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            <div class="field field--name-field-component-lab-banner-descr field--type-text-long field--label-hidden field__item"><p>The Laboratory of Protein Conformation and Dynamics integrates complementary biophysical and biochemical techniques to understand the molecular mechanisms of amyloid formation.</p>
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<img loading="lazy" src="/modules/custom/nhlbi_blazy/images/clear.png" width="200" height="200" alt="Jennifer Lee" data-src="/sites/default/files/styles/square_image/public/2022-10/JCLeeHeadshot2022crop.jpg?itok=7d6j9YRV" class="b-lazy image-style-square-image" />


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<span>Jennifer Lee, Ph.D.</span>

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              <div class="field__item"><p>Dr. Lee’s laboratory integrates a variety of biophysical and biochemical techniques to understand the molecular mechanisms of amyloid formation. Aggregation of proteins into amyloid structures is a hallmark of human diseases such as Alzheimer’s, Parkinson’s, and Hungtington’s. Interestingly, amyloid fibrils can also serve essential biological roles in organisms ranging from bacteria to humans. Moreover, many polypeptides with widely varying amino acid sequences and folded states can form amyloid in vitro, implying common formation pathways.</p>

<p>Dr. 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. A central question under investigation is: what are the distinguishing features between functional and pathological amyloids? For example, do functional amyloids aggregate such that specific pathogenic conformations are avoided? Or is the formation and degradation of amyloids regulated more efficiently in healthy cells? </p>

<p>To begin to understand these differences, Dr. Lee is currently investigating the mechanisms of amyloid formation for two human proteins: α-synuclein, which is localized to nerve terminals and associated with Parkinson’s disease, and Pmel17, which serves as structural scaffolding for melanin deposition in skin and eyes.</p>

<p>To determine the critical features guiding amyloid formation, Dr. Lee is characterizing how individual amino acid residues affect protein-protein interaction during the amyloid assembly process. A broad approach is taken to gain insights at the residue- to ultrastructural-level. Steady-state and time-resolved fluorescence and anisotropy measurements are utilized to probe local conformational changes. Protein secondary structure is determined using circular dichroism spectroscopy, and transmission electron microscopy is used to visualize filament morphology. Complementary methods, such as dynamic light scattering and atomic force microscopy, are also used. 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. Emerging methods such as neutron reflectometry are also employed to investigate protein-lipid interactions. 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.</p>

