SHENZHEN, China, Aug. 6, 2012 /PRNewswire-Asia-FirstCall/-- Mindray Medical International Limited (MR), a leading developer, manufacturer and marketer of medical devices worldwide, announced today its selected unaudited financial results for the second quarter ended June 30, 2012.

Highlights for Second Quarter 2012

"Despite the challenging environments in various international regions, we have once again achieved very solid performance in sales, profits and cash generation," commented Xu Hang, Mindray's chairman and co-chief executive officer. "All major geographical areas have delivered strong growth for the quarter. We are particularly encouraged by our good performance in developed markets, considering the volatility of those regions over the past year. We have also improved our gross margin and the healthy cash conversion cycle reflected our efforts in improving operational efficiency. In addition, we have launched new products in our IVD line and closed the orthopedics acquisition recently. Our reagent sales are continuing to accelerate. All of these are in line with the company's strategy to capture opportunities in the fast-growing consumable products markets. Going forward, we intend to prudentlydeploy our strong cashposition and continue to look for attractive investment opportunities worldwide."

SUMMARY Second Quarter 2012

(in $ millions, except per-share data)

Three Months Ended

June 30

2012

2011

% chg

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Mindray Announces Second Quarter 2012 Financial Results

Edward A. Dennis is Distinguished Professor of Chemistry and Biochemistry, and of Pharmacology in the School of Medicine at UCSD. He

Edward Dennis

received his BA from Yale University in 1963, 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.

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 a 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.

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.

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Edward Dennis takes scholarly approach to long career in science

Aug. 1, 2012

Susan Henry wins prestigious award in lipid biochemistry

Susan Henry, professor of molecular biology and genetics and the Ronald P. Lynch Dean of the College of Agriculture and Life Sciences (CALS) from 2000 to 2010, won the 2013 Avanti Award in Lipids, according to the August issue of the magazine of the American Society for Biochemistry and Molecular Biology, ASBMB Today.

The award recognizes outstanding research contributions in the area of lipids, naturally occurring molecules that are structural components of cell membranes involved in energy storage and signaling. Henry is noted for her research on regulation of lipid metabolism and lipid-mediated signaling, using yeast as a model system.

A fellow of the American Association for the Advancement of Science and the American Academy of Microbiology, Henry is also past chair of the National Institutes of Health Advisory Committee on Research on Minority Health.

As part of the honor, Henry has been invited to present a lecture at the 2013 ASBMB Annual Meeting, which will be held in Boston in April 2013.

##

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Susan Henry wins prestigious award in lipid biochemistry

01.08.2012 - (idw) Goethe-Universitt Frankfurt am Main

Ivan Dikic will receive the William C. Rose Award 2013 FRANKFURT. Prof. Ivan Dikic, Head of the Institute of Biochemistry II and Director of the Buchmann Institute of Molecular Life Sciences at the Goethe University Frankfurt, was awarded with the William C. Rose Award 2013, as announced today by the American Society for Biochemistry and Molecular Biology.

With this Award, the American Society for Biochemistry and Molecular Biology recognizes outstanding contributions of Ivan Dikic to biochemical and molecular biological research and in particular his pioneering work in understanding the Ubiquitin Code that regulates multiple biological processes. The Award consists of a plaque and 3.000 US$ and will the awarded at the Annual Meeting in Spring, 2013, where Prof. DIkic will be invited to present his research.

Ivan Dikic has been working at the Medical Faculty of the Goethe University in Frankfurt since 2002. More then 10 years ago, he started to concentrate his work on the Ubiquitin Research. Prof. Dikic showed that Ubiquitin acts as a multivalent cellular signal recognized by an expanding number of binding proteins that in turn translate this molecular signal into appropriate cellular phenotypes. His group have identified several novel Ubiquitin binding domains and used structural and functional studies to demonstrate their roles in the regulation of DNA repair, inflammation, receptor endocytosis, and proteasomal degradation. Despite their biological relevance, modern-day tools to study Ub chains in their physiological environment remain rudimentary and mainly focus on the biochemical characterization of chains, substrates or ubiquitin-binding domains (UBDs). Lately, Ivan Dikics group described the development and in vivo application of highly versatile chain-specific Ub sensors.

