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  • richardmitnick 4:46 pm on January 25, 2016 Permalink | Reply
    Tags: , Crouching Protein Hidden Enzyme, , Scripps Institute   

    From Scripps: “Crouching Protein, Hidden Enzyme” 

    Scripps
    Scripps Research Institute

    January 25, 2016
    Office of Communications
    Tel: 858-784-2666
    Fax: 858-784-8136
    press@scripps.edu

    Rpn11
    The new research shows the workings of a crucial molecular enzyme. In this image, the green glow in the structure denotes the location of the Rpn11 enzymatic active site in its inhibited conformation at the heart of the isolated lid complex.

    A new study led by scientists at The Scripps Research Institute (TSRI) and the University of California (UC), Berkeley shows how a crucial molecular enzyme starts in a tucked-in somersault position and flips out when it encounters the right target.

    The new findings, published recently in the journal eLife, give scientists a clearer picture of the process through which cells eliminate proteins that promote diseases such as cancer and Alzheimer’s.

    “Having an atomic-resolution structure and a better understanding of this mechanism gives us the ability to someday design therapeutics to combat cancer and neurodegeneration,” said TSRI biologist Gabriel Lander, who was co-senior of author of the study with Andreas Martin of UC Berkeley.

    Keeping Cells Healthy

    The new study sheds light on the proteasome, a molecular machine that serves as a recycling center in cells. Proteasomes break down spent or damaged proteins and can even eliminate harmful misfolded proteins observed in many diseases.

    The new research is the first study in almost 20 years to solve a large component of the proteasome at near-atomic resolution. Lander said the breakthrough was possible with recent advances in cryo-electron microscopy (EM), an imaging technique in which a sample is bombarded with an electron beam, producing hundreds of thousands of protein images that can be consolidated into a high-resolution structure.

    Using cryo-EM, scientists investigated part of the proteasome that contains a deubiquitinase enzyme called Rpn11. Rpn11 performs a crucial function called deubiquitination, during which it cleaves molecular tags from proteins scheduled for recycling in the proteasome. This is a key step in proteasomal processing—without Rpn11, the protein tags would clog the proteasome and the cell would die.

    From previous studies, scientists knew Rpn11 and its surrounding proteins latch onto the proteasome to form a sort of lid. “The lid complex wraps around the proteasome like a face-hugger in the movie ‘Alien,’” said Lander.

    The lid complex can also exist separately from the proteasome—which poses a potential problem. If Rpn11 cleaves tags from proteins that haven’t gotten to the proteasome yet, those proteins could skip the recycling stage and cause disease. Scientists had wondered how nature had solved this problem.

    A Guide for Future Therapies

    The study provides an answer, showing the lid complex as it floats freely in cells. In this conformation, Rpn11 is carefully nestled in the crook of surrounding proteins, stabilized and inactive.

    “There’s a sophisticated network of interactions that pin the Rpn11 deubiquitinase against neighboring subunits to keep it inhibited in the isolated proteasome lid,” explained Corey M. Dambacher, a researcher at TSRI at the time of the study and now a senior scientist at Omniome, Inc., who was first author of the study with TSRI Research Associate Mark Herzik Jr. and Evan J. Worden of UC Berkeley.

    “In order for Rpn11 to perform its job, it has to flip out of this inhibited conformation,” said Herzik.

    The new study also shows that, to flip out of the conformation at the proteasome, the proteins surrounding deubiquitinase pivot and rotate—binding to the proteasome and releasing the deubiquitinase active site from its nook.

    Lander called the system “finely tuned,” but said there may be ways to manipulate it. The study collaborators at UC Berkeley made small mutations to the proteins holding Rpn11 in position, and found that any small change will release the deubiquitinase, even when the lid is floating freely.

    Lander said the new understanding of the mechanism that activates Rpn11 could guide future therapies that remove damaged or misfolded proteins.

    “Accumulation of these toxic proteins can lead to diseases such as Parkinson’s and Alzheimer’s, as well as a variety of cancers,” Lander said. “If we can harness the proteasome’s ability to remove specific proteins from the cell, this gives us incredible power over cellular function and improves our ability to target certain cells for destruction.”

    Going forward, the researchers hope to use the same cryo-EM techniques to investigate other components of the proteasome—and figure out exactly how it recognizes and destroys proteins. “There’s still a lot to learn,” said Lander.

    For more information on the study, “Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition,” see http://elifesciences.org/content/early/2016/01/08/eLife.13027

    This research was supported by the Damon Runyon Cancer Research Foundation (grant DFS-#07-13), the Pew Scholars program, the National Institutes of Health (grants DP2 EB020402 and R01-GM094497), the Searle Scholars Program, the National Science Foundation CAREER Program (grant NSF-MCB-1150288), the Howard Hughes Medical Institute and a National Science Foundation Graduate Research Fellowship.

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    The Scripps Research Institute (TSRI), one of the world’s largest, private, non-profit research organizations, stands at the forefront of basic biomedical science, a vital segment of medical research that seeks to comprehend the most fundamental processes of life. Over the last decades, the institute has established a lengthy track record of major contributions to the betterment of health and the human condition.

    The institute — which is located on campuses in La Jolla, California, and Jupiter, Florida — has become internationally recognized for its research into immunology, molecular and cellular biology, chemistry, neurosciences, autoimmune diseases, cardiovascular diseases, virology, and synthetic vaccine development. Particularly significant is the institute’s study of the basic structure and design of biological molecules; in this arena TSRI is among a handful of the world’s leading centers.

    The institute’s educational programs are also first rate. TSRI’s Graduate Program is consistently ranked among the best in the nation in its fields of biology and chemistry.

     
  • richardmitnick 4:21 pm on January 18, 2016 Permalink | Reply
    Tags: , , Scripps Institute   

    From Scripps: “TSRI Scientists Solve 3D Structure of Protein that Guides the Immune System” 

    Scripps
    Scripps Research Institute

    January 18, 2016
    No writer credit found
    Office of Communications
    Tel: 858-784-2666
    Fax: 858-784-8136
    press@scripps.edu

    Temp 1
    A new study from The Scripps Research Institute (TSRI) and the Duke University Medical Center reveals the three-dimensional structure of a crucial ion channel, shedding light on its role in the immune system.

