Jennifer Lippincott-Schwartz

Last updated

Jennifer Lippincott-Schwartz
Jennifer-Lippincott-Schwartz.jpg
Born
Jennifer Lippincott

(1952-10-19) October 19, 1952 (age 71)
Manhattan, Kansas
Alma mater
SpouseJonathan Schwartz
Scientific career
Fields
  • Organelle Biology
Institutions

Jennifer Lippincott-Schwartz is a Senior Group Leader at Howard Hughes Medical Institute's Janelia Research Campus and a founding member of the Neuronal Cell Biology Program at Janelia. [1] Previously, she was the Chief of the Section on Organelle Biology in the Cell Biology and Metabolism Program, in the Division of Intramural Research in the Eunice Kennedy Shriver National Institute of Child Health and Human Development at the National Institutes of Health from 1993 to 2016. Lippincott-Schwartz received her PhD from Johns Hopkins University, and performed post-doctoral training with Richard Klausner at the NICHD, NIH in Bethesda, Maryland. [2]

Contents

Lippincott-Schwartz's research revealed that the organelles of eukaryotic cells are dynamic, self-organized structures that constantly regenerate themselves through intracellular vesicle traffic, rather than static structures. [2] [3] She is also a pioneer in developing live cell imaging techniques to study the dynamic interactions of molecules in cells, including photobleaching and photoactivation [4] techniques which allow investigation of subcellular localization, mobility, transport routes, and turnover of important cellular proteins related to membrane trafficking and compartmentalization. Lippincott-Schwartz's lab also tests mechanistic hypotheses related to protein and organelle functions and dynamics by utilizing quantitative measurements through kinetic modeling and simulation experiments. [5] Along with Craig Blackstone, Lippincott-Schwartz utilized advanced imaging techniques to reveal a more accurate picture of how the peripheral endoplasmic reticulum is structured. Their findings may yield new insights for genetic diseases affecting proteins that help shape the endoplasmic reticulum. [6] Additionally, Lippincott-Schwartz's laboratory demonstrated that Golgi enzymes constitutively recycle back to the endoplasmic reticulum and that such recycling plays a central role in the maintenance, biogenesis, and inheritance of the Golgi apparatus in mammalian cells. [7]

Within Lippincott-Schwartz lab, current projects include several cell biological areas. For example, protein transport and cytoskeleton interaction, organelle assembly and disassembly, and cell polarity generation. There are also projects analyzing the dynamics of proteins that have been fluorescently labeled. These proteins are labeled using several live cell imaging techniques such as FRAP, FCS, and photoactivation. [8]

Lippincott-Schwartz has dedicated her most recent lab research to photoactivation localization microscopy (PALM), which allows the viewing of molecular distributions of high densities at the nano-scale. [2]

Early life

Jennifer Lippincott-Schwartz was born on October 19, 1952, in Manhattan, Kansas. Her father was a professor of physical chemistry at the University of Maryland [9] and a periodic table could be found hanging in her family's household kitchen. Lippincott-Schwartz's exposure to her father's work is what sparked her love of science. The family moved to a farm in Northern Virginia that had several horses and various other animals. This is where Lippincott-Schwartz found her love of biology.

Education

Lippincott-Schwartz attended Swarthmore College, where she majored in psychology and philosophy and graduated with honors from Swarthmore College in 1974. [2] She taught science at a girl's high school in Kenya for two years before returning to the USA and entering a Master's program in Biology at Stanford University where she worked on DNA repair in the laboratory of Philip Hanawalt. [2] She then entered a Biochemistry Ph.D. program at Johns Hopkins University, where she worked in Douglas Fambrough's lab in the Carnegie Institution of Embryology [2] and studied the dynamics of lysosomal membrane proteins. [10] [11]

Career

Postdoctoral work

After graduating from Johns Hopkins in 1986, Lippincott-Schwartz joined Richard D. Klausner's lab at the National Institutes of Health. Using the drug brefeldin A to perturb membrane trafficking, she showed that membranes cycle between the endoplasmic reticulum and the Golgi, [12] [13] leading to a recognition that cellular organelles are dynamic, self-organized structures that constantly regenerate themselves through intracellular vesicle traffic. [3] [14]

