Linda M. McAllister-Lucas, MD, PhD
- Division Director, Hematology-Oncology, Professor of Pediatrics and Microbiology & Molecular Genetics
Administrative Assistant: Carla Clarke
Dr. Linda McAllister-Lucas is an NIH-funded physician-scientist who investigates how dysregulated intracellular signaling contributes to inflammatory and neoplastic disease. She co-directs a research laboratory with Dr. Peter Lucas, a member of the faculty in the Department of Pathology. Their joint laboratory, the Lucas-McAllister Lab, comprises ten scientists at varying stages of training, and their group is pursuing two related areas of research.
Professional and Scientific Society Memberships
- Sigma Xi, Associate Member, 1987
- American Academy of Pediatrics, 1996-1999
- American Society of Hematology, 2002-Present
- American Society of Pediatric Hematology and Oncology, 2002-Present
- Society for Pediatric Research, 2006-Present
- American Association for Cancer Research, 2006-Present
- Midwest Society for Pediatric Research, 2007-Present
- American Society for Clinical Investigation, 2014-Present
- American Pediatric Society (APS), 2015-Present
Education & Training
- BA, Carleton College, 1987
- PhD, Vanderbilt University, 1994
- MD, Vanderbilt University, 1996
- Resident, University of Michigan, 1999
- Fellow, University of Michigan, 2002
- Research Fellow, University of Michigan, 2002
Buffington LA, Blackburn DW, Hamilton CL, Jarvis JJ, Knowles JJ, Lodwick PA, McAllister LM, Neidhart DJ and Serumgard JL (1989)Effects of solvent and anomeric configuration upon the circular dichroism, temperature dependence of amide proton chemical shifts, amide proton exchange rates, and infrared absorption of methyl 2-acetamido-2-deoxy-D-glucopyranosides. J. Amer. Chem. Soc., 111:2451-2454.
Colbran JL, Frances SH Leach AB, Thomas MK, Jiang H, McAllister LM and Corbin JD (1992) A phenylalanine in peptide substrates provides for selectivity between cGMP-and cAMP-dependent protein kinases. J. Biol. Chem., 267:9589-9594
Corbin JL, Woodall CC, Colbran JL, McAllister LM, Sekhar KR and Francis SH (1993) Identifying protein kinases in crude extracts that phosphorylate cGMP-binding cGMP-specific phosphodiesterase. Agents and Actions Supplements,43: 27-33
McAllister-Lucas LM, Sonnenburg WK, Kadlecek A, Seger D, Le Trong H, Colbran JL, Thomas MK, Walsh KA, Francis SH, Corbin JD and Beavo JA (1993) The structure of a bovine lung cGMP-binding, cGMP-specific phosphodiesterase deduced from a cDNA clone. J. Biol. Chem., 268:22863-22873
Francis SH, Colbran JL, McAllister-Lucas LM and Corbin JD (1994) Zinc interactions and conserved motifs of the cGMP-binding cGMP-specific phosphodiesterase suggest that it is a zinc hydrolase. J. Biol. Chem., 269:22477-22480
McAllister-Lucas LM, Haik TL, Colbran JL, Sonnenburg WK, Seger D, Turko IV, Francis SH and Corbin JD (1995) An essential aspartic acid at each of two allosteric cGMP-binding sites of a cGMP-specific phosphodiesterase.J. Biol. Chem., 270:30671-30679.
Turko IV, Haik TL, McAllister-Lucas LM, Burns F, Francis SH and Corbin JD (1996) Identification of key amino acids in a conserved cGMP-binding site of cGMP-binding phosphodiesterases. A putative NKXnD motif for cGMP binding.J. Biol. Chem., 271:22240-22244.
Loughney K, Hill TR, Florio VA, Uher L, Rosman GJ, Wolda SL, Jones BA, Howard ML, McAllister-Lucas LM, Sonnenburg WK, Francis SH, Corbin JD, BeavoJA and Ferguson K (1998) Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3’,5’-cyclic nucleotide phosphodiesterase.Gene, 216:139-147.
Lucas PC, Yonezumi M, Inohara N, McAllister-Lucas LM, Abazeed ME, Chen FF, Yamaoka S, Seto M, and Nunez G (2001) Bcl10 and MALT1, independent targets of chromosomal translocation in MALT lymphoma, cooperatein a novel NF-kB signaling pathway. J. Biol. Chem., 276:19012-19019.
McAllister-Lucas LM, Inohara N, Lucas PC, Ruland J, Benito A, Li Q, Chen S, Chen FF, Yamaoka S, Verma IM, Mak TW, and Nunez G (2001) Bimp1, a MAGUK family member linking protein kinase Cactivation to Bcl10-mediated NF-kB induction. J. Biol. Chem., 276: 30589-30597.