Chemistry and Biochemistry

The right zinc levels are key to human health, researchers find

Anonymous — Mon, 24 Jul 2023 17:39:30 +0000

The right zinc levels are key to human health, researchers find Anonymous (not verified) Mon, 07/24/2023 - 11:39

Rachel Sauer

Using innovative fluorescent sensors and computational modeling, �� Boulder biochemistry researcher Amy Palmer tracked naturally cycling cells to better understand an essential micronutrient

Zinc is one of those micronutrients that many people know they need but are otherwise a little vague on the particulars.

Unlike, say, calcium, which most people know can be gained from a glass of milk, or the potassium found in a banana, sources of zinc sometimes aren’t as well-known.

The unknowns about zinc further extend to how it works in the body. While research has demonstrated that zinc is essential for a host of vital functions—from cell growth and proliferation to DNA creation, immune system support, building proteins and many others—not much has been known about how zinc does its work. In fact, a lot of what scientists know about how zinc functions in the body, especially its role in growth, has been learned by studying its absence in cases of zinc deficiency.

Amy Palmer, professor of biochemistry, developed innovative technology to measure zinc in naturally cycling cells over 60 hours.

However, newly published research led by Amy Palmer, a professor in the University of Colorado Boulder Department of Biochemistry, sheds new light—fluorescent light, in fact—on zinc’s role in cell growth. The research shows that when zinc levels are too low or too high, all cell proliferation stops until zinc levels come back into an acceptable range. It also revealed a phenomenon the researchers called a “zinc pulse"—right after a cell divides, it experiences a transient increase in zinc that comes back down after about an hour.

Palmer and her research colleagues, post-doctoral research associate Ananya Rakshit and graduate student Samuel Holtzen, were able to arrive at this new understanding of zinc’s vital role by using genetically encoded fluorescent sensors that change color and give off light when zinc binds to them.

“For the field, these fluorescent sensors were a big breakthrough because they allowed us to measure and quantify zinc in individual cells over many hours,” Palmer explains. “We can watch the zinc as the cell gets ready to divide, as it divides and as the two daughter cells go through the same process.

“We need to understand at the cellular level why is it that zinc is required, where is it required, how much is required. One missing piece of the puzzle, particularly when we think of zinc supplementation, is understanding and knowing when cells need zinc and how much they actually need.”

Using fluorescence

Palmer, who is internationally recognized for her work in developing the fluorescent sensors that detect metals in cells without disrupting cell function, and her research colleagues used a bit of biochemistry and a bit of engineering to create a sensor that will bind to zinc and only zinc.

“These fluorescent reporters are less perturbing to cells, letting them naturally cycle, and they’re really the wave of the future for this field of research,” Palmer says. “My colleague Sabrina Spencer really pioneered the approach of studying naturally cycling cells, and we learned a lot from her and her lab. Our angle was to take these fluorescent reporters and create some specifically for zinc.”

When Palmer initiated her lab at ��, she and her colleagues began developing these fluorescent sensors, building on post-doctoral research that Palmer completed with her advisor, Roger Tsien. Tsien won the Nobel Prize in Chemistry for discovering and developing the green fluorescent protein, which he and other scientists used to track when and where certain genes are expressed in cells.

“What’s really fun about these fluorescent sensors is they’re made out of proteins that are genetically encoded,” Palmer says. “They have a DNA sequence, and that one piece of DNA encodes a protein that will bind to zinc.

“This color switch when it binds to zinc specifically, this was a big breakthrough. It’s easy to get a very small response, but it’s harder to get a really big, robust response that can be used to track cells over 60 hours. We went through a lot of iterative optimization of our tools to get them to work the way we want.”

The effort paid off, though, because a lot of previous research added chemicals to cells to stop them from dividing or removed their growth serum—a process that could also remove zinc. Then, removing the chemical or adding the growth serum reinitiated cell division, aligning the cells so that they were all doing the same thing at the same time. That scenario, however, is not representative of what happens in a human body.

By introducing the fluorescent reporters to cells, Palmer and her colleagues could not only measure zinc levels, but also track each individual cell over 60 hours. Working with naturally cycling cells allowed the cells do their normal business in real time. Then, the researchers computationally figured out what state each cell was in and how much zinc it contained at each point during that time.

