Bi-weekly: Thursdays, 12 pm EDT/EST, 9 am PT/PST, 5 pm BST/BDT, 6 pm CEST/CET
https://dfci.zoom.us/webinar/register/WN_m7JJaw52T8yZYt8-ykL6UQ
Some seminars were recorded and accessible for a limited time on our youtube channel.
Upcoming Speakers
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February 19th, 2026
Host: Katherine Donovan / Mikolaj Slabicki
Chase Suiter
University of Washington
Multiplex design and discovery of proximity handles for programmable proteome editing.
Chase Suiter develops technologies to profile and program protein degradation. As part of his graduate work, he combined computational protein design and high-throughput cellular screening methods to discover “proximity handles” that enable programmable proteome editing using effectors from the UPS and autophagy pathways. His long-term goal is to develop computationally designed therapeutics to treat complex human disease.
Carles Galdeano
University of Barcelona
From Exploiting Binding Sites on E3 ligases to Developing Allosteric Modulators of the FBW7 E3 Ligase.
Dr Carles Galdeano is currently an Associate Professor at the University of Barcelona. He obtained his PhD in medicinal chemistry at the University of Barcelona. After that, he spent three years post-doc in Alessio Ciulli’s lab (first at the University of Cambridge and later at the University of Dundee) where they developed the first potent VHL ligands described. His postdoctoral discoveries represented a breakthrough in the PROTACs field. In 2015, he returned to the University of Barcelona to work in collaboration with Prof Barril until 2019, when he started his independent research group. Dr Galdeano is also co-founder of Oniria Therapeutics. His lab is interested in expanding the druggable proteome since most proteins are still considered undruggable for conventional drug discovery approaches.
March 5th, 2026
Host: Breanna Zerfas
Safety of Targeted Protein Degraders: HESI Global’s Collaborative Framework and Portfolio Highlights.
Targeted protein degraders (TPDs) represent a rapidly expanding therapeutic modality, yet their novel mechanisms introduce unique and unresolved safety challenges. The Targeted Protein Degrader Safety Committee at the Health and Environmental Sciences Institute (HESI Global) is a precompetitive, multi-sector consortium dedicated to advancing scientific consensus on the translational safety assessment of TPDs. The session will highlight two collaborative efforts from the Cereblon (CRBN) Workgroup: 1) a review that synthesizes current knowledge on the biology of CRBN, off-target neosubstrate degradation, species differences, and best practices for safety testing of CRBN-recruiting molecular glue degraders and PROTACs; 2) ongoing experimental work designed to directly link neosubstrate degradation with human-relevant in vitro teratogenicity signals using cell–based assays and proteomics. Together, these efforts exemplify HESI Global’s role in generating science-based actionable, translational reference information to support the safe development of next-generation TPDs.
HESI TPD Safety Committee Website: https://hesiglobal.org/targeted-protein-degrader-safety/
Cissy Li
HESI Global
Cissy Li is a scientific program manager at the Health and Environmental Sciences Institute (HESI Global). She holds a PhD in Molecular and Translational Toxicology from the Johns Hopkins Bloomberg School of Public Health and a Certificate in Risk Sciences and Public Policy. She has eight years of experience at the U.S. Food and Drug Administration, where she served in the Center for Food Safety and Applied Nutrition and the Center for Tobacco Products. Her work spanned chemical safety and risk assessment, regulatory science, and interdisciplinary research focused on evaluating toxicity and public health impact, where she led cross-functional scientific teams and helped advance evidence-based regulatory decision-making. At HESI, she now manages multi-stakeholder, collaborative, precompetitive research in the Targeted Protein Degrader Safety and Antibody-Drug Conjugate Safety programs.
James Sidaway
ApconiX
James Sidaway is an innovative mechanistic toxicologist with over 25 years of experience in the pharmaceutical industry. As a molecular-investigative toxicologist at AstraZeneca, he helped resolve safety issues for drug discovery and development projects across the major therapy areas. At AstraZeneca and as an independent consultant, he pioneered advanced in vitro models for organ toxicity screening and applied novel technology and informatics platforms for safety assessment. In 2021, James joined ApconiX, a UK-based company specializing in nonclinical toxicology and ion channel electrophysiology, to enhance its target safety assessment function. He is now head of ApconiX’s Safety Science Group, leading over 20 toxicologists and data scientists to deliver target safety and drug toxicity solutions through expert insight and state-of-the-art informatics.
Benjamin Elser
Bristol Myers Squibb
Benjamin Elser is a Senior Scientist in the Developmental and Reproductive Toxicology group at Bristol Myers Squibb. He obtained his PhD in Human Toxicology from the University of Iowa. In his current role at BMS, he is responsible for the design, oversight, and interpretation of developmental and reproductive toxicology studies, as well as the development of in vitro screening methods to assess the teratogenic risk of drug candidates. As a member of the HESI Targeted Protein Degrader Safety Committee, he contributes to a collaborative project focused on evaluating the relationship between neosubstrate degradation and in vitro teratogenicity signals for Cereblon-engaging targeted protein degraders.
March 19th, 2026
Host: Mikolaj Slabicki
Daniel Finley
Harvard Medical School
Global remodeling of the proteome.
Dr. Finley's group is interested in various aspects of the ubiquitin-proteasome system. Current work on the proteasome mainly involves factors that reversibly associate with it and regulate its activity, such as the deubiquitinating enzyme Ubp6, the ubiquitin ligase Hul5, and the proteasome inhibitor Ecm29. Ubp6 attacks ubiquitin chains on proteins that have docked at the proteasome, suppressing their degradation, while Hul5 opposes Ubp6, adding to these chains to promote processive degradation of the ubiquitinated protein. Another project involves global proteome remodeling, which occurs in various cell types undergoing differentiation, and may involve thousands of proteins. Proteome-wide remodeling programs play a key role in transitioning cells to differentiated states, and are principally driven by a handful of specialized ubiquitin ligases.
