Tudor Moldoveanu, PhD, Faculty, Structural Biology, St. Jude Children’s Research Hospital

    Tudor Moldoveanu, PhD

    Research Associate, St. Jude Faculty

    Departments

    Structural Biology
    Chemical Biology & Therapeutics

    Contact Information

    Tudor Moldoveanu, PhD
    Structural Biology
    MS 311, Room D1034D
    St. Jude Children's Research Hospital
    262 Danny Thomas Place
    Memphis, TN 38105-3678
    Email: tudor.moldoveanu@stjude.org
    Phone: (901) 595-7471
    FAX: (901) 595-3032

    Education

    BSc with honors – Queen’s University, Kingston, Ontario, Canada
    PhD – Queen’s University, Kingston, Ontario, Canada


    Research Interests


    Selected Publications

    Moldoveanu T, Viacava Follis A, Kriwacki RW, Green DR. Many Players in BCL-2 Family Affairs. Trends Biochem Sci 39:101, 2014.

    McCoy F, Darbandi R, Lee HC, Bharatham K, Moldoveanu T, Royappa G, Dodd K, Lin W, Chen S-I, Tangallapally RP, Kurokawa M, Lee EL, Shelat A, Chen T, Green DR, Harris RA, Lin S-H, Fissore RA, Colbran RJ, Nutt LK. Metabolic activation of CaMKII by Coenzyme A. Mol Cell 52:325, 2013.

    Moldoveanu T, Grace CR, Llambi F, Nourse A, Gehring K, Kriwacki R, Green DR. BID-induced structural changes in BAK promote apoptosis. Nat Struct Mol Biol 20:589, 2013.

    Llambi F, Moldoveanu T, Tait SWG, Bouchier-Hayes L, Temirov J, McCormick LL, Dillon CP, Green DR. A unified model of BCL-2 family interactions at the mitochondria. Mol Cell 44:517, 2011.

    Du H, Wolf J, Schafer B, Moldoveanu T, Chipuk JE, Kuwana T. BH3-domains other than BIM and BID can directly activate BAX/BAK J Biol Chem 286:491, 2011.

    Koyanagi M, Kerns JA, Chung L, Zhang Y, Brown S, Moldoveanu T, Malik HS, Bix M. Diversifying selection and functional analysis of interleukin-4 suggests antagonism-driven evolution at receptor-binding interfaces. BMC Evol Biol 10:223, 2010.

    Liu Q, Moldoveanu T, Sprules T, Matta-Camacho E, Mansur-Azzam N, Gehring K. Apoptotic Regulation of MCL-1 through heterodimerization. J Biol Chem 285:19615-19624, 2010.

    Chipuk JE, Moldoveanu T, Lambii F, Parsons M, Green DR. The BCL-2 family reunion. Mol Cell 37:299-310, 2010.

    Moldoveanu T, Gehring K, Green DR. Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains. Nature 465:404-8, 2008. (News and Views Enzyme knocked for a loop. Nature 465:337-8, 2008.)

    Kozlov G, Peschard P, Zimmerman B, Lin T, Moldoveanu T, Mansur-Azzam N, Gehring K, Park M. Structural basis for UBA-mediated dimerization of c-Cbl ubiquitin ligase. J Biol Chem 282:27547-55, 2007.

    Cuerrier D, Moldoveanu T, Campbell RJ, Kelly J, Yoruk B, Verhelst SH, Greenbaum D, Bogyo M, Davies PL. Development of calpain-specific inactivators by screening of positional-scanning epoxide libraries. J Biol Chem 282:9600-11, 2007.

    Moldoveanu T, Qian L, Tocilj A, Watson M, Shore G, Gehring K. The X-ray Structure of a BAK homodimer reveals an inhibitory zinc binding site. Mol Cell 24:677-88, 2006.

    Cuerrier D, Moldoveanu T, Davies PL, Campbell RL. Calpain inhibition by α-ketoamide and cyclic hemithioacetal inhibitors revealed by X-ray crystallography. Biochemistry 45:7446-52, 2006.

    Denisov AY, Chen G, Sprules T, Moldoveanu T, Beauparlant P, Gehring K. Structural model of the Bcl-w-Bid-peptide complex and its interactions with phospholipid micelles. Biochemistry 45:2250-6, 2006.

    Cuerrier D, Moldoveanu T, Davies PL. Determination of the peptide substrate specificity for μ-calpain by a peptide library-based approach. J Biol Chem 280:40632-41, 2005.

    Moldoveanu T, Campbell RL, Cuerrier D, Davies PL. Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site. J Mol Biol 343:1313-26, 2004.

    Diaz BG, Moldoveanu T, Kuiper MJ, Campbell RL, Davies PL. Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide. J Biol Chem 279:27656-66, 2004.

    Moldoveanu T, Jia Z, Davies PL. Calpain activation by cooperative Ca2+ binding at two non-EF-hand sites. J Biol Chem 279:6106-14, 2004.

    Moldoveanu T, Hosfield CM, Lim D, Jia Z, Davies PL. Calpain silencing by a reversible intrinsic mechanism. Nat Struct Mol Biol 10:371-78, 2003.

    Moldoveanu T, Hosfield CM, Lim D, Elce JS, Jia Z, Davies PL. A Ca2+ switch aligns the active site of calpain. Cell 108:649-60, 2002. (News and Views How calpain is activated by calcium. Nat Struct Mol Biol 9:239-41, 2002.)

    Jia Z, Petrounevitch V, Wong A, Moldoveanu T, Davies PL, Elce JS, Beckmann JS. Mutations in calpain 3 associated with limb girdle muscular dystrophy: analysis by molecular modeling and by mutation in m-calpain. Biophys J 80:2590-6, 2001.

    Moldoveanu T, Hosfield CM, Jia Z, Elce JS, Davies PL. Ca2+-induced structural changes in rat m-calpain revealed by partial proteolysis. Biochim Biophys Acta 1545:245-54, 2001.

    Hosfield CM, Moldoveanu T, Davies PL, Elce JS, Jia Z. Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C2-like domain. J Biol Chem 276:7404-7, 2001.

    Last update: March 2014