Vahe Bandarian, Phd
Professor and Associate Provost for Mission-Aligned Planning
|
University of Utah
IMB Seminar Series
Apr 7, 2026 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Cyclic and polycyclic peptides are of considerable interest as therapeutic agents because the conformational restriction resulting from macrocyclization ensure specificity and resistance to proteolytic degradation. However, assembly of polymacrocyclic structures is often challenging because of the necessity for multi-step syntheses involving orthogonal protecting groups. In this presentation, a scalable, radical-mediated enzyme process for catalyzing formation of thioether crosslinks across a broad spectrum of peptide substrates is discussed.
Kamena Kostova, Phd
Assistant Investigator
|
Stower's Institute for Medical Research
IMB Seminar Series
Apr 14, 2026 | 12:00 pm | Knight Campus Beetham Family Seminar Room
The ribosome is the essential molecular machine responsible for translation of mRNA to protein. Its composition is complex; it comprises four ribosomal RNAs (rRNAs) and approximately 80 ribosomal proteins that form two subunits: the small 40S and the large 60S. For decades, the composition of the ribosome has been deemed static; ribosomes are assembled and they do not change in response to environmental stimuli, in different tissues or organs, or during disease initiation and progression. Now we know that this notion is simply not true, as changes in both rRNA and proteins have been documented. In general, there are two ways in which the ribosome composition can change: as a result of damage or due to programmed changes in ribosomal components. Indeed, mutations, environmental stress, or mistakes during assembly can lead to defective ribosomes. Accumulation of such faulty ribosomes is associated with diseases such as neurodegeneration, cancer and ribosomopathies, further emphasizing the importance of these pathological changes for human health. Alterations in the ribosomal RNA and proteins have also been associated with normal physiological processes, such as development, differentiation, and adaptation. For example, zebrafish larvae assemble two structurally distinct types of ribosomes, maternal and somatic, during early development. Although we now know that the composition of the ribosome is dynamic, we have a limited understanding of how changes in the ribosome impact protein production and facilitate complex physiological processes. In my laboratory, we have developed unique tools and biological systems to answer two outstanding questions in the translation field: 1) What are the quality control factors that cope with defective ribosomes? and 2) How do programmed changes in the ribosome composition regulate translation to facilitate development?
James Fraser, PhD
Chair and Ernest L. Prien Professor Department of Bioengineering and Therapeutic Sciences
|
University of California, San Francisco
IMB Seminar Series
Apr 21, 2026 | 4:00 pm | Willamette 110
In a post-"AlphaFold has solved structure prediction" world, our lab is obsessed with the concept of statistical structural biology. First, we collect large datasets (X-ray fragment screens from 1000s of individual crystals) and use new statistical approaches to identify small molecule binders. This inspires new inhibitors, allosteric modulators, and enzyme design strategies. Second, we examine how experimental information in X-ray crystallography and CryoEM encodes statistical distributions of conformations. This inspires software (e.g. qFit) that reveals hidden conformations and new guidance frameworks for diffusion models. Our work reveals the extent of memorization in current models and suggests experiments to extract even more information for improved training. These two statistical approaches to structural biology are synergistic in examining many aspects of biological mechanism. A current focus is the promiscuity of ligand binding in drug metabolizing proteins, as part of the OpenADMET consortium.
Jeffrey Tabor, PhD
Professor of Bioengineering & BioSciences
|
Rice University
IMB Seminar Series
Apr 28, 2026 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Jennifer Bridwell-Rabb, PhD
Associate Professor of Chemistry
|
University of Michigan
IMB Seminar Series
May 5, 2026 | 4:00 pm | Willamette 110
One of Nature’s underexplored strategies for facilitating C–H bond functionalization involves the class of Rieske Oxygenases. These enzymes use a high valent Fe-based oxidant to facilitate a diverse set of powerful and specific transformations, including monooxygenation, dioxygenation, and sequential monooxygenation reactions. This chemistry is vital to a number of biosynthetic and degradative pathways and thus, these enzymes have been recognized for their potential use in building complex natural products and degrading environmental pollutants. However, the practical applicability of Rieske Oxygenases is limited by a gap in knowledge regarding the structure–function relationships in this class of enzymes. Here, I will detail our progress towards identifying the architectural motifs that Rieske Oxygenases employ to dictate site-selectivity, substrate specificity, and reaction outcome. Collectively, this work provides a framework for structurally reprogramming a Rieske oxygenase for use as a biocatalyst.
