Developmental Neurobiology

Research in the Developmental Neurobiology Laboratory, led by Dr. Herbert M. Geller, focuses on understanding the mechanisms that control axonal growth and pathfinding during neural development and also the mechanisms that stimulate regeneration after injury to the brain or spinal cord.

Herbert Geller

Research Interests

Research Interests

Research in the Laboratory of Developmental Neurobiology, headed by Dr. Herbert Geller, is focused on understanding how extracellular signals provide guidance cues to axons.  Our primary focus is on signals derived from the extracellular matrix, especially proteoglycans, as well as responses of growing neurons to biophysical properties of their environment, such as substrate stiffness.  Our overall goal is to improve recovery of function following brain or spinal cord injury.  This involves use of all methods of modern biology, including light and electron microscopy, including multi-photon and superresolution microscopy, cell biology, including proteomics, constrol of gene expression using CRISPR/Cas systems, and animal models.

Videos

EB3 localizes points of microtubule polymerization

Produced in the laboratory of Dr. Herbert Geller at the NIH's National Heart, Lung, and Blood Institute, this movie shows a cultured neonatal mouse cerebellar granule neuron transfected with a construct of monomeric RFP-EB3.

Growth cones turn at a boundary

Resources

Western Blotting for Chondroitin Sulfate Proteoglycans

This protocol was developed by Dr. Panpan Yu, Associate Professor, Guangdong–Hongkong–Macau Institute of CNS Regeneration, Jinan University, Guangzhou, China when she was a Research Fellow in the lab.  Please contact her at: yupanpan21@gmail.commailto: for further help.

  1. Protein samples are separated by SDS-PAGE on a 6% polyacrylamide gel under reducing conditions.

  2. Electroblot the SDS-PAGE-separated samples onto the PVDF membrane using semi-dry or wet transfer device. (Note: Reduce the methanol concentration in transfer buffer to 10 % instead of 20%, to facilitate transfer of high molecular weight proteins such as CSPGs).

  3. Block the membrane in blocking buffer (5% milk in PBS-Tween) at room temperature for 1 h or overnight at 4°C on the shaker.

  4. Incubate the membrane overnight at 4°C on the shaker with primary antibody CS-56 (1:500, Sigma) diluted in 5% milk in PBS-Tween; incubate for additional 2 h the following day at room temperature.

  5. Wash the membrane 3 times for 10 min each with PBS-Tween.

  6. Incubate the membrane with HRP-conjugated goat anti-mouse IgM secondary antibody at room temperature for 35 min.

  7. Wash the membrane 6 times for 5 min each with PBS-Tween.

  8. Detect the signals using chemiluminescent methods. (Note: use high sensitive chemiluminescent reagents)

Images

Structhre of Glycosaminoglycan Chains
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Proteoglycan GAG Chains

Proteoglycans are comprised of a core protein decorated by one or more glycosaminoglycan (GAG) chains.  GAG chains are attached to the serine of a core protein through a linkage region of Xyl-Gly-Gly.  The remainder of the GAG chain is comprised of an alternating series of GlcA-GalNAc sugars.  Some of the GlcA residues are epimerized to IdoA, while either of the two sugars in a disaccharide pair can be sulfate on any of several positions.  The length of the GAG chain and the position of sulfation are not template-driven, leading to an enormous number of possible permutations.  Our research has demonstrated that the GAG chains are essential for signaling guidance cues to neurons: elimination of GAG chains or preventing their synthesis reduces the biological activity of chondroitin sulfate proteoglycans.  Moreover, our recent research has shown that CSPG signaling is dependent on 4-sulfation of GalNAc, especially at the non-reducing end (the furthest from the protein core).  Reducing terminal 4-sulfation with the enzyme arylsulfatase B can significantly alter the actions of CSPGs.  Future research is directed at appyling this discovery to promote recovery of function after spinal cord or brain injury.   

