Richard G Fehon
University Of Chicago
Project start date: 1996-01-01
Project end date: 2014-12-31
Sponsored Links Excellgen http://Excellgen.com
Function Of Merlin, A Drosophila NF2 Gene Homologue
Richard G Fehon, Professor
Molecular Genetics And Cell Biology (mgcb)university Of Chicago
5801 S Ellis Ave
chicago, Il 60637
Grant 5R01NS034783-13 from National Institute Of Neurological Disorders And Stroke IRG: MDCN
Abstract: Neurofibromatosis type 2 (NF2), a dominantly inherited disease, is caused by mutations in Merlin (Schwannomin), a member of the Protein 4.1 superfamily. Symptoms of NF2, which usually appear by early adult life, are caused by the formation of bilateral vestibular Schwannomas (resulting in deafness) and other benign tumors. The cellular functions of Merlin and its role in tumor suppression are still largely unknown. Identifying specific proteins and signal transduction pathways with which Merlin interacts is especially important because these partners may act as genetic modifiers of NF2 disease phenotypes and provide potential targets for therapeutic agents. The common fruit fly, Drosophila, has proven to be a useful model system for understanding gene function in the context of a developing organism. The overall goal of this proposal is therefore to examine the cellular functions of Merlin and the closely related ERM protein Moesin in Drosophila, particularly in relation to the control of cell proliferation, cell polarity, and the regulation of epithelial identity. In the next funding period, we plan to continue our studies of Merlin function in developing organisms and in individual cells. Specifically, the proposed experiments will 1) Examine the mechanisms by which Merlin regulates cell proliferation. Specifically, we will test the hypothesis that Merlin functions to negatively regulate the EGF receptor pathway. 2) Examine the mechanism by which the closely related ERM proteins function to regulate Rho pathway activity, and how this relates to apical/basal polarity and epithelial integrity. 3) Explore the functional relationship between Merlin and the ERM proteins, testing for synergistic or antagonistic interactions between them. These experiments are expected to provide insights into the functions of Merlin and the ERM proteins. Thus they will contribute to our understanding of human NF2, tumor suppression in general, and carcinogenesis. In addition, the proposed experiments should lead to a better understanding of the cellular processes that establish specialized membrane domains in epithelial cells and neurons. Finally, these studies should contribute to work on the mechanisms by which cellular interactions function to control cell growth and determine cell fate during development
Keywords: cytoskeletal protein, intermolecular interaction, membrane protein, protein structure function cell growth regulation, cell proliferation, developmental genetics, epithelium, gene mutation, genetic regulation, guanine nucleotide binding protein, nerve sheath neoplasm, neurofibromatosis, phosphorylation, protein protein interaction, tumor suppressor gene, tumor suppressor protein Drosophilidae, guinea pig, immunocytochemistry, laboratory mouse, laboratory rabbit, laboratory rat, tissue /cell culture, transfection