NIH

Lippincott-Schwartz became a staff fellow at the National Institute of Child Health and Human Development at NIH in 1990. During this time, Lippincott-Schwartz began developing techniques to use green fluorescent protein (GFP) to visualize cellular trafficking pathways in living cells. [2] [15] She refined the technique of fluorescence recovery after photobleaching (FRAP) to use in studying the dynamics of membrane proteins. In this method, GFP-tagged membrane proteins are subjected to photobleaching in a small area of the cell, and then the cell is imaged to discover how long it takes for non-bleached proteins to replace the bleached ones, i.e. how long it takes for the fluorescence to recover. Before this work, it was thought that the membrane proteins in organelles such as the ER, Golgi, and plasma membrane were fixed in place. However, the FRAP technique proved that molecules within cells move quite rapidly and are able to diffuse freely. [16] Lippincott-Schwartz subsequently introduced photoactivatable GFP that increases its fluorescence after irradiation. [4] This allowed Lippincott-Schwartz and her post-doc George Patterson to track the transport of cargo molecules through the Golgi with great precision, [17] leading to the realization that cargo transport is not an ordered sequential process; instead, the apparently separate membranous stacks of the Golgi are a single continuous structure, and proteins rapidly equilibrate through the layers. [18]

Lippincott-Schwartz's work on photoactivatable GFP led to a collaboration with Eric Betzig of Howard Hughes Medical Institute's Janelia Farm Research Campus in which the ability to turn GFP fluorescence on and off was used to develop one of the first "superresolution imaging" technologies, photoactivation localization microscopy (PALM). [19] The development of "super-resolved fluorescence microscopy" was recognized in 2014 by the award of the Nobel Prize in Chemistry to Eric Betzig along with William E. Moerner of Stanford University, and Stefan W. Hell of Max Planck Institute for Biophysical Chemistry. [20] [21]

Lippincott-Schwartz has used PALM to assess the stoichiometry and composition of membrane receptors [22] and has collaborated with Vladislav Verkhusha of Albert Einstein College of Medicine in New York to develop two-color PALM. [23] She used a combination of five super-resolution techniques to show that the endoplasmic reticulum is composed of a dense tubular matrix, instead of the sheets seen at lower resolution. [24]

Janelia Research Center

In 2016, Lippincott-Schwartz moved from NIH to the Janelia Research Campus of the Howard Hughes Medical Institute to initiate the Neuronal Cell Biology Program at Janelia. [1]

Professional awards

Lippincott-Schwartz in 2017 Jennifer Lippincott-Schwartz (33059648222).jpg
Lippincott-Schwartz in 2017

Related Research Articles

Cell biology is a branch of biology that studies the structure, function, and behavior of cells. All living organisms are made of cells. A cell is the basic unit of life that is responsible for the living and functioning of organisms. Cell biology is the study of the structural and functional units of cells. Cell biology encompasses both prokaryotic and eukaryotic cells and has many subtopics which may include the study of cell metabolism, cell communication, cell cycle, biochemistry, and cell composition. The study of cells is performed using several microscopy techniques, cell culture, and cell fractionation. These have allowed for and are currently being used for discoveries and research pertaining to how cells function, ultimately giving insight into understanding larger organisms. Knowing the components of cells and how cells work is fundamental to all biological sciences while also being essential for research in biomedical fields such as cancer, and other diseases. Research in cell biology is interconnected to other fields such as genetics, molecular genetics, molecular biology, medical microbiology, immunology, and cytochemistry.

<span class="mw-page-title-main">Endoplasmic reticulum</span> Cell organelle that synthesizes, folds and processes proteins

The endoplasmic reticulum (ER) is a part of a transportation system of the eukaryotic cell, and has many other important functions such as protein folding. It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae, and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa.