    Many cells have microscopic gates, called ion channels, which open to allow the flow of ions across the cell membrane. Thanks to these gates, cells can detect stimuli such as heat, pain, pressure and even spicy food.

    In a new study, researchers from The Scripps Research Institute (TSRI) and the Duke University Medical Center reveal the three-dimensional structure of a crucial ion channel. Their findings depict this channel in more detail than ever before, shedding light on the channel’s possible role in immune functions such as detecting infection and inflammation.

    “Our ability to perceive our environment—which includes sensing temperature and pain—is heavily reliant on these channels. Understanding their 3D structure paves the way for the development of a wide variety of new therapies,” said TSRI biologist Gabe Lander, who was co-senior of author of the study with biochemist Seok-Yong Lee of the Duke University Medical Center.

    The new study was published January 18, 2016, in the journal Nature Structural and Molecular Biology.

    An Important Sensor

    Lander and his colleagues focused on an ion channel called the transient receptor potential vanilloid-2 (TRPV2), which resides within the membranes of cells throughout the body. Previous research had suggested TRPV2 was involved in sensing physical stresses, such as changes in pressure and temperature, as well as in detecting immune challenges and activating the immune system’s T cells.

    In the new study, the researchers used an imaging technique called cryo-electron microscopy, in which a sample is pelted with high-energy electrons. Through the use of new sample preparation techniques, computer programs and a new generation of cameras, researchers at TSRI have improved the potential resolution of cryo-electron microscopy images to the point that TRPV2 could be imaged with near-atomic precision.

    “The fact that the field of cryo-electron microscopy has advanced to where we can now solve the structures of these small membrane-embedded complexes to such high resolution is exciting,” said TSRI Research Associate Mark Herzik Jr., who was co-first author of the study with Lejla Zubcevic of Duke University. “The methodological insights from this study will help advance other projects in the lab.”

    When the researchers compared the structure of TRPV2 with TRPV1, a genetically similar ion channel found only in the nervous system, they noticed some significant differences. TRPV2’s architectural components near the central gate and the peripheral domains were in a previously unobserved configuration. Together, this led the authors to propose that this configuration represents a “desensitized” state, providing a new molecular snapshot of these ion channels at work.

    “The TRVP2 ion channel is likely a global internal sensor—playing an important role in our immune response,” said Lander.

    Lander said the next step is to find the structures of TRPV2 at different stages of opening and closing its gate. With the entire cycle imaged, researchers will have a better idea of how the ion channel works and how it might be manipulated therapeutically to treat autoimmune diseases.

    The other co-authors on the paper, Cryo-electron microscopy structure of the TRPV2 ion channel,” were Ben Chung and Zhirui Liu of the Duke University Medical Center.

    This study was supported by the Duke University Medical Center, the National Institutes of Health (grants R01GM100894, DP2OD008380 and DP2EB020402), the Searle Scholars Program and The Pew Charitable Trusts.

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    The Scripps Research Institute (TSRI), one of the world’s largest, private, non-profit research organizations, stands at the forefront of basic biomedical science, a vital segment of medical research that seeks to comprehend the most fundamental processes of life. Over the last decades, the institute has established a lengthy track record of major contributions to the betterment of health and the human condition.

    The institute — which is located on campuses in La Jolla, California, and Jupiter, Florida — has become internationally recognized for its research into immunology, molecular and cellular biology, chemistry, neurosciences, autoimmune diseases, cardiovascular diseases, virology, and synthetic vaccine development. Particularly significant is the institute’s study of the basic structure and design of biological molecules; in this arena TSRI is among a handful of the world’s leading centers.

    The institute’s educational programs are also first rate. TSRI’s Graduate Program is consistently ranked among the best in the nation in its fields of biology and chemistry.

     
  • richardmitnick 12:43 pm on January 14, 2016 Permalink | Reply
    Tags: , , Scripps Institute   

    From Scripps: “Getting closer to an HIV Vaccine” 

    Scripps
    Scripps Research Institute

    January 2016
    No writer credit found

    1
    Authors of the new paper [no paper reference in article] included (left to right) James Voss, Raiees Andrabi, Dennis Burton, Bryan Briney and Chi-Hui Liang.

    For more than 30 years, an effective vaccine against HIV has eluded scientists, and more than two million people are still newly infected with the virus each year. In a recent study, scientists at The Scripps Research Institute gained a new weapon in that long fight. They identified four antibodies targeting a specific weak spot on HIV that provided key information for the design of a potential HIV vaccine candidate.

    “This study [no paper reference in article]is an example of how we can learn from natural infection and translate that information into vaccine development,” said TSRI Research Associate Raiees Andrabi. “This is an important advance in the field of antibody-based HIV vaccine development.”

    Dr. Andrabi served as first author of the study, working in the lab of senior author TSRI Professor Dennis R. Burton, who is also scientific director of the International AIDS Vaccine Initiative (IAVI) Neutralizing Antibody Center and of the National Institutes of Health’s Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery (CHAVI-ID) at TSRI.

    The findings build on the success of several recent TSRI studies showing that, with prompting, the immune system can develop antibodies to neutralize many strains of HIV. In the new study, the researchers carried out a series of experiments involving virus modifications and protein and antibody engineering. They found that four antibodies targeted a single spot on HIV’s surface called the V2 apex. This was significant because the V2 apex could be recognized by these antibodies on about 90 percent of known HIV strains – and even related strains that infect other species, meaning a vaccine that targets this region could protect against many forms of the virus.

    “This region helps stabilize the virus, so it’s an important area to target if you want to neutralize HIV,” said Dr. Andrabi.

    Investigating further, the researchers noticed that two of the four antibodies had an unusual feature that could prove important in vaccine design. The immune system usually begins its fight against infection by activating immune B cells that express “germline” forms of antibodies on their surface to bind invading pathogens. Germline antibodies rarely bind viruses very effectively themselves; instead, they are precursors for more developed antibodies, which mutate and hone their response to the invader.

    Yet in the new study, two of the antibodies did not need to mutate to bind with the V2 apex; instead, these antibodies used part of their basic germline structure, encoded by non-mutated genes. This means any patient with HIV should, in theory, have the ability to kick-start the right immune response.

    To generate that response, it was critical for the scientists to find the right proteins in HIV that the antibodies could recognize and bind to. In the new study, the researchers succeeded in mimicking a structure on HIV called the native HIV coat protein. This enabled them to design proteins that do indeed bind well to the germline antibodies and hopefully start a useful immune response. The next step will be to test the vaccine candidates in animal models.