• Pearson, C. S., Mencio, C. P., Barber, A. C., Martin, K. R. and Geller, H. M. Identification of a critical sulfation in chondroitin that inhibits axonal regeneration, eLife, 7:e37139, 2018. [link]external link

• Yu, P., Pearson, C. S., Geller, H. M. Flexible roles for proteoglycan sulfation and receptor signaling, Trends Neurosci.,  41:47-61, 2018. [abstract]

• Janecke, A. R., Li, B., Boehm, M., Krabichler, B., Rohrbach, M., Müller, T., Fuchs, I., Golas, G., Katagiri, Y. Ziegler, S. G., Gahl, W. A., Wilnai, Y., Zoppi, N., Geller, H. M., Giunta, C., Slavotinek, A., Steinmann, B. The phenotype of the musculocontractural type of Ehlers-Danlos syndrome due to CHST14 mutations, Am. J. Med. Genetics Part A, 2015. [abstract]

• Susarla, B. T. S., Laing, E. D., Yu, P., Katagiri, Y., Geller, H. M. and Symes, A. J. SMAD proteins differentially regulate TGF-β mediated induction of chondroitin sulfate proteoglycans, J. Neurochem., 119:868-78, 2011.  [abstract]

• Wang, H., Katagiri, Y., McCann, T. E., Unsworth, E., Goldsmith, P., Yu, Z.-Y., Tan, F., Mills, E. M., Wang, Y., Symes, A. J. and Geller, H. M. 4-sulfation of chondroitin is critical for inhibition of axonal growth, J. Cell Sci., 121:3083-3091, 2008. [abstract]

• Laabs, T., Wang, H., McCann, T. E., Katagiri, Y., Fawcett, J. W . and Geller, H. M. Inhibiting GAG chain polymerization decreases the inhibitory activity of astrocyte-derived chondroitin sulfate proteoglycans, J. Neurosci., 27:14494-14501, 2007.  [abstract]

• Powell, E. M., Fawcett, J. W. and Geller, H. M. Neurite guidance by astrocyte proteoglycans, Mol. Cell. Neurosci., 10:27-42, 1997. [abstract]

GAG Chain Receptors
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GAG Chain Receptors

When growth cones of neurons encounter CSPGs, they stop or alter their direction of movement.  Our major hypothesis is that CSPGs interact with receptors to initiate an intracellular signaling cascade resulting in an alteration of cytoskeletal dynamics.  Both chondroitin sulfate and heparan sulfate interact with two families of receptors: the LAR family, which includes Receptor Protein Tyrosine Phosphatase RPTP) σ RPTP-δ and the Leukocyte Common Antigen Receptor (LAR), and two members of the Nogo Receptor familiy, NgR1 and NgR3.  This leads to the question of how HS promotes growth and CS inhibits growth. We have establihed that all of these interactions depend upon sulfation: HS and highly sulfated CS bind with high affinity to all five of these receptors.  Another major issue is how binding results in alterations of signaling. We have identified diifferences in the interaction of the LAR family members with proteoglycans which may explain their differential actions on neurons.  Current research is directed at understanding the structural features of these receptors that mediate their interactions with proteoglycan GAG chains.  An additional issue is that there is no binding of these receptors to GAG chains in normal brain, suggesting that there are other ligands involved in normal brain function.  We are in the process of identifying these ligands. 

• Katagiri, Y., Morgan, A. A., Yu, P., Bangayan, N. J., Junka, R., Geller, H. M., Identification of novel binding sites for heparin in RPTPσ: Implications for proteoglycan signaling, J. Biol. Chem., 293:11639-11647, 2018.

• Yi, J. H., Katagiri, Y., Yu, P., Lourie, J., Bangayan, N. J., Symes, A. J. and Geller, H. M. Receptor protein tyrosine phosphatase σ binds to neurons in the adult mouse brain, Exptl. Neurol., 255:12-18, 2014.

