chances of winning yet again. Though this process an animal can be drawn into a positive-feedback lop, in which victory leads to raised testosterone levels which in turn leads to further victory.

So does this winner effect also occur in humans? Coates thinks so. He cites a study, in which researchers rigorously examined a database of 630,000 professional tennis matches and found that the winner of the first set had a 60% chance of winning the second one and, since the win in these matches comes down to the best of three sets, winning the match itself. (Anecdotally, a quick glance at Michael Phelps's Olympic scorecard would suggest a similar conclusion.)

See more here:
The Hormone Surges That Keep Winners Winning

DUBLIN--(BUSINESS WIRE)--

Research and Markets (http://www.researchandmarkets.com/research/bpl7ss/comprehensive_chir) has announced the addition of John Wiley and Sons Ltd's new book "Comprehensive Chiroptical Spectroscopy. Applications in Stereochemical Analysis of Synthetic Compounds, Natural Products, and Biomolecules" to their offering.

This book provides an introduction to the important methods of chiroptical spectroscopy in general, and circular dichroism (CD) in particular, which are increasingly important in all areas of chemistry, biochemistry, and structural biology. The book can be used as a text for undergraduate and graduate students and as a reference for researchers in academia and industry.

Experimental methods and instrumentation are described with topics ranging from the most widely used methods (electronic and vibrational CD) to frontier areas such as nonlinear spectroscopy and photoelectron CD, as well as the theory of chiroptical methods and techniques for simulating chiroptical properties. Applications of chiroptical spectroscopy to problems in organic stereochemistry, inorganic stereochemistry, and biochemistry and structural biology are also discussed, and each chapter is written by one or more leading authorities with extensive experience in the field.

Key Topics Covered:

PART I A HISTORICAL OVERVIEW

PART II ORGANIC STEREOCHEMISTRY

PART III INORGANIC STEREOCHEMISTRY

PART IV BIOMOLECULES

For more information visit http://www.researchandmarkets.com/research/bpl7ss/comprehensive_chir

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Research and Markets: Comprehensive Chiroptical Spectroscopy. Applications in Stereochemical Analysis of Synthetic ...

In an advance that could be used in masks to protect against nerve gas, scientists are reporting development of proteins that are up to 15,000 times more effective than their natural counterpart in destroying chemical warfare agents. Their report appears in ACS' journal Biochemistry.

Frank Raushel, David Barondeau and colleagues explain that a soil bacterium makes a protein called phosphotriesterase (PTE), which is an enzyme that detoxifies some pesticides and chemical warfare agents like sarin and tabun. PTE thus has potential uses in protecting soldiers and others. Natural PTE, however, works against only one of the two molecular forms of these chemical warfare agents, and it happens to be the less toxic form. The scientists thus set out to develop new versions of PTE that were more effective against the most toxic form.

To improve the enzyme's activity, Raushel and colleagues used an approach called "directed evolution." This technique imitates the way natural selection leads to improved forms of the biochemical substances in living things. In using directed evolution, the team made small random changes to the natural enzyme's chemical architecture and then tested resulting mutant enzymes for their ability to break down nerve agents. They isolated several mutants that fit the bill, including one that proved to be 15,000 times more effective than the natural enzyme.

More information: Enzymes for the Homeland Defense: Optimizing Phosphotriesterase for the Hydrolysis of Organophosphate Nerve Agents Biochemistry, Article ASAP. DOI: 10.1021/bi300811t

Abstract Phosphotriesterase (PTE) from soil bacteria is known for its ability to catalyze the detoxification of organophosphate pesticides and chemical warfare agents. Most of the organophosphate chemical warfare agents are a mixture of two stereoisomers at the phosphorus center, and the SP-enantiomers are significantly more toxic than the RP-enantiomers. In previous investigations, PTE variants were created through the manipulation of the substrate binding pockets and these mutants were shown to have greater catalytic activities for the detoxification of the more toxic SP-enantiomers of nerve agent analogues for GB, GD, GF, VX, and VR than the less toxic RP-enantiomers. In this investigation, alternate strategies were employed to discover additional PTE variants with significant improvements in catalytic activities relative to that of the wild-type enzyme. Screening and selection techniques were utilized to isolate PTE variants from randomized libraries and site specific modifications. The catalytic activities of these newly identified PTE variants toward the SP-enantiomers of chromophoric analogues of GB, GD, GF, VX, and VR have been improved up to 15000-fold relative to that of the wild-type enzyme. The X-ray crystal structures of the best PTE variants were determined. Characterization of these mutants with the authentic G-type nerve agents has confirmed the expected improvements in catalytic activity against the most toxic enantiomers of GB, GD, and GF. The values of kcat/Km for the H257Y/L303T (YT) mutant for the hydrolysis of GB, GD, and GF were determined to be 2 106, 5 105, and 8 105 M1 s1, respectively. The YT mutant is the most proficient enzyme reported thus far for the detoxification of G-type nerve agents. These results support a combinatorial strategy of rational design and directed evolution as a powerful tool for the discovery of more efficient enzymes for the detoxification of organophosphate nerve agents.