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    The Scripps Research Institute (TSRI), one of the world’s largest, private, non-profit research organizations, stands at the forefront of basic biomedical science, a vital segment of medical research that seeks to comprehend the most fundamental processes of life. Over the last decades, the institute has established a lengthy track record of major contributions to the betterment of health and the human condition.

    The institute — which is located on campuses in La Jolla, California, and Jupiter, Florida — has become internationally recognized for its research into immunology, molecular and cellular biology, chemistry, neurosciences, autoimmune diseases, cardiovascular diseases, virology, and synthetic vaccine development. Particularly significant is the institute’s study of the basic structure and design of biological molecules; in this arena TSRI is among a handful of the world’s leading centers.

    The institute’s educational programs are also first rate. TSRI’s Graduate Program is consistently ranked among the best in the nation in its fields of biology and chemistry.

     
  • richardmitnick 2:44 pm on January 8, 2016 Permalink | Reply
    Tags: , , Scripps Institute   

    From Scripps: ” Scientists Advance Physics of Single ‘Transformer’ Proteins with Role in Cancer” 

    Scripps
    Scripps Research Institute

    January 11, 2016
    Madeline McCurry-Schmidt

    1
    Authors of the new paper included TSRI’s Associate Professor Ashok Deniz (right) and Research Associate Priya Banerjee. (Photo by John Dole.)

    A new study led by scientists at The Scripps Research Institute (TSRI) and St. Jude Children’s Research Hospital shows how a protein involved in cancer twists and morphs into different structures.

    “We’re studying basic biophysics, but we believe the complexity and rules we uncover for the physics of protein disorder and folding could one day also be used for better designs of therapeutics,” said TSRI Associate Professor Ashok Deniz, senior author of the new study along with Richard Kriwacki, faculty member at St. Jude.

    The study, published recently in the journal Angewandte Chemie, focuses on a protein called nucleophosmin (NPM1). This protein has many functions and, when mutated, has been shown to interfere with cells’ normal tumor-suppressing ability. NPM1 has been implicated in cancers such as non-Hodgkin lymphoma and acute myelogenous leukemia.

    Previous research led by study collaborators Kriwacki and Diana Mitrea at St. Jude had shown that a section of NPM1, called the N-terminal domain (Npm-N), doesn’t have a defined, folded structure. Instead, the protein morphs between two forms: a one-subunit disordered monomer and a five-subunit folded pentamer.

    Until now, the mechanism behind this transformation was unknown, but scientists believed this monomer-pentamer equilibrium could be important for the protein’s location and functioning in the cell.

    To shed light on how this transformation occurred, Deniz and his colleagues used an innovative combination of three techniques—single-molecule biophysics, fluorescence resonance energy transfer (FRET) and circular dichroism—which enabled them to study individual molecules and collections of molecules.

    Temp 1
    FRET Jablonski diagram with typical timescales. Alex M Mooney

    Single-molecule methods are especially useful for such studies because they can uncover important information that remains hidden in conventional studies.

    Remarkably, the researchers found that the transformation can proceed through more than one pathway. In one pathway, the transformation begins when the cell sends signals to attach phosphoryl groups to NPM1. This modification, called phosphorylation, prompts the ordered pentamer to become disordered and likely causes NPM1 to shuttle outside the cell’s nucleus. A meeting with a binding partner can mediate the reverse transformation to a pentamer.

    Interestingly, when NPM1 does become a pentamer again under these conditions, which likely causes it to move back to the nucleolus, it takes a different path instead of just retracing its earlier steps.

    Priya Banerjee, an American Heart Association-supported postdoctoral research associate at TSRI and the first author of the study, compared these complicated transitions to the morphing of a “Transformers” toy, where a robot can become a car and then a jet. “Phosphorylation and partner-binding are like different cellular switches driving these changes,” said Banerjee.

    Banerjee said the new study also reveals many intermediate states between monomer and pentamer structures—and that these states can be manipulated or “tuned” by changing conditions such as salt levels, phosphorylation and partner binding, which may explain how cells regulate the protein’s multiple functions. The researchers said future studies could shed more light on the biological functions of these different structures and how they might be used in future cancer therapies.

    The researchers added that combining the three techniques used in this study, plus a novel protein-labeling technique for single-molecule fluorescence, could be a useful strategy for studying other unstructured, “intrinsically disordered proteins” (IDPS). IDPS are involved in a host of cellular functions, as well as neurodegenerative disease, heart disease, infectious disease, type 2 diabetes and other conditions.

    The study, “Asymmetric Modulation of Protein Order-Disorder Transitions by Phosphorylation and Partner Binding,” was supported by the National Institutes of Health (NIH) (grants R01 GM066833, 1R01GM115634, 2R01GM083159 and 2R01CA082491), National Science Foundation (grant MCB1121959), the NIH National Cancer Institute (grant P30CA21765), ALSAC and the American Heart Association. See http://onlinelibrary.wiley.com/doi/10.1002/anie.201507728/abstract

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    The Scripps Research Institute (TSRI), one of the world’s largest, private, non-profit research organizations, stands at the forefront of basic biomedical science, a vital segment of medical research that seeks to comprehend the most fundamental processes of life. Over the last decades, the institute has established a lengthy track record of major contributions to the betterment of health and the human condition.

    The institute — which is located on campuses in La Jolla, California, and Jupiter, Florida — has become internationally recognized for its research into immunology, molecular and cellular biology, chemistry, neurosciences, autoimmune diseases, cardiovascular diseases, virology, and synthetic vaccine development. Particularly significant is the institute’s study of the basic structure and design of biological molecules; in this arena TSRI is among a handful of the world’s leading centers.

    The institute’s educational programs are also first rate. TSRI’s Graduate Program is consistently ranked among the best in the nation in its fields of biology and chemistry.

     
  • richardmitnick 6:19 pm on December 21, 2015 Permalink | Reply
    Tags: , , , Scripps Institute   

    From phys.org: “Scientists study single ‘transformer’ proteins with role in cancer” 

    physdotorg
    phys.org

    December 21, 2015
    Provided by: The Scripps Research Institute
    No writer credit

    1
    Authors of the new paper include the Scripps Research Institute’s Ashok Deniz (right) and Priya Banerjee. Credit: The Scripps Research Institute.