<span class="mw-page-title-main">Endomembrane system</span> Membranes in the cytoplasm of a eukaryotic cell

The endomembrane system is composed of the different membranes (endomembranes) that are suspended in the cytoplasm within a eukaryotic cell. These membranes divide the cell into functional and structural compartments, or organelles. In eukaryotes the organelles of the endomembrane system include: the nuclear membrane, the endoplasmic reticulum, the Golgi apparatus, lysosomes, vesicles, endosomes, and plasma (cell) membrane among others. The system is defined more accurately as the set of membranes that forms a single functional and developmental unit, either being connected directly, or exchanging material through vesicle transport. Importantly, the endomembrane system does not include the membranes of plastids or mitochondria, but might have evolved partially from the actions of the latter.

<span class="mw-page-title-main">Golgi apparatus</span> Cell organelle that packages proteins for export

The Golgi apparatus, also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. Part of the endomembrane system in the cytoplasm, it packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus.

<span class="mw-page-title-main">COPI</span> Protein complex

COPI is a coatomer, a protein complex that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized, and between Golgi compartments. This type of transport is retrograde transport, in contrast to the anterograde transport associated with the COPII protein. The name "COPI" refers to the specific coat protein complex that initiates the budding process on the cis-Golgi membrane. The coat consists of large protein subcomplexes that are made of seven different protein subunits, namely α, β, β', γ, δ, ε and ζ.

<span class="mw-page-title-main">Brefeldin A</span> Chemical compound

Brefeldin A is a lactone antiviral produced by the fungus Penicillium brefeldianum. Brefeldin A inhibits protein transport from the endoplasmic reticulum to the golgi complex indirectly by preventing association of COP-I coat to the Golgi membrane. Brefeldin A was initially isolated with hopes to become an antiviral drug but is now primarily used in research to study protein transport.

The coatomer is a protein complex that coats membrane-bound transport vesicles. Two types of coatomers are known:

Fluorescence Loss in Photobleaching (FLIP) is a fluorescence microscopy technique used to examine movement of molecules inside cells and membranes. A cell membrane is typically labeled with a fluorescent dye to allow for observation. A specific area of this labeled section is then bleached several times using the beam of a confocal laser scanning microscope. After each imaging scan, bleaching occurs again. This occurs several times, to ensure that all accessible fluorophores are bleached since unbleached fluorophores are exchanged for bleached fluorophores, causing movement through the cell membrane. The amount of fluorescence from that region is then measured over a period of time to determine the results of the photobleaching on the cell as a whole.

The unfolded protein response (UPR) is a cellular stress response related to the endoplasmic reticulum (ER) stress. It has been found to be conserved between mammalian species, as well as yeast and worm organisms.

<span class="mw-page-title-main">Valosin-containing protein</span> Protein-coding gene in the species Homo sapiens

Valosin-containing protein (VCP) or transitional endoplasmic reticulum ATPase also known as p97 in mammals and CDC48 in S. cerevisiae, is an enzyme that in humans is encoded by the VCP gene. The TER ATPase is an ATPase enzyme present in all eukaryotes and archaebacteria. Its main function is to segregate protein molecules from large cellular structures such as protein assemblies, organelle membranes and chromatin, and thus facilitate the degradation of released polypeptides by the multi-subunit protease proteasome.

<span class="mw-page-title-main">KDELR1</span> Protein-coding gene in the species Homo sapiens

KDEL (Lys-Asp-Glu-Leu) endoplasmic reticulum protein retention receptor 1, also known as KDELR1, is a protein which in humans is encoded by the KDELR1 gene.

<span class="mw-page-title-main">RRBP1</span> Protein-coding gene in the species Homo sapiens

Ribosome-binding protein 1, also referred to as p180, is a protein that in humans is encoded by the RRBP1 gene.

<span class="mw-page-title-main">BET1</span> Protein-coding gene in the species Homo sapiens

BET1 homolog is a protein that in humans is encoded by the BET1 gene.

<span class="mw-page-title-main">KDELR2</span> Protein-coding gene in the species Homo sapiens

ER lumen protein retaining receptor 2 is a protein that in humans is encoded by the KDELR2 gene.

EosFP is a photoactivatable green to red fluorescent protein. Its green fluorescence (516 nm) switches to red (581 nm) upon UV irradiation of ~390 nm due to a photo-induced modification resulting from a break in the peptide backbone near the chromophore. Eos was first discovered as a tetrameric protein in the stony coral Lobophyllia hemprichii. Like other fluorescent proteins, Eos allows for applications such as the tracking of fusion proteins, multicolour labelling and tracking of cell movement. Several variants of Eos have been engineered for use in specific study systems including mEos2, mEos4 and CaMPARI.