Eileen Kennedy, PhD
Division Chair, Chemical Biology and Medicinal Chemistry; Distinguished Professor
|
Eshelman School of Pharmacy, the University of North Carolina at Chapel Hill
IMB Seminar Series
May 12, 2026 | 12:00 pm | Knight Campus Beetham Family Seminar Room
My research program is centered on developing synthetic modulators of allosteric and spatiotemporal regulation of kinases in cells using a chemical biology approach. From a chemical standpoint, we have developed synthetic strategies to generate biologically active beta-turn mimics and constrained alpha-helical scaffolds that target PPI interfaces involved in protein kinase regulation. These projects have laid the foundation for my group to now pursue allosteric inhibition or spatiotemporal disruption of kinases within a cellular context. Going forward, we are partly chemistry-focused where we explore different synthetic strategies to constrain peptide-based scaffolds with different secondary structures including loops, beta sheets and entities that contain two or more secondary structural elements. These compounds can be used to target kinases as well as other well-defined protein-protein interfaces that mediate protein complex formation. We are also focused on taking a more in-depth approach to studying the effectiveness of our compounds in different disease model systems. I will present work on current projects targeting LRRK2 in Parkinson’s and the WASF3 regulatory complex in cancer.
Julie Theriot, PhD
Chief Scientific Advisor
|
Allen Institute
George Streisinger Memorial Lecture Series
May 26, 2026 | 3:00 pm | Knight Campus Beetham Family Seminar Room
Julie Theriot attended college at the Massachusetts Institute of Technology, earning dual B. S. degrees in physics and biology. She completed her Ph.D. in cell biology at the University of California at San Francisco, and then returned to Cambridge as a Whitehead Fellow at the Whitehead Institute for Biomedical Research. She joined the faculty of the Stanford University School of Medicine in 1997, with appointments in the Department of Biochemistry and the Department of Microbiology & Immunology, and an Investigator of the Howard Hughes Medical Institute (HHMI). Julie is currently a Professor at the University of Washington, Department of Biology, a continuing HHMI Investigator, and as Chief Scientist at the Allen Institute for Cell Science.The experimental work of her research group focuses on quantitative measurement of the dynamic and mechanical behavior of structural components in living cells, exploring the molecular and biophysical mechanisms of various forms of cell motility and shape determination across a variety of eukaryotic and bacterial cell types. Julie has won numerous awards for her research, including the David and Lucile Packard Foundation Fellowship for Science and Engineering and the John D. and Catherine T. MacArthur Foundation Fellowship. She has also received multiple teaching awards from both M. D. and Ph. D. students at Stanford. Julie is a coauthor of the textbook “Physical Biology of the Cell.”
Karla Kirkegaard, PhD
Violetta L. Horton Research Professor of Genetics
|
Stanford University School of Medicine
George Streisinger Memorial Lecture Series
May 27, 2026 | 11:00 am | Knight Campus Beetham Family Seminar Room
Karla Kirkegaard, Ph.D., is the Violetta L. Horton Research Professor of Genetics and former Chair of the Department of Microbiology and Immunology in the Stanford University School of Medicine. She received her Ph.D. in Biochemistry and Molecular Biology with James C. Wang at Harvard University, and performed her postdoctoral work in the laboratory of David Baltimore at the Whitehead Institute. As an Assistant and Associate Professor at the University of Colorado in Boulder, she received numerous awards, including a fellowship from the David and Lucile Packard Foundation, an American Cancer Society Young Investigator Award, a Searle Scholar Award, and sponsorship by the Howard Hughes Medical Institute. Dr. Kirkegaard combined her interests in biochemistry, cell biology, and genetics in the study of RNA virology, using poliovirus and other positive-strand RNA viruses to understand the cell biology of viral infections and the genetics of viral variability. Since her move to Stanford University School of Medicine in 1996, her interests have focused increasingly on the impact of basic science discoveries on the transmission of viruses in infected hosts. Kirkegaard’s honors include an Ellison Foundation Senior Scholar Award in Global Infectious Disease and, in 2006, the NIH Director’s Pioneer Award, for her approach to guide the selection of antiviral targets with the goal of suppressing the drug-resistant RNA genomes that will inevitably be formed due to the high error rates of RNA replication. She has been recently elected as a Member of the National Academies of Arts and Sciences and a Fellow of the American Association for the Advancement of Science. Her work continues to focus on the mechanisms of diversity and propagation of viruses and suppression of this diversity and spread.