Informations: Prof. Ivan Dikic, Institut fr Biochemie II and Buchmann Institute for Molecular Lifesciences, Campus Niederrad, Tel.: (069) 6301-5652; ivan.dikic@biochem2.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://static.ak.facebook.com/images/share/facebook_share_icon.gif?6:26981) no-repeat top left; } Share on Facebook Weitere Informationen: http://www2.uni-frankfurt.de/42409151/038

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American Society for Biochemistry and Molecular Biology honors outstanding Scientists

Editor's Choice Main Category: Cancer / Oncology Also Included In: Biology / Biochemistry Article Date: 31 Jul 2012 - 12:00 PDT

Current ratings for: Cancer Research May Benefit From Recent Protein Discovery

4 (1 votes)

Esther Verheyen, an SFU professor of molecular biology and biochemistry, and her Master's of Science student Joanna Chen managed to reveal how Hipk, a protein kinase, can be manipulated to stop Yorkie, a protein that leads to overgrowth of cell tissue in eyes, legs and wings of flies, from causing tissue overgrowth in flies.

Hipk is an enzyme which deposits a phosphate residue on other proteins to control their activity, whilst the Yorkie protein, also known as 'Yap' in humans, causes overgrowth of cell tissue in the eyes, legs and wings of flies. Human tumors often contain high levels of Yap.

During experiments on Drosophila (fruit flies), the team discovered that Hipk was able to cause overgrowths, which were comparable with those found on tissue with too much Yorkie. The team then genetically modified the flies so that their normal organ and limb tissue contained a higher concentration of Yorkie and a lower concentration of Hipk.

Chen comments: "When we did that. Yorkie could not cause overgrowths anymore. We were able to show this need for Hipk to be present in a number of different fly tissues, such as the eyes, legs and wings."

Verheyen continued:

Next we tested a mutant form of Hipk that had lost its ability to add phosphates to Yorkie. This form of Hipk could no longer prompt Yorkie to trigger cell proliferation or do anything to regulate cell growth. Hipk is the first discovery of a protein kinase that regulates Yorkie by stimulating its cell proliferation ability. All other known protein kinases either directly inhibit or block Yorkie from working."

According to Verheyen and Chen, the discovery is causing great excitement in the molecular biology science community. Chen who graduated in June, and who will be working as a research assistant at the Vancouver Prostate Centre in August, explains:

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Cancer Research May Benefit From Recent Protein Discovery

Public release date: 26-Jul-2012 [ | E-mail | Share ]

Contact: Natasha Pinol npinol@aaas.org 202-326-6440 American Association for the Advancement of Science

When Brian White was a child, his kindergarten teacher wrote in his student record that he would only talk to the other children if the topic was science. Throughout his childhood, White's fascination with science led him to take batteries apart, blow things up, and to build radios and computer components.

Now an associate professor in the biology department at the University of Massachusetts, Boston, White is the winner of the Science Prize for Inquiry-Based Instruction (IBI). He won the award for his creation of Aipotu, a computer-simulated world in which students apply the tools of genetics, biochemistry, molecular biology and evolution to develop an understanding of the formation of color in a flower.

"What I'm trying to do is give people the tools to play around," says White, who explains that Aipotu is "utopia" backward. "What I've always liked about science is what you could do with what you learned."

Science's IBI Prize was developed to showcase outstanding materials, usable in a wide range of schools and settings, for teaching introductory science courses at the college level. The materials must be designed to encourage students' natural curiosity about how the world works, rather than to deliver facts and principles about what scientists have already discovered. Organized as one free-standing "module," the materials should offer real understanding of the nature of science, as well as providing an experience in generating and evaluating scientific evidence. Each month, Science publishes an essay by a recipient of the award, which explains the winning project. The essay about Aipotu will be published on July 27.

"We're trying to advance science education," says Bruce Alberts, editor-in-chief of Science. "This competition provides much-needed recognition to innovators in the field whose efforts promise significant benefits for students and for science literacy in general. The publication in Science of an article on each laboratory module will help guide educators around the globe to valuable free resources that might otherwise be missed."

After many hours of experiments in his parents' basement, White went on to MIT for his undergraduate work. Many of his classes were lectures, but by his junior year, he was able to take a class that had him in the lab all afternoon every day.

"I cooked up many harebrained experiments," White says. "In the lab, you learn problem-solving. Most of the time, what you attempt doesn't work, so you have to figure out why."

Throughout his education, White had some wonderful teaching experiences, he says, including at a science camp in Woods Hole, Massachusetts, where one of his students built a pinball machine that kept score. White said demonstrating the machine to the student's parents was an amazing moment, one of many that White had early on that drew him into education.