<p>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. 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.</p>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Genetically encoded lysine photocage for spatiotemporal control of TDP-43 nuclear import" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2024-03/231130_Graphical_Abstract.jpg?itok=54fliAFF" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Shadish, J.R. & <strong>Lee, J.C.</strong> (2024) Genetically encoded lysine photocage for spatiotemporal control of TDP-43 nuclear import, Biophys. Chem. 307, 107191. DOI: </span><a href="https://www.sciencedirect.com/science/article/pii/S0301462224000206" rel="noreferrer"><span>10.1016/j.bpc.2024.107191</span></a></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Water bend‒libration as a cellular Raman imaging probe of hydration" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2024-01/Ramos_PNAS_0_0.png?h=5649ff21&itok=Nc8eVt4l" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p>Ramos, S. & <strong>Lee, J.C.</strong> (2023) Water bend‒libration as a cellular Raman imaging probe of hydration, <em>Proc. Natl. Acad. Sci</em>. U.S.A., 120, e2313133120. DOI: <a href="https://www.pnas.org/doi/10.1073/pnas.2313133120" rel="noreferrer">10.1073/pnas.2313133120</a></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2023-01/Graphical_Abstract01b.jpg?itok=IypR8phk 1x" media="all and (min-width: 1824px)" type="image/jpeg" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2023-01/Graphical_Abstract01b.jpg?itok=IypR8phk 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/jpeg" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2023-01/Graphical_Abstract01b.jpg?itok=IypR8phk 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/jpeg" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Genetically encoded aryl alkyne for Raman imaging of intracellular α-synuclein fibrils" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2023-01/Graphical_Abstract01b.jpg?itok=IypR8phk" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p>Watson, M.D. & <strong>Lee, J.C.</strong> (2023) Genetically encoded aryl alkyne for Raman imaging of intracellular α-synuclein fibrils, <em>J. Mol. Biol</em>. 435, 167716. DOI: <a href="https://doi.org/10.1016/j.jmb.2022.167716" rel="noreferrer">10.1016/j.jmb.2022.167716</a></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/1_0.png?itok=1DUjF0wX 1x" media="all and (min-width: 361px) and (max-width:767px)" type="image/png" width="768" height="512"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/1_0.png?itok=1DUjF0wX 1x" media="all and (min-width: 0px) and (max-width:360px)" type="image/png" width="768" height="512"/>
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/1_0.png?itok=EJYiLos4 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/1_0.png?itok=EJYiLos4 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Tryptophan probes of TDP-43 C-terminal domain amyloid formation" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/1_0.png?itok=EJYiLos4" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Shuster, S.O. & <strong>Lee, J.C.</strong> (2021) Tryptophan probes of TDP-43 C-terminal domain amyloid formation, <em>J. Phys. Chem. B</em>., 125, 3781-3789. <a href="https://pubs.acs.org/doi/abs/10.1021/acs.jpcb.1c00767" rel="noreferrer"><span>DOI: </span><span>10.1021/acs.jpcb.1c00767</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/2_0.png?itok=qFY92Xi1 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/2_0.png?itok=qFY92Xi1 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Membrane interactions of α-synuclein probed by neutrons and photons" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/2_0.png?itok=qFY92Xi1" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p>Kaur U. & <strong>Lee, J.C.</strong> (2021) Membrane interactions of α-synuclein probed by neutrons and photons, <em>Acc. Chem. Res</em>. 54, 302-310. <a href="https://dx.doi.org/10/1021/acs.accounts.0c00453" rel="noreferrer"><span>DOI:</span><span> 10.1021/acs.accounts.0c00453</span></a></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/3_0.png?itok=2oLWriMm 1x" media="all and (min-width: 361px) and (max-width:767px)" type="image/png" width="768" height="512"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/3_0.png?itok=2oLWriMm 1x" media="all and (min-width: 0px) and (max-width:360px)" type="image/png" width="768" height="512"/>
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/3_0.png?itok=SfwkoxWr 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/3_0.png?itok=SfwkoxWr 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Raman spectral imaging of 13C2H15N-labeled α-synuclein amyloid fibrils in cells" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/3_0.png?itok=SfwkoxWr" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Watson, M.D., Flynn, J.D., <strong>Lee, J.C.</strong> (2021) Raman spectral imaging of 13C2H15N-labeled α-synuclein amyloid fibrils in cells, <em>Biophys. Chem</em>. 269, 106528. DOI: <a href="https://doi.org/10.1016/j.bpc.2020.106528" target="_blank" title="Persistent link using digital object identifier" rel="noopener noreferrer"><span>10.1016/j.bpc.2020.106528</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/4_0.png?itok=rsL3y5WT 1x" media="all and (min-width: 0px) and (max-width:360px)" type="image/png" width="768" height="512"/>