Implications for nutrition and disease

Palmer’s research was not only important because of the innovative tools being developed and used to study the cell cycle, but because zinc’s essentiality is not widely known yet the impacts of zinc deficiency can be significant. �� 17% of the world’s population is zinc deficient and zinc deficiency represents a public health crisis in some parts of the world.

Palmer and her co-researchers found that a cell experiences a “zinc pulse" right after it divides and has a transient increase in zinc that comes back down after about an hour.

Severe zinc deficiency can result in slowing or cessation of growth and development, delayed sexual maturation, impaired immune function and wound healing and many others. However, scientists are just now beginning to understand when cells need zinc and how much of it they need.

By using fluorescent sensors to track zinc uptake in individual cells over 60 hours, Palmer and her co-researchers were able to discover the zinc pulse that occurs right after a cell divides.

“We don’t yet know exactly why that happens, but we speculate that the two new daughter cells need to bring in a lot of zinc to set up growth in the individual cell,” Palmer says. “If they don’t have that pulse then they can’t keep going and they have to pause.”

The researchers also saw that zinc levels need to be just right—if they’re too high or too low then cell function pauses until zinc levels return to normal. During that pause, they observed that cells struggled to make DNA.

Building on the results of the recently published study, undergraduate researchers in Palmer’s lab are studying the very high levels of zinc often found in breast cancer cells and why those cells don’t pause in response to high zinc levels the way healthy cells would. It’s almost as though cells have a safety switch that cancer is somehow able to bypass, Palmer says.

Digging deeper into when and why cells need zinc and how much of it may “have implications for understanding human nutrition at the whole-organism level, implications for understanding zinc dysregulation or dysfunction in disease,” Palmer says. “We’re really working to understand that set point and that fundamental mechanism that each cell has where it senses its zinc status and how, within a certain range, it can regulate how much zinc it has.

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Using innovative fluorescent sensors and computational modeling, �� Boulder biochemistry researcher Amy Palmer tracked naturally cycling cells to better understand an essential micronutrient.

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Chemist to study molecular inner workings of Alzheimer’s disease

Anonymous — Wed, 05 Jul 2023 17:00:16 +0000

Chemist to study molecular inner workings of Alzheimer’s disease Anonymous (not verified) Wed, 07/05/2023 - 11:00

Jaxon Parker

Maciej Walczak, �� Boulder associate professor of chemistry, won a $2 million NIH grant to investigate how certain sugars modify a brain protein associated with neurodegeneration

A research laboratory at the University of Colorado Boulder has won a $2 million grant from the National Institutes of Health to explore an uncharted region of Alzheimer’s disease: the chemical interaction of a protein called tau with biomolecules known as glycans.

On the surface, “there’s nothing special about tau. It was discovered in 1975 and was described as just a protein, and there are thousands of proteins in neurons,” says Maciej Walczak, an associate professor of chemistry at �� Boulder and the principal investigator of the Walczak Group.

“But in Alzheimer’s disease patients, that particular protein has an unusually high number of post-translational modifications compared to healthy individuals. We don’t know why that is.”

Maciej Walczak is researcher studying strategies to manipulate and understand the function of biomolecules in human health and disease.

Tau is found in all humans and is abundant in neurons, where it stabilizes the cell’s internal skeleton. Once the protein is produced, different molecules can attach themselves to tau, a process that is called post-translational modification, and change its structure, function and localization.

“Tau is like a string: It’s very floppy, flexible and binds to all sorts of things. It’s intrinsically disordered, which means it doesn’t have a stable structure,” Walczak says. “What that means is that all these residues on tau are available to different enzymes to add small molecules or modifications on the chain site.”

Alzheimer’s is a notoriously perplexing disease, with no treatment in sight after being discovered more than a century ago. Although in past decades most scientists have focused on the protein beta-amyloid as the main component of toxic plaques that cause neurodegeneration, tau was recently brought into the limelight as a key element to understanding the progression of Alzheimer’s.