Past Events
Dr. Deepak Thirunavukarasu
Lead Scientist
|
Labcorp Drug Development
Career Exploration Speaker Series
Apr 1, 2026 | 4:00 pm | Novick Room - Streisinger 225
Refreshments served at 3:45 PM prior to talk at 4:00 PM for all attendees.
Hannah McMillan, PhD
NSF PRFB Postdoctoral Fellow | He Lab Department of Biology Howard Hughes Medical Institute
|
Duke University
IMB Seminar Series
Mar 31, 2026 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Rising global temperatures threaten plant health by exacerbating abiotic and biotic stress. In plants, the cuticle serves as the first defense against microbes and a major protective layer against adverse abiotic conditions. My lab’s research explores how three-way interactions between plants, microbiota, and the environment lead to emergent properties on the leaf surface at elevated temperature with negative implications for plant health. Using a combination of molecular and -omics approaches, we have shown that natural variation influences plant-microbiome interaction outcomes at elevated temperature. Our results reveal new agricultural targets to overcome negative effects of altered three-way interactions and improve plant resilience in a changing climate.
Fitnat Yildiz, PhD
Associate Dean of Research & Research Impact, PBSci Division Distinguished Professor
|
University of California - Santa Cruz
IMB Seminar Series
Mar 10, 2026 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Nucleotide-based second messengers play a central role in the physiology of many bacterial pathogens. One of the most widely conserved signaling molecules, cyclic dimeric GMP (c-di-GMP), regulates motility, biofilm formation, and virulence in various organisms. Despite its importance, the mechanisms linking c-di-GMP signaling to these processes remain incompletely understood.In this presentation, I will focus on Vibrio cholerae, the causative agent of cholera, to examine how c-di-GMP regulates the transition from a motile to a sessile lifestyle and promotes biofilm formation. Specifically, I will present data that reveal the mechanisms by which c-di-GMP controls flagellar function, thereby orchestrating the transition from motility to biofilm formation.
Dr. Mitra Mojtahedi
Staff Field Applications Scientist
|
Thermo Fisher Scientific
Career Exploration Speaker Series
Mar 4, 2026 | 4:00 pm | Novick Room - Streisinger 225
Refreshments served at 3:45 PM prior to talk at 4:00 PM for all attendees.
POSTPONED - Ben Brown, PhD
Assistant Professor
|
Vanderbilt University
IMB Seminar Series
Mar 3, 2026 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Rapid and accurate estimation of protein-ligand binding affinities is crucial for early-stage drug discovery, yet hindered by a trade-off between the accuracy of gold-standard physics-based methods and the speed of simpler empirical scoring functions. Machine learning (ML) promised to bridge this gap, but its potential is unrealized due to limited model generalizability. Current ML models often fail when predicting affinities for novel proteins or chemical series unseen during training. We hypothesize that this failure stems from a competition within these models during training, where the learning of spurious correlations from structural motifs prevalent in the training data competes with the learning of transferable, physicochemical principles governing molecular interaction. Here, we introduce CORDIAL, a deep learning framework designed with an inductive bias toward learning the distance-dependent physicochemical interaction signatures between proteins and ligands, explicitly avoiding direct parameterization of their chemical structures. This interaction-only approach proves effective. Through leave-superfamily-out validation that simulates encounters with novel protein families, we demonstrate that CORDIAL maintains predictive performance and calibration. This contrasts with diverse contemporary ML models, whose predictive ability is degraded under these conditions. Our results highlight the value of encoding appropriate task-specific physicochemical principles into ML architectures and offer a validated strategy for developing generalizable models for structure-based drug discovery.