    A new study led by scientists at The Scripps Research Institute (TSRI) and St. Jude Children’s Research Hospital shows how a protein involved in cancer twists and morphs into different structures.

    “We’re studying basic biophysics, but we believe the complexity and rules we uncover for the physics of protein disorder and folding could one day also be used for better designs of therapeutics,” said TSRI Associate Professor Ashok Deniz, senior author of the new study along with Richard Kriwacki, faculty member at St. Jude.

    The study, published recently in the journal Angewandte Chemie, focuses on a protein called nucleophosmin (NPM1). This protein has many functions and, when mutated, has been shown to interfere with cells’ normal tumor suppressing ability. NPM1 has been implicated in cancers such as non-Hodgkin lymphoma and acute myelogenous leukemia.

    Previous research led by study collaborators Kriwacki and Diana Mitrea at St. Jude had shown that a section of NPM1, called the N-terminal domain (Npm-N), doesn’t have a defined, folded structure. Instead, the protein morphs between two forms: a one-subunit disordered monomer and a five-subunit folded pentamer.

    Until now, the mechanism behind this transformation was unknown, but scientists believed this monomer-pentamer equilibrium could be important for the protein’s location and functioning in the cell.

    To shed light on how this transformation occurred, Deniz and his colleagues used an innovative combination of three techniques—single-molecule biophysics, fluorescence resonance energy transfer (FRET) and circular dichroism—which enabled them to study individual molecules and collections of molecules. Single-molecule methods are especially useful for such studies because they can uncover important information that remains hidden in conventional studies.

    Remarkably, the researchers found that the transformation can proceed through more than one pathway. In one pathway, the transformation begins when the cell sends signals to attach phosphoryl groups to NPM1. This modification, called phosphorylation, prompts the ordered pentamer to become disordered and likely causes NPM1 to shuttle outside the cell’s nucleus. A meeting with a binding partner can mediate the reverse transformation to a pentamer.

    Interestingly, when NPM1 does become a pentamer again under these conditions, which likely causes it to move back to the nucleolus, it takes a different path instead of just retracing its earlier steps.

    Priya Banerjee, an American Heart Association-supported postdoctoral research associate at TSRI and the first author of the study, compared these complicated transitions to the morphing of a “Transformers” toy, where a robot can become a car and then a jet. “Phosphorylation and partner-binding are like different cellular switches driving these changes,” said Banerjee.

    Banerjee said the new study also reveals many intermediate states between monomer and pentamer structures—and that these states can be manipulated or “tuned” by changing conditions such as salt levels, phosphorylation and partner binding, which may explain how cells regulate the protein’s multiple functions. The researchers said future studies could shed more light on the biological functions of these different structures and how they might be used in future cancer therapies.

    The researchers added that combining the three techniques used in this study, plus a novel protein-labeling technique for single-molecule fluorescence, could be a useful strategy for studying other unstructured, “intrinsically disordered proteins” (IDPs). IDPS are involved in a host of cellular functions, as well as neurodegenerative disease, heart disease, infectious disease, type 2 diabetes and other conditions.

    Explore further: Scientists find new source of versatility so ‘floppy’ proteins can get things done

    More information: Priya R. Banerjee et al. Asymmetric Modulation of Protein Order-Disorder Transitions by Phosphorylation and Partner Binding, Angewandte Chemie International Edition (2015). DOI: 10.1002/anie.201507728

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    About Phys.org in 100 Words

    Phys.org™ (formerly Physorg.com) is a leading web-based science, research and technology news service which covers a full range of topics. These include physics, earth science, medicine, nanotechnology, electronics, space, biology, chemistry, computer sciences, engineering, mathematics and other sciences and technologies. Launched in 2004, Phys.org’s readership has grown steadily to include 1.75 million scientists, researchers, and engineers every month. Phys.org publishes approximately 100 quality articles every day, offering some of the most comprehensive coverage of sci-tech developments world-wide. Quancast 2009 includes Phys.org in its list of the Global Top 2,000 Websites. Phys.org community members enjoy access to many personalized features such as social networking, a personal home page set-up, RSS/XML feeds, article comments and ranking, the ability to save favorite articles, a daily newsletter, and other options.

     
  • richardmitnick 6:15 pm on December 16, 2015 Permalink | Reply
    Tags: , , Scripps Institute   

    From Scripps: “New Scripps Florida Compound Successfully Targets Hard-to-Treat Breast Cancer” 

    Scripps

    Scripps Research Institute

    December 16, 2015
    No Writer Credit

    Temp 1
    Scripps Florida’s Associate Professor Derek Duckett led the collaborative study.

    Findings from a new study led by scientists from the Florida campus of The Scripps Research Institute (TSRI) suggest a potent new therapeutic approach for a number of hard-to-treat breast cancers.

    The study points to an enzyme called casein kinase 1δ (CK1δ), a critical regulator of growth, as a novel and highly vulnerable therapeutic target. Increased CK1δ expression is common to breast cancer, including the difficult-to-treat subtype called “triple negative breast cancer” (those cancers not driven by estrogen, progesterone, or the HER-2/neu gene), affecting 10 to 20 percent of breast cancer patients.

    The study, which was published today in the journal Science Translational Medicine, was a collaboration among the Florida labs of Derek Duckett and William R. Roush, both of TSRI, and John Cleveland, formerly of TSRI and currently at the Moffitt Cancer Center.

    “Our findings confirm that aberrant CK1δ regulation promotes tumor growth in breast cancers by activating the protein β-catenin,” said Duckett, an associate professor at Scripps Florida. “The best news, however, is that we have been able to treat CK1δ-expressing breast cancers with a highly selective and potent CK1δ inhibitor developed by Bill Roush’s lab that triggers rapid tumor cell death.”

    At the beginning of the study, the team knew that the β-catenin protein was an oncogene in many cancers, but it was unclear why it was activated in these breast cancer types since they lacked typical mutations in those pathways. The researchers suspected the link could be overexpression of CK1δ. Their experiments showed that indeed to be the case.

    To confirm the new target, the study used the Roush lab compound, called SR-3029. SR-3029 was remarkably successful at blocking the growth of tumors in both animal models and in studies with tumor tissue from breast cancer patients.