A target peptide is a short peptide chain that directs the transport of a protein to a specific region in the cell, including the nucleus, mitochondria, endoplasmic reticulum (ER), chloroplast, apoplast, peroxisome and plasma membrane. Some target peptides are cleaved from the protein by signal peptidases after the proteins are transported.

<span class="mw-page-title-main">Ronald Vale</span> American biochemist

Ronald David Vale ForMemRS is an American biochemist and cell biologist. He is a professor at the Department of Cellular and Molecular Pharmacology, University of California, San Francisco. His research is focused on motor proteins, particularly kinesin and dynein. He was awarded the Canada Gairdner International Award for Biomedical Research in 2019, the Shaw Prize in Life Science and Medicine in 2017 together with Ian Gibbons, and the Albert Lasker Award for Basic Medical Research in 2012 alongside Michael Sheetz and James Spudich. He is a fellow of the American Academy of Arts and Sciences and a member of the National Academy of Sciences. He was the president of the American Society for Cell Biology in 2012. He has also been an investigator at the Howard Hughes Medical Institute since 1995. In 2019, Vale was named executive director of the Janelia Research Campus and a vice president of HHMI; his appointment began in early 2020.

David Domingo Sabatini is an Argentine-American cell biologist and the Frederick L. Ehrman Professor Emeritus of Cell Biology in the Department of Cell Biology at New York University School of Medicine, which he chaired from 1972 to 2011. Sabatini's major research interests have been on the mechanisms responsible for the structural complexity of the eukaryotic cell. Throughout his career, Sabatini has been recognized for his efforts in promoting science in Latin America.

<span class="mw-page-title-main">Suliana Manley</span> American biophysicist

Suliana Manley is an American biophysicist. Her research focuses on the development of high-resolution optical instruments, and their application in studying the organization and dynamics of proteins. She is a professor at École Polytechnique Fédérale de Lausanne and heads the Laboratory of Experimental Biophysics.

Harald Frederick Hess is an American physicist and Senior Group Leader at Howard Hughes Medical Institute's Janelia Research Campus, known for his work in scanning probe microscopy, light microscopy and electron microscopy.