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/4_0.png?itok=Eff33L6M 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/4_0.png?itok=Eff33L6M 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Terminal alkynes as Raman probes of α-synuclein in solution and in cells" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/4_0.png?itok=Eff33L6M" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Flynn, J.D., Gimmen, M., Dean, D.N., Lacy, S.M., <strong>Lee, J.C.</strong> (2020) Terminal alkynes as Raman probes of </span><span lang="DE" xml:lang="DE" xml:lang="DE">α</span><span>-synuclein in solution and in cells, <em>ChemBioChem,</em> 21, 1582-1586. <span>DOI: </span><a href="https://doi.org/10.1002/cbic.202000026" target="_blank" rel="noopener noreferrer"><span>10.1002/cbic.202000026</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/5_0.png?itok=3jaqbrWj 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/5_0.png?itok=3jaqbrWj 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="N-terminal acetylation affects α-synuclein fibril polymorphism" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/5_0.png?itok=3jaqbrWj" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Watson, M.D. & <strong>Lee, J.C.</strong> (2019) N-terminal acetylation affects </span><span lang="DE" xml:lang="DE" xml:lang="DE">α</span><span>-synuclein fibril polymorphism, <em>Biochemistry</em>, 58, 3630-3633. DOI: <a href="https://pubs.acs.org/doi/10.1021/acs.biochem.9b00629" rel="noreferrer"><span>10.1021/acs.biochem.9b00629</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/6.png?itok=wJwA3c58 1x" media="all and (min-width: 361px) and (max-width:767px)" type="image/png" width="768" height="512"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/6.png?itok=wJwA3c58 1x" media="all and (min-width: 0px) and (max-width:360px)" type="image/png" width="768" height="512"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/6.png?itok=vHteT4b8 1x" media="all and (min-width: 1824px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/6.png?itok=vHteT4b8 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/6.png?itok=vHteT4b8 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="J. Mol. Biol cover" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/6.png?itok=vHteT4b8" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Ni, X., McGlinchey, R.P., Jiang, J., <strong>Lee, J.C.</strong> (2019) Structural insights into </span><span><span lang="DE" xml:lang="DE" xml:lang="DE">α-synuclein </span><span>fibril polymorphism: Effects of Parkinson’s disease-related C-terminal truncations, <em>J. Mol. Biol</em>. 431, 3913-3919</span></span><span>. DOI: <a href="https://doi.org/10.1016/j.jmb.2019.07.001" rel="noreferrer"><span>10.1016/j.jmb.2019.07.001</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/7.png?itok=uUKnG7KY 1x" media="all and (min-width: 0px) and (max-width:360px)" type="image/png" width="768" height="512"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/7.png?itok=Pdva3Mmg 1x" media="all and (min-width: 1824px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/7.png?itok=Pdva3Mmg 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/7.png?itok=Pdva3Mmg 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Segmental 13C-labeling and Raman microspectroscopy of α-synuclein amyloid formation" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/7.png?itok=Pdva3Mmg" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Flynn, J.D., Jiang, Z., <strong>Lee, J.C.</strong> (2018) Segmental 13C-labeling and Raman microspectroscopy of α-synuclein amyloid formation, <em>Angew. Chem. Int. Ed. Engl. </em>57, 17069-17072.<em> </em><a href="https://doi.org/10.1002/anie.201809865" target="_blank" rel="noopener noreferrer"><span lang="EN" xml:lang="EN" xml:lang="EN">DOI: </span><span lang="EN" xml:lang="EN" xml:lang="EN">10.1002/anie.201809865</span></a></span></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Raman fingerprints of amyloid structures" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/8.png?itok=JbikS4X1" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Flynn, J.D. & <strong>Lee, J.C.</strong> (2018) Raman fingerprints of amyloid structures, <em>Chem. Commun. </em>54, 6983-6986. DOI: <a href="http://pubs.rsc.org/en/content/articlehtml/2018/cc/c8cc03217c" rel="noreferrer"><span>10.1039/c8cc03217c</span></a></span></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Stimulation of α-synuclein amyloid formation by phosphatidyglycerol micellar tubules," data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/9.png?itok=4i5HJAD0" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Jiang, Z., Flynn, J.D., Teague, W.E., Gawrisch, K., <strong>Lee, J.C.</strong> (2018) Stimulation of α-synuclein amyloid formation by phosphatidyglycerol micellar tubules, <em>Biochim. Biophys. Acta Biomembr.</em>1860, 1840-1847<em>. </em></span><span><span lang="EN" xml:lang="EN" xml:lang="EN">DOI:</span></span><a href="https://www.sciencedirect.com/science/article/pii/S000527361830066X" rel="noreferrer"><span><span lang="EN" xml:lang="EN" xml:lang="EN">10.1016/j.bbamem.2018.02.025</span></span></a></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="J. Biol. Chem. Cover" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/10.png?itok=lyGrYCcf" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Flynn, J.D., McGlinchey, R.P., Walker III, R.L., <strong>Lee, J.C.</strong> (2018) Structural features of α-synuclein amyloid fibrils revealed by Raman spectroscopy, <em>J. Biol. Chem. </em>293, 767-776.<em> </em></span><span><span lang="EN" xml:lang="EN" xml:lang="EN">DOI:</span></span><span><a href="http://www.jbc.org/content/early/2017/11/30/jbc.M117.812388.short?rss=1" rel="noreferrer"><span lang="EN" xml:lang="EN" xml:lang="EN">10.1074/jbc.M117.812388</span></a></span></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Journal Cover - Biochemistry " data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/11_0.png?itok=VtnQ0hA9" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p>McGlinchey, R.P., Dominah, G., <strong>Lee, J.C.</strong> (2017) Taking a bite out of amyloid: Mechanistic insights into α-synuclein degradation by cathepsin L, <em>Biochemistry, </em>56, 3881-3884. DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/acs.biochem.7b00360" target="_new" rel="noopener noreferrer"><span>10.1021/acs.biochem.7b00360</span></a></p>

