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Thomas Hollis, Ph.D.

Thomas Hollis, Ph.D.

Associate Professor, Biochemistry
Contact Information
Office:
336-716-0768
Research Interests
cancer/oncogenesis, hematologic system, microorganisms, obesity, cardiovascular system, lymphatic & reticulo-endotheli, animals, cells/membranes/tissu, biological/chemical compounds, endocrine system, molecular biology/molecular me, human, cells only, immunology/allergy/inflammatio, cell growth, differentiation,d, genetics/genome, basic mechanisms, structural biology, diabetes
Recent Publications


Small molecule induction of MSH2-dependent cell death suggests a vital role of mismatch repair proteins in cell death. Vasilyeva A, Clodfelter JE, Rector B, Hollis T, Scarpinato KD, Salsbury FR Jr. DNA Repair. 2009 8(1) : 103-113


DNA binding induces active site conformational change in the human TREX2 3'-exonuclease. de Silva U, Perrino FW, Hollis T. Nucleic Acids Res. 2009 37(7) : 2411-2417


Lesion bypass of N2-ethylguanine by human DNA polymerase Iota. Pence MG, Blans P, Zink CN, Hollis T, Fishbein JC, Perrino FW. J Biol Chem. 2009 284(3) : 1732-1740


RNaseH2 mutants that cause Aicardi-Goutieres syndrome are active nucleases. Perrino FW, Harvey S, Shaban NM, Hollis T. J Mol Med. 2009 87(1) : 25-30


Mutations in the 3 '-5 ' DNA exonuclease TREX1 cause monogenic and complex forms of lupus erythematosus [abstract]. Lee-Kirsch M, Gong M, Chowdhury D, Senenko L, Engel K, De Silva U, Bailey SL, Harvey S, Hollis T, Perrino FW, et al. Eur J Pediatr. 2008 167(3) : 365


The TREX1 double-stranded DNA degradation activity is defective in dominant mutations associated with autoimmune disease. Lehtinen DA, Harvey S, Mulcahy MJ, Hollis T, Perrino FW. J Biol Chem. 2008 283(46) : 31649-56


Cooperative DNA binding and communication across the dimer interface in the TREX2 3 '--> 5 '-exonuclease. Perrino FW, de Silva U, Harvey S, Pryor EE Jr, Cole DW, Hollis T. J Biol Chem. 2008 283(31) : 21441-52


Crystallization of protein-DNA complexes. Hollis T. Methods Mol Biol. 2007 363 : 225-237


Structural basis for 3-methyladenine recognition and removal by a highly-specific DNA glycosylase: the crystal structure of TAG in complex with DNA [abstract]. Herrin A, Hollis T, Eichman BF. J Biomol Struct Dyn. 2007 24(6) : 614


Heterozygous mutations in TREX1 cause familial chilblain lupus and dominant Aicardi-Goutieres syndrome. Rice G, Newman WG, Dean J, Patrick T, Parmar R, Flintoff K, Robins P, Harvey S, Hollis T, Perrino FW, et al. Am J Hum Genet. 2007 80(4) : 811-815


The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partnering. de Silva U, Choudhury S, Bailey SL, Harvey S, Perrino FW, Hollis T. J Biol Chem. 2007 282(14) : 10537-43


A mutation in TREX1 that impairs susceptibility to granzyme A-mediated cell death underlies familial chilblain lupus. Lee-Kirsch MA, Chowdhury D, Harvey S, Gong M, Senenko L, Engel K, Pfeiffer C, Hollis T, Gahr M, Perrino FW, et al. J Mol Med. 2007 85(5) : 531-537


DNA damage recognition and repair by 3-methyladenine DNA glycosylase I (TAG). Metz AH, Hollis T, Eichman BF. EMBO J. 2007 26(9) : 2411-2420


The molecular mechanism of DNA damage recognition by MutS homologs and its consequences for cell death response. Salsbury FR Jr, Clodfelter JE, Gentry MB, Hollis T, Scarpinato KD. Nucleic Acids Res. 2006 34(8) : 2173-2185
All Publications

For a listing of recent publications, refer to PubMed, a service provided by the National Library of Medicine.

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