POSTPONED - Binyam Mogessie, PhD
Assistant Professor of Molecular, Cellular, and Developmental Biology and of Obstetrics, Gynecology, and Reproductive Sciences
|
Yale University
IMB Seminar Series
Feb 24, 2026 | 4:00 pm | Willamette 110
The molecular causes of age-related oocyte aneuploidy have remained elusive, mainly because reproductive aging has been difficult to study experimentally. To address this challenge, we developed a synthetic oocyte aging system that uses PROTAC-mediated targeted protein degradation to induce a controlled, “aging-like” weakening of meiotic cohesion in fully grown oocytes. This method separates cohesion loss from general cellular decline, allowing for a detailed investigation of how specific age-related failures develop. Using this system, we discovered that spindle actin and centromeric CENP-A serve as parallel safeguards that help ensure proper chromosome segregation. When cohesion is experimentally weakened, aging-like disruptions of spindle actin dynamics or centromeric CENP-A composition work together to increase segregation errors, revealing new combined failure modes that could explain the very high rates of aneuploidy in human eggs. Besides uncovering these mechanisms, the system offers a scalable platform for testing FDA-approved drug libraries to identify compounds that stabilize these pathways. These efforts could guide future strategies to reduce egg aneuploidy and improve outcomes in assisted reproductive technologies.
POSTPONED - Scott Coyle, PhD
Assistant Professor, Department of Biochemistry
|
University of Wisconsin Madison
IMB Seminar Series
Feb 17, 2026 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Kim McKim, PhD
Professor
|
Rutgers University
IMB Seminar Series
Feb 10, 2026 | 4:00 pm | Willamette 110
Meiosis is characterized by the first, or reductional, division. We use Drosophila melanogaster females as a model to understand the mechanisms that promote accurate chromosome segregation on the acentrosomal spindle of oocytes. Furthermore, we are interested in understanding the features of the oocyte spindle that make it susceptible to chromosome segregation errors. An important part of this process is how the kinetochores on the chromosomes interact with the microtubules of the spindle. The kinetochore interacts with the microtubules in two ways. First, lateral attachments, where the kinetochores move along the sides of microtubules. Second, end-on attachments, where the kinetochores make a stable attachment to the ends of microtubules, maintain connections to a pole and segregate the homologs. The lateral interactions occur between the kinetochores and central spindle, which is composed of overlapping antiparallel microtubules and may be particularly important for acentrosomal oocytes. We hypothesize that the transition between lateral and end-on attachments is regulated to avoid errors in chromosome segregation.
Dr. Rebecca Abergel
Associate Professor, UC Berkeley and Senior Faculty Scientist
|
Lawrence Berkeley National Laboratory
Career Exploration Speaker Series
Feb 4, 2026 | 4:00 pm | Novick Room - Streisinger 225
Refreshments served at 3:45 PM prior to talk at 4:00 PM for all attendees.
Dan Jarosz, PhD
Principal Investigator
|
Stanford University
IMB Seminar Series
Feb 3, 2026 | 4:00 pm | Willamette 110
Christopher Lapointe, PhD
Assistant Professor
|
Fred Hutchinson Cancer Center
RNA Club
Jan 30, 2026 | 10:55 am | B040 - Price Science Commons
To establish the reading frame for protein synthesis, the human translation initiation machinery must recognize the translation start codon (AUG) with single-nucleotide precision. Yet, foundational studies in the 1980’s demonstrated that non-AUG start codons (e.g., CUG) can also drive protein synthesis. More recent studies indicate widespread and regulated use of non-AUG codons, with critical roles in the cell cycle, stress responses, and disease. I will share how we have been applying in vitro single-molecule, biochemical, and structural strategies to understand how the initiation machinery balances the need for both precision and flexibility.