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Science magazine prize goes to virtual world where undergrads explore DNA

Chris Neaves, a student and musician, died of undetermined causes July 21 at his Columbia home. He was 21.

Born David Christopher Neaves in Lewisville, Texas, he moved to Howard County in 2006 after spending three years in Windsor, England, with his family, where he attended the TASIS American School and played rugby. He was a 2010 graduate of Chapelgate Christian Academy in Marriottsville. He spent a year at Clemson University in Clemson, S.C.

At his death, he was a biochemistry student at Howard Community College and worked as a lot attendant at Antwerpen Toyota in Clarksville.

Family members said he enjoyed snow skiing and fly fishing at Copper Mountain, Colo. A guitarist he owned numerous instruments and vocalist, he once performed at the Rock and Roll Hotel in Washington, D.C.

Active in a church youth group, he made three trips to Guatemala, where he worked with schoolchildren. He was fluent in Spanish.

Services will be held at 1 p.m. Thursday at Chapelgate Presbyterian Church, 2600 Marriottsville Road in Marriottsville.

Survivors include his parents, David Neaves, chief financial officer for Onemain Financial, and Lori Holman Neaves, a homemaker; a sister, Katie Neaves, all of Ellicott City; his maternal grandparents, Jack and Elizabeth Holman; and his paternal grandmother, Linda Neaves, all of Little Rock, Ark.

jacques.kelly@baltsun.com

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Chris Neaves, biochemistry student

Public release date: 24-Jul-2012 [ | E-mail | Share ]

Contact: Angela Hopp 240-283-6614 American Society for Biochemistry and Molecular Biology

Human defensins, aptly named antimicrobial peptides, are made in immune system cells and epithelial cells (such as skin cells and cells that line the gut). One of these peptides, human neutrophil peptide 1, under certain circumstances hinders HIV infection, but exactly how it works remains unclear.

HIV entry into mature T-helper cells (cells essential to the immune system) proceeds by attachment of the virus to specific targets on T-helper cells, uptake of the virus, fusion of its envelope with the cell membranes, and release of the virus into the cells. In a forthcoming Journal of Biological Chemistry Paper of the Week, Gregory Melikyan at Emory University and colleagues investigated the ability of human neutrophil peptide 1 to impede each step of this process.

Using model cell lines, Melikyan's group showed that human neutrophil peptide 1 effectively prevented HIV entry into cells in multiple ways. First, human neutrophil peptide 1 reduced the number of specific targets on the cells available for HIV attachment. Second, this defensin also bound to specific targets on both the HIV envelope and the cells, preventing early and late stages of HIV-cell fusion. Finally, human neutrophil peptide 1 prevented HIV uptake into the cells without compromising the general ability of the cells to engulf other molecules.

While human neutrophil peptide 1 hinders HIV entry into cells under these lab conditions, it does not do so as effectively in the presence of serum -- meaning that it may not be as successful at blocking HIV in our bodies. But Melikyan's team showed that human neutrophil peptide 1 remained attached to its specific targets in the presence of serum, despite its reduced efficacy. Their work suggests that the structure of human neutrophil peptide 1 is important for its anti-HIV activity, and they propose that serum may interfere with the ability of this defensin to form complexes, reducing its ability to block HIV.

"Our work provides new insights into the ability of defensins to recognize and neutralize diverse pathogens, including HIV," Melikyan says. This research reveals that human neutrophil peptide 1 can bind various viral and cellular targets and that a previously unappreciated feature is essential for its anti-HIV activity, possibly its propensity to form large complexes, Melikyan explains.

The team's findings suggest a new avenue of research for combatting HIV and viruses that infiltrate cells in a similar manner.

###

From the article: "Multifaceted mechanisms of HIV-1 entry inhibition by human alpha-defensin" by Lusine H. Demirkhanyan, Mariana Marin, Sergi Padilla-Parra, Changyou Zhan, Kosuke Miyauchi, Maikha Jean-Baptiste, Gennadiy Novitskiy, Wuyuan Lu, and Gregory B. Melikyan (to be published in the Aug. 17 issue of the Journal of Biological Chemistry and currently online as a Paper in Press at http://www.jbc.org/content/early/2012/06/25/jbc.M112.375949.full.pdf)

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Under the right conditions, peptide blocks HIV infection at multiple points along the way

DUBLIN--(BUSINESS WIRE)--

Research and Markets (http://www.researchandmarkets.com/research/m5pjfs/biomedical_hydroge) has announced the addition of Woodhead Publishing Ltd's new book "Biomedical Hydrogels: Biochemistry, Manufacture and Medical Applications" to their offering.