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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Segmental deuteration of α-synuclein for neutron reflectometry on tethered bilayers" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/12_0.png?itok=9ad--R0_" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Jiang, Z., Heinrich, F., McGlinchey, R.P., Gruschus, J.M., <strong>Lee, J.C.</strong> (2017) Segmental deuteration of α-synuclein for neutron reflectometry on tethered bilayers, <em>J. Phys. Chem. Lett.</em> 8, 29-34. DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/acs.jpclett.6b02304" target="_new" rel="noopener noreferrer"><span>10.1021/acs.jpclett.6b02304</span></a> </span></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Apolipoprotein C-III nanodiscs studied by site-specific tryptophan fluorescence" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/13_0.png?itok=Fyg5RhBx" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Brisbois, C.A. & <strong>Lee, J.C.</strong> (2016) Apolipoprotein C-III nanodiscs studied by site-specific tryptophan fluorescence, <em>Biochemistry</em>, 55, 4939-4948<em>. </em>DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/acs.biochem.6b00599" target="_new" rel="noopener noreferrer"><span>10.1021/acs.biochem.6b00599</span></a></span></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Single particle-tracking of human lipoproteins" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/14_0.png?itok=jOw6cCC0" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>de Messieres M., Ng A., </span><span lang="EN-GB" xml:lang="EN-GB" xml:lang="EN-GB">Duarte, C.J., Remaley,<em> </em>A.T., <strong>Lee, J.C.</strong> (2016) Single particle-tracking of human lipoproteins, <em>Anal. Chem</em>. 88, 596-599. DOI: </span><span><a href="http://pubs.acs.org/doi/abs/10.1021/acs.analchem.5b03749" target="_new" rel="noopener noreferrer"><span>10.1021/acs.analchem.5b03749</span></a></span></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Tryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-III" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/15_0.png?itok=vVxGnf_R" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Pfefferkorn, C.M., Walker III, R.L., He, Y., <strong>Lee, J.C.</strong> (2015) Tryptophan probes reveal residue-specific phospholipid interactions of apolipoprotein C-III,<em> Biochim. Biophys. Acta Biomembr.,</em>1848, 2821-2828. DOI: <a href="https://doi.org/10.1016/j.bbamem.2015.08.018" rel="noreferrer"><span>10.1016/j.bbamem.2015.08.018</span></a></span></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Molecular details of α-synuclein membrane association probed by neutrons and photons" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/16.png?itok=VVnwi4si" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Jiang, Z., Hess, S.K., Heinrich, F., <strong>Lee, J.C.</strong> (2015) Molecular details of α-synuclein membrane association probed by neutrons and photons, <em>J. Phys. Chem. B </em>119, 4812-4823. DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/jp512499r" target="_new" rel="noopener noreferrer"><span>10.1021/jp512499r</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/17.png?itok=8sLqaiZ_ 1x" media="all and (min-width: 0px) and (max-width:360px)" type="image/png" width="768" height="512"/>
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/17.png?itok=9jXnBai5 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/17.png?itok=9jXnBai5 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/17.png?itok=9jXnBai5" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Yap, T.L., Jiang, Z., Heinrich, F., Gruschus, J.M., Pfefferkorn, C.M., Barros M., Curtis, J.E., Sidransky, E., <strong>Lee, J.C.</strong> (2015) Structural features of membrane-bound glucocerebrosidase and α-synuclein probed by neutron reflectometry and fluorescence spectroscopy, <em>J. Biol. Chem. </em>290, 744-754. DOI: <a href="https://doi.org/10.1074/jbc.M114.610584" rel="noreferrer"><span>10.1074/jbc.M114.610584</span></a> </span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/18.png?itok=9PCukBPh 1x" media="all and (min-width: 361px) and (max-width:767px)" type="image/png" width="768" height="512"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/18.png?itok=9PCukBPh 1x" media="all and (min-width: 0px) and (max-width:360px)" type="image/png" width="768" height="512"/>
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/18.png?itok=AUh2k8ct 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/18.png?itok=AUh2k8ct 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/18.png?itok=AUh2k8ct" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Jiang, Z. & <strong>Lee, J.C.</strong> (2014) Lysophospholipid-containing membranes modulate the fibril formation of the repeat domain of a human functional amyloid, Pmel17, <em>J. Mol. Biol</em>. 426, 4074-4086. DOI: <a href="https://doi.org/10.1016/j.jmb.2014.10.009" rel="noreferrer"><span>10.1016/j.jmb.2014.10.009</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_phone/public/2021-07/19.png?itok=strr8Odx 1x" media="all and (min-width: 0px) and (max-width:360px)" type="image/png" width="768" height="512"/>
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/19.png?itok=MXb-TDO8 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/19.png?itok=MXb-TDO8 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Journal Cover - Chem Bio Chem " data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/19.png?itok=MXb-TDO8" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>McGlinchey, R.P., Jiang, Z., <strong>Lee, J.C.</strong> (2014) Molecular origin of</span><span lang="DE" xml:lang="DE" xml:lang="DE"> the pH dependent fibril formation of a functional amyloid</span><span>, <em>ChemBioChem</em>, 15, 1569-1572. DOI: <a href="https://doi.org/10.1002/cbic.201402074" rel="noreferrer"><span>10.1002/cbic.201402074</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/20.png?itok=-0OHaRkh 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/20.png?itok=-0OHaRkh 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Membrane remodeling by α-synuclein and effects on amyloid formation" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/20.png?itok=-0OHaRkh" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Jiang, Z., de Messieres, M., <strong>Lee, J.C.</strong> (2013) Membrane remodeling by α-synuclein and effects on amyloid formation, <em>J. Am. Chem. Soc</em>. 135, 15970-15973. DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/ja405993r" target="_new" rel="noopener noreferrer"><span>10.1021/ja405993r</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/21.png?itok=OUcXFge4 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Saposin C protects glucocerebrosidase against α-synuclein inhibition" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/21.png?itok=OUcXFge4" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Yap, T.L., Gruschus, J.M., Velayati, A., Sidransky, E., <strong>Lee, J.C.</strong> (2013) <span>Saposin C protects glucocerebrosidase against </span>α</span><span lang="DE" xml:lang="DE" xml:lang="DE">-</span><span>synuclein inhibition</span><span>, <em>Biochemistry</em> 52, 7161-7163. DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/bi401191v" target="_new" rel="noopener noreferrer"><span>10.1021/bi401191v</span></a></span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/22.png?itok=lBG5fmze 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/22.png?itok=lBG5fmze 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="NMR structure of calmodulin complexed to an N-terminally acetylated α-synuclein peptide" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/22.png?itok=lBG5fmze" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Gruschus, J.M., Yap, T.L., Pistolesi, S., Maltsev, A.S., <strong>Lee, J.C.</strong> (2013) NMR structure of calmodulin complexed to an N-terminally acetylated α-synuclein peptide, <em>Biochemistry</em> 52, 3436-3445.</span></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/23.png?itok=EyC00pjy 1x" media="all and (min-width: 1824px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/23.png?itok=EyC00pjy 1x" media="all and (min-width: 1440px) and (max-width: 1823px)" type="image/png" width="450" height="300"/>
              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/23.png?itok=EyC00pjy 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/23.png?itok=EyC00pjy" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p>McGlinchey, R.P., Gruschus, J.M., Nagy, A., <strong>Lee, J.C.</strong> (2011) Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level, <em>Biochemistry</em> 50, 10567-10569. DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/bi201578h" target="_new" rel="noopener noreferrer"><span>10.1021/bi201578h</span></a></p></div>
      
