Martin Gross
Research Summary / Selected Publications
Translational control of protein synthesis, regulation of polypeptide chain initiation, role of accessory proteins in promoting the protein folding and renaturation activity of hsp 70, mechanism by which Herpes Simplex Virus-1 defends against the interferon-mediated, host cell response to viral infection.
Heller, A., Won, L., Bubula, N., Hessefort, S., Kurutz, J.W., Reddy, G.A., and Gross, M. Long-chain fatty acids increase cellular dopamine in an immortalized cell line (MN9D) derived from mouse mesencephalon, Neuroscience Letters, Volume 376, Issue 1, 7 March 2005, Pages 35-39
B. He, M. Gross and B. Roizman: The g134.5 protein of herpes simplex virus 1 has the structural and functional attributes of a protein phosphatase 1 regulatory subunit and is present in a high molecular weight complex with the enzyme in infected cells. J. Biol. Chem. 273:20737-20743, 1998. View Article
K. A. Cassady, M. Gross, and B. Roizman: The second site mutation in the herpes simplex virus recombinants lacking the g134.5 genes precludes the shutoff of protein synthesis by blocking the phosphorylation of eIF-2a. J. Virol. 72: 7005-7011, 1998. View Article
K. A. Cassady, M. Gross, and B. Roizman: The herpes simplex virus US11 protein effectively compensates for the g134.5 gene if present before activation of protein kinase R by precluding its phosphorylation and that of the a subunit of translation initiation factor eIF-2a. J. Virol. 72: 8620-8626, 1998. View Article
M. Gross, S. Hessefort, and A. Olin: Purification of a 38-kDa protein from rabbit reticulocyte lysate that promotes protein renaturation by hsp 70 and its identification as d-aminolevulinic acid dehydratase and as a putative DnaJ protein. J. Biol. Chem. 274:3125-3134, 1999. View Article