Hydrogels are very important for biomedical applications because they can be chemically manipulated to alter and control the hydrogel's interaction with cells and tissues. Their flexibility and high water content is similar to that of natural tissue, making them extremely suitable for biomaterials applications. "Biomedical hydrogels" explores the diverse range and use of hydrogels, focusing on processing methods and novel applications in the field of implants and prostheses.

Part one of this book concentrates on the processing of hydrogels, covering hydrogel swelling behaviour, superabsorbent cellulose-based hydrogels and regulation of novel hydrogel products, as well as chapters focusing on the structure and properties of hydrogels and different fabrication technologies. Part two covers existing and novel applications of hydrogels, including chapters on spinal disc and cartilage replacement implants, hydrogels for ophthalmic prostheses and hydrogels for wound healing applications. The role of hydrogels in imaging implants in situ is also discussed.

With its distinguished editor and international team of contributors, "Biomedical hydrogels" is an excellent reference for biomedical research scientists and engineers in industry and academia, as well as others involved in research in this area, such as research clinicians.

Key features:

- examines the diverse range and use of hydrogels, focusing on processing methods and novel applications

- comprehensive book explores the structure and properties of hydrogels and different fabrication technologies

- covers important areas such as processing of hydrogels, covering hydrogel swelling behaviour, superabsorbent cellulose-based hydrogels and regulation of novel hydrogel products

Key Topics Covered:

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Research and Markets: Biomedical Hydrogels: Biochemistry, Manufacture and Medical Applications

National Autonomous University of Mexico uses dynamic light scattering for allosteric transition characterization

Using the Zetasizer V dynamic light scattering (DLS) system from Malvern Instruments, Professor Mario L. Calcagno and his team at the Biochemistry Department of the Faculty of Medicine, Universidad Nacional Autnoma de Mxico (UNAM, the National Autonomous University of Mexico) have been able to distinguish allosteric transition [structural rearrangements] in a single E. coli protein. Characterizing protein allostery is challenging because of its sensitivity to experimental conditions, however, a quantitative description of allosteric transition is important in understanding and controlling metabolic and other biochemical processes.

We use the Zetasizer V to characterize the size of proteins and how they interact to produce multimeric forms or even supramolecular arrangements of the protein such as viral capsids [shells], said Dr Ismael Bustos-Jaimes, from Laboratory of Physical Chemistry and Protein Engineering at UNAM commented The Zetasizer V allows us to work with sizes in the range of 1 nm to 500 nm and follow each assembly and stability parameter, such as pH, temperature and ionic strength, guiding us to the optimal production conditions for these virus-like particles.

The sensitivity of the Zetasizer V has additionally allowed my colleague, Prof Calcagno, to analyze allosteric transitions explained Dr Bustos-Jaimes. The size of the hexameric glucosamine-6-phosphate deaminase protein from E. coli changes its shape to a more compact form upon allosteric-activator binding, and this change can be measured.

The Zetasizer V software is user-friendly and in addition to measuring particle size it delivers information about the quality of sample preparation. This is very important when you work with molecules which are prone to uncontrolled aggregation, said Dr Bustos-Jaimes.

The UNAM team studies allosteric transitions and the assembly of virus-like particles (VLPs) for use in diagnostics and disease control. VLPs are biological nanoparticles that resemble natural viruses but contain no genetic material. As non-infective agents, they are suitable for use in the analysis of viral infection mechanisms, vaccine production, tissue-specific drug delivery and as biological nanomaterials.

The Zetasizer V is part of a range of Zetasizer dynamic light scattering systems from Malvern Instruments. For more information, visit http://www.malvern.com/zetasizer

About Malvern Instruments Malvern Instruments is a market leader in measuring performance controlling material properties. These include particle size, particle shape, zeta potential, molecular weight, size and conformation, rheological properties and chemical identification. Malvern delivers the systems, support and expertise that ensure the analytical integrity and productivity needed to drive research, development and manufacturing.

Malverns measurement solutions for scientists, technologists and engineers advance continually through customer collaboration. Complementary materials characterization systems deliver inter-related measurements that reflect the complexities of particulates and disperse systems, nanomaterials and macromolecules. Combining intelligently implemented technologies with in-depth industry applications knowledge and support, Malvern provides customers with the competitive advantage they demand.