    “SR-3029 removes β-catenin from cancer cells, killing the tumors,” explained Duckett. “This is an extraordinarily promising strategy for targeted treatment with SR-3029, especially in breast cancers that lack targeted treatment options.”

    “These results are just the tip of the iceberg,” added Roush, who is professor, associate dean and executive director of medicinal chemistry at TSRI. “Inhibitors such as SR-3029 are being studied in a host of different cancers, and we are hopeful this platform can be translated into clinical applications.”

    The first author of the study, “Therapeutic Targeting of Casein Kinase 1δ in Breast Cancer,” is Laura H. Rosenberg, a TSRI research associate at the time of the study. In addition to Rosenberg, Duckett, Roush and Cleveland, other authors include Marie Lafitte, Victor Quereda, Wayne Grant, Weimin Chen, Mathieu Bibian, Yoshihiko Noguchi and Mohammad Fallahi of TSRI; Chunying Yang of Moffitt Cancer Center and Research Institute; and Jenny C. Chang of Houston Methodist Hospital.

    This work was supported in part by the National Institutes of Health (grants CA175094, U54MH074404, P30-CA076292), Rendina Family Foundation, Shear Family Foundation, ThinkPink Kids Foundation, the State of Florida and Moffitt Cancer Center & Research Institute.

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    Scripps Institute Campus

    The Scripps Research Institute (TSRI), one of the world’s largest, private, non-profit research organizations, stands at the forefront of basic biomedical science, a vital segment of medical research that seeks to comprehend the most fundamental processes of life. Over the last decades, the institute has established a lengthy track record of major contributions to the betterment of health and the human condition.

    The institute — which is located on campuses in La Jolla, California, and Jupiter, Florida — has become internationally recognized for its research into immunology, molecular and cellular biology, chemistry, neurosciences, autoimmune diseases, cardiovascular diseases, virology, and synthetic vaccine development. Particularly significant is the institute’s study of the basic structure and design of biological molecules; in this arena TSRI is among a handful of the world’s leading centers.

    The institute’s educational programs are also first rate. TSRI’s Graduate Program is consistently ranked among the best in the nation in its fields of biology and chemistry.

     
  • richardmitnick 9:59 am on December 15, 2015 Permalink | Reply
    Tags: , , Scripps Institute   

    From Scripps: “BIOMEDICAL ADVANCES” 

    Scripps

    Scripps Research Institute

    December 2015

    Scientists at The Scripps Research Institute (TSRI) pursue the quest to understand the fundamental processes of life and advance human health. Here is a small sampling of highlights of their findings from 2015.

    1

    A NEW APPROACH TO ALZHEIMER’S

    Most people with Alzheimer’s disease have a smattering of brain cells with an abnormally high number of copies of a gene linked to the dangerous amyloid plaques, according to a new study. The research provides a completely new understanding of brain disease and could lead to new treatments and better diagnostics.

    “Our findings open a new window into the normal and diseased brain by providing the first evidence that DNA variation in individual neurons could be related to brain function and Alzheimer’s disease,” said Jerold Chun, professor at TSRI and its Dorris Neuroscience Center, whose research was also supported in part by the Shaffer Family Foundation.

    At Scripps Florida, while studying prion diseases that include “mad cow,” Professor Corinne Lasmésas discovered a killing mechanism that could underpin a range of intractable neurodegenerative diseases, including Alzheimer’s Parkinson’s and ALS.

    PROJECT FIGHTS OSTEOPOROSIS WITH BONE-FORMING CELLS

    The possibility of a broken hip can be a real concern – but researchers on TSRI’s Florida campus are bringing hope to those at risk. Their therapeutic approach, while still preliminary, could promote the development of new bone-forming cells in patients suffering from bone loss.

    In basic lab tests, treatments with the compound (called SR2595) led to a significant increase in osteoblast formation, a cell type known to form bone. Interestingly, the protein targeted by this potential treatment is involved in many diseases, including diabetes.

    “The next step is to perform an in-depth analysis of the drug’s efficacy in animal models of bone loss, aging, obesity and diabetes,” said Patrick Griffin, chair of the Department of Molecular Therapeutics.

    FOUND: NEW TOOLS AGAINST HIV

    A team at Scripps Florida has found a powerful anti-HIV agent that attacks all viral strains tested, including the hardest-to-stop variants.

    “Our compound is the broadest and most potent entry inhibitor described so far,” said Professor Michael Farzan, who has won a grant from the Bill and Melinda Gates Foundation to continue his investigations. “This is the culmination of more than a decade’s worth of work on the biochemistry of how HIV enters cells.”

    In other work, virologist Professor Susana Valente and colleagues showed a natural compound called Cortistatin A greatly reduces residual HIV in the body, potentially offering a “functional cure.”

    On the California campus, Professors Dennis Burton, William Schief and David Nemazee designed an effective way to “prime” the immune system to fight off HIV that could become part of a series of anti-HIV vaccines and booster shots.

    FINDINGS POINT TO ROOT CAUSE OF CYSTIC FIBROSIS – AND POTENTIAL NEW THERAPIES

    Scientists uncovered a clue that could lead to new treatments for cystic fibrosis – a mutant protein present in most cases of the disease is so busy “talking” to the wrong cellular neighbors that it cannot function normally.

    The team, supported in part by the National Institutes of Health and the Cystic Fibrosis Foundation, found a way to disrupt this unhelpful chatter, partially restoring the protein’s normal function under laboratory conditions. Therapies like this could one day treat the root cause of cystic fibrosis, not just the symptoms.

    “The proteins and the interactions we’ve identified really fuel the pipeline for new drug targets to treat cystic fibrosis,” said Casimir Bamberger, a research associate in the lab of TSRI Professor John R. Yates and co-first author of the new study with TSRI Staff Scientist Sandra Pankow.

    TEAM TAKES AIM AT AGE-RELATED DISEASES

    A TSRI collaboration with the Mayo Clinic and other institutions identified a new class of drugs that dramatically slows the aging process in animal models. The drugs, dubbed “senolytics,” target senescent cells (cells that have stopped dividing) that accumulate and damage tissues as we age.

    Animal models of aging showed improvements in heart function and osteoporosis after a single course of treatment.