The Walczak Group first started researching tau and its correlation with Alzheimer’s several years ago in a project led by Wyatt Powell, a PhD student in chemistry who is advised by Walczak.

Researchers in the Walczak Group include (front row, left to right) Kajal Thakur, Ruiheng Jing, (back row, left to right) James Greenwood, Maciej Walczak, Wyatt Powell and Patrick Holland.

“Neurodegeneration is very complex, so there won’t be any one specific factor. Most of the students in the lab are chemists who have a very unique take on this problem because they’re thinking very molecularly,” Walczak says.

With the NIH grant, the Walczak Group plans to study a specific molecular modification to tau that could be causing the spread of neurodegeneration: Glycosylation.

“You’re familiar with sugars and carbohydrates: You eat them, digest them; they’re a source of energy. That’s one role of sugars,” Walczak says. “Their second role is much more interesting from the biological perspective because when they’re added to proteins, they change their structure and function.”

In glycosylation, molecules of sugar known as glycans are added to proteins such as tau and change their structure, an example of post-translational modification. In Alzheimer’s disease patients, the glycosylation of tau is more prominent than in healthy people.

For the NIH project, “We would like to understand the molecular role of glycans attached to tau. Does it change their ability to aggregate and propagate?”

Because neurodegeneration is a progressive disease, toxic fibers of modified tau jump from neuron to neuron. Over several years or decades, large quantities of neurons are killed from this spread. “We want to understand how sugars modulate that process,” Walczak says.

It’s a very important and unsolved problem that will become more pressing because of the increasing aging population in the next few decades.

Although Walczak thinks the lab’s research into the glycosylation of tau is not focused on therapeutic discovery at the moment, he stressed that understanding Alzheimer’s molecular progression will help fill in critical gaps in our knowledge about the disease.

“It’s a very important and unsolved problem that will become more pressing because of the increasing aging population in the next few decades,” Walczak says. “And what I think is fascinating about this disease is that it has various factors, and we don’t really understand what those are.”

“That complexity and challenge has drawn me to pursue this direction. There are a number of fundamental discoveries to be made in the basic biology and mechanism of the disease,” Walczak says.

Walczak also emphasized the importance of the lab’s graduate students, who will be studying neurodegeneration by focusing on glycan’s modifications with various models such as stem cells.

“The modeling of the disease in the lab is very challenging because it’s such a slow process,” Walczak says. “I think we are very lucky we got the NIH grant because it will sustain us to really pursue our goals and create opportunities for new discoveries.”

Maciej Walczak, �� Boulder associate professor of chemistry, won a $2 million NIH grant to investigate how certain sugars modify a brain protein associated with neurodegeneration.

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�� Boulder’s Marvin Caruthers wins inaugural Merkin Prize in Biomedical Technology for developing technology that efficiently synthesizes DNA

Anonymous — Wed, 28 Jun 2023 20:51:25 +0000

�� Boulder’s Marvin Caruthers wins inaugural Merkin Prize in Biomedical Technology for developing technology that efficiently synthesizes DNA Anonymous (not verified) Wed, 06/28/2023 - 14:51

The $400,000 award recognizes the far-reaching medical impact of Caruthers’ development, in the early 1980s, of an efficient and fast method to synthesize nucleic acids

[video:https://www.youtube.com/watch?v=P8Pt-W0Wb40]

Marvin H. Caruthers explains the importance of developing technology for synthesizing DNA.

Marvin H. Caruthers, distinguished professor of chemistry and biochemistry at the University of Colorado Boulder, has won the inaugural Richard N. Merkin Prize in Biomedical Technology for developing an efficient, automated technology for synthesizing DNA.

The chemical reactions that Caruthers discovered in the early 1980s, which accurately and quickly assemble nucleotides into strands of DNA, provided an essential element in the development of modern molecular medicine, according to the Merkin Prize selection committee. Today, scientists use these reactions to produce customizable DNA and RNA molecules that enable genetic sequencing, drug and vaccine development, pathogen tests, cancer diagnostics, and many aspects of basic biomedical research.