Headquartered in Malvern, UK, Malvern Instruments has subsidiary organizations in all major European markets, North America, China, Japan and Korea, a joint venture in India, a global distributor network and applications laboratories around the world. For more information, visit http://www.malvern.com

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Zetasizer µV Used In Measuring Protein Structural Transition

The Irish Times - Tuesday, July 17, 2012

DOMINIC COYLE

Q&A:Last June I completed a biochemistry degree in Dublin and moved to England to start graduate medicine. When I started to look for ways to finance the degree, I hit about a 100 brick walls. My parents are not in a position to fund me.

I went to the local branch of the bank, where I have always banked, and was told there were no such loans for graduate students but to apply for a student loan with a reduced rate APR. Although a four-year course, I was told to apply for the funds for year one and to review it in year two.

The initial 11,000 interest- only facility proved to be too little. When I went to top up my loan to 20,000, the student officer became involved. She was surprised that a loan for the four years wasnt put in place, but when I tried to get a four-year plan in place for a loan of 80,000, I was told I would need to put up front some sort of security. They released the extra money for first year but are looking for that security before releasing more funds and that they will probably want me to start full repayments on the loan.

The bank said they could look at topping up my parents mortgage on an interest-only basis and they could give me that money, but their mortgage isnt with the AIB. I cannot afford to make full repayments either until I am a qualified doctor in 2015. Essentially, I am making the interest repayments from the loan money.

I need to find a solution as my funds will dry up in August and if I cannot get the financial support I will have to quit college to get a job and pay back this 20,000 the bank has already given me.

Ms S.OB., England

There are two issues here. First, you are in an incredibly difficult position because of the rules covering grant aid across national boundaries; second, your bank appears to have been, at best, unhelpful in the mixed messages it has given on funding options, especially in your original application for financial support.

Desperate to fund your course, you have embarked without a clear four-year funding plan. I dont have a clear answer for you and am running your query as much in the hope that someone may provide an answer to your plight as anything else. If colleges are accepting cross-border students, I would assume there must be some funding options available as not everyone is in a position to fund 80,000 or more from their own, or their parents, resources.

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Bank won't fund my medical course in England

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

Contact: Kathleen Phillips ka-phillips@tamu.edu 979-845-2872 Texas A&M AgriLife Communications

COLLEGE STATION Top-notch molecular research swung into gear at Texas A&M University this week literally.

A crane lowered a high-field 800 megahertz Nuclear Magnetic Resonance spectrometer through an opening in the roof of a biochemistry and biophysics building Wednesday, putting the university on par with leading U.S. research institutions, according to Dr. Gregory Reinhart, department head.

The German-made instrument, which was flown on a cargo plane accompanied by an engineer and transported to the Texas A&M campus on a special truck, is expected to be fully operational by the first of September.

The Nuclear Magnetic Resonance technique, commonly called NMR, is the forerunner of the more widely known MRI. Reinhart explained that an MRI makes images of human tissue for medical diagnostics, but NMR makes images at the molecular level for scientific exploration.

"This is a major step forward in the capability of the university in the general area of structural biology," said Reinhart, whose department collaborated with Texas AgriLife Research, a part of the Texas A&M System, to obtain the equipment.

The equipment will benefit researchers from across Texas A&M, officials noted.

"We are excited to partner with Texas A&M University to bring this powerful instrument to campus," said Dr. Craig Nessler, AgriLife Research director. "It is critical that we find ways to collaboratively provide such state of the art equipment to our scientists to maintain our research competitiveness."

Structural biology means looking at macromolecules which consist of hundreds or thousands of atoms and then deducing the way these are built and how they move, Reinhart said. Knowing how the molecules work helps scientists create solutions for a variety of needs.

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Science goes through the roof

Eagle photo by Dave McDermand Workers carefully line up placement Thursday for a super-conducting magnet that arrived on Texas A&Ms West Campus.

A 100-ton crane sat outside Texas A&M Universitys biochemistry and biophysics building Thursday not an uncommon site for the construction-heavy campus.

But the cranes presence had nothing to do with raising another new building. Instead, it was there to lift a four-metric-ton, 800 megahertz Nuclear Magnetic Resonance spectrometer through an opening in the roof of the building.

The installation of the NMR, which will be complete in two to three months, puts A&M on par with other top national research institutions, Dr. Gregory Reinhart, head of the biochemistry and biophysics department, said.

NMR spectroscopy functions similar to the way an MRI takes images of the body, Reinhart said. NMR was developed first, and expanded into the imaging technique known as MRI. NMR, however, allows for higher precision for molecular information.