Alexander Cartagena-Rivera, PhD
Investigator (Tenure-Track)
|
National Institute of Biomedical Imaging and Bioengineering
IMB Seminar Series
Jan 27, 2026 | 4:00 pm | Willamette 110
The cellular glycocalyx plays a crucial role in making pancreatic cancer one of the deadliest malignancies globally. It complicates early detection and reduces the effectiveness of conventional therapies. In pancreatic cancer, the components of the glycocalyx are often upregulated or abnormally glycosylated, promoting tumor progression through immune evasion, enhanced metastasis, and drug resistance. While these biochemical effects are known, the biophysical impact of the glycocalyx on cancer cells is less understood. In our study, we explored the structural and biomechanical effects of modifying the glycocalyx architecture in pancreatic cancer cells using various chemical compounds. We employed a recently developed Atomic Force Microscopy nanomechanical mapping method to visualize cellular mechanical heterogeneities in a high spatiotemporal context. Our new approach allows for the viscoelastic inversion of high-resolution spatiotemporal data at rates which are orders of magnitude faster (more than 37,386-fold) than optimizing a traditional rheological model for each pixel. Then, we investigated the architectural and biophysical effects of glycocalyx architectural modulation in pancreatic cancer cells. Perturbations of hyaluronic acid (HA), sialic acid (SA), mucins, and N-glycans through enzymatic treatments led to significant architectural remodeling of the cell surface. Interestingly, removal of SA and mucins resulted in a softer and more fluid cell surface, while removal of HA softened and increased viscosity. In addition, preliminary cytokine expression results suggested that SA removal leads to a pronounced pro-inflammatory response (IL-2, IL-8, INF-γ among others) of human cytotoxic CD8+ T Lymphocytes, greater than removing other glycocalyx components. Lastly, a glycomics study also revealed unique changes in the structure of N- and O-glycans, with significantly more heterogeneity in the structure of N-glycans on pancreatic cancer cells, and O-glycans showing a particularly higher degree of SA deposition. Our findings suggest that the glycocalyx of human pancreatic ductal adenocarcinoma cells fundamentally regulate extracellular surface architecture, mechanical properties, composition, and function, thereby promoting tumor progression and metastasis by acting as a physical barrier to antitumor responses.
Natalie Jaeger (Harms lab), “Many mutations have different effects on different protein conformations”
Molecular Biosciences Trainee Talks
Jan 26, 2026 | 3:00 pm | Allen 141 and via Zoom (via IMB mailing list)
Learn more about the talks and see the full MBTT schedule at http://par.uoregon.edu/ (site only accessible from the UO network or VPN)
Stefanie Redemann, PhD
Associate Professor
|
University of Virginia
IMB Seminar Series
Jan 20, 2026 | 4:00 pm | Willamette 110
Sarah Clark, PhD
Assistant Professor, Department of Biochemistry & Biophysics
|
Oregon State University
IMB Seminar Series
Jan 13, 2026 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Abstract: Cells and cellular organelles are surrounded by membranes that are constantly undergoing lipid modification due to processes like cell growth, organelle biogenesis, exocytosis, and phagocytosis. Bridge-like lipid transport proteins (BLTPs) have emerged as key players in all of these processes due to their role in lipid transport. BLTPs localize to membrane contact sites, where they fold into hydrophobic tunnels that are proposed to function like “lipid superhighways” that mediate the bulk transfer of lipids from donor to acceptor membranes. Despite the fundamental importance of BLTPs for cellular function, the mechanism of lipid transfer remains enigmatic. Here, we present the subunit composition and cryo-electron microscopy structure of the native LPD-3 BLTP complex isolated from transgenic C. elegans. Our results suggest a model for how the LPD-3 complex mediates bulk lipid transport and provide a foundation for mechanistic studies of BLTPs.