Project start date: 1996-01-01
Project end date: 2009-12-31
5R01NS034783-13 (2008): $300799
5R01NS034783-12 (2007): $300799
5R01NS034783-11 (2006): $309782
5R01NS034783-06 (2001): $301487
5R01NS034783-05 (2000): $292740
5R01NS034783-08 (2003): $319562
FUNCTIONS OF DMERLIN--A NF2 GENE HOMOLOGUE
Richard G Fehon, Professor
Zoologyduke University
2200 W. Main St.
durham, Nc 27705
Grant 5R01NS034783-03 from National Institute Of Neurological Disorders And Stroke IRG: NEUC
Keywords: Drosophilidae, cytoskeletal protein, membrane protein, neurofibromatosis, protein structure /function cell growth regulation, chimeric protein, endocytosis, gene mutation, intermolecular interaction, tumor suppressor gene animal genetic material tag, human genetic material tag, larva, site directed mutagenesis, tissue /cell culture, transfection
Project start date: 1996-01-01
Project end date: 1998-12-31
5R01NS034783-03 (1998): $166737
5R01NS034783-02 (1997): $160325
Grants awarded to Richard G Fehon
BIOCHEMISTRY OF CHROMATIN STRUCTURE AND FUNCTION - ARRA
Richard G Fehon
University Of Chicago, 5801 S Ellis Ave, Chicago, Il 60637
Grant 5P30GM092409-02 from National Institute Of General Medical Sciences
Abstract: The department of Molecular Genetics and Cell Biology is applying to the NIGMS for a Recovery Act grant (RFA-OD-09-005) to recruit a tenure track Assistant Professor in the area of Biochemistry of Chromatin Structure and Function. The department had determined the lack of this important discipline at the University and had obtained permission from Dean James Madara in September 2008 to recruit in this area, novel for the Department and the University. Subsequently, Dean Madara requested that we stop this search because of a shortage of funds. Recruitment will be a coordinated effort led by the Department of Molecular Genetics and Cell Biology (MGCB), together with the Institute of Genomics and Systems Biology (IGSB) and the Department of Biochemistry and Molecular Biology (BMB). The recruit will have a primary appointment in MGCB with the potential for membership in IGSB depending on interests. A core search committee has been formed consisting of key faculty in MGCB, BMB, and IGSB with interests in chromatin and gene expression. The position will be advertised in major scientific journals and will emphasize that the University is interested in applications from ethnic minorities and women. The new investigator will have a Ph.D. or M.D. degree, an outstanding publication record and several years of postdoctoral experience in a laboratory that is a pioneer in chromatin biochemistry/proteomics. The potential recruit will be housed in completely renovated space within MGCB. Up-to-date research facilities that cover essentially every current methodology will be available to the young investigator within the Division of Biological Sciences. A mentoring plan for junior faculty is in place in MGCB and will be streamlined for the needs of the recruit in consultation with the chair. If NIH grants us an ARRA to recruit, the Dean of the Division of Biological Sciences is committed to supplement the first two years and to extend funding for this tenure track position for additional two years and beyond
Relevance: While the genetic makeup of an individual is of major importance, it has become obvious in recent years, that epigenetics (chromatin modifications) play almost as important a role in normal development and disease. Therefore, the study of chromatin has wide implications for the understanding of disease processes and potentially the development of diagnostic and therapeutic tools
Project start date: 2009-09-30
Project end date: 2011-08-31
Budget start date: 1-SEP-2010
Budget end date: 31-AUG-2011
PFA/PA: RFA-OD-09-005
5P30GM092409-02 (2010): $362000
1P30GM092409-01 (2009): $374880
FUNCTIONAL ANALYSIS OF ERM PROTEINS IN EPITHELIAL MORPHOGENESIS
Richard G Fehon, Professor And Chairman
University Of Chicago, 5801 S Ellis Ave, Chicago, Il 60637
Grant 1R01GM087558-01A1 from National Institute Of General Medical Sciences
Abstract: The ability to form specialized membrane domains composed of unique sets of transmembrane proteins, associated cytoplasmic proteins, and phospholipids, is a fundamental property of polarized epithelial cells. Membrane domains, such as the apical surface or junctional complex, allow spatial segregation of functions at the plasma membrane that are essential for polarized epithelia. Central to this process is the formation of protein complexes on the cytoplasmic side of the membrane that localize transmembrane proteins, regulate their signaling output and control their abundance via regulated endocytosis. The Ezrin, Radixin, Moesin (ERM) proteins organize a key role in this process. In this proposal we describe experiments designed to take advantage of the combined expertise of two investigators, Andrea McClatchey (Harvard/MGH) and Richard Fehon (University of Chicago), to extend our understanding of ERM function. The investigators and their laboratories bring together expertise in two powerful experimental systems, the mouse and Drosophila. The proposed research utilizes a multifaceted approach, including genetics, biochemistry, cell biology and proteomics to better understand the functions of these highly conserved proteins. Specifically, we plan to 1) Determine the molecular mechanisms that link the ERM proteins to the activation state of Rho in developing epithelial cells. 