John Hanna
Brigham & Women’s Hospital
Development of Novel Proteasome Inhibitors Based on the Endogenous Inhibitor PI31
John Hanna is an Associate Professor at Harvard Medical School and an associate Pathologist in the Department of Pathology at the Brigham & Women’s Hospital. John received his undergraduate degree from Stanford and his MD and PhD degrees from HMS. John’s lab studies the basic mechanisms of protein degradation by the proteasome, with an emphasis on the assembly and regulation of the proteasome’s core particle, which is the subcomplex that harbors its proteolytic active sites. John is also a practicing physician focused on skin and soft tissue pathology, and has separate investigative interests in the molecular and cellular basis of cutaneous tumors.
April 2nd, 2026
Host: John Che
Qian Cong
UT Southwestern
Computing the human interactome.
Dr. Cong is a computational biologist interested in mining large-scale data for biological insights. She focused on evolutionary genomics as a graduate student and worked on computational structural biology as a postdoctoral fellow. Leveraging on her expertise in genomics, evolution, and protein structure modeling, her lab uses coevolution signals between proteins to predict protein-protein interaction (PPI) and model 3D structures of protein complexes on a proteome-wide scale. The approach showed comparable performance to large-scale experimental screens in bacteria. Recent breakthroughs in modeling protein structures to atomic accuracy using deep learning (DL) methods (AlphaFold and RoseTTAFold) further empowered our PPI screen. In a project she co-led, they identified and modeled hundreds of Yeast protein complexes that provided functional insights into many biological processes. This advance was recognized as part of “the breakthrough of the year 2021” by Science. Despite the success of the methods in yeast, applying them to human proteins posed significant challenges. Recently, she overcame these hurdles by enhancing coevolution signals with draft genomes and developing new deep-learning methods designed explicitly for PPI prediction. With these substantial methodological advancements, she is now poised to explore the human interactome and uncover insights into protein function and human diseases.
Link to your lab website:
April 16th, 2026
Host: Zuzanna Kozicka / Sean Gao
Hong-Yu Li
University of Texas Health Science Center
Endocytic Medicinal Chemistry: Overcoming Delivery Barriers in Induced-Proximity Therapeutics.
Dr. Hong-yu Li is a medicinal chemist and drug hunter trained at the University of Tokyo (Ph.D.), with postdoctoral research at Columbia University and Harvard University. He previously worked in oncology drug discovery at Eli Lilly & Company, where he contributed to multiple clinical candidates, including the development of the FDA-approved CDK4/6 inhibitor abemaciclib (Verzenio®).
His academic research, conducted at the University of Arizona, the University of Arkansas for Medical Sciences, and currently at the University of Texas Health Science Center at San Antonio, focuses on achieving translational impact by overcoming fundamental limitations in small-molecule drug design.
In the field of protein degradation, his research group was the first to demonstrate the degradation of previously undrugable targets through DNA double-helix–based molecular recognition, establishing translational feasibility for a new class of degraders. The Li laboratory has also made key chemical contributions, including the identification of 3-phthalimide acid as a cereblon ligand and the development of scalable synthetic methodologies for VHL ligands. More recently, his team discovered that CD36 functions as a receptor mediating the endocytic uptake of PROTACs and other large or polar molecules, leading to the establishment of an endocytic medicinal chemistry framework that addresses a central delivery bottleneck in induced-proximity therapeutics.
Vanessa Narin Dippon
Harvard University
Identification of an Allosteric Site on the E3 Ligase Adapter Cereblon.
Born in San Francisco, California, Vanessa Narin Dippon received her Bachelor of Arts in Chemistry from Columbia University in 2021 where she studied under Professor Tomislav Rovis. In the Rovis lab, Vanessa studied the directed evolution of monomeric streptavidin rhodium(III) artificial metalloenzyme to catalyzes the formation of enantioenriched d-lactams. Vanessa is currently a PhD candidate and National Science Foundation (NSF) Graduate Research Fellow at the Harvard University Department of Chemistry and Chemical Biology studying under Professor Christina Woo. Her research utilizes chemical biology, organic synthesis, and mass spectrometry to study the E3 ligase substrate adapter protein cereblon. Specially, Vanessa is investigating the functional contribution of a novel allosteric site on cereblon and its implications for treating hematopoietic malignancies.
April 30th, 2026
Host: Mikolaj Slabicki
Ning Zheng
University of Washington
Orthosteric Molecular Glue (OMG) Inhibitors: A Selective Blockage.
Dr. Ning Zheng obtained his PhD from University of Texas Southwestern Medical Center in 1997 after he attended Fudan University in Shanghai, China. He did his postdoctoral studies at Memorial Sloan-Kettering Cancer Center and joined the faculty at the Department of Pharmacology in the University of Washington in 2002. He is currently Howard Hughes Medical Institute Investigator and an AAAS Fellow. His current research focuses on structural and functional analyses of ubiquitin ligases, their roles in human biology and plant hormone signaling, and their potential in mediating targeted protein degradation for novel therapeutic drug development. A pioneer in Targeted Protein Degradation, he originated the "molecular glue" concept to explain the action of auxin and jasmonate. His research continues to elucidate how this powerful effect is utilized by nature and leveraged for novel therapeutics.