• Dickendesher, T. L., Baldwin, K. T., Mironova, Y. A., Koriyama, Y., Raiker, S. J., Askew, K. L., Geoffroy, C. G., Zheng, B., Liepmann, C. D., Katagiri, Y., Benowitz, L. I., Geller, H. M., Giger, R. J. NgR1 and NgR3 are inhibitory receptors for chondroitin sulfate proteoglycans, Nature Neurosci., 15:703-12, 2012.

Intracellular Signaling
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Intracellular Signaling Pathways

When growth cones of neurons encounter CSPGs, they stop or alter their direction of movement.  Our major hypothesis is that CSPGs interact with receptors to initiate an intracellular signaling cascade resulting in an alteration of cytoskeletal dynamics.  The major cytoskeletal proteins in growth cones are actin, myosin and tubulin.  Our research has demonstrated alterations in the rate of tubulin polymerization as neurites encounter CSPGs.  We later found that inhibition of myosin II function with blebbistatin can increase axonal growth on CSPG substrates.  While these targeted approaches determined the involvement of these known proteins, a more global approach to identify proteins whose phosphorylation was changed in response to CSPG application resulted in the identificaiton of many different classes of proteins, not only cytoskeletal, involved in the response to CSPGs.  The protein whose phosphorylation was most altered was Lipid Protein Phosphatase Related protein-1, also known as Plasticity Related Gene-3.  Further proteomic experiments determined that LPPR1 interacts with other members of the LPPR family to mediate their biological actions.  Our current research is to investigate the biology and mechanism of action of the LPPR proteins using cell biological and transgenic approaches.

• Yu, P., Agbaegbu, C., Malide, D., Wu, X., Katagiri, Y., Hammer, J. A. and Geller, H. M. Cooperative interactions of LPPR/PRG family members in membrane localization and alteration of cellular morphology, J. Cell Sci., pii: jcs.169789, 2015.

• Yu, P., Pisitkun, T., Wang, G., Wang, R., Katagiri, Y., Gucek, M., Knepper, M. A. and Geller, H. M. Global analysis of neuronal phosphoproteome regulation by chondroitin sulfate proteoglycans, PLoS One, 8:e59285, 2013.

• Yu, P., Santiago, L. Y., Wang, H., Katagiri, Y. and Geller, H. M. Myosin II activity regulates neurite outgrowth and guidance in response to chondroitin sulfate proteoglycans., J. Neurochem., 120:1117-1128, 2012.

• Kelly, T.-A. N., Katagiri, Y., Kumar, P., Chen, I.-I., Vartanian, K. B., Rosoff, W. J., Urbach, J. S. and Geller, H. M. Localized alteration of microtubule polymerization in growth cones at inhibitory boundaries, J. Neurosci. Res., 88:3024-33, 2010.

Astrocyte Extracellular Matrix
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Astrocyte Extracellular Matrix

Astrocytes are the major cell type of the brain, whose numbers far surpass that of neurons.  In the uninjured brain, astrocytes surround neurons and provide nourishment. After injury, astrocytes become hypertrophic and change their physiology to become a major part of the glial scar that inhibits regeneration.  This inhibition is primarily mediated by an increased secretion of extracellular matrix ECM) molecules, especially chondroitin sulfate proteoglycans.  Our research is focused on understanding the regulatory mechanisms that result in this secretion and in changing the composition of the ECM, as well as identifying methods to reduce it and promote regeneration and recovery of function. 

• Pearson, C. S., Solano, A. G., Tilve, S., Mencio, C. P., Martin, K. R. and Geller, H. M. Spatiotemporal distribution of chondroitin sulfate proteoglycans after optic nerve injury in rodents, Exptl. Eye Res., in press.

• Jin, J., Tilve, S., Huang, Z., Geller, H. M., Yu, P. The effect of CSPGs on neuronal cell adhesion, spreading and neurite growth in culture, Neural Regen. Res., 13:289-297, 2018.