Bio: Sarah Clark is an Assistant Professor in the Department of Biochemistry and Biophysics at Oregon State University. Research in the Clark lab is focused on gaining mechanistic insight into two important areas of cellular biology: sensory transduction and lipid transport. Sarah earned her B.S. in Biochemistry from the University of California, Davis, where she conducted organic chemistry research. She received her Ph.D. from Oregon State University in Molecular and Cellular Biology under the supervision of Elisar Barbar, where she studied the dynamics and function of intrinsically disordered proteins. Sarah completed her post-doctoral training in Eric Gouaux’s lab at Oregon Health and Science University, where she studied the molecular mechanisms that underlie the sensations of hearing and balance in vertebrates. During her postdoc, Sarah solved the cryo-electron microscopy structures of the protein complexes that are necessary for hearing and developed methods to study native membrane protein complexes. The Clark lab applies these methods to explore how organisms sense touch and how cells shuttle lipids from one organelle to another. The lab uses cryo-electron microscopy to visualize the architecture of the protein complexes at the heart of these cellular processes and complements structural studies with other biophysical, biochemical, and functional techniques.
Dr. Michiko Shimoda
Director, Core Immunology Lab, UCSF
|
Co-Founder VGN BIO
Career Exploration Speaker Series
Nov 5, 2025 | 4:00 pm | Novick Room - Streisinger 225
Refreshments served at 3:45 PM prior to talk at 4:00 PM for all attendees.
Nick Pokorzynski, PhD
Assistant Professor
|
Oregon State University
IMB Seminar Series
Nov 4, 2025 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Most antibiotics only kill growing bacteria. Thus, slower bacterial growth leads to antibiotic tolerance. During infection, Salmonella enterica serovar Typhimurium faces low cytoplasmic Mg2+, which slows growth and increases tolerance to antibiotics targeting cell wall synthesis and DNA gyrase. We now report that this same condition renders S. Typhimurium vulnerable to the RNA polymerase (RNAP) inhibitor rifampicin. This specific vulnerability results from a reduction in the amounts of RNAP subunits RpoB and RpoC that is dependent on the protease Lon and master virulence regulator PhoP. By decreasing RNAP amounts, S. Typhimurium advances specific transcription of virulence determinants. Our results uncover a pathogen vulnerability concealed by clinical microbiology conditions that emerges from the activation of bacterial virulence.
Mike Harms, PhD
Associate Professor
|
University of Oregon
IMB Seminar Series
Oct 28, 2025 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Claire Richardson, PhD
Assistant Professor
|
University of Wisconsin
IMB Seminar Series
Oct 21, 2025 | 12:00 pm | Knight Campus Beetham Family Seminar Room
Neurons have exceptionally long lifespans. By contrast, the proteins and organelles within neurons are continuously being degraded, largely by lysosomes, and replaced to ensure their quality and proper abundance. Illustrating this importance of this continuous turnover for neuron maintenance, dysfunctional degradation of neuronal subcellular components leads to neurodegenerative diseases including Alzheimer’s disease, and it contributes to aging and diseases of aging, wherein degradative cargoes accumulate. I will discuss two ongoing projects in my lab that use Caenorhabditis elegans to investigate aspects of lysosome-mediated turnover within neurons. First, we ask how neuronal lysosomal capacity is regulated. We show that Transcription Factor EB (TFEB)/HLH-30 has a basal role of expanding neuronal lysosomal capacity in early adulthood, which is required to maintain neuron morphological integrity during aging. Second, we ask how synaptic vesicle protein turnover is controlled, as the proper abundance and composition of synaptic vesicles is important for neurotransmission. To address this, we developed a fully genetically encoded, fluorescence microscopy method to visualize protein turnover with subcellular resolution in vivo, called ARGO (Analysis of Red Green Offset). I will show how we used ARGO to begin to understand the turnover of Synpatogyrin/SNG-1.
RNA Club Film Screening
"Cracking the Code: Phil Sharp and the Biotech Revolution"
RNA Club
Oct 20, 2025 | 4:00 pm | EMU, Redwood Auditorium 214
Host:
Oregon RNA Club
"Cracking the Code: Phil Sharp and the Biotech Revolution"
Cracking the Code, narrated by Mark Ruffalo, is an inspiring story of vision, perseverance, and the power of science to change the world. Phil Sharp’s journey from a Kentucky farm boy to Nobel laureate embodies the American Dream and the triumph of entrepreneurial spirit. His 1977 groundbreaking discovery of RNA splicing rewrote the rules of molecular biology and ignited a life-saving scientific revolution, laying the foundation for an industry that has become a cornerstone of global innovation and economic growth – and transformed the health of billions of patients worldwide.
