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POST-DOCTORAL FELLOW
Post-doctoral fellowships will be available in 2007 to study the biology and biochemistry of ADAMTS proteases. ADAMTS proteases have been implicated in arthritis, inherited connective tissue disorders, cell migration and angiogenesis. The overall goal of the laboratory is to understand the role of ADAMTS proteases in molecular networks.
The laboratory has characterized a number of ADAMTS proteases and ADAMTS-like molecules. Ongoing projects include the mechanisms of phenotypes in ADAMTS null mice, analysis of post-translational modification of ADAMTS proteases and ADAMTS-like molecules, proteomics for identification of substrates and intermolecular interactions, and interfaces with cell signaling mechanisms.
The laboratory will suit highly motivated new or recent PhD or MD/PhD graduates who are interested in augmenting or developing skills in mouse genetics, embryology, cell biology, enzymology and protein chemistry, including structural biology. The laboratory offers a stimulating and constructive environment for your professional development. The CONTACT _Con-418F7AA81 \c \s \l Lerner Research Institute has state of the art research facilities in a major clinical center, the Cleveland Clinic Foundation, and is affiliated with the adjacent Case Western Reserve University. Cleveland and its vicinity offer an affordable, high quality of life with outstanding recreational and cultural opportunities.
Recent publications
Koo, B-H, Longpre, J-M., Somerville, RPT, Alexander, J.P., Leduc, R.,Apte, SS. Cell surface processing of pro-ADAMTS9 by furin. J Biol Chem, 2006 281(18):12485-94
LeGoff C, Somerville, RPT, Kesteloot, F, Powell, K, Birk, D.E., Colige, A., Apte, S.S. Regulation of procollagen amino-propeptide processing during mouse embryogenesis by specialization of homologous ADAMTS proteases; Insights on collagen biosynthesis and dermatosparaxis. Development, 2006 133(8):1587-96
Oblander SA, Zhou Z, Galvez BG, Starcher B, Shannon JM, Durbeej M, Arroyo AG, Tryggvason K, ApteSS. Distinctive functions of membrane type 1 matrix-metalloprotease (MT1-MMP or MMP-14) in lung and submandibular gland development are independent of its role in pro-MMP-2 activation. Dev Biol. 2005 ;277:255-69.
Somerville R P T, Longpre JM, Apel ED, Lewis RM, Wang LW, Sanes J, Leduc R, ApteSS. ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin sulphate-proteoglycan containing a mucin domain. J Biol Chem.2004 279; 35159-35175
Contact:
Suneel S. APTE, MD, PhD
aptes@ccf.org
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