• George, N. and Geller, H. M. Extracellular matrix and traumatic brain injury, J. Neurosci. Res., 96:573-588, 2018.

 • Yi, M., Wei, T., Wang, Y., Liu, Q.,  Yu, P., Lu, Q., Chen, G., Gao, X., Geller, H. M., Chen, H. and Yu, Z.  The potassium channel KCa3.1 constitutes a pharmacological target for astrogliosis associated with ischemia stroke,  J. Neuroinflamm., 14:203, 2017

• Yi, M., Yu, P., Lu, Q., Geller, H. M. Yu, Z., and Chen, H. KCa3.1 constitutes a pharmacological target for astrogliosis associated with Alzheimer's Disease, Mol. Cell. Neurosci., S1044-7431, 2016

• Susarla, B., Villapol, S., Yi, J. H., Geller, H. M., Symes, A. J. Temporal patterns of cortical proliferation of glial cell populations after traumatic brain injury in mice, ASN Neuro, 6:159-70 2014.

• Yu, Z.-H., Yu, P., Chen, H.-Z., Geller, H. M. Targeted inhibition of KCa3.1 attenuates TGF-β-induced reactive astrogliosis through the Smad2/3 signaling pathway, J. Neurochem., 130:41-9, 2014

• Yi, J. H., Katagiri, Y., Susarla, B., Figge, D., Symes, A. J. and Geller, H. M. Detection of sulfated chondroitin glycosaminoglycans following controlled cortical impact injury in mice, J. Comp. Neurol., 520:3295-313, 2012.

• Yu, P., Wang, H., Katagiri, Y. and Geller, H. M. An in vitro model of reactive astrogliosis and its effect on neuronal growth. In: Astrocytes, Methods and Protocols, R. Milner, ed., Humana Press, Methods in Molecular Biology, 814:327-40, 2012

• Susarla, B. T. S., Laing, E. D., Yu, P., Katagiri, Y., Geller, H. M. and Symes, A. J. SMAD proteins differentially regulate TGF-β mediated induction of chondroitin sulfate proteoglycans, J. Neurochem., 119:868-78, 2011.

• Laabs, T., Wang, H., McCann, T. E., Katagiri, Y., Fawcett, J. W . and Geller, H. M. Inhibiting GAG chain polymerization decreases the inhibitory activity of astrocyte-derived chondroitin sulfate proteoglycans, J. Neurosci., 27:14494-14501, 2007.

• Powell, E. M., Calle-Patino, Y. A., Mercado, M. L. T. and Geller, H. M. Protein kinase C mediates neurite guidance at an astrocyte boundary, Glia, 33:288-297, 2001.

Biophysics of Growth Cones
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Biophysics of Growth Cones

Studies of axonal growth and guidance cues have primarily focused on soluble and substrate-bound molecules. However, axons are growing in a physical as well as a chemical environment.  In addition, growth cones exert physical forces on their substrates. This part of our research, in collaboration with Dr. Jeffrey Urbach of Georgetown University, is directed as understanding the role of physical forces in the regulation of axonal growth. Thus, different neuronal populations react differently to the stiffness of their substrate. We are also investigating the forces generated by growing axons using a combination of traction force and total internal reflection (TIRF) microscopy. 

• Polackwich, J., Koch, D., McAllister, R., Urbach, J. S. , Geller, H. M. Traction force and tension fluctuations in growing axons, Frontiers In Cellular Neuroscience, 2015 doi:10.3389/fncel.2015.00417

• Koch, D., Rosoff, W. J., Jian, J., Geller, H. M. and Urbach, J. S. Strength in the periphery: Growth cone biomechanics and substrate rigidity response in peripheral and central nervous system neurons, Biophys. J., 102:452-460, 2012.