2) Examine the molecular mechanisms that regulate ERM activity, particularly in the context of how ERM activity is dynamically regulated. 3) Delineate the function of the ERM proteins in cellcell junction remodeling. 4) To build an integrated model of ERM-mediated complex formation. These experiments are expected to provide novel insight into the functions of ERM proteins in biological processes such as apical-basal polarity cytoskeletal regulation, intestinal lumen formation and homeostasis, and metastasis. They should also yield a better understanding of the cellular processes that establish specialized membrane domains in polarized cells, and inform our understanding of cytoskeletal and junctional dynamics during morphogenesis and in disease. We will carry out complementary and synergistic studies in two powerful model systems - Drosophila and the mouse - to examine the function of ERM proteins in epithelial morphogenesis. Specifically, we will test the hypothesis that ERM proteins provide local regulation of RhoGTPase activity in response to upstream signals/receptors using molecular tools and genetic models that we have developed in each system. We will also delineate the function of ERM proteins in cell junction remodeling/stability as suggested by the phenotypes of ERM loss in both flies and mammals
Keywords: Actins; Adherens Junction; Adhering Junction; Adhesions; Adhesive Junction; Anchoring Junction; Apical; Autoregulation; Biochemistry; Biological; Biological Function; Biological Models; Biological Process; Body Tissues; Cell Communication and Signaling; Cell Function; Cell Junctions; Cell Process; Cell Shape; Cell Signaling; Cell membrane; Cell physiology; Cell to Cell Communication and Signaling; Cell-Cell Signaling; Cells; Cellular Function; Cellular Matrix; Cellular Physiology; Cellular Process; Cellular biology; Chemistry, Biological; Chicago; Complex; Cytoplasmic Membrane; Cytoplasmic Protein; Cytoskeletal System; Cytoskeleton; Disease; Disorder; Drosophila; Drosophila genus; EC 2.7; Endocytosis; Epithelial; Epithelial Cells; Epithelium; Epithelium, Intestinal; Family; Flies; Fruit Fly, Drosophila; Genetic; Genetic Models; Goals; Homeostasis; Integral Membrane Protein; Intercellular Junctions; Intestinal; Intestines; Intracellular Communication and Signaling; Intrinsic Membrane Protein; Investigators; Kinases; Laboratories; Link; Mammalia; Mammalian Cell; Mammals; Mammals, General; Mammals, Mice; Mediating; Membrane; Metastasis; Metastasize; Metastatic Neoplasm; Metastatic Tumor; Mice; Model System; Modeling; Models, Biologic; Models, Genetic; Molecular; Morphogenesis; Murine; Mus; Neoplasm Metastasis; Output; Phenotype; Phosphatides; Phospholipids; Phosphorylation; Phosphotransferases; Physiological Homeostasis; Plasma Membrane; Play; Post-Translational Modifications; Post-Translational Protein Processing; Posttranslational Modifications; Process; Property; Property, LOINC Axis 2; Protein Modification; Protein Modification, Post-Translational; Protein Phosphorylation; Protein Processing, Post-Translational; Protein Processing, Posttranslational; Protein/Amino Acid Biochemistry, Post-Translational Modification; Proteins; Proteomics; Racial Segregation; Receptor Signaling; Regulation; Research; Research Personnel; Researchers; Role; Secondary Neoplasm; Secondary Tumor; Side; Signal Transduction; Signal Transduction Systems; Signaling; Sterility; Structure of intestinal epithelium; Subcellular Process; Surface; System; System, LOINC Axis 4; Testing; Tissues; Transmembrane Protein; Transphosphorylases; Tumor Cell Migration; Universities; Work; biological signal transduction; bowel; cancer metastasis; cell biology; design; designing; disease/disorder; experiment; experimental research; experimental study; ezrin; fly; fruit fly; gene product; in vivo; insight; intercellular communication; intestinal epithelium; intracellular skeleton; membrane structure; membrane-organizing extension spike protein; moesin; mutant; novel; phosphoprotein p81; plasmalemma; polarized cell; protein complex; public health relevance; radixin; radixin protein; research study; response; rho; segregation; social role; sterile; tool