    “We view this study as a big, first step toward developing treatments that can be given safely to patients to extend healthspan or to treat age-related diseases and disorders,” said Professor Paul Robbins, who led the portion of the work at Scripps Florida with Associate Professor Laura Niedernhofer. Their labs are funded in part by the Glenn Foundation.

    The Petrascheck lab also showed in worms that one antidepressant, mianserin, reduces transcriptonal drift and increases longevity.

    BACTERIAL BUILDUP LINKED TO COLON CANCER

    Scientists made a surprising link between bacterial “biofilms” in the colon and the development of life-threatening colon cancer. Their research suggests a vicious cycle in which cancerous changes in colon cells promote the growth of bacterial conglomerations called biofilms, and biofilms in turn promote cancer development.

    The work, led by Professor Gary Siuzdak and supported in part by the California Institute for Regenerative Medicine (CIRM), suggests that removing biofilms could be a key strategy for preventing and treating colon cancers, which currently kill about 50,000 Americans per year.

    In other cancer research, chemist Ben Shen, vice chair of the Department of Chemistry at Scripps Florida, demonstrated how a natural antibiotic adds sulfur atoms to its structure, boosting its tumor-fighting abilities.

    CHEMISTS PRODUCE BRAIN-PROTECTING COMPOUND

    Chemists devised an efficient way to create large quantities of a molecule with brain-protecting potential. The plant-derived molecule, called jiadifenolide, might be useful in conditions such as Alzheimer’s, stroke and traumatic brain injury.

    Until now, chemists had found it difficult to synthesize useful amounts of the compound. “With our new method, someone could make the gram to kilogram quantities needed for tests in animals and humans,” said chemist Ryan A. Shenvi, whose work was funded by the National Science Foundation, as well as Amgen, Boehringer Ingelheim, the Baxter Foundation, Bristol-Myers Squibb, Eli Lilly, Novartis and the Sloan Foundation.

    In other remarkable organic chemistry work, Phil Baran, the Darlene Shiley Chair of Chemistry at TSRI, discovered a broad and strikingly inexpensive method for synthesizing “amines,” organic compounds prominent in drugs and other modern products.

    STEPS TOWARD A LIFE-LONG FLU VACCINE

    Seasonal flu typically causes more than 200,000 hospitalizations and 36,000 deaths every year in the United States, according to the U.S. Centers for Disease Control and Prevention. While a yearly flu shot provides some protection, strains not covered by the vaccine can emerge rapidly.

    Now scientists from TSRI and the Janssen Pharmaceutical Companies of Johnson & Johnson have found a way to induce the body to make rare but powerful antibodies that fight a wide range of influenza subtypes – work that could one day provide broader protection and eliminate the need for repeated seasonal flu shots.

    “This was the proof of principle,” said Ian Wilson, Hansen Professor of Structural Biology and chair of the Department of Integrative Structural and Computational Biology. “These tests showed that antibodies elicited against one influenza subtype could protect against a different subtype.”

    RESEARCHERS TARGET MEMORIES TO PREVENT METH RELAPSE

    Recovering addicts often grapple with the ghosts of their addiction – memories that tempt them to relapse even after rehabilitation and months of drug-free living. Now, scientists have made a discovery that brings them closer to a new therapy based on selectively erasing these dangerous and tenacious drug-associated memories.

    The new research, led by Scripps Florida Associate Professor Courtney Miller, demonstrates the effectiveness of a single injection of an early drug candidate called blebbistatin in preventing relapse in animal models of methamphetamine addiction.

    “We now have a viable target and by blocking that target, we can disrupt, and potentially erase, drug memories, leaving other memories intact,” said Miller. “The hope is that, when combined with traditional rehabilitation and abstinence therapies, we can reduce or eliminate relapse for meth users after a single treatment by taking away the power of an individual’s triggers.”

    LEUKEMIA CELLS MADE TO KILL EACH OTHER

    Researchers found a way to use antibodies to transform leukemia cells into leukemia-killing immune cells. The surprise finding could lead to a powerful new therapy for leukemia and possibly other cancers.

    “It’s a totally new approach to cancer, and we’re working to test it in human patients as soon as possible,” said Richard A. Lerner, Institute Professor and the Lita Annenberg Hazen Professor of Immunochemistry at TSRI whose study was supported by the JPB Foundation and Zebra Biologics. “We’re in discussions with pharmaceutical companies to take this straight into humans after the appropriate preclinical toxicity studies.”

    In other research related to leukemia, a study from the Reed lab showed that too much of a key protein, called cyclin E, slows down DNA replication and introduces potentially harmful cancer-linked mutations when cells divide.

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    The Scripps Research Institute (TSRI), one of the world’s largest, private, non-profit research organizations, stands at the forefront of basic biomedical science, a vital segment of medical research that seeks to comprehend the most fundamental processes of life. Over the last decades, the institute has established a lengthy track record of major contributions to the betterment of health and the human condition.

    The institute — which is located on campuses in La Jolla, California, and Jupiter, Florida — has become internationally recognized for its research into immunology, molecular and cellular biology, chemistry, neurosciences, autoimmune diseases, cardiovascular diseases, virology, and synthetic vaccine development. Particularly significant is the institute’s study of the basic structure and design of biological molecules; in this arena TSRI is among a handful of the world’s leading centers.

    The institute’s educational programs are also first rate. TSRI’s Graduate Program is consistently ranked among the best in the nation in its fields of biology and chemistry.

     
  • richardmitnick 4:06 pm on November 16, 2015 Permalink | Reply
    Tags: , Scripps Institute, ,   

    From UCSD: “From the Field: Chilean Tsunami Rocks Antarctica’s Ross Ice Shelf” 

    UC San Diego bloc

    UC San Diego

    Scripps Institution of Oceanography UCSD
    Scripps Institution of Oceanography

    Chance timing leads to first seismic observations of tsunami impacts on an ice shelf

    Nov 13, 2015
    Peter Bromirski

    1
    Servicing a seismic station in subzero temperatures and high winds. Photo courtesy of Spencer Niebuhr

    The magnitude 8.3 earthquake on Sept.16, 2015 off the coast of Chile generated a tsunami that was felt throughout the Pacific. Serendipitously, a Scripps Institution of Oceanography, UC San Diego-led project has a broadband seismic array deployed on the Ross Ice Shelf (RIS) in Antarctica.