• Kelly, T.-A. N., Katagiri, Y., Kumar, P., Chen, I.-I., Vartanian, K. B., Rosoff, W. J., Urbach, J. S. and Geller, H. M. Localized alteration of microtubule polymerization in growth cones at inhibitory boundaries, J. Neurosci. Res., 88:3024-33, 2010.

Tissue Engineering
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Tissue Engineering

The glial scar is a major impediment to regrowing axons.  Our goal is to develop tissue engineering methods to encourage neurons to grow through the scar.  These methods include understanding how neurons grow in confinement as well as developing substrates that promote axonal growth.  Further research will use new methods of substrate fabrication as well as new biomatierials. 

• Smirnov, M. S., Cabral, K. A., Geller, H. M. and Urbach, J. S. The effects of confinement on neuronal growth cone morphology and velocity, Biomaterials, 35:6750-7, 2014.

• Mora, K. E., Cohen, J. D., Yu, P., Geller, H. M. and Morgan, N. Y., Microfluidic deposition of chondroitin sulfate proteoglycan surface gradients for neural cell culture. Microsystems for Measurement and Instrumentation (MAMNA), 20-23, 2013.

• Zhou, Z., Yu, P., Geller, H. M. and Ober, C. Biomimetic polymer brushes containing tethered acetylcholine analogs for protein and hippocampal neuronal cell patterning, Biomacromolecules, 14:529-37, 2013.

• Zhou, Z., Yu, P., Geller, H. M. and Ober, C. The role of hydrogels with tethered acetylcholine functionality on the adhesion and viability of hippocampus neurons and glial cells. Biomaterials, 33:2473-2481, 2012.

• Krsko, P., McCann, T. E., Thach, T.-T., Laabs, T.L., Geller, H. M. and Libera, M. Length-scale mediated adhesion and directed growth of neural cells by surface-patterned poly(ethylene glycol) hydrogels, Biomaterials, 30:721-729, 2009.

• Geller, H. M. and Fawcett, J. W. Building a bridge: Engineering spinal cord repair, Exptl. Neurol, 174:125-36, 2002.

Meet the Team

Herbert Geller

Herbert Geller, Ph.D.

Senior Investigator

Herbert Geller graduated with a Ph.D.in Biomedical Engineering from Case Western Reserve University and was Postdoctoral Fellow in Physiology at the University of Rochester. He was a Professor in the Departments of Pharmacology and Neurology at Robert Wood Johnson Medical School in New Jersey before moving to NIH in 2001. Dr. Geller has authored or co-authored more than 150 papers, and he sits on the editorial boards of the International Journal of Developmental Neuroscience and the Journal of Neuroscience Methods.  At NIH, he has been a mentor in the Biomedical Engineering Summer Internship Program.  His former trainees have gone onto careers in Academia, Industry and Government. Dr. Geller is a member of the Society for Neuroscience and a Fellow of the American Association for the Advancement of Science.  In 2018, Dr. Geller was awarded the Bernice Grafstein Award for Outstanding Accomplishments in Mentoring from the Society for Neuroscience. 

Contact the lab

Caitlin Mencio

Caitlin Mencio, Ph.D.

Postdoctoral Fellow

Alumni

Sanya Springfield, Ph.D.

Postdoctoral Fellow
1981 - 1985
Sanya Springfield, Ph.D. is currently a Director at Center to Reduce Cancer Health Disparities, National Cancer Institute, NIH, Bethesda, MD.

Roseann Ventimiglia

Graduate Fellow
1984 - 1987
Roseann Ventimiglia is currently a medical communications professional at an independent communications firm in CT .

Jeremy P. Grierson, Ph.D.

Postdoctoral Fellow, Instructor
1986 - 1989
Jeremy P. Grierson, Ph.D. is currently a Project Manager, Clinical Writing at Servier, Paris, France.

Douglas S. F. Ling, Ph.D.

Graduate Fellow
1985 - 1990
Douglas S. F. Ling, Ph.D. is currently a Associate Professor at SUNY Downstate Medical Center, Brooklyn, NY.