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              <source srcset="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/24.png?itok=u8zf8A0I 1x" media="all and (min-width: 1200px) and (max-width: 1439px)" type="image/png" width="450" height="300"/>
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Residue-specific fluorescent probes of α-synuclein: Detection of early events at the N- and C-termini during fibril assembly" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/24.png?itok=u8zf8A0I" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p>Yap, T.L., Pfefferkorn, C.M., <strong>Lee, J.C.</strong> (2011)<em> </em>Residue-specific fluorescent probes of α-synuclein: Detection of early events at the N- and C-termini during fibril assembly, <em>Biochemistry </em>50, 1963-1965. DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/bi2000824" target="_new" rel="noopener noreferrer"><span>10.1021/bi2000824</span></a></p>

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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Evidence for copper-dioxygen reactivity during α-synuclein fibril formation" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/25.png?itok=L-LN74K1" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Lucas, H.R., DeBeer, S., Hong, M.-S., <strong>Lee, J.C.</strong> (2010) Evidence for copper-dioxygen reactivity during α-synuclein fibril formation, <em>J. Am. Chem. Soc. </em>132, 6636-6637.DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/ja101756m" target="_new" rel="noopener noreferrer"><span>10.1021/ja101756m</span></a></span></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Tryptophan probes at the α-synuclein and membrane interface" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/26.png?itok=xKtpOjBW" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p>Pfefferkorn, C.M. & <strong>Lee, J.C.</strong> (2010) Tryptophan probes at the α-synuclein and membrane interface, <em>J. Phys. Chem. B</em>. 114, 4615-4622. DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/jp908092e" target="_new" rel="noopener noreferrer"><span>10.1021/jp908092e</span></a></p></div>
      