References

  1. 1 2 "Neuronal Cell Biology Research Program Added at Janelia Research Campus". HHMI.org. March 15, 2016. Retrieved February 2, 2019.
  2. 1 2 3 4 5 6 7 Davis, Tinsley H. (July 7, 2009). "Profile of Jennifer Lippincott-Schwartz". Proceedings of the National Academy of Sciences. 106 (27): 10881–10883. Bibcode:2009PNAS..10610881D. doi: 10.1073/pnas.0905805106 . ISSN   0027-8424. PMC   2708775 . PMID   19567833.
  3. 1 2 Lippincott-Schwartz, J.; Yuan, L.; Tipper, C.; Amherdt, M.; Orci, L.; Klausner, R. D. (November 1, 1991). "Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic". Cell. 67 (3): 601–616. doi:10.1016/0092-8674(91)90534-6. ISSN   0092-8674. PMID   1682055. S2CID   2114431.
  4. 1 2 Patterson, G. H. (2002). "A Photoactivatable GFP for Selective Photolabeling of Proteins and Cells". Science. 297 (5588): 1873–1877. Bibcode:2002Sci...297.1873P. doi:10.1126/science.1074952. ISSN   0036-8075. PMID   12228718. S2CID   45058411.
  5. ↑ "Jennifer A. Lippincott-Schwartz, Ph.D." NIH | Intramural Research Program.
  6. ↑ "Re-envisioning the endoplasmic reticulum". National Institutes of Health (NIH). November 7, 2016. Retrieved February 3, 2018.
  7. ↑ Sengupta, Prabuddha; Satpute-Krishnan, Prasanna; Seo, Arnold Y.; Burnette, Dylan T.; Patterson, George H.; Lippincott-Schwartz, Jennifer (December 8, 2015). "ER trapping reveals Golgi enzymes continually revisit the ER through a recycling pathway that controls Golgi organization". Proceedings of the National Academy of Sciences. 112 (49): E6752–E6761. Bibcode:2015PNAS..112E6752S. doi: 10.1073/pnas.1520957112 . ISSN   0027-8424. PMC   4679030 . PMID   26598700.
  8. ↑ The Marine Biological Laboratory, "Meet the Faculty: Jennifer Lippincott-Schwartz", 2011
  9. ↑ Bonetta, Laura (May 21, 2018). "Profile of Jennifer Lippincott-Schwartz, Ph.D." BioTechniques. 40 (4): 419. doi: 10.2144/06404SP01 . PMID   16629387.
  10. ↑ Lippincott-Schwartz, J.; Fambrough, D.M. (May 1, 1986). "Lysosomal membrane dynamics: structure and interorganellar movement of a major lysosomal membrane glycoprotein". The Journal of Cell Biology. 102 (5): 1593–1605. doi:10.1083/jcb.102.5.1593. ISSN   0021-9525. PMC   2114232 . PMID   2871029.
  11. ↑ Lippincott-Schwartz, J.; Fambrough, D. M. (June 5, 1987). "Cycling of the integral membrane glycoprotein, LEP100, between plasma membrane and lysosomes: kinetic and morphological analysis". Cell. 49 (5): 669–677. doi:10.1016/0092-8674(87)90543-5. ISSN   0092-8674. PMID   3107839. S2CID   46230310.
  12. ↑ Lippincott-Schwartz, J.; Yuan, L. C.; Bonifacino, J. S.; Klausner, R. D. (March 10, 1989). "Rapid redistribution of Golgi proteins into the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER". Cell. 56 (5): 801–813. doi:10.1016/0092-8674(89)90685-5. ISSN   0092-8674. PMC   7173269 . PMID   2647301.
  13. ↑ Lippincott-Schwartz, J.; Donaldson, J. G.; Schweizer, A.; Berger, E. G.; Hauri, H. P.; Yuan, L. C.; Klausner, R. D. (March 9, 1990). "Microtubule-dependent retrograde transport of proteins into the ER in the presence of brefeldin A suggests an ER recycling pathway". Cell. 60 (5): 821–836. doi:10.1016/0092-8674(90)90096-W. ISSN   0092-8674. PMID   2178778. S2CID   45505382.
  14. ↑ Lippincott-Schwartz, J.; Donaldson, J. G.; Klausner, R. D. (March 1, 1992). "Brefeldin A: insights into the control of membrane traffic and organelle structure". The Journal of Cell Biology. 116 (5): 1071–1080. doi:10.1083/jcb.116.5.1071. ISSN   0021-9525. PMC   2289364 . PMID   1740466.
  15. ↑ Presley, J. F.; Cole, N. B.; Schroer, T. A.; Hirschberg, K.; Zaal, K. J.; Lippincott-Schwartz, J. (September 4, 1997). "ER-to-Golgi transport visualized in living cells". Nature. 389 (6646): 81–85. Bibcode:1997Natur.389...81P. doi:10.1038/38001. ISSN   0028-0836. PMID   9288971. S2CID   5467632.