Robert E. Petroski, Ph.D.

Graduate Fellow
1985 - 1991
Robert E. Petroski, Ph.D. is currently a Scientific Liaison at Neuroservices Alliance, San Diego, CA..

Kevin D. Phelan, Ph.D.

Postdoctoral Fellow
1989 - 1990
Kevin D. Phelan, Ph.D. is currently a Professor at University of Arkansas For Medical Sciences.

Vanya Quiñones, Ph.D.

Graduate Fellow
1988 - 1992
Vanya Quiñones, Ph.D. is currently a Provost at Pace University.

Smi Choi-Kwon, Ph.D.

Postdoctoral Fellow
1989 - 1990
Smi Choi-Kwon, Ph.D. is currently a Dean at College of Nursing, Seoul National University, Korea.

Michael Saporito, Ph.D.

Postdoctoral Fellow
0089 - 1991
Michael Saporito, Ph.D. is currently a Principal at Shaw's Bridge Advisors LLC.

Maria Marone, Ph.D.

Postdoctoral Fellow
1991 - 1994
Maria Marone, Ph.D. is currently a Italian Teacher and Translator at Leiden, Provincie Zuid-Holland, Netherlands.

G. Stanley Okoye, M.D., Ph.D.

Fellow
1991 - 1994
G. Stanley Okoye, M.D., Ph.D. is currently a Medical Director at St. Jude Eye Clinic & Skin Care, Brandon, FL.

Nicholas DiProspero, M.D., Ph.D.

Graduate Fellow
1994 - 1997
Nicholas DiProspero, M.D., Ph.D. is currently a Senior Director, Translational Medicine at Johnson & Johnson, Raritan, NJ.

Erick J. Morris, Ph.D.

Graduate Fellow, Postdoctoral Fellow
1992 - 1998
Erick J. Morris, Ph.D. is currently a Lab Head at Novartis Oncology Translational Research, Boston, MA.

Elizabeth M. Powell, Ph.D.

Graduate Fellow, Postdoctoral Fellow
1993 - 1998
Elizabeth M. Powell, Ph.D. is currently a Program Director at National Institute on Alcohol Abuse and Alcoholism, Rockville, MD.

John C. Dreixler, Ph.D.

Postdoctoral Fellow
1996 - 1998
John C. Dreixler, Ph.D. is currently a Research Associate, Department of Anesthesia & Critical Care at University of Chicago.

Mary Lynn Mercado, Ph.D.

Graduate Fellow
1998 - 2002
Mary Lynn Mercado, Ph.D. is currently a US Group Head Regulatory Medical Writing, Pharma at Novartis Pharmaceuticals.

Alex Romero, Ph.D.

Graduate Fellow
1998 - 2003
Alex Romero, Ph.D. is currently a Digital Health Innovation Specialist at Bayer Consumer Health Warren, NJ.

Stephane Gross, Ph.D.

Postdoctoral Fellow
2000 - 2002
Stephane Gross, Ph.D. is currently a Lecturer in Cellular Biology, School of Life and Health Sciences at Aston University Birmingham B4 7ET UK.

Hang Wang M. D., Ph.D.

Research Fellow
2001 - 2008
Hang Wang M. D., Ph.D. is currently a Psychiatrist at Adventist Behavioral Health, Rockville, MD.

Meredith Wagner

Postbaccalaureate IRTA Fellow
2002 - 2003
Meredith Wagner is currently a Pediatric Anesthesiologist at Pediatric Anesthesiologist, Wyckoff, NJ.

Keri Vartanian

Postbaccalaureate IRTA Fellow
2003 - 2004
Keri Vartanian is currently a Research Scientist at The Center for Outcomes Research and Education, Providence Health and Services.

Tracy Laabs, Ph.D.