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<img loading="eager" src="/modules/custom/nhlbi_blazy/images/clear.png" width="450" height="300" alt="Energy transfer probes of GluR2 ligand binding core" data-src="/sites/default/files/styles/component_lab_image_slide_desktop/public/2021-07/27.png?itok=jg7Mcncr" class="b-lazy" />

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            <div class="field field--name-field-component-lab-image-descri field--type-text-long field--label-hidden field__item"><p><span>Petrik, A.F., Strub, M.-P., <strong>Lee, J.C.</strong> (2010)<em> </em>Energy transfer probes of GluR2 ligand binding core, <em>Biochemistry </em>49, 2051-2057. DOI: <a href="http://pubs.acs.org/doi/abs/10.1021/bi9020007" target="_new" rel="noopener noreferrer"><span>10.1021/bi9020007</span></a></span></p></div>
      
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            <span>
            Proceedings of the National Academy of Sciences of the United States of America
      
                2020 Aug 11</span>;117(32):18977-18983
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                                                    <a href="https://pubmed.ncbi.nlm.nih.gov/32719116/" aria-label="Unroofing site-specific α-synuclein–lipid interactions at the plasma membrane" class="read-publications">Read Publication</a>
                            
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                                                    <h3>
            <div class="field field--name-field-publication-title field--type-string-long field--label-hidden field__item">C-terminal α-synuclein truncations are linked to cysteine cathepsin activity in Parkinson’s disease</div>
      </h3>
            <div class="publicationAuthors">
               <span>Authors: </span>Ryan P. McGlinchey, Shannon M. Lacy, Katherine E. Huffer, Nahid Tayebi, Ellen Sidransky, Jennifer C. Lee
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            <span>
            The Journal of Biological Chemistry
      
                2019 Jun 21</span>;294(25):9973-9984
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                                                    <a href="https://pubmed.ncbi.nlm.nih.gov/31092553/" aria-label="C-terminal α-synuclein truncations are linked to cysteine cathepsin activity in Parkinson’s disease" class="read-publications">Read Publication</a>
                            
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                                                    <h3>
            <div class="field field--name-field-publication-title field--type-string-long field--label-hidden field__item">Effects of phosphatidylcholine membrane fluidity on the conformation and aggregation of N-terminally acetylated α-synuclein</div>
      </h3>
            <div class="publicationAuthors">
               <span>Authors: </span>Emma I. O'Leary, Zhiping Jiang, Marie-Paule Strub, Jennifer C. Lee
            </div>
                                                                                                                        
            <span>
            The Journal of Biological Chemistry
      
                2018 Jul 18</span>;293(28):11195-11205
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        <div class="flex-item">
                                                    <a href="https://pubmed.ncbi.nlm.nih.gov/29853639/" aria-label="Effects of phosphatidylcholine membrane fluidity on the conformation and aggregation of N-terminally acetylated α-synuclein" class="read-publications">Read Publication</a>
                            
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<img loading="lazy" src="/modules/custom/nhlbi_blazy/images/clear.png" width="250" height="250" alt="Jennifer Lee" data-src="/sites/default/files/styles/square_image_250x250/public/2022-10/JCLeeHeadshot2022crop.jpg?itok=JkiTjNVB" class="b-lazy image-style-square-image-250x250" />


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                <h3 class="senior-name">
                    Jennifer Lee, Ph.D.
                </h3>
                <div class="senior-title">
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Senior Investigator</div>
      
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                <div class="senior-bio">
                    
            <div class="clearfix text-formatted field field--name-field-person-bio field--type-text-with-summary field--label-hidden field__item"><p>Jennifer C. Lee graduated with a B.S. in chemistry and a B.A. 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. 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. In 2006, Dr. Lee joined the NHLBI as a tenure-track Investigtor. 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.</p>
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            <div class="field field--name-field-lab-location field--type-address field--label-hidden field__item"><p class="address" translate="no"><span class="address-line1">50 South Dr</span><br>
<span class="locality">Bethesda</span>, <span class="administrative-area">MD</span> <span class="postal-code">20814</span><br>
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<img loading="lazy" src="/modules/custom/nhlbi_blazy/images/clear.png" width="200" height="200" alt="Headshot of Staff Scientist Matthew Watson" data-src="/sites/default/files/styles/square_image/public/2018-01/MatthewWatson_2017.jpg?itok=lfw3tZAw" class="b-lazy image-style-square-image" />