Relevance: We will carry out complementary and synergistic studies in two powerful model systems - Drosophila and the mouse - to examine the function of ERM proteins in epithelial morphogenesis. Specifically, we will test the hypothesis that ERM proteins provide local regulation of RhoGTPase activity in response to upstream signals/receptors using molecular tools and genetic models that we have developed in each system. We will also delineate the function of ERM proteins in cell junction remodeling/stability as suggested by the phenotypes of ERM loss in both flies and mammals
Project start date: 2010-01-01
Project end date: 2013-12-31
Budget start date: 1-JAN-2010
Budget end date: 31-DEC-2010
PFA/PA: PA-07-070
1R01GM087558-01A1 (2010): $504960
FUNCTION OF MERLIN, A DROSOPHILA NF2 GENE HOMOLOGUE
Richard G Fehon, Professor And Chairman
University Of Chicago, 5801 S Ellis Ave, Chicago, Il 60637
Grant 2R01NS034783-14A1 from National Institute Of Neurological Disorders And Stroke
Abstract: Neurofibromatosis type 2 (NF2), a dominantly inherited disease, is caused by mutations in Merlin (Schwannomin), a member of the Protein 4.1 superfamily. Symptoms of NF2, which usually appear by early adult life, are caused by the formation of bilateral vestibular Schwannomas (resulting in deafness) and other benign tumors. The cellular functions of Merlin and its role in tumor suppression are still largely unknown, though recent studies in our laboratory and others have made significant progress. Identifying specific proteins and signal transduction pathways with which Merlin interacts is especially important because these partners may act as genetic modifiers of NF2 disease phenotypes and provide potential targets for therapeutic agents. The common fruit fly, Drosophila, has proven to be a useful model system for understanding gene function in the context of a developing organism. The overall goal of this proposal is therefore to examine the cellular functions of Merlin and its functional partner Expanded in Drosophila, particularly in relation to the control of cell proliferation by the Hippo pathway. In the next funding period, we plan to continue our studies of Merlin and Expanded function in developing organisms and in individual cells. Specifically, the proposed experiments will 1) Elucidate functional interactions between Merlin/Expanded and the HSW pathway. Specifically we will test the hypothesis that Expanded functions downstream of Hippo to regulate the transcriptional coactivator Yorkie. 2) Understand the role of Merlin and Expanded in regulating receptor localization and availability at the plasma membrane. 3) Examine the role of signaling by the Hippo, Salvador, Warts pathway on regulating receptor abundance at the cell surface. These experiments are expected to provide insights into the functions of Merlin, Expanded and the Hippo pathway in regulating proliferation. Thus they will contribute to our understanding of human NF2, tumor suppression in general, and carcinogenesis. In addition, the proposed experiments should lead to a better understanding of the cellular processes that establish specialized membrane domains in epithelial cells and neurons. Finally, these studies should contribute to work on the mechanisms by which cellular interactions function to control cell growth and determine cell fate during development. The experiments in this proposal are designed to provide insights into the functions of Merlin (the Neurofibromatosis 2 tumor suppressor), Expanded and the Hippo pathway in regulating receptor trafficking and proliferation. In addition, the proposed experiments should lead to a better understanding of the cellular processes that establish specialized membrane domains in specialized cells such as neurons and epithelial cells. Finally, these studies should contribute to work on the mechanisms by which cellular interactions function to control cell growth and determine cell fate during development
Keywords: 21+ years old; Adherens Junction; Adhering Junction; Adhesive Junction; Adult; Anchoring Junction; Apical; Attention; Benign; Biological Models; Body Tissues; Cancer Induction; Cell Communication and Signaling; Cell Function; Cell Growth in Number; Cell Multiplication; Cell Process; Cell Proliferation; Cell Signaling; Cell membrane; Cell physiology; Cell surface; Cells; Cellular Expansion; Cellular Function; Cellular Growth; Cellular Physiology; Cellular Process; Cellular Proliferation; Central Neurofibromatosis; Cytoplasm; Cytoplasmic Membrane; Deafness; Development; Disease; Disorder; Dmerlin; Drosophila; Drosophila genus; Drosophila merlin; EC 2.7; Epithelial Cells; Family; Fertility/Fertilization; Fertilization; Flies; Fruit Fly, Drosophila; Funding; GeneHomolog; Genes; Genetic; Genetic Alteration; Genetic Change; Genetic defect; Goals; Hereditary; Homolog; Homologous