    These seismic stations made the first large-scale broadband seismic array observations of the response of an ice shelf to tsunami arrivals. A team of Scripps researchers now in Antarctica is recovering seismic data from 34 seismic stations spanning the ice shelf. Strong signals generated by the tsunami impacting the shelf were detected at all stations from which data has been recovered, with the expectation that the entire ice shelf was rocked.

    Because the shortest direct path for the tsunami to the RIS goes through West Antarctica, refraction and scattering by seafloor ridges and seamounts must have diverted the tsunami energy that impacted the RIS.

    Ice shelves are slabs of ice that extend from land over the ocean like a half-cover on a jacuzzi. Ice shelves provide a buttressing effect, restraining the flow of grounded ice sheets to the sea. When this restraint is removed, the flow of land ice into the ocean accelerates, raising sea level. The Ross Ice Shelf is the largest ice shelf in Antarctica that covers an area of the Ross Sea roughly the size of Texas, and restrains West Antarctic grounded ice sheet that could contribute as much as three meters of sea-level rise.

    The seismic survey studying the vibrations of the Ross Ice Shelf (RIS) in response to ocean wave impacts will provide information on the structure and strength of the RIS, giving baseline “state-of-health” ice shelf measurements that will be used to identify the magnitude of changes in its integrity over time.

    The servicing of the stations installed in November 2015 involves flying by Twin Otter aircraft to the stations and uncovering the instrument recording boxes buried by about 3-4 feet of snow. The Scripps team, led by Peter Bromirski with Anja Diez, Zhao Chen, and Jerry Wanetick, swap out the disc drives that contain the full year of data. Temperatures at the stations during data recovery have ranged from about -15 to -26° C (5 to -15° F), with winds as high as 40 knots.

    The National Science Foundation Division of Polar Programs-funded project will continue collecting seismic and GPS data for another full year, including through the austral winter.

    The triggers that initiated the collapse of the Larsen B Ice Shelf in 2002 and the Wilkens Ice Shelf in 2008 have not been identified. While tsunamis were not factors in those events, West Antarctic ice shelves are exposed to circum-Pacific-generated tsunamis that could provide the trigger for the collapse of weakened ice shelves, removing their restraining influence.

    Institutions participating in the study include Woods Hole Oceanographic Institution, Washington University in St. Louis, Colorado State University, and Penn State University.

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    UC San Diego Campus

    The University of California, San Diego (also referred to as UC San Diego or UCSD), is a public research university located in the La Jolla area of San Diego, California, in the United States.[12] The university occupies 2,141 acres (866 ha) near the coast of the Pacific Ocean with the main campus resting on approximately 1,152 acres (466 ha).[13] Established in 1960 near the pre-existing Scripps Institution of Oceanography, UC San Diego is the seventh oldest of the 10 University of California campuses and offers over 200 undergraduate and graduate degree programs, enrolling about 22,700 undergraduate and 6,300 graduate students. UC San Diego is one of America’s Public Ivy universities, which recognizes top public research universities in the United States. UC San Diego was ranked 8th among public universities and 37th among all universities in the United States, and rated the 18th Top World University by U.S. News & World Report ‘s 2015 rankings.

     
  • richardmitnick 4:30 pm on September 17, 2015 Permalink | Reply
    Tags: , , , Scripps Institute,   

    From UCSD and Scripps: “UC San Diego and TSRI Launch New Consortium to Create ‘Virtual Cell’” 

    UC San Diego bloc

    UC San Diego

    Scripps Institute
    Scripps Research Institute

    1
    Credit: Art Olson and TSRI

    Drawing on complementary strengths, the University of California, San Diego and The Scripps Research Institute have formed a new consortium with a big mission: to map cells in space and time.

    The consortium will offer fellowship funding for 10 to 12 graduate students and postdoctoral fellows to work on collaborative projects that build bridges between the campuses and different disciplines to assemble and simulate a virtual model of a cell, down to an atomic level of detail.

    “Leveraging existing strengths at UC San Diego and Scripps, the collaboration will advance scientific excellence and research infrastructure at both institutions,” said UC San Diego Chancellor Pradeep K. Khosla. “The goal of building virtual cells poses an important challenge to researchers in fields from experimental biology to computation and information analysis.”

    “We are entering into this promising collaboration between our campuses with great optimism,” said TSRI Acting President and CEO Jim Paulson. “The Visible Molecular Cell Consortium aims to bring together the best minds from different disciplines to understand and articulate how the body’s cells work, which will lay important groundwork to understanding health and disease.”

    The Visible Molecular Cell Consortium will be directed jointly by Art Olson, professor at TSRI and Rommie Amaro, associate professor of chemistry and biochemistry at UC San Diego.

    “This is a particularly exciting time for such efforts, due to a number of technological and scientific factors,” said Amaro. “Advances in various imaging technologies, modeling frameworks and cyber-infrastructure are enabling us to make new strides in the creation of 3D virtual cells. This timely new inter-institutional alliance will provide new insights into the inner workings of cell machinery, some of which may present opportunities for novel therapeutics.”

    In recent years, more powerful imaging devices and automated programs in high resolution imaging have provided more detailed pictures of cells and their proteins than ever before, but scientists have not yet translated the huge amounts of data into a single, atomic-level cellular model. This is a “big data” challenge, Olson points out, applied to the uncharted territory of cellular architecture and ecology.

    “Even the simplest living cells contain 1 to 2 million proteins, of 3,000 to 4,000 different types,” said Olson. “Figuring out how they work together over time will shed light on the cell as a living, working individual entity. Just like you couldn’t build a car from just its wiring diagram, we can’t have a complete understanding of a cell unless we know how all of its physical parts work together in 3D.”

    The researchers hope to one day be able to zoom into cells at the atomic level and zoom out to see “nano neighborhoods,” where cells interact. On top of that, they aim to visualize protein interactions in real time to better understand cellular function. The new consortium will help scientists put the pieces together.

    TSRI is known for its structural biology using both cryo-electron microscopy and X-ray crystallography, and both Olson’s and Amaro’s labs develop and use advanced graphics programs to visualize complex cellular machinery. UC San Diego is home to the only publicly available supercomputer in California and the National Biomedical Computation Resource, a National Institutes of Health-sponsored national resource that develops multi-scale modeling tools.

