M
Mark A. Miller
Researcher at University of Tennessee Health Science Center
Publications - 64
Citations - 2972
Mark A. Miller is an academic researcher from University of Tennessee Health Science Center. The author has contributed to research in topics: Francisella tularensis & Antigen. The author has an hindex of 30, co-authored 64 publications receiving 2840 citations. Previous affiliations of Mark A. Miller include Emory University & Allegheny General Hospital.
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Journal ArticleDOI
A formalin-inactivated whole SIV vaccine confers protection in macaques
Michael Murphey-Corb,Louis N. Martin,Billie Davison-Fairburn,Ronald C. Montelaro,Mark A. Miller,Melanie West,Susumu Ohkawa,Gary B. Baskin,Jing Yu Zhang,Scott D. Putney,Anthony C. Allison,Deborah A. Eppstein +11 more
TL;DR: Results demonstrate that a whole virus vaccine is highly effective in inducing immune responses that can protect against lentivirus infection and AIDS-like disease.
Journal Article
Regulation of murine macrophage IL-12 production. Activation of macrophages in vivo, restimulation in vitro, and modulation by other cytokines.
TL;DR: Macrophages were maximally activated within 48 h in vivo during infection with Listeria and a systematic survey of potential stimulatory agents showed that microbial heat shock proteins, crude bacterial extracts, bacterial superantigens, a yeast extract, and dsRNA induced IL-12 in vitro.
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Inflammasome-dependent Pyroptosis and IL-18 Protect against Burkholderia pseudomallei Lung Infection while IL-1β Is Deleterious
TL;DR: It is shown that the Nod-like receptors (NLR) NLRP3 and NLRC4 differentially regulate pyroptosis and production of IL-1β and IL-18 and are critical for inflammasome-mediated resistance to melioidosis.
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Uveitis and Pseudojaundice During a Regimen of Clarithromycin, Rifabutin, and Ethambutol
TL;DR: The occurrence of uveitis and pseudojaundice in patients with AIDS who were receiving the combination of clarithromycin, rifabutin, and ethambutol for the treatment of Mycobacterium avium complex bacteremia is reported.
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Alterations in cell membrane permeability by the lentivirus lytic peptide (LLP-1) of HIV-1 transmembrane protein.
Mark A. Miller,Miles W. Cloyd,James Liebmann,Charles R. Rinaldo,Kazi Islam,Sherry Z.S. Wang,Timothy A. Mietzner,Ronald C. Montelaro +7 more
TL;DR: It is demonstrated that the peptide homolog of HIV-1 LLP-1 can indeed perturb membranes by forming pores of defined size in cytoplasmic membranes and the analog studies described here reveal that the amphipathy and high positive charge of this protein segment are required for the membrane perturbative properties.