Gene; Homologue; Human; Human, Adult; Human, General; Individual; Inherited; Intracellular Communication and Signaling; Kinases; Laboratories; Lead; Life; Lipid Rafts, Cell Membrane; Mammalia; Mammalian Cell; Mammals; Mammals, General; Mammals, Mice; Man (Taxonomy); Man, Modern; Mediating; Membrane; Membrane Microdomains; Merlin; Mice; Model System; Modeling; Models, Biologic; Moesin-Ezrin-Radixin-Like Protein; Molecular; Molecular Genetic; Molecular Genetics; Monomeric G-Proteins; Monomeric GTP-Binding Proteins; Multiple Neurofibromas; Murine; Mus; Mutation; NF2 Gene Product; Nerve Cells; Nerve Unit; Neural Cell; Neurocyte; Neurofibromatoses; Neurofibromatosis; Neurofibromatosis 2; Neurofibromatosis 2 Gene Product; Neurofibromatosis II; Neurofibromatosis Syndrome; Neurofibromatosis Type 2 Protein; Neurofibromatosis, Acoustic, Bilateral; Neurofibromatosis, Central, NF 2; Neurofibromatosis, Central, NF2; Neurofibromatosis, Type 2; Neurofibromatosis, Type II; Neurofibromin 2; Neurons; Organism; Pathway interactions; Pb element; Phenotype; Phosphorylation; Phosphotransferases; Plasma Membrane; Protein Phosphorylation; Proteins; Receptor Protein; Recruitment Activity; Research; Role; Schwannomerlin; Schwannomin; Schwannomin Protein; Signal Transduction; Signal Transduction Pathway; Signal Transduction Systems; Signaling; Small G-Proteins; Small GTPases; Sphingolipid Microdomains; Sphingolipid-Cholesterol Rafts; Sterility; Subcellular Process; Symptoms; Testing; Therapeutic Agents; Tissues; Transcription Activator; Transcription Coactivator; Transcription Factor Coactivator; Transcriptional Activator; Transcriptional Activator/Coactivator; Transcriptional Coactivator; Transphosphorylases; Tumor Suppression; Tumor Suppression, Molecular; Tumor Suppressor Proteins; Type 2s, Neurofibromatosis; Work; acoustic neurofibromatosis; adult human (21+); bilateral vestibular Schwannoma; biological signal transduction; carcinogenesis; cell growth; design; designing; disease phenotype; disease/disorder; experiment; experimental research; experimental study; ezrin; fly; fruit fly; gene function; gene product; genome mutation; heavy metal Pb; heavy metal lead; insight; lipid raft; living system; member; membrane structure; membrane-organizing extension spike protein; merlin, Drosophila; moesin; mutant; neuronal; neuronal tumor; pathway; phosphoprotein p81; plasmalemma; positional cloning; protein 4.1; public health relevance; radixin; radixin protein; receptor; recruit; research study; reverse genetics; rho; social role; sterile; trafficking; transcription factor; tumor; tumor suppressor
Relevance: These experiments in this proposal are designed to provide insights into the functions of Merlin (the Neurofibromaosis 2 tumor suppressor), Expanded and the Hippo pathway in regulating receptor trafficking and proliferation. In addition, the proposed experiments should lead to a better understanding of the cellular processes that establish specialized membrane domains in specialized cells such as neurons and epithelial cells. Finally, these studies should contribute to work on the mechanisms by which cellular interactions function to control cell growth and determine cell fate during development
Project start date: 1996-01-01
Project end date: 2014-12-31
Budget start date: 15-JAN-2010
Budget end date: 31-DEC-2010
PFA/PA: PA-07-070
2R01NS034783-14A1 (2010): $336546
7R01NS034783-10 (2005): $317238
2R01NS034783-09 (2004): $320513
2R01NS034783-04 (1999): $246130
3R01NS034783-04S1 (1999): $25000
Richard G Fehon, Professor And Chairman
Duke University, 2200 W. Main St., Suite 820, Durham, Nc 27705
Abstract: CONFOCAL MICROSCOPY SHARED RESOURCE David McClay, Ph.D., Richard Fehon, Ph.D., Co-Directors The Confocal Microscopy Shared Resource provides a state-of-the-art Facility for obtaining images of cells in which single molecules are tagged with fluorescent markers. By confocal microscopy and computation methods, 3-D images resolve the spatial location of any tagged molecule in cells, tissues or organisms. The Facility provides training for use of the microscope and the microscope plus computational components are maintained and frequently upgraded. The Confocal Microscopy Shared Resource supports more than 47 laboratories in the Cancer Center. In recent years the Facility has been booked for more than 98% of available time and used by more than 100 different investigators per year. The output of papers that include confocal instrumentation is high. Over the past five years more than 80 papers plus 10 journal covers come from facility usage. This proposal provides a list of upgrades and eventual replacement of the Zeiss 410 instrument that constitutes the Facility. There will be a continuation of policies that kept the instrument on line for all but 4 days in 2003. This will maximize availability of the instrument. Fee charges will be kept at the minimum necessary to keep the instrument in operation at a high efficiency. Policies for maintaining the instrument as a high quality and effective tool for obtaining confocal images will be continued. A new instrument will be purchased in about two years in order to provide the community with a state-of-the-art facility
Keywords: 3D image; Arts; Back; Body Tissues; Books; Budgets; Cancer Center; Cancers; Cells; Communities; Confocal Microscopy; Doctor of Philosophy; Dorsum; Drops; Fees and Charges; Grant; Hour; Image; Images, 3-D; Instrumentation, Other; Investigators; Journals; Laboratories; Location; Magazine; Malignant Neoplasms; Malignant Tumor; Methods; Microscope; Neck; Operation; Operative Procedures; Operative Surgical Procedures; Organism; Outcome; Output; Paper; Peer Review Grants; Ph.D.; PhD; Policies; Protocol; Protocols documentation; Research; Research Personnel; Researchers; Resolution; Resource Sharing; SCHED; Schedule; Surgical; Surgical Interventions; Surgical Procedure; Three-Dimensional Image; Time; Tissues; Training; Work; cell imaging; cellular imaging; cost; imaging; instrument; instrumentation; living system; malignancy; member; neoplasm/cancer; single molecule; success; surgery; time use; tool
Budget start date: 30-SEP-2009
Budget end date: 29-SEP-2011
3P30CA014236-35S5_9003 (2009): $219
3P30CA014236-35S4_9003 (2009): $6667
Sponsored Links Excellgen http://Excellgen.com
Functions Of The Epithelial Septate Junction
Richard G Fehon, Professor
University Of Chicago 5801 S Ellis Ave Chicago, Il 60637
Grant 5R01GM074063-02 from National Institute Of General Medical Sciences IRG: DEV
Abstract: A central problem in the development and function of epithelial cells is the process by which specialized membrane domains are formed and maintained. These domains, including the apical and basolateral membranes, the junctional complex, and other subdomains, are important in organizing and compartmentalizing membrane-related functions. Intercellular junctions, including adherens, tight, and septate junctions, have well-defined structural functions in intercellular adhesion and preventing paracellular flow. In addition, there is an increasing body of evidence that these junctions, and other specialized membrane domains, play an essential role in regulating signaling pathways. The overall goal of this proposal is to better understand how specialized membrane domains, including intercellular junctions and signaling complexes, are established and regulated in developing epithelial cells. More specifically, we plan to elucidate the functions of the epithelial septate junction, a key part of the junctional complex that forms between Drosophila epithelial cells. Septate junctions are structurally and molecularly homologous to the mammalian paranodal junction that separates the node of Ranvier from the myelinated portion of the axon. Studies in our laboratory and others have identified a handful of septate junction components, but we still have a very limited understanding of either its structure or function. To shed light on these important questions, we plan to 1) Identify novel septate junction components using a genetic and cellular approaches. 2) Study the functions of Ankyrin, a membrane associated protein that is believed to interact with some septate junction components, in organizing the basolateral membrane. 3) Examine functional interactions between the septate junction and mechanisms that establish and maintain apical/basal epithelial polarity. These experiments are expected to provide insights into questions of fundamental importance in all developing tissues and in particular epithelia. Knowing more about the mechanisms by which epithelial cells establish and maintain contacts, regulate paracellular diffusion, and form specialized membrane domains is important not only for understanding normal physiology and development, but also for elucidating processes associated with a variety of human diseases.
Keywords: ankyrin, membrane, Chordata, Drosophilidae, adhesion, allele, antiserum, axon, base, basolateral membrane, cell, cell proliferation, diffusion, emotion, epithelium, evolution, gene, gene mutation, genetics, genome, hand, human, insight, intercellular connection, lighting, molecular genetics, node of Ranvier, oogenesis, phenotype, physiology, play, protein, role, thinking, tissue, transfection
Project start date: 2006-04-01
Project end date: 2010-03-31
5R01GM074063-02 (2007): $275612
1R01GM074063-01A1 (2006): $283404
FUNCTIONS OF DMERLIN--A NF2 GENE HOMOLOGUE
Richard G Fehon, Professor
Duke University 2200 W. Main St. Durham, Nc 27705
Grant 1R01NS034783-01 from National Institute Of Neurological Disorders And Stroke IRG: NEUC
Project start date: 1996-01-01
Project end date: 1998-12-31
1R01NS034783-01 (1996): $154159