Past BECUR Keynote Speakers
2019: Amy Pasquinelli, PhD
2018: Brian Kelch, PhD
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University of Massachusetts Medical School
Assistant Professor, Biochemistry and Molecular Pharmacology Pew's Scholar PhD, University of California, San Francisco The Kelch lab is interested in determining how macromolecular machines work, with special emphasis on machines involved in DNA replication and repair. Understanding how these machines work will not only illuminate the underpinnings of these critically important cellular pathways, but can also lead to new targets for the development of novel cancer therapeutics and antibiotics. We use a combination of biochemistry, biophysics and structural methods to elucidate how these vitally important protein complexes are integrated into cellular pathways. |
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2017: James M. Berger, PhD
Johns Hopkins Medical School
Co-Director, Cancer Chemical and Structural Biology Program, Johns Hopkins Sidney Kimmel Comprehensive Cancer Center.
Professor of Biophysics and Biophysical Chemistry
"Stepping Mechanism and Dynamical Control of a Biomolecular Rotary Motor"
My laboratory’s research is focused on understanding how multi-subunit assemblies use ATP for overcoming topological challenges within the chromosome and controlling the flow of genetic information. We are particularly interested in developing mechanistic models that explain how macromolecular machines transduce chemical energy into force and motion, and in determining how cells exploit these complexes and their activities for regulating the initiation of DNA replication, chromosome superstructure, and other essential nucleic acid transactions. Our principal approaches rely on a variety of structural, biochemical, and biophysical methods to define the architecture, function, evolution, and regulation of biological complexes. We also have extensive interests in mechanistic enzymology and the study of small-molecule inhibitors of therapeutic potential, the development of chemical approaches to trapping weak protein/protein and protein/nucleic acid interactions, and in using microfluidics for biochemical investigations of protein dynamics and structure.
Co-Director, Cancer Chemical and Structural Biology Program, Johns Hopkins Sidney Kimmel Comprehensive Cancer Center.
Professor of Biophysics and Biophysical Chemistry
"Stepping Mechanism and Dynamical Control of a Biomolecular Rotary Motor"
My laboratory’s research is focused on understanding how multi-subunit assemblies use ATP for overcoming topological challenges within the chromosome and controlling the flow of genetic information. We are particularly interested in developing mechanistic models that explain how macromolecular machines transduce chemical energy into force and motion, and in determining how cells exploit these complexes and their activities for regulating the initiation of DNA replication, chromosome superstructure, and other essential nucleic acid transactions. Our principal approaches rely on a variety of structural, biochemical, and biophysical methods to define the architecture, function, evolution, and regulation of biological complexes. We also have extensive interests in mechanistic enzymology and the study of small-molecule inhibitors of therapeutic potential, the development of chemical approaches to trapping weak protein/protein and protein/nucleic acid interactions, and in using microfluidics for biochemical investigations of protein dynamics and structure.
2016: Michael Rossmann, PhD
Purdue University
Hanley Distinguished Professor of Biological Science
Michael Rossmann is a German-American biophysicist, crystallographer and Hanley Distinguished Professor of Biological Sciences at Purdue University. In 1956 he received his PhD at the University of Glasgow for chemical crystallography. Dr. Rossmann worked on the structure of hemoglobin along with Max Perutz at Cambridge University, down the hall from Nobel Prize winners Francis Crick and James Watson. In 1973 Rossmann published the description of the Rossmann fold, a structural motif found in proteins associated with nucleotide-binding properties. FAD and NADP cofactor binding in proteins thus use Rossmann fold motifs; examples of such proteins are glutamate dehydrogenase and dihydrolipoamide dehydrogenase, which are components of amino acid catabolism, cellular respiration, and the citric acid cycle. Currently the Rossmann group is studying structural features of enteroviruses, which have profound implications in combating viral infections.
Hanley Distinguished Professor of Biological Science
Michael Rossmann is a German-American biophysicist, crystallographer and Hanley Distinguished Professor of Biological Sciences at Purdue University. In 1956 he received his PhD at the University of Glasgow for chemical crystallography. Dr. Rossmann worked on the structure of hemoglobin along with Max Perutz at Cambridge University, down the hall from Nobel Prize winners Francis Crick and James Watson. In 1973 Rossmann published the description of the Rossmann fold, a structural motif found in proteins associated with nucleotide-binding properties. FAD and NADP cofactor binding in proteins thus use Rossmann fold motifs; examples of such proteins are glutamate dehydrogenase and dihydrolipoamide dehydrogenase, which are components of amino acid catabolism, cellular respiration, and the citric acid cycle. Currently the Rossmann group is studying structural features of enteroviruses, which have profound implications in combating viral infections.
2015: Olke Uhlenbeck, PhD
Northwestern University
Professor Emeritus
Research summary
Elongation during protein synthesis is a regulated process that involves activation and transportation of tRNA. Activation of tRNA occurs when an amino acid, catalyzed by aminoacyl tRNA synthase, binds to the tRNA structure. Activated tRNA is then transported by elongation factor Tu (EF-Tu), which is bound by GTP in its active state, to the ribosome. Hydrolysis of GTP occurs and causes EF-Tu dissociation from the ribosome and tRNA. The Uhlenbeck lab has written extensively on tRNA and its associated proteins. Recently, the Uhlenbeck lab developed an assay to monitor activity between EF-Tu and tRNA as well as EF-Tu and ribosomal L11. These assays are particularly relevant in high throughput screening for ribosomal antibiotics, such as a streptomycin and paromomycin.