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            <h4>
            
<span>Matthew Watson, Ph.D.</span>

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            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Staff Scientist</div>
      
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<article class="node node--type-nhlbi-person node--view-mode-lab-member-component">

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<img loading="lazy" src="/modules/custom/nhlbi_blazy/images/clear.png" width="200" height="200" alt="Ryan McGlinchey" data-src="/sites/default/files/styles/square_image/public/2017-12/Ryan%20McGlinchey_2014.jpg?itok=Bk7Z0hcV" class="b-lazy image-style-square-image" />


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            <h4>
            
<span>Ryan McGlinchey, Ph.D.</span>

        </h4>
        

    <div class="node__content">
        
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Staff Scientist</div>
      
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        <div class="node__content contact-info">
                <div class="contact-info-email">
            <i class="fas fa-envelope"></i>
             <a href="mailto:mcglincheyr@mail.nih.gov" >
                 mcglincheyr@mail.nih.gov
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            <div class="field__item">
<article class="node node--type-nhlbi-person node--view-mode-lab-member-component">

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<img loading="lazy" src="/modules/custom/nhlbi_blazy/images/clear.png" width="200" height="200" alt="Sashary Ramos" data-src="/sites/default/files/styles/square_image/public/2022-09/RamosHeadshot.jpg?itok=xDXAWXQi" class="b-lazy image-style-square-image" />


</div>
      
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            <h4>
            
<span>Sashary Ramos, Ph.D. </span>

        </h4>
        

    <div class="node__content">
        
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postdoctoral Fellow</div>
      
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        <div class="node__content contact-info">
                <div class="contact-info-email">
            <i class="fas fa-envelope"></i>
             <a href="mailto:sashary.ramos@nih.gov" >
                 sashary.ramos@nih.gov
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</div>
            <div class="field__item">
<article class="node node--type-nhlbi-person node--view-mode-lab-member-component">

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<img loading="lazy" src="/modules/custom/nhlbi_blazy/images/clear.png" width="200" height="200" alt="Dan SanGiovanni" data-src="/sites/default/files/styles/square_image/public/2023-05/DanSanGiovanni_2023.jpg?itok=RwaMuK-h" class="b-lazy image-style-square-image" />


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            <h4>
            
<span>Daniel SanGiovanni </span>

        </h4>
        

    <div class="node__content">
        
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postbaccalaureate fellow</div>
      
    </div>

        <div class="node__content contact-info">
                <div class="contact-info-email">
            <i class="fas fa-envelope"></i>
             <a href="mailto:daniel.sangiovanni@nih.gov" >
                 daniel.sangiovanni@nih.gov
            </a>
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            </div>
    </article>
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                </div>
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            <div class="field field--name-field-vacancy-type field--type-list-string field--label-hidden component-jobs-job-kicker field__item">Current Vacancy</div>
      

  
      <h3 class="component-jobs-job-name">
      
<span>Postdoctoral Fellowship </span>

    </h3>
    

  <div>
    
            <div class="field field--name-field-the-role field--type-text-long field--label-hidden field__item">  <p>In expanding the scope of our research, a candidate with strong backgrounds in cell biology and fluorescence microscopy, including...</p>

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            <div class="field field--name-field-component-alumni field--type-entity-reference-revisions field--label-hidden field__item">  <div class="paragraph paragraph--type--component-alumni paragraph--view-mode--default responsive-container responsive-container-constrained">
  	      <h2>
            <div class="clearfix text-formatted field field--name-field-component-alumni-title field--type-text field--label-hidden field__item">Alumni</div>
      </h2>
        

<div class="field field--name-field-component-alumni-person field--type-entity-reference field--label-hidden component-theme-blue">
      <div class="field__items">
        <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Jared Shadish, Ph.D.</span>

        </h3>
        

    <div class="node__content">
        <div class='nhlbi-years-and-role'>
                            <div class='nhlbi-role'>
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postdoctoral Fellow</div>
      
                </div>
                                        <div class='years-at-nhlbi'>
                    
            2020

      -
            2024

      
                </div>
                    </div>
        <div class='current-role-and-institution'>
            Jared Shadish, Ph.D. is currently a Senior Scientist at AstraZeneca.
        </div>
    </div>
</article></div>
      <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Genevieve  A. Verville </span>