In NMR, we dont look at large objects, rather we look at individual molecules, like proteins and nucleic acids, Tatyana Igumenova, assistant professor and director of the NMR facility, said. This kind of instrument will allow us to determine the structure and dynamics of those molecules.

The NMR will be extremely powerful for research in drug design, Igumenova said.

You can identify potential drug candidates and use an NMR to determine where exactly they bind to the protein or enzyme, and what kind of effect they have on the structure and dynamics, Igumenova said.

With these capabilities, researchers will be able to design improved inhibitors to prevent the spread of disease.

The NMR, along with the upgrade and relocation of two other instruments to the NMR facility, cost a total of $2.7 million. The NMR itself cost more than $2 million, Reinhart said.

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Installation of new spectrometer gets under way on A&M campus

Norman Frederick Haard, a retired UC Davis food biochemist who found expression of his faith and science as a noted expert on fish, died June 29 of prostate cancer in Magalia, his family said. He was 70.

Dr. Haard was a pioneering researcher and teacher in the field of food biochemistry. He studied fruits and vegetables before devoting the last 25 years of his career to the sub-cellular biochemistry of fish and marine organisms.

He was a fellow of the Institute of Food Technologists and received prestigious awards for his research and contributions to fisheries technology. He advised and mentored more than 100 graduate students worldwide and established or aided food biochemistry programs in Canada, China, India, Mexico, Pakistan, Thailand and Uruguay.

He was a professor at Rutgers University in New Jersey and Memorial University in Newfoundland, Canada, before joining UC Davis in 1986.

"When we brought him in, we were looking for the best in the country for that type of work," retired UC Davis professor Larry Merson said. "That's what we got."

Fish were more than a research subject for Dr. Haard. An avid fisherman, he trolled waters in many countries and the Atlantic and Pacific oceans. His favorite meal was seafood, and he sat down to freshly boiled Maine lobster at dinner every Father's Day.

"He had a totally open mind about seafood," said his wife, Victoria. "In Japan, he ate live abalone, and he'd eat squid and octopus and eel. He would try anything."

The fisherman was also an important symbol of faith for Dr. Haard, who had a religious awakening soon after settling in Davis and became a devout Christian, his wife said. He was an active member of First Baptist Church in Davis and Ridge Presbyterian Church in Paradise. He supported missions and shared his scientific expertise in developing countries that rely on fish as a food staple.

He helped spread the word of God as a longtime member of The Gideons International. As distribution chairman for the Chico Gideon Camp, he placed thousands of Bibles at colleges, hotels and hospitals.

"He summed up his faith in the verse in Matthew (4:19), where Jesus says, 'Follow me, and I will make you fishers of men,' " his wife said.

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Obituary: UC Davis food biochemist Norman Frederick Haard

Newswise ST. LOUIS -- Alireza Ray Rezaie, Ph.D., professor of biochemistry and molecular biology at Saint Louis University School of Medicine, has received a $1.52 million NIH grant to study how the key blood clotting inhibitor antithrombin might be exploited to prevent premature death from heart disease.

The National Heart Lung and Blood Institute awarded the four-year grant, which will allow Rezaie to continue studying how to maintain the delicate balance between the life-preserving and life-threatening activity of blood clotting.

Blood clotting factors must be turned on and off at exactly the right time so a person does not bleed to death or die of an episode such as a heart attack, which is triggered by a blood clot, said Rezaie, who has engineered molecules that impose equilibrium on the delicate system.

Rezaie recently discovered that antithrombin, which is a molecule produced by the liver that turns off several proteins in the coagulation system, can block inflammation in the blood vessel wall. This inflammation can lead to heart disease as well as a violent, life-threatening reaction to blood infections called acute sepsis.

Rezaie is working on harnessing the anti-inflammatory activity of antithrombin to reduce the incidence and severity of heart disease and to save the lives of those who suffer from acute sepsis. He has studied the control of blood clotting factors for 23 years.

Blood carries nutrients and oxygen to the bodys organs and tissues as well as the ordnance of immunityantibodies and white blood cellsthat defend organs and tissues from infection. Given these critical functions, it is essential that bodies preserve blood against loss from bleeding injuries.

Imbedded in blood is the chemistry to stop bleeding before too much blood is lost. Whenever small cuts or bruises occur, the blood at the site of injury rapidly mobilizes clotting factors that build a plug at the breech in the blood vessel to prevent blood loss.

However, the ability to make blood clot is also the cause of vascular disease and sudden death for some when it is not controlled properly.

