Research
General Information
ZIRC
ZFIN ID: ZDB-PERS-020719-1
Schroeter, Eric H.
Schroeter Lab
Department of Biology
Loyola University Chicago
Quinlan Life Sciences Center 224
6525 N. Sheridan Rd.
Chicago, IL
60626
USA

Phone: (773) 508-3653 Email: eschro2@luc.edu
FAX: (773) 508-3646 URL: http://www.luc.edu/depts/biology/schroeter.htm

Biography and Research Interests:


Publications:

Non-Zebrafish Publications:

Lohmann C., Mumm J. S., Morgan J., Godinho L., Schroeter E.H., Stacy R., Wong W.T., Oakley D., Wong R.O.L. (2005) Imaging the Developing Retina. In: Imaging in Neuroscience and Development (Yuste R, Konnerth A, eds), pp 171-183. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.

Mumm, J. S., Godinho, L., Morgan, J. L., Oakley, D. M., Schroeter, E.H., and Wong, R. O. (2004). Laminar circuit formation in the vertebrate retina. Prog Brain Res 147, 155-169.

Vooijs, M., Schroeter, E.H., Pan, Y., Blandford, M., and Kopan, R. (2004). Ectodomain shedding and intramembrane cleavage of mammalian Notch proteins is not regulated through oligomerization. J Biol Chem 279, 50864-50873.

Schroeter, E.H., Ilagan, Ma. X. G., Brunkan, A. L., Hecimovic, S., Li, Y., Xu M., Lewis, H. D., Saxena, M. T., De Strooper, B., Coonrod, A., Tomita T., Iwatsubo, T., Moore, C. L., Goate, A., Wolfe. M. S., Shearman, M., and R. Kopan. (2003) A presenilin dimer at the core of the -secretase enzyme: Insights from parallel analysis of Notch 1 and APP proteolysis. PNAS, 100(22):13075-80.

Saxena, M. T., Schroeter, E.H., Mumm, J.M. and R. Kopan (2001). Murine notch homologs (N1-4) undergo presenilin-dependent proteolysis. J Biol Chem 276(43):40268-73.

Hadland B.K., Manley N.R., Su D.M., Longmore G.D., Moore C.L., Wolfe M.S., Schroeter E.H., Kopan R. (2001) Gamma-secretase inhibitors repress thymocyte development. Proc. Natl. Acad. Sci. USA, 98(13):7487-7491.

Kopan, R., Huppert, S., Mumm, J.S., Saxena, M.T., Schroeter, E.H., Ray, W. J., and Goate, A. (2001). The NEXT step in Notch processing and its relevance to Amyloid Precursor Protein. In: Neurodegenerative disorders: loss of function through gain of function, K. Beyreuther, Y. Christen, and C. L. Masters, eds. (New York, Springer-Verlag), pp. 119-128.

Mumm, J.S., Schroeter, E.H., Saxena, M.T., Tian, X., Griesemer, A., Ray W.J., Pan D.J., and R. Kopan. (2000). A Ligand Induced Extracellular Cleavage Regulates g-secretase-like Proteolytic Activation of Notch 1. Molecular Cell, 5:197-206.

Huppert, S.S., Le, A., Schroeter, E.H., Mumm, J.S., Saxena, M.T., Milner, L..A., and R. Kopan. (2000) Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1. Nature, 405(6789):966-977.

Ray, W.J., Yao, M., Mumm, J., Schroeter, E.H., Saftig, P., Wolfe, M., Selkoe, D.J., Kopan, R., and A.M. Goate, (1999) Cell Surface Presenilin-1 participates in the g-secretase-like proteolysis of Notch. J. Biol. Chem., 274(51):36801-36807.

De Strooper, B., Annaert W., Cupers P., Saftig P., Craessaerts K., Mumm J.S., Schroeter E.H., Schrijvers V., Wolfe M.S., Ray W.J., Goate A., and R. Kopan. (1999) A Presenilin-1-dependent g-secretase-like Protease Mediates Release of Notch Intracellular domain. Nature, 398(6727):518-522.

Schroeter, E.H., Kisslinger, J.A., and R. Kopan. (1998). Notch-1 signaling requires ligand-induced proteolytic release of intracellular domain. Nature, 393(6683):382-386.

Kopan, R., Schroeter, E.H., Weintraub, H., and J.S. Nye. (1996). Signal transduction by activated mNotch: Importance of proteolytic processing and its regulation by the extracellular domain. Proc. Natl. Acad. Sci. USA, 93:1683-1687.

Jarriault, S., Brou, C., Logeat, F., Schroeter, E.H., Kopan, R., and A. Israel. (1995). Signaling downstream of activated mammalian Notch. Nature, 37:355-8.