Graduate Fellow
2003 - 2008
Tracy Laabs, Ph.D. is currently a Assistant Director at Wyss Center for Bio and Neuro-engineering, Geneva, Switzerland.

Cerise Elliott, Ph.D.

Technology Transfer Fellow
2004 - 2005
Cerise Elliott, Ph.D. is currently a Program Director at National Institute on Aging.

Thomas McCann

Postbaccalaureate IRTA Fellow
2005 - 2006
Thomas McCann is currently a Radiologist at Coastal Imaging, LLC, Toms River, NJ.

Thu-Trang Thach

Postbaccalaureate IRTA Fellow
2006 - 2008
Thu-Trang Thach is currently a Research Study Assistant at Brigham and Womens Hospital, Boston, MA.

Terri-Ann Natalie Kelly, Ph.D.

Postdoctoral Fellow
2006 - 2009
Terri-Ann Natalie Kelly, Ph.D. is currently a Tissue Engineer at EpiBone, Inc.

Lizzie Santiago, Ph.D.

IRTA Fellow
2007 - 2008
Lizzie Santiago, Ph.D. is currently a Assistant Professor at West Virginia University School of Engineering..

Michael E. Zavaski

Postbaccalaureate IRTA Fellow
2008 - 2009
Michael E. Zavaski is currently a Urological Physician at Pioneer Valley Urology.

David Figge

Postbaccalaureate IRTA Fellow
2009 - 2010
David Figge is currently a MSTP Student at University of Alabama at Birmingham.

Elisa Gutierrez

Postbaccalaureate IRTA
2008 - 2009
Elisa Gutierrez is currently a Family Medicine Physician at University of New Mexico.

Abigail Mabe Goosie, Ph.D.

Postdoctoral IRTA Fellow
2009 - 2009
Abigail Mabe Goosie, Ph.D. is currently a Associate Professor of Biology at Walters State Community College, TN.

Jae-Hyuk (John) Yi, Ph.D.

Postdoctoral Fellow
2009 - 2012
Jae-Hyuk (John) Yi, Ph.D. is currently a Technical Consultant and BD Manager at MedClaris, Seoul, Korea.

Claire Liepmann

Postbaccalaureate Fellow
2010 - 2011
Claire Liepmann is currently a Pediatrics PGY-3 at Western Michigan University, Kalamazoo, MI.

Radislav Junka

Postbaccalaureate Fellow
2011 - 2012
Radislav Junka is currently a Graduate Student at Princeton University.

Joshua Bangayan

Postbaccalaureate Fellow
2011 - 2012
Joshua Bangayan is currently a Graduate Student at UCLA.

Misha Smirnov

Graduate Student
2011 - 2014
Misha Smirnov is currently a Postdoctoral Fellow at Max Planck Florida Institute for Neuroscience.

Panpan Yu, Ph.D.

Visiting Research Fellow
2009 - 2015
Panpan Yu, Ph.D. is currently a Associate Professor at Guangdong–Hongkong–Macau Institute of CNS Regeneration, Jinan University, Guangzhou, China.

Ashlea Morgan

Postbaccalaureate Fellow
2013 - 2015
Ashlea Morgan is currently a Graduate Student at Columbia University.

Naijil George, Ph.D.

Postdoctoral Fellow
2016 - 2017
Naijil George, Ph.D. is currently a Assistant Professor, Department of Biotechnology at St. Joseph's College, Irinjalakuda, India.

Sayuri Higashi

Visiting Graduate Fellow
2016 - 2017
Sayuri Higashi is currently a Graduate Student at Gifu University.

Craig Pearson, Ph.D.

Graduate Fellow
2014 - 2018
Craig Pearson, Ph.D. is currently a Medical Student at Washington University.

Chinyere Agbaebu Iweka, Ph.D.

Graduate Fellow
2013 - 2019
Chinyere Agbaebu Iweka, Ph.D. is currently a Postdoctoral Fellow at Stanford University.