Efficient blood clotting can be a double-edged sword when clots appear at the wrong places and times. Heart attack, stroke and pulmonary embolism are life-threatening conditions stemming from clots that block blood circulation to the heart, brain or lung.

Currently, a patient who suffers a heart attack, stroke or pulmonary embolism is treated with heparin, a medication that prevents the formation of additional life-threatening blood clots. At the same time, heparin treatment puts patients at risk of uncontrolled bleeding by inhibiting antithrombin, which upsets the bodys normal response to injury and infections.

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True Blood: SLU Scientist Investigates Clotting Factors

Public release date: 11-Jul-2012 [ | E-mail | Share ]

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

Next week's Journal of Biological Chemistry "Paper of the Week" by Wai Mun Huang and colleagues at the University of Utah Health Sciences Center and the University of Minnesota reveals new insights into the molecular properties of the rod-shaped soil bacterium Agrobacterium tumefaciens, the pathogen responsible for crown gall disease, a tumor-forming infection in plants, such as tomatoes, walnuts, grapes and beets.

The bacterium is parasitic: It infects its plant host by entering through an open wound, inserts a small segment of its genetic code into the plant's genome, devours energy made by the plant, and forms knobby brown lesions on the plant stem.

Huang's group focused on the pathogen's genetic material. Most bacteria have circular chromosomes. But A. tumefaciens C58, the strain studied by Huang's group, contains one circular chromosome and one linear chromosome (along with two circular plasmids). Huang's research illuminates how this bacterium maintains its linear chromosome.

Huang's team ascertained the DNA sequence for the telomeres, or the protective end caps, of the linear chromosome in A. tumefaciens C58 and confirmed that an enzyme, TelA, actually forms them by making hairpin loops. These end caps are important for maintaining the stability of linear chromosomes. Interestingly, TelA also binds the telomeres. This activity is unique among bacterial enzymes of this kind and may protect the telomeres (which degrade over time and thus lose their ability to preserve DNA), as telomere binding proteins do in eukaryotes.

"Hairpin-ended linear chromosomes and plasmids are found in a number of branches of bacteria and viruses," Huang says. "They are simple and elegant to form and to maintain." But what remains to be understood is why this linear configuration is not more common or even the preferred configuration for bacteria, Huang emphasizes.

###

From the article: "Linear chromosome generating system of Agrobacterium tumefaciens C58: Protelomerase generates and protects hairpin ends" by Wai Mun Huang, Jeanne DaGloria, Heather Fox, Qiurong Ruan, John Tillou, Ke Shi, Hideki Aihara, John Aron, and Sherwood Casjens

Link to Paper in Press version of article: http://bit.ly/MfBz8C

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A deeper look into the pathogen responsible for crown gall disease in plants

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Dominican University of California associate professor Dr. Maggie Louie.

There will be no summer vacation for Dr. Maggie Louie, an associate professor of biochemistry at Dominican University in San Rafael.

Louie and her two student assistants are working through the summer, continuing their research into the role that the heavy metal cadmium plays in the incidence of breast cancer. She and her team have received more than $450,000 in grants from the National Cancer Institute at the National Institutes of Health to fund their work.

In April, Louie released research results that show cancer cells become increasingly aggressive the longer they are exposed to small concentrations of cadmium, commonly found in cosmetics, food, water and air particles. While other studies had previously shown links between acute cadmium exposure and breast cancer, Louie's study is one of only a few to link chronic cadmium exposure to the disease.

Now, Louie says she is investigating further to understand the biochemical process involved, and she believes she has found a protein that plays a key role.

"We've identified a potential player, which is stromal cell-derived factor-1 (SDF-1)," Louie said, "and we're trying to figure out how this small protein is being regulated by cadmium and what its role is in terms of increasing the cancer's ability to metastasize."

Louie said, "Unfortunately, cadmium is all around us. Cadmium is in our food, our water, our makeup, and our air."

Cadmium is produced mainly as a byproduct

Louie said many people believe there is nothing to worry about because the levels of exposure are so low. She, however, has her doubts.

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Dominican University professor explores links to breast cancer

Peter Cornish is the first at MU to be named a Pew Scholar.

By Brent Pearson

Published July 10, 2012

Nick Ehrhard/Senior Staff Photographer

Peter Cornish was recognized as a 2012 Pew Scholar in biomedical sciences. The Biochemistry assistant professor came to MU in 2010.

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Finding a treatment to HIV or cancer might not be far away for one MU professor.

