Biology Reference
In-Depth Information
Fisher, M. (1956). An unusual variant of acute idiopathic polyneuritis (syndrome of
ophthalmoplegia, ataxia and areflexia). The New England Journal of Medicine , 255 , 57-65.
Flatley, J., Barrett, J., Pullan, S. T., Hughes, M. N., Green, J., & Poole, R. K. (2005). Tran-
scriptional responses of Escherichia coli to S -nitrosoglutathione under defined chemostat
conditions reveal major changes in methionine biosynthesis. The Journal of Biological
Chemistry , 280 , 10065-10072.
Fouts, D. E., Mongodin, E. F., Mandrell, R. E., Miller, W. G., Rasko, D. A., Ravel, J., et al.
(2005). Major structural differences and novel potential virulence mechanisms from the
genomes of multiple Campylobacter species. PLoS Biology , 3 , e15.
Frey, A. D., Farres, J., Bollinger, C. J., & Kallio, P. T. (2002). Bacterial hemoglobins and
flavohemