Dr. Linda M Mcallister-lucas MD
Hematologist (Pediatric) | Pediatric Hematology-Oncology
1500 East Medical Center Dr B1 Floor Cancer & Ge Ann Arbor MI, 48109About
Dr. Linda Mcallister-lucas is a pediatric hematologist practicing in Ann Arbor, MI. Dr. Mcallister-lucas specializes in treating children that have a blood disease or cancer. Such blood diseases include disorders of red blood cells, white blood cells and/or platelets. The types of cancers that Dr. Mcallister-lucas treats include leukemias, lymphomas and certain tumors. Dr. Mcallister-lucas can also treat bleeding disorders in children. Pediatric hematologists can be found in childrens hospitals, community hospitals, university medical centers and more.
Education and Training
Univ of Mi Med Sch, Ann Arbor Mi MD
Board Certification
PediatricsAmerican Board of PediatricsABP- Pediatric Hematology-Oncology
Provider Details
Expert Publications
Data provided by the National Library of Medicine- A requirement for CARMA1 in TCR-induced NF-kappa B activation.
- Thoracic neural crest tumors in Beckwith-Wiedemann syndrome.
- NF-kappaB signaling in lymphocytes: a new cast of characters.
- A dual role for the API2 moiety in API2-MALT1-dependent NF-kappaB activation: heterotypic oligomerization and TRAF2 recruitment.
- Cleavage of NIK by the API2-MALT1 fusion oncoprotein leads to noncanonical NF-kappaB activation.
- Protease activity of the API2-MALT1 fusion oncoprotein in MALT lymphoma development and treatment.
- From MALT lymphoma to the CBM signalosome: three decades of discovery.
- Thalidomide therapy for aggressive histiocytic lesions in the pediatric population.
- The API2-MALT1 fusion exploits TNFR pathway-associated RIP1 ubiquitination to promote oncogenic NF-κB signaling.
- Zinc interactions and conserved motifs of the cGMP-binding cGMP-specific phosphodiesterase suggest that it is a zinc hydrolase.
- The structure of a bovine lung cGMP-binding, cGMP-specific phosphodiesterase deduced from a cDNA clone.
- An essential aspartic acid at each of two allosteric cGMP-binding sites of a cGMP-specific phosphodiesterase.
- Identification of key amino acids in a conserved cGMP-binding site of cGMP-binding phosphodiesterases. A putative NKXnD motif for cGMP binding.
- Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase.
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