Peter Cornish, a biochemistry assistant professor in the MU School of Medicine, became the first MU recipient of the Pew Scholar Award.

The Pew Scholars Program in the Biomedical Sciences provides funding to young investigators of outstanding promise in science relevant to the advancement of human health, the Pew Charitable Trusts website stated.

Cornish graduated from Graceland University with bachelor's degrees in biology, chemistry and mathematics in 2000. He received his doctorate in biochemistry from Texas Tech University in 2005. After five years of working in a post-doctoral program at the University of Illinois-Urbana-Champaign, Cornish arrived at MU in 2010, where he has conducted research on disrupting protein factories inside bacteria and viruses throughout the body.

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Biochemistry assistant professor recognized for HIV and cancer research

Public release date: 6-Jul-2012 [ | E-mail | Share ]

Contact: Timothy Wall walltj@missouri.edu 573-882-3346 University of Missouri-Columbia

COLUMBIA, Mo. -- The bacterium Escherichia coli (E. coli) has a rudimentary molecular "memory" that allows it to swim toward the richest sources of food. MU biochemistry professor Gerald Hazelbauer's continuing discoveries about how bacteria do this could shed light on human and animal sensory, memory and response systems.

"My doctoral work was with Julius Adler, the first scientist to study the molecules behind bacterial behavior. His work led to the discovery that bacteria have a molecular 'memory' system that allows them to 'remember' the past, compare it to the present and thus move toward the area that is most favorable," Hazelbauer said. "When I began my work as a researcher in the late 1960s, studying bacterial behavior was a curiosity and its significance unclear. Now, decades later, the research done by my group and others has grown into a body of knowledge about the fundamental processes used by all living things to recognize, remember and respond to changes in their environments."

The National Institute of General Medical Sciences (NIGMS) recently recognized and rewarded Hazelbauer's scientific contributions by granting him a "Method to Extend Research in Time" (MERIT) Award. The award, which is worth at least $5.5 million over 10 years, will allow him to continue his research without re-applying for funding. Hazelbauer joins only 11 other MU researchers who have received the MERIT award, including his wife, Linda Randall, who is also a biochemistry professor.

MERIT awards are intended to foster creativity and allow researchers to take more time to develop new techniques. The awards are given only to scientists who have proven themselves by succeeding in at least 10 years of previous NIGMS-funded research and who seem likely to continue making valuable contributions to their field.

Hazelbauer is professor and chair/director of biochemistry, a department/division jointly administered by the University of Missouri's School of Medicine and College of Agriculture, Food and Natural Resources. Linda Randall is the Wurdack Professor of Biological Chemistry in that unit.

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Originally posted here:
Like humans bacteria remember (if only for 4 seconds), says MU researcher

The bacterium Escherichia coli (E. coli) has a rudimentary molecular "memory" that allows it to swim toward the richest sources of food. MU biochemistry professor Gerald Hazelbauer's continuing discoveries about how bacteria do this could shed light on human and animal sensory, memory and response systems.

"My doctoral work was with Julius Adler, the first scientist to study the molecules behind bacterial behavior. His work led to the discovery that bacteria have a molecular 'memory' system that allows them to 'remember' the past, compare it to the present and thus move toward the area that is most favorable," Hazelbauer said. "When I began my work as a researcher in the late 1960s, studying bacterial behavior was a curiosity and its significance unclear. Now, decades later, the research done by my group and others has grown into a body of knowledge about the fundamental processes used by all living things to recognize, remember and respond to changes in their environments."

The National Institute of General Medical Sciences (NIGMS) recently recognized and rewarded Hazelbauer's scientific contributions by granting him a "Method to Extend Research in Time" (MERIT) Award. The award, which is worth at least $5.5 million over 10 years, will allow him to continue his research without re-applying for funding. Hazelbauer joins only 11 other MU researchers who have received the MERIT award, including his wife, Linda Randall, who is also a biochemistry professor.

MERIT awards are intended to foster creativity and allow researchers to take more time to develop new techniques. The awards are given only to scientists who have proven themselves by succeeding in at least 10 years of previous NIGMS-funded research and who seem likely to continue making valuable contributions to their field.

Hazelbauer is professor and chair/director of biochemistry, a department/division jointly administered by the University of Missouri's School of Medicine and College of Agriculture, Food and Natural Resources. Linda Randall is the Wurdack Professor of Biological Chemistry in that unit.

Provided by University of Missouri-Columbia

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Like humans bacteria remember (if only for 4 seconds), says researcher