“I am honored to acknowledge the incredible and transformative impact of Dr. Caruthers’ technology on human health over the last four decades,” said Dr. Richard Merkin, founder and CEO of Heritage Provider Network, one of the country’s largest physician-founded and physician-owned integrated health care systems. “He deserves our support and recognition. I hope this prize not only raises awareness of this work but underscores and encourages others to realize the broader importance of developing new scientific technologies to transform health care.”

The Merkin Prize, which recognizes novel technologies that have improved human health, carries a $400,000 cash award. The prize was created by the Merkin Family Foundation and is administered by the Broad Institute of MIT and Harvard.

Caruthers will be honored in a prize ceremony held this fall.

“I’m really very happy that this work is being recognized,” Caruthers said. “It’s been amazing to see the technology have such widespread use over the years.”

“The method developed by Dr. Marvin Caruthers was truly revolutionary. It exemplifies how a powerful technology can promote discovery and improve medical care. There are now whole fields of biology, medicine and public health that one cannot imagine practicing without his methods for synthesis of polynucleotides,” said Dr. Harold Varmus, chair of the Merkin Prize selection committee. Varmus is the Lewis Thomas University Professor at Weill Cornell Medicine, a senior associate at the New York Genome Center and a recipient of the Nobel Prize in Physiology or Medicine for his work on the origins of cancer.

More than 50 technologies and scores of scientists from around the globe who invented them were nominated for the 2023 Merkin Prize. Those nominations were evaluated by the selection committee, composed of eight scientific leaders from academia and industry in the U.S. and Europe.

Paving the Way for a Genetics Revolution

Today, scientists routinely manipulate genetic material to study human health and diagnose and treat disease. They sequence genes to diagnose inherited conditions and cancers, synthesize DNA and RNA strands by the millions to detect pathogens, manufacture drugs and edit the sequences of genes as potential therapy. Just a few decades ago, before the synthetic methodologies developed in the Caruthers laboratory, none of this was possible.

Caruthers is a �� Boulder distinguished professor of biochemistry and internationally recognized expert in chemical biology and genetics.

Born in 1940 in Des Moines, Iowa, Caruthers became enamored with science in the third grade, when his parents gave him a chemistry set. The color-changing liquids and exploding mixtures of chemicals fascinated him.

He went on to study chemistry at Iowa State University before joining the lab of Robert Letsinger at Northwestern University in 1963, a decade after the discovery of DNA’s double helix structure.

During his graduate education at Northwestern, Caruthers learned how to assemble nucleotides—the building blocks of DNA and RNA—into short sequences using methods Letsinger pioneered. But the approach was slow and inefficient.

“To make one little piece of synthetic DNA a few nucleotides long could take two months,” Caruthers recalled.

While at Northwestern, he assembled five nucleotides into a strand of DNA, representing a major breakthrough at the time. He then became a postdoctoral fellow in the University of Wisconsin lab of Gobind Khorana, who shared the Nobel Prize in Physiology or Medicine for discovering how the order of nucleotides in DNA encodes proteins. There, Caruthers became interested in how DNA was regulated and what its many sequences meant. Studying these problems was hard, though, without a way to build new pieces of DNA.

By the time Caruthers joined the chemistry and biochemistry department at the University of Colorado Boulder in 1973, he had set a goal to improve DNA synthesis.

“It was clear to me at the time that none of the current technologies were really very good for general, everyday use by most biologists,” he said. “But most scientists in the biological and biochemistry communities couldn’t care less.”

At conferences and in hallways, colleagues frequently questioned why he wanted to develop new methods to synthesize DNA; most did not see any benefit, Caruthers said.

Over the coming years, with significant contributions from graduate student Mark Matteucci and postdoctoral fellow Serge Beaucage, Caruthers’ lab tackled the problem. They first probed how to provide structural support for fragile, lengthening strands of DNA, and discovered that a highly porous silica glass known as “controlled pore glass” worked far better than the polystyrene that researchers had been using.

Colleagues frequently questioned why develop new methods to synthesize DNA; most did not see any benefit. Suddenly, in less than a day, you could make a piece of synthetic DNA that would have taken months using older methods."