Journal reference: Biochemistry

Provided by American Chemical Society

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New substances 15,000 times more effective in destroying chemical warfare agents

Short-term supplementation with vitamin E may support the function of cells lining blood cells from potential damage during the increase in blood sugar levels after eating, says a new study.

Five days of supplementation with a gamma-tocopherol-rich mixture of tocopherols maintained vascular endothelial function the function of the cells lining blood vessels, according to findings published in the Journal of Nutritional Biochemistry .

The vitamin E supplement was also associated with supporting blood flow in the arteries and a reduction in increases of malondialdehyde (MDA - a reactive carbonyl compound and a well-established marker of oxidative stress).

This study demonstrates that short-term gamma-tocopherol-rich mixture of tocopherols supplementation in healthy men maintains vascular endothelial function that is otherwise impaired by postprandial hyperglycemia likely by decreasing lipid peroxidation [] without affecting inflammatory responses, report researchers from the University of Connecticut (USA) and Changwon National University (South Korea).

There are eight forms of vitamin E: four tocopherols (alpha, beta, gamma, delta) and four tocotrienols (alpha, beta, gamma, delta). Alpha-tocopherol is the main source found in supplements and in the European diet, while gamma-tocopherol is the most common form in the American diet.

Study details

Led by Richard Bruno, the researchers recruited 15 health men with an average age of 22 to participate in their randomized, crossover study. The men were randomly assigned to receive the vitamin E supplement or no supplement for five days prior to fasting and then receiving 75 grams of glucose.

The vitamin E supplement provided 500 milligrams of gamma-tocopherol, 60 mg of alpha-tocopherol, 170 mg of delta-tocopherol, and 9 mg of beta-tocopherol (Archer Daniels Midland, USA).

Results showed that the glucose test produced significant increases in MDA levels, and decreases of 30-44% in blood flow, as measured by brachial artery flow-mediated dilation (FMD). However, vitamin E supplementation prevented such changes, said the researchers.

The researchers also report for the first time that vascular endothelial function was maintained in the men after consuming the vitamin E supplement.

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Mixed vitamin E may support blood vessel health in healthy adults

Edward A. Dennis is Distinguished Professor of Chemistry and Biochemistry, and of Pharmacology in the School of Medicine at UCSD. He received his BA from Yale University in 1963 and a Ph.D. from Harvard University in 1967, a Doctorate in Medicine (honorary) from Goethe University in Frankfurt in 2008, and he served as a Research Fellow at Harvard Medical School 1967-69.

Edward Dennis

At UCSD, Dr. Dennis has served as Chair of the Department of Chemistry and Biochemistry, Chair of the Faculty Academic Senate, and on the Board of Overseers. He has also been Visiting Professor at several universities and is an adjunct professor at The Scripps Research Institute. He has authored 350 research publications, patented 15 inventions, and edited 13 books. Dr. Dennis was named an inaugural Fellow of the American Association for the Advancement of Science (AAAS) in 1984, and was the recipient of the American Society of Biochemistry and Molecular Biologys Avanti Award in Lipid Enzymology in 2000, the European Federation for Lipid Science and Technologys European Lipid Science Award in 2007, and Yale Universitys Yale Medal in 2008.

What brought you to La Jolla? On Jan. 1, 1970 I started on a cross-country drive to a little village on the other ocean for my first job as an assistant professor in the formative days of UCSD. It was a great move and I never looked back.

What are your favorite places to go in La Jolla? I enjoy walking on the La Jolla Shores beach, the Coast Walk cliff and alongside La Jolla Cove.

If you could snap your fingers and have it done, what might you add to improve La Jolla? Rebalance the human and animal interests in the Cove.

Who or what inspires you? Im inspired by the creativity, curiosity, and inventiveness of the many outstanding educational/research institutions of La Jolla.

If you hosted a dinner party for eight, whom (living or deceased) would you invite? It would be a potluck six-course dinner, hosted by my wife and I with six memorable chefs, both past and present, each bringing their favorite dish. The list of chefs includes Julia Child, Pierre Troisgros, Tetsuya Wakuda, Alex Atala, Eric Pras and Thomas Keller.I

Tell us about what you are reading. The Entrepreneurial President, a recently published book about the leadership of Dick Atkinson, former Chancellor of UCSD and president of the University of California.

What would be your dream vacation? A flying tour of the greatest vineyards of the world starting in California and progressing south to Argentina and Chile, west to New Zealand, across Australia, on to South Africa, then to Germany, and finally, France.

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Edward Dennis of La Jolla takes scholarly approach to his long career in science