  16. ↑ Cole, N. B.; Smith, C. L.; Sciaky, N.; Terasaki, M.; Edidin, M.; Lippincott-Schwartz, J. (August 9, 1996). "Diffusional mobility of Golgi proteins in membranes of living cells" (PDF). Science. 273 (5276): 797–801. Bibcode:1996Sci...273..797C. doi:10.1126/science.273.5276.797. ISSN   0036-8075. PMID   8670420. S2CID   9426667. Archived from the original (PDF) on March 8, 2019.
  17. ↑ Patterson, George H.; Hirschberg, Koret; Polishchuk, Roman S.; Gerlich, Daniel; Phair, Robert D.; Lippincott-Schwartz, Jennifer (June 13, 2008). "Transport through the Golgi apparatus by rapid partitioning within a two-phase membrane system". Cell. 133 (6): 1055–1067. doi:10.1016/j.cell.2008.04.044. ISSN   1097-4172. PMC   2481404 . PMID   18555781.
  18. ↑ Simon, Sanford M. (June 13, 2008). "Golgi governance: the third way". Cell. 133 (6): 951–953. doi:10.1016/j.cell.2008.05.037. ISSN   1097-4172. PMC   2711685 . PMID   18555771.
  19. ↑ Betzig, E.; Patterson, G. H.; Sougrat, R.; Lindwasser, O. W.; Olenych, S.; Bonifacino, J. S.; Davidson, M. W.; Lippincott-Schwartz, J.; Hess, H. F. (2006). "Imaging Intracellular Fluorescent Proteins at Nanometer Resolution". Science. 313 (5793): 1642–1645. Bibcode:2006Sci...313.1642B. doi: 10.1126/science.1127344 . ISSN   0036-8075. PMID   16902090. S2CID   807611.
  20. ↑ The Royal Swedish Academy of Sciences (October 8, 2014). "Scientific Background on the Nobel Prize in Chemistry 2014: Super-Resolved Fluorescence Microscopy" (PDF). Retrieved April 20, 2015.
  21. ↑ "NIH Grantee Honored With 2014 Nobel Prize in Chemistry: Early prototype microscope built at NIH". National Institute of Health: Eunice Kennedy Shriver National Institute of Child Health and Human Development (NICHD). October 8, 2014. Retrieved April 20, 2015.
  22. ↑ Renz, Malte; Daniels, Brian R.; Vámosi, György; Arias, Irwin M.; Lippincott-Schwartz, Jennifer (October 30, 2012). "Plasticity of the asialoglycoprotein receptor deciphered by ensemble FRET imaging and single-molecule counting PALM imaging". Proceedings of the National Academy of Sciences of the United States of America. 109 (44): E2989–2997. doi: 10.1073/pnas.1211753109 . ISSN   1091-6490. PMC   3497821 . PMID   23043115.
  23. ↑ Subach, Fedor V; Patterson, George H; Manley, Suliana; Gillette, Jennifer M; Lippincott-Schwartz, Jennifer; Verkhusha, Vladislav V (2009). "Photoactivatable mCherry for high-resolution two-color fluorescence microscopy". Nature Methods. 6 (2): 153–159. doi:10.1038/nmeth.1298. ISSN   1548-7091. PMC   2901231 . PMID   19169259.
  24. ↑ Lippincott-Schwartz, Jennifer; Blackstone, Craig; Betzig, Eric; Hess, Harald F.; Harvey, Kirsten; Pasolli, H. Amalia; Xu, C. Shan; Legant, Wesley R.; Li, Dong (October 28, 2016). "Increased spatiotemporal resolution reveals highly dynamic dense tubular matrices in the peripheral ER". Science. 354 (6311): aaf3928. doi:10.1126/science.aaf3928. ISSN   0036-8075. PMC   6528812 . PMID   27789813.
  25. ↑ "E.B. Wilson Award Winners" . Retrieved August 25, 2020.
  26. ↑ "2019 Fellows and International Honorary Members with their affiliations at the time of election". members.amacad.org. Archived from the original on March 2, 2020.
  27. ↑ "Jennifer Lippincott-Schwartz". ASCB – An International Forum for Cell Biology. Retrieved April 20, 2015.
  28. ↑ "Honorary Fellowship: List of Honorary Fellows". Royal Microscopical Society. 2015. Archived from the original on September 24, 2015. Retrieved April 20, 2015.
  29. ↑ "Membrane Kinesis – Shaping and Transport of Cell Membranes". Membrane Transport SFB 807. October 22, 2013. Retrieved April 20, 2015.
  30. ↑ "Keith R. Porter Lecture Award". ASCB – An International Forum for Cell Biology. Retrieved April 20, 2015.
  31. ↑ "Scientists & Research – Scientists – Non-Resident Fellows". Salk Institute. 2015. Retrieved April 20, 2015.
  32. ↑ "Society Fellows". Biophysical Society. Retrieved April 21, 2015.
  33. ↑ Eunice Kennedy Shriver National Institute of Child Health and Development, "Jennifer Lippincott-Schwartz", 2014
  34. ↑ "Jennifer Lippincott-Schwarz CV" (PDF). Retrieved April 20, 2015.
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