Then, the team developed a chemical method to protect nucleotides from undergoing unwanted reactions during DNA synthesis — a major reason DNA synthesis had been so inefficient. Caruthers’ group discovered how to create protected “deoxynucleoside phosphoramidites” that didn’t undergo the unwanted reactions. This made the synthesis reaction far more efficient. A series of chemical reactions could be carried out again and again, with each new iteration successively adding a new nucleotide to a growing strand of DNA in a matter of seconds.

“Suddenly, in less than a day, you could make a piece of synthetic DNA that would have taken months using older methods,” Caruthers said.

A Lasting Impact

With the new technique, the Caruthers lab could rapidly synthesize strands of up to 30 nucleotides. In 1981, Caruthers and Matteucci described the controlled pore glass support in Journal of the American Chemical Society and Caruthers and Beaucage published the new approach for DNA synthesis in Tetrahedron Letters. Other scientists quickly began using the methods, and soon adapted the approach for synthesizing the other important polynucleotide, RNA.

At the same time, Caruthers imagined the technique could become even more widespread with machines to automate the repetitive process. He teamed up with world-leading protein scientist and systems biology pioneer Leroy Hood, then at the California Institute of Technology, to develop instruments for DNA and protein synthesis and protein sequencing, described in a seminal 1984 Nature paper. Together, the pair launched a company—Applied Biosystems—that would produce both machines.

“I knew from day one that if people had to make their own reagents and chemically synthesize DNA in their own labs, it was never going to take off,” Caruthers said. “If they could instead order DNA from a supplier, or have a really good machine to automate it, that could appeal to biologists.”

The Caruthers' lab is desinged to generate and manipulate DNA. Photo courtesy of Caruthers.

Caruthers’ foresight paid off. Such machines now produce strands of DNA hundreds of nucleotides long; DNA microchips can produce millions of these sequences at a time.

Today, scientists frequently synthesize short stretches of DNA to act as “primers,” binding to genes of interest for the purpose of sequencing those genes or making new copies of them. Caruthers’ technology was critical for developing polymerase chain reaction (PCR), which rapidly amplifies DNA or RNA so it can be detected or studied in greater detail. This technology also underlies many new diagnostic methods, including tests for COVID-19, for selection of cancer therapies and for noninvasive prenatal screening for fetal abnormalities.

Longer synthetic DNA and RNA molecules also are critical for modern biologic drugs. These strands of genetic material carry the instructions for cells to produce antigens and therapeutic proteins, with the potential to prevent or treat infectious and metabolic diseases and cancers.

“The ability to synthesize genetic information has changed the face of medicine,” said Varmus. “Synthesis of DNA and RNA is not only used directly for making diagnostics and therapies; its effects are magnified when you consider all the medical advances that have come out of research dependent on gene sequencing.”

Caruthers is a recipient of the National Medal of Science and an elected member of the National Academy of Sciences, the American Academy of Arts & Sciences, the National Academy of Inventors, and the National Inventors Hall of Fame. In addition to his role at Applied Biosystems, he is a co-founder of companies including Amgen, Array BioPharma, miRagen Therapeutics, SynGenis and ProGenis.

Nominations for the 2024 Merkin Prize will open in September 2023. Visit merkinprize.org for more information.

The $400,000 award recognizes the far-reaching medical impact of Caruthers’ development, in the early 1980s, of an efficient and fast method to synthesize nucleic acids.

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A long and winding road to success

Anonymous — Thu, 31 Jan 2019 23:41:39 +0000

A long and winding road to success Anonymous (not verified) Thu, 01/31/2019 - 16:41

Clay Bonnyman Evans

Army, non-traditional path at �� Boulder led Olester Benson to 2018 George Norlin Award

Olester Benson, Jr. chuckles when he remembers his first run at a college education. Though talented enough student to gain acceptance to Eckerd College, in his hometown of St. Petersburg, Florida, he acknowledges that his motivation for enrolling wasn’t exactly academic.

“It was the height of the Vietnam War, and I got the Selective Service classification 1A” — essentially, first in line for the draft, he says. “So, I enrolled in school primarily to get a deferment. Because my intentions and motivations were not what they should have been, I did not apply myself.”

Olester Benson.

After a year and a half, grades sagging, he was kicked out.

Yet, in an ironic twist, it was the very thing that he ran from that would eventually lead Benson to the University of Colorado Boulder, and his eventual winning in October of the prestigious George Norlin Award from the �� Boulder Alumni Association in recognition of his extensive career accomplishments and the untraditional path he took.

“His career and achievements are clearly a credit to the University of Colorado, and I am proud to have served a small part in his education,” wrote Tad H. Koch, professor of chemistry and biochemistry, in nominating his former student for the award.

After tiring of a series of “odd jobs,” he enlisted in the U.S. Army as part of the new, all-volunteer military, as an infantry soldier. By then, however, it was 1973 and he was not sent to Vietnam.

“The thing I ran away from was the thing that saved me,” says Benson, who went on to serve in the Army for 24 years, retiring as a master sergeant. “It gave me focus, made me much more disciplined and helped me grow up. I got to travel the world and encounter many more cultures and a lot of different types of people.”

The Army also paved the way for him to pursue the education that had previously eluded him, culminating in a PhD in chemistry from the University of Colorado Boulder in 1988 and a subsequent career as a top researcher with Minnesota-based 3M Corp.

Benson took his second run at higher education while serving at Fort Lewis, Washington, where he enrolled in a few math classes. When he was posted to Europe, he eagerly studied German, history, physics and other subjects to start building a “good, strong, liberal-arts background.”

When his Army hitch came to an end, he decided to re-enlist. But he wanted to prepare for a future in something that wasn’t “carrying a rifle.” He trained to be a medical and pharmacy specialist at the U. S. Army Academy of Health Sciences at Fort Sam Houston in San Antonio, Texas.

“The classes were taught by registered pharmacists, Army pharmacists and specialists,” he recalls. “I asked a lot of chemistry questions that they were not really able to answer, so what I did was sign up for evening classes in chemistry at San Antonio College.”

Sometimes it just takes that one little thing in life, for someone to take an interest in another person and say, ‘You can do this, we see this in you.’”

Posted to Fitzsimons Army Medical Center in Aurora in 1978, he hoped to enroll at �� Denver to continue studying chemistry. But by the time he arrived, enrollment had closed for the summer session, prompting him to petition the department head to ask for a late-enrollment waiver.

“Nothing ventured, nothing gained,” he says.

The gambit paid off in ways he could not have imagined. The department chair was Robert Damrauer, now associate vice chancellor for research at �� Denver. (He and Benson are shown at the top of the page.) Damrauer not only got Benson into classes right away, but later recognized his talent and urged him to pursue a graduate degree in chemistry. Then, he personally drove him to Boulder.

“Here I am, 30 years old, it’s 1982. Bob Damrauer comes to my house, takes me to the university, shows me around Boulder, shows me the department, introduces me to the professors. … He was so much more than just a teacher,” Benson says.

Still on active duty at Fitzsimons when he arrived at �� Boulder, he had earned a BA in chemistry from �� Denver, owned a home and was married with a young daughter. He became a “decidedly non-traditional student,” commuting nearly an hour each way, four days a week, to attend classes and labs.

He recalls how difficult it was to connect with his classmates and he missed out on joining study groups. Also, because his tuition was being paid largely by the U.S. Army, he did not need to teach to make ends meet.

“My contemporaries were all teaching assistants, but I never got that camaraderie or pedagogy of being a TA,” Benson says.

But, thanks to the Army and “just growing up,” at ��, Benson was a decidedly different student than the unfocused youth who failed chemistry and was asked to leave Eckerd College more than a decade earlier.

“At that fairly liberal Presbyterian college, class attendance was optional, and I took chemistry at 8 o’clock. Not a good idea,” he says, laughing. “At ��, I took the hardest classes at 8 o’clock and was alwaysthere ahead of schedule. In fact, I was incensed if the professor was late.”

After earning a PhD in 1988, a 3M recruiter interviewed him on campus, and he was soon hired.

“I’m still in the same research group I joined the first day. On Sept. 6, I celebrated my 30^thanniversary at 3M, and in those 30 years I’ve only moved 12 feet,” says Benson, who holds the company’s highest research title, corporate scientist.

Working at the corporate laboratory, he specializes in photochemistry, acquiring 71 patents and helping to design technology that has led to more than 300 products, from sandpaper to optical components on NASA’s Deep Space 1 spacecraft.

Among his other accolades, Benson received the Percy Julian Award from the National Organization of Black Chemists and Chemical Engineers, named after the first African-American inducted into the National Academy of Sciences.

He served for many years as a graduate recruiter for 3M, a position that allowed him to bring many �� and Colorado State University scientists to the company. He also served on the �� Boulder Graduate Student Advisory Council for nine years and has made significant donations to every school he has attended.

“I still give to my high school, even the school I dropped out of. I’m a Science Fellow of that school now,” he says.

He credits the then-all-female staff at the �� Boulder Veteran and Military Affairs Office for giving him the practical financial strategies to succeed as a veteran student.

“Even though I got off active duty in 1984,” he continued as a reservist until retiring from the Army in 1997. “I still had another four years. Other than my graduate stipend, my only other source of income was the GI Bill. The women in the (VMAO) knew the system so well, they helped me strategize about when to take my benefits to maximize my return,” Benson says.

He also praises Damrauer, Koch and other faculty for believing in him.

“I was privileged, I was blessed, to have professors at the university who saw my potential and who helped guide me and encourage me to get me through,” he says. “Sometimes it just takes that one little thing in life, for someone to take an interest in another person and say, ‘You can do this, we see this in you.’”

Army, non-traditional path at �� Boulder led Olester Benson to 2018 George Norlin Award.

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Biochemistry and cinema studies now have department status

Anonymous — Fri, 22 Jun 2018 16:17:52 +0000

Biochemistry and cinema studies now have department status Anonymous (not verified) Fri, 06/22/2018 - 10:17

At its regular meeting on Thursday at the �� Boulder campus, the University of Colorado Board of Regents voted to approve a new online Bachelor of Arts degree in interdisciplinary studies and two new departments for the Boulder campus.

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Nobel Laureate, MD-to-be shed light on epigenetic roots of cancer

Anonymous — Wed, 13 Jun 2018 20:53:21 +0000

Nobel Laureate, MD-to-be shed light on epigenetic roots of cancer Anonymous (not verified) Wed, 06/13/2018 - 14:53

Forty years after researchers first discovered it in fruit flies, a once-obscure cluster of proteins called PRC2 has become a key target for new cancer-fighting drugs, due to its tendency—when mutated—to bind to and silence tumor suppressing genes.

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National Academy of Sciences inducts two �� Boulder professors

Anonymous — Tue, 08 May 2018 23:40:45 +0000

National Academy of Sciences inducts two �� Boulder professors Anonymous (not verified) Tue, 05/08/2018 - 17:40

�� Boulder professors Natalie Ahn and Karolin Luger have been inducted into the National Academy of Sciences, an honor that recognizes "distinguished and continuing achievements in original research."

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Professors honored for work in cell signals, ultrafast lasers

Anonymous — Fri, 20 Apr 2018 21:33:22 +0000

Professors honored for work in cell signals, ultrafast lasers Anonymous (not verified) Fri, 04/20/2018 - 15:33

Two �� Boulder professors are among the latest group of scientists, politicians, artists and more elected to the American Academy of Arts and Science.

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2 �� Boulder faculty named 2017 National Academy of Inventors fellows

Anonymous — Tue, 19 Dec 2017 23:47:31 +0000

2 �� Boulder faculty named 2017 National Academy of Inventors fellows Anonymous (not verified) Tue, 12/19/2017 - 16:47

The National Academy of Inventors (NAI) named two �� Boulder faculty members to its class of fellows for 2017.

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Arthritis, autoimmune disease discovery could lead to new treatments

Anonymous — Mon, 20 Nov 2017 21:56:38 +0000

Arthritis, autoimmune disease discovery could lead to new treatments Anonymous (not verified) Mon, 11/20/2017 - 14:56

�� Boulder researchers have discovered a potent, drug-like compound that could someday revolutionize treatment of autoimmune diseases by inhibiting a protein instrumental in prompting the body to start attacking its own tissue.

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