Cracking the Code, narrated by Mark Ruffalo, is an inspiring story of vision, perseverance, and the power of science to change the world. Phil Sharp’s journey from a Kentucky farm boy to Nobel laureate embodies the American Dream and the triumph of entrepreneurial spirit. His 1977 groundbreaking discovery of RNA splicing rewrote the rules of molecular biology and ignited a life-saving scientific revolution, laying the foundation for an industry that has become a cornerstone of global innovation and economic growth – and transformed the health of billions of patients worldwide.
Carole LaBonne, PhD
Professor and Chair, Department of Molecular Biosciences, Erastus O. Haven Professor of Life Sciences
|
Northwestern
IMB Seminar Series
Oct 14, 2025 | 12:00 pm | Knight Campus Beetham Family Seminar Room
The neural crest is a vertebrate-specific stem cell population that helped drive the origin and evolution of vertebrates. A distinguishing feature of these cells is their multi-germ layer potential, which has parallels to another stem cell population—pluripotent stem cells of the vertebrate blastula. Our recent studies have shown that neural crest potency derives in part from the deployment of pluripotency gene regulatory network (GRN) components. We have shown that soxB1 factors, krüppel-like factors (klfs), and the pluripotency regulator pou5f cooperate with neural play border genes such as pax3 and zic1 to establish neural plate border identity, but soxB1 expression must be extinguished for neural crest progression to occur. soxb1 factors are replaced in the neural crest GRN by soxE factors and studies of this change of sox provides novel insights into how GRNs evolve. Moreover our recent work suggests that pluripotent blastula (inner cell mass) cells evolved from an ancient neural progentor cell population, and that this was driven in part by duplication and divergence of an ancestral pou3f like protein leading to the pou5f proteins of extant vertebrates.
POSTPONED Kamena Kostova, PhD
Assistant Investigator
|
Stower's Institute for Medical Research
IMB Seminar Series
Oct 7, 2025 | 12:00 pm | Knight Campus Beetham Family Seminar Room
The ribosome is the essential molecular machine responsible for translation of mRNA to protein. Its composition is complex; it comprises four ribosomal RNAs (rRNAs) and approximately 80 ribosomal proteins that form two subunits: the small 40S and the large 60S. For decades, the composition of the ribosome has been deemed static; ribosomes are assembled and they do not change in response to environmental stimuli, in different tissues or organs, or during disease initiation and progression. Now we know that this notion is simply not true, as changes in both rRNA and proteins have been documented. In general, there are two ways in which the ribosome composition can change: as a result of damage or due to programmed changes in ribosomal components. Indeed, mutations, environmental stress, or mistakes during assembly can lead to defective ribosomes. Accumulation of such faulty ribosomes is associated with diseases such as neurodegeneration, cancer and ribosomopathies, further emphasizing the importance of these pathological changes for human health. Alterations in the ribosomal RNA and proteins have also been associated with normal physiological processes, such as development, differentiation, and adaptation. For example, zebrafish larvae assemble two structurally distinct types of ribosomes, maternal and somatic, during early development. Although we now know that the composition of the ribosome is dynamic, we have a limited understanding of how changes in the ribosome impact protein production and facilitate complex physiological processes. In my laboratory, we have developed unique tools and biological systems to answer two outstanding questions in the translation field: 1) What are the quality control factors that cope with defective ribosomes? and 2) How do programmed changes in the ribosome composition regulate translation to facilitate development?
Dr. Todd Howren
Chief Commercial Officer
|
Northern RNA
Career Exploration Speaker Series
Oct 1, 2025 | 4:00 pm | Novick Room - Streisinger 225
Refreshments served at 3:45 PM prior to talk at 4:00 PM for all attendees.