Following a one-year postdoctoral stint at the University of Southern California, she became a Beckman Senior Research Fellow at the Beckman Institute Laser Resource Center at the California Institute of Technology where she investigated the structures and dynamics of an intrinsically disordered and amyloid forming protein using time-resolved spectroscopic measurements. 1-877-NHLBI4U (1-877-645-2448) Biography Jennifer C. Lee graduated with a B.S. Biochim Biophys Acta Proteins Proteom. 2019 Oct 01;1867(10):961-969. in chemistry and a B.A. She was awarded an NIH Graduate Partnerships Program Outstanding Mentor Award in 2009. Dr. Lee is a member of the American Chemical Society and the Protein Society.Dr. She was awarded an NIH Graduate Partnerships Program Outstanding Mentor Award in 2009. Fate plasticity and reprogramming in genetically distinct populations of Danio leucophores.Lewis VM, Saunders LM, Larson TA, Bain EJ, Sturiale SL, Gur D, Chowdhury S, Flynn JD, Allen MC, Deheyn DD, Lee JC, Simon JA, Lippincott-Schwartz J, Raible DW, Parichy DM Interestingly, amyloid fibrils can also serve essential biological roles in organisms ranging from bacteria to humans. Interestingly, amyloid fibrils can also serve essential biological roles in organisms ranging from bacteria to humans.
Steady-state and time-resolved fluorescence and anisotropy measurements are utilized to probe local conformational changes. Bethesda, MD 20892. 31 Center Drive. Lysophospholipids induce fibrillation of the repeat domain of Pmel17 through intermediate core-shell structuresPedersen JN, Jiang Z, Christiansen G, Lee JC, Pedersen JS, Otzen DE. Aggregation of proteins into amyloid structures is a hallmark of human diseases such as Alzheimer’s, Parkinson’s, and Hungtington’s. 2019 Jun 21;294(25):9973-9984.
More recently, she has studied the interaction between α-synuclein and glucocerebrosidase, the enzyme deficient in Gaucher disease, to explain why mutations in GBA, the gene encoding glucocerebrosidase, is a risk factor for Parkinsonism.Ultimately, Dr. Lee wants to understand the mechanisms of amyloid aggregation and function at a detailed level in the context of the multiple cellular compartments with which they interact. View Jennifer C. Lee’s profile on LinkedIn, the world's largest professional community. Jennifer C. Lee graduated with a B.S. She studies amyloids, highly disordered proteins that act like chameleons and change their shape and stability in ways that are bad for human health. Dr. Lee is a member of the American Chemical Society and the Protein Society. in economics from the University of California, Berkeley, in 1997, and earned her Ph.D. in chemistry from the California Institute of Technology in 2002. Jennifer Lee, Ph.D., is searching to find order in a chaotic system—and to discover how that chaos begins.
In 2006, Dr. Lee joined the NHLBI as a tenure-track Investigtor. Structural Insights into α-Synuclein Fibril Polymorphism: Effects of Parkinson's Disease-Related C-Terminal Truncations. in chemistry and a B.A.
J Mol Bio Jennifer C. has 3 jobs listed on their profile. Receive automatic alerts about NHLBI related news and highlights from across the Institute.Receive automatic alerts about NHLBI related news and highlights from across the Institute.Receive automatic alerts about NHLBI related news and highlights from across the Institute.COVID-19 is an emerging, rapidly evolving situation She would like to not only describe the self-assembly process and its critical features, but also determine points of intervention in which amyloid assembly is linked to pathology.Jennifer C. Lee graduated with a B.S. in chemistry and a B.A. In 2006, Dr. Lee joined the NHLBI as a tenure-track Investigtor.
Moreover, many polypeptides with widely varying amino acid sequences and folded states can form amyloid in vitro, implying common formation pathways.Dr. J Biol Chem. Jennifer has 7 jobs listed on their profile. Dr. Lee is also particularly interested in the effect of metal ions and the influence of different cellular membrane compartments on protein misfolding and aggregation. Complementary methods, such as dynamic light scattering and atomic force microscopy, are also used. Dr. Lee is a member of the American Chemical Society and the Protein Society.Yap TL, Jiang Z, Heinrich F, Gruschus JM, Pfefferkorn CM, Barros M, Curtis JE, Sidransky E, Lee JC. A broad approach is taken to gain insights at the residue- to ultrastructural-level. 2019 Sep 06;431(19):3913-3919. in economics from the University of California, Berkeley, in 1997, and earned her Ph.D. in chemistry from the California Institute of Technology in 2002. Jennifer has 6 jobs listed on their profile. A central question under investigation is: what are the distinguishing features between functional and pathological amyloids? Proc Natl Acad Sci U S A. For example, do functional amyloids aggregate such that specific pathogenic conformations are avoided? A broad approach is taken to gain insights at the residue- to ultrastructural-level. JENNIFER C. LEE, PH.D., NHLBI Senior Investigator, Laboratory of Protein Conformation and Dynamics, National Heart, Lung, and Blood Institute Education: University of California at Berkeley, Berkeley, Calif. (B.S. A central question under investigation is: what are the distinguishing features between functional and pathological amyloids? Lee’s laboratory integrates a variety of biophysical and biochemical techniques to understand the molecular mechanisms of amyloid formation. 2019 Jun 11;116(24):11806-11811. Lee focuses her research efforts on studying changes in protein conformation and dynamics important for the mechanisms by which amyloid structures assemble under normal and pathological conditions.
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