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Timothy A Mietzner

Explore the profile of Timothy A Mietzner including associated specialties, affiliations and a list of published articles. Areas
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Articles 24
Citations 652
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Recent Articles
1.
Paranjape S, Lauer T, Montelaro R, Mietzner T, Vij N
F1000Res . 2014 Feb; 2:36. PMID: 24555033
Background: Host-derived (LL-37) and synthetic (WLBU-2) cationic antimicrobial peptides (CAPs) are known for their membrane-active bactericidal properties. LL-37 is an important mediator for immunomodulation, while the mechanism of action of...
2.
Deslouches B, Steckbeck J, Craigo J, Doi Y, Mietzner T, Montelaro R
Antimicrob Agents Chemother . 2013 Mar; 57(6):2511-21. PMID: 23507278
The emergence of multidrug-resistant (MDR) pathogens underscores the need for new antimicrobial agents to overcome the resistance mechanisms of these organisms. Cationic antimicrobial peptides (CAPs) provide a potential source of...
3.
Parker Siburt C, Mietzner T, Crumbliss A
Biochim Biophys Acta . 2011 Sep; 1820(3):379-92. PMID: 21933698
Background: Gram negative bacteria require iron for growth and virulence. It has been shown that certain pathogenic bacteria such as Neisseria gonorrhoeae possess a periplasmic protein called ferric binding protein...
4.
Weaver K, Gabricevic M, Anderson D, Adhikari P, Mietzner T, Crumbliss A
Biochemistry . 2010 May; 49(29):6021-32. PMID: 20496864
Ferric binding protein A (FbpA) plays a central role in the iron acquisition processes of pathogenic Neisseria gonorrheae, Neisseria meningitidis, and Haemophilus influenzae. FbpA functions as an iron shuttle within...
5.
Parker Siburt C, Roulhac P, Weaver K, Noto J, Mietzner T, Cornelissen C, et al.
Metallomics . 2010 Feb; 1(3):249-55. PMID: 20161024
Neisseria gonorrhoeae has the capacity to acquire iron from its human host by removing this essential nutrient from serum transferrin. The transferrin binding proteins, TbpA and TbpB constitute the outer...
6.
Heymann J, Gabricevic M, Mietzner T, Crumbliss A
J Biol Inorg Chem . 2009 Oct; 15(2):237-48. PMID: 19813031
The bacterial transferrin ferric binding protein A (FbpA) requires an exogenous anion to facilitate iron sequestration, and subsequently to shuttle the metal across the periplasm to the cytoplasmic membrane. In...
7.
Chan Y, Liu J, Pociask D, Zheng M, Mietzner T, Berger T, et al.
J Immunol . 2009 Apr; 182(8):4947-56. PMID: 19342674
Antimicrobial proteins comprise a significant component of the acute innate immune response to infection. They are induced by pattern recognition receptors as well as by cytokines of the innate and...
8.
Weaver K, Heymann J, Mehta A, Roulhac P, Anderson D, Nowalk A, et al.
J Biol Inorg Chem . 2008 May; 13(6):887-98. PMID: 18461372
The obligate human pathogens Haemophilus influenzae, Neisseria gonorrhoeae, and N. meningitidis utilize a highly conserved, three-protein ATP-binding cassette transporter (FbpABC) to shuttle free Fe(3+) from the periplasm and across the...
9.
Roulhac P, Weaver K, Adhikari P, Anderson D, DeArmond P, Mietzner T, et al.
Biochemistry . 2008 Mar; 47(14):4298-305. PMID: 18338854
Ferric binding protein, FbpA, is a member of the transferrin superfamily whose function is to move an essential nutrient, iron, across the periplasm and into the cytosol through formation of...
10.
Deslouches B, Gonzalez I, DeAlmeida D, Islam K, Steele C, Montelaro R, et al.
J Antimicrob Chemother . 2007 Jul; 60(3):669-72. PMID: 17623696
Objectives: We describe the antimicrobial activity against Pseudomonas aeruginosa of the de novo-derived antimicrobial peptide WLBU2 in an animal model of infection. Methods: For this study, an intravenous (iv) model...