        </h3>
        

    <div class="node__content">
        <div class='nhlbi-years-and-role'>
                            <div class='nhlbi-role'>
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postbaccalaureate Fellow </div>
      
                </div>
                                        <div class='years-at-nhlbi'>
                    
            2020

      -
            2021

      
                </div>
                    </div>
        <div class='current-role-and-institution'>
            
        </div>
    </div>
</article></div>
      <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Sydney O. Shuster </span>

        </h3>
        

    <div class="node__content">
        <div class='nhlbi-years-and-role'>
                            <div class='nhlbi-role'>
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postbaccalaureate Fellow </div>
      
                </div>
                                        <div class='years-at-nhlbi'>
                    
            2019

      -
            2021

      
                </div>
                    </div>
        <div class='current-role-and-institution'>
            Sydney O. Shuster  is currently a Ph.D. Student at Chemistry Department, Yale University.
        </div>
    </div>
</article></div>
      <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Dexter N. Dean, Ph.D.</span>

        </h3>
        

    <div class="node__content">
        <div class='nhlbi-years-and-role'>
                            <div class='nhlbi-role'>
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postdoctoral Fellow</div>
      
                </div>
                                        <div class='years-at-nhlbi'>
                    
            2018

      -
            2021

      
                </div>
                    </div>
        <div class='current-role-and-institution'>
            Dexter N. Dean, Ph.D. is currently a Instructional Laboratory Instrumentation Manager at College of Sciences, Georgia Institute of Technology.
        </div>
    </div>
</article></div>
      <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Upneet Kaur </span>

        </h3>
        

    <div class="node__content">
        <div class='nhlbi-years-and-role'>
                            <div class='nhlbi-role'>
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postbaccalaureate Fellow</div>
      
                </div>
                                        <div class='years-at-nhlbi'>
                    
            2019

      -
            2020

      
                </div>
                    </div>
        <div class='current-role-and-institution'>
            Upneet Kaur  is currently a M.D./Ph.D. Student at University of California, San Francisco.
        </div>
    </div>
</article></div>
      <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Jessica D. Flynn, Ph.D.</span>

        </h3>
        

    <div class="node__content">
        <div class='nhlbi-years-and-role'>
                            <div class='nhlbi-role'>
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postdoctoral Fellow</div>
      
                </div>
                                        <div class='years-at-nhlbi'>
                    
            2015

      -
            2020

      
                </div>
                    </div>
        <div class='current-role-and-institution'>
            Jessica D. Flynn, Ph.D. is currently a Staff Fellow at U.S. Food and Drug Administration.
        </div>
    </div>
</article></div>
      <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Shannon M. Lacy </span>

        </h3>
        

    <div class="node__content">
        <div class='nhlbi-years-and-role'>
                            <div class='nhlbi-role'>
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postbaccalaureate Fellow</div>
      
                </div>
                                        <div class='years-at-nhlbi'>
                    
            2016

      -
            2018

      
                </div>
                    </div>
        <div class='current-role-and-institution'>
            Shannon M. Lacy  is currently a Ph.D. Student at Cellular and Molecular Biology Program, University of Michigan.
        </div>
    </div>
</article></div>
      <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Emma I. O'Leary </span>

        </h3>
        

    <div class="node__content">
        <div class='nhlbi-years-and-role'>
                            <div class='nhlbi-role'>
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Postbaccalaureate Fellow</div>
      
                </div>
                                        <div class='years-at-nhlbi'>
                    
            2016

      -
            2018

      
                </div>
                    </div>
        <div class='current-role-and-institution'>
            Emma I. O'Leary  is currently a M.D./Ph.D. Student at University of Pittsburgh.
        </div>
    </div>
</article></div>
      <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Zhiping Jiang, Ph.D.</span>

        </h3>
        

    <div class="node__content">
        <div class='nhlbi-years-and-role'>
                            <div class='nhlbi-role'>
                    
            <div class="field field--name-field-employment-title field--type-string field--label-hidden field__item">Visiting Fellow and Research Fellow</div>
      
                </div>
                                        <div class='years-at-nhlbi'>
                    
            2011

      -
            2017

      
                </div>
                    </div>
        <div class='current-role-and-institution'>
            Zhiping Jiang, Ph.D. is currently a Senior Scientist  at Pfizer.
        </div>
    </div>
</article></div>
      <div class="field__item">
    


<article class="node node--type-nhlbi-person a_class node--view-mode-person-alumnus-card">

    
            <h3>
            
<span>Gifty Dominah </span>

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