Professor Emeritus
Research summary
Elongation during protein synthesis is a regulated process that involves activation and transportation of tRNA. Activation of tRNA occurs when an amino acid, catalyzed by aminoacyl tRNA synthase, binds to the tRNA structure. Activated tRNA is then transported by elongation factor Tu (EF-Tu), which is bound by GTP in its active state, to the ribosome. Hydrolysis of GTP occurs and causes EF-Tu dissociation from the ribosome and tRNA. The Uhlenbeck lab has written extensively on tRNA and its associated proteins. Recently, the Uhlenbeck lab developed an assay to monitor activity between EF-Tu and tRNA as well as EF-Tu and ribosomal L11. These assays are particularly relevant in high throughput screening for ribosomal antibiotics, such as a streptomycin and paromomycin.
2014: Roy Parker, PhD
University of Colorado, Boulder
Cech-Leinwand Endowed Chair of Biochemistry
The control of biological processes, such as cellular growth and differentiation, is dependent on how the genetic material within a cell is expressed. The cellular physiology of mRNA—including mRNA processing, transport, localization, and turnover—is central to the process of gene expression. In my laboratory, we are focusing on understanding how cells regulate the translation and degradation of mRNAs. In eukaryotic cells the decay rates and the translation rates of individual mRNAs can be quite different and these processes can be regulated in response to a variety of signals, including specific hormones and viral infection, or as a consequence of differentiation. Our goal is to understand the molecular mechanisms that control mRNA stability and translation rate in eukaryotic cells, using yeast as a model system.
Cech-Leinwand Endowed Chair of Biochemistry
The control of biological processes, such as cellular growth and differentiation, is dependent on how the genetic material within a cell is expressed. The cellular physiology of mRNA—including mRNA processing, transport, localization, and turnover—is central to the process of gene expression. In my laboratory, we are focusing on understanding how cells regulate the translation and degradation of mRNAs. In eukaryotic cells the decay rates and the translation rates of individual mRNAs can be quite different and these processes can be regulated in response to a variety of signals, including specific hormones and viral infection, or as a consequence of differentiation. Our goal is to understand the molecular mechanisms that control mRNA stability and translation rate in eukaryotic cells, using yeast as a model system.
2013: Kim Orth, PhD
UT Southwestern Medical Center
Professor, Department of Biochemistry & Molecular Biology
Earl A. Forsythe Chair in Biomedical Science
Dr. Orth is interested in elucidating the activity of virulence factors from pathogenic bacteria to gain novel molecular insight into eukaryotic signaling systems. Many virulence factors are secreted by bacteria using a type III secretion system (T3SS) resembling a needle-like structure that efficiently translocates effector proteins from bacteria into the cytosol of a host cell. Effectors have evolved in a manner similar to many of the viral oncogenes; a eukaryotic activity is usurped and modified by the pathogen for its own advantage. Her lab works on T3SS systems and bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by bacterial pathogens. These studies provide novel insight into the molecular workings of eukaryotic signal transduction.
Professor, Department of Biochemistry & Molecular Biology
Earl A. Forsythe Chair in Biomedical Science
Dr. Orth is interested in elucidating the activity of virulence factors from pathogenic bacteria to gain novel molecular insight into eukaryotic signaling systems. Many virulence factors are secreted by bacteria using a type III secretion system (T3SS) resembling a needle-like structure that efficiently translocates effector proteins from bacteria into the cytosol of a host cell. Effectors have evolved in a manner similar to many of the viral oncogenes; a eukaryotic activity is usurped and modified by the pathogen for its own advantage. Her lab works on T3SS systems and bacterial effectors to understand how signaling systems in the eukaryotic host can be manipulated by bacterial pathogens. These studies provide novel insight into the molecular workings of eukaryotic signal transduction.
2012: Daniel Herschlag, PhD
Stanford University School of Medicine
Professor of Biochemistry, Senior Associate Dean of Graduate Education and Postdoctoral Affairs
The Herschlag group is currently studying the catalysis of ketosteroid isomerase and group I ribozymes. Their research is based on the notion that enzymes are not "simply a collection of catalytic amino acids and cofactors" The unique arrangement of the protein scaffold allows certain intramolecular interactions that yields a precise active site. In effect, the study of enzyme catalysis, from a kinetics perspective, provides the next level of biochemical understanding.
Professor of Biochemistry, Senior Associate Dean of Graduate Education and Postdoctoral Affairs
The Herschlag group is currently studying the catalysis of ketosteroid isomerase and group I ribozymes. Their research is based on the notion that enzymes are not "simply a collection of catalytic amino acids and cofactors" The unique arrangement of the protein scaffold allows certain intramolecular interactions that yields a precise active site. In effect, the study of enzyme catalysis, from a kinetics perspective, provides the next level of biochemical understanding.
2011: Indraneel Ghosh, PhD
University of Arizona
Professor, Department of Chemistry & Biochemistry
Dr. Ghosh and his lab have recently constructed a new family of discrete supramolecules comprising designed peptides (coiled-coils) non-covalently assembled upon cognate peptides fused to a dendrimer core. These novel structures are being utilized for the multivalent display of proteins for protein inhibition and in the construction of novel biomaterials. The team is pursuing new approaches for labeling Quantum Dots with peptides to provide a means to image receptors on living cells.e to edit.
Professor, Department of Chemistry & Biochemistry
Dr. Ghosh and his lab have recently constructed a new family of discrete supramolecules comprising designed peptides (coiled-coils) non-covalently assembled upon cognate peptides fused to a dendrimer core. These novel structures are being utilized for the multivalent display of proteins for protein inhibition and in the construction of novel biomaterials. The team is pursuing new approaches for labeling Quantum Dots with peptides to provide a means to image receptors on living cells.e to edit.