    Olson and Amaro plan to host their first “lightning talk” workshop, where any scientist can present their work and seek out collaborators, on Oct. 2. They also plan to organize a bi-annual conference to encourage new collaborations and share results. Researchers interested in learning more about the consortium are encouraged to contact visiblemolecularcell@gmail.com.

    The organizers anticipate the consortium will be particularly strong in neurological diseases and infectious diseases, such as influenza, HIV and Ebola virus, although the insights into cellular behavior will be applicable across many fields.

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    UC San Diego Campus

    The University of California, San Diego (also referred to as UC San Diego or UCSD), is a public research university located in the La Jolla area of San Diego, California, in the United States.[12] The university occupies 2,141 acres (866 ha) near the coast of the Pacific Ocean with the main campus resting on approximately 1,152 acres (466 ha).[13] Established in 1960 near the pre-existing Scripps Institution of Oceanography, UC San Diego is the seventh oldest of the 10 University of California campuses and offers over 200 undergraduate and graduate degree programs, enrolling about 22,700 undergraduate and 6,300 graduate students. UC San Diego is one of America’s Public Ivy universities, which recognizes top public research universities in the United States. UC San Diego was ranked 8th among public universities and 37th among all universities in the United States, and rated the 18th Top World University by U.S. News & World Report ‘s 2015 rankings.

    Scripps Institute Campus

    The Scripps Research Institute (TSRI), one of the world’s largest, private, non-profit research organizations, stands at the forefront of basic biomedical science, a vital segment of medical research that seeks to comprehend the most fundamental processes of life. Over the last decades, the institute has established a lengthy track record of major contributions to the betterment of health and the human condition.

    The institute — which is located on campuses in La Jolla, California, and Jupiter, Florida — has become internationally recognized for its research into immunology, molecular and cellular biology, chemistry, neurosciences, autoimmune diseases, cardiovascular diseases, virology, and synthetic vaccine development. Particularly significant is the institute’s study of the basic structure and design of biological molecules; in this arena TSRI is among a handful of the world’s leading centers.

    The institute’s educational programs are also first rate. TSRI’s Graduate Program is consistently ranked among the best in the nation in its fields of biology and chemistry.

     
  • richardmitnick 10:39 am on September 10, 2015 Permalink | Reply
    Tags: , , Scripps Institute   

    From Scripps: “Pinpointing a Cause of Autism” 

    Scripps

    Scripps Research Institute

    September 2015
    No Writer Credit

    1
    The Scripps Florida team included Amy Clipperton-Allen, Youjun Chen, Wen-Chin “Brian” Huang, Julien Séjourné and Damon Page.

    As early as 1943, when autism was first described by psychiatrist Leo Kanner, reports were made that some, but not all, children with autism spectrum disorder have relatively enlarged heads. But even today, more than half a century later, the exact cause of this early abnormal growth of the head and brain has remained unclear.

    Now, scientists from the Scripps Florida campus have uncovered how mutations in a specific gene linked to autism can alter the basic trajectory of early brain development in animal models.

    Autism spectrum disorder is a neurodevelopmental disorder characterized by social deficits and communication difficulties, repetitive behaviors and interests, as well as cognitive delays in some individuals. The disorder affects approximately 1% of the population, some 80% of whom are male.

    The new study focused on the gene PTEN (Phosphatase and tensin homolog), which is mutated in around 20% of individuals with autism spectrum disorder who have enlarged heads (macrocephaly).

    The team, led by Scripps Florida biologist Damon Page, found that mutations in the mouse version of PTEN, which approximate those found in a subgroup of individuals with autism spectrum disorder, lead to changes in the number of two key cell types that make up the brain – neurons and glia. At birth, neurons in animals with the mutation are more abundant than normal. Surprisingly, in adulthood the number becomes virtually the same as normal, but glia, which provide support for neurons, are overrepresented.

    “In the adult brain, excess glia are a primary cause of the overall change in brain size,” said Dr. Page. “This raises the intriguing possibility that these excess glia may, in fact, contribute to abnormal development and function of brain circuitry when PTEN is mutated.”

    The team observed that the greatest increase in brain size occurred at birth and during adulthood and the least during the early juvenile period. They noted that this abnormal pattern of growth appears to be caused by an amplification of the normal process of brain development, where neurons are generated in over-abundance before birth. The unnecessary neurons are then trimmed off by a natural program of cell death called apoptosis. The glia are generated after the neurons, and in adulthood, the number of glial cells in the PTEN mutant mice increased by more than 20%. The scientists traced these effects back to an increase in signaling through a molecule known as β-Catenin (beta Catenin).

    “PTEN and β-catenin are two important molecules that control growth in the developing brain in both mice and humans,” said Dr. Page. “We have found that these work together in a common pathway to regulate brain growth trajectory by controlling the number and types of cells produced. Although caveats apply when extrapolating from mice to humans, this suggests that an imbalance in this relationship may contribute to abnormal brain growth in a subset of individuals with autism spectrum disorder.”

    Interestingly, Dr. Page noted that in spite of the profound effects of PTEN mutations on brain growth, the mice are largely able to adapt at the behavioral level, with the important exception of social behavior and a few other behaviors relevant to autism spectrum disorder.

    “Our findings across studies indicate that it may be a multiple-hit process,” he said. “While abnormal growth puts stress on the developing brain, the brain works hard to compensate for that. How well an individual can adapt to an abnormal pattern of brain growth may shape their outcome in terms of behavior and cognition. The capacity to adapt may, in turn, be influenced by genetic or environmental factors.”

    See the full article here .

    Please help promote STEM in your local schools.

    STEM Icon

    Stem Education Coalition

    The Scripps Research Institute (TSRI), one of the world’s largest, private, non-profit research organizations, stands at the forefront of basic biomedical science, a vital segment of medical research that seeks to comprehend the most fundamental processes of life. Over the last decades, the institute has established a lengthy track record of major contributions to the betterment of health and the human condition.

    The institute — which is located on campuses in La Jolla, California, and Jupiter, Florida — has become internationally recognized for its research into immunology, molecular and cellular biology, chemistry, neurosciences, autoimmune diseases, cardiovascular diseases, virology, and synthetic vaccine development. Particularly significant is the institute’s study of the basic structure and design of biological molecules; in this arena TSRI is among a handful of the world’s leading centers.

    The institute’s educational programs are also first rate. TSRI’s Graduate Program is consistently ranked among the best in the nation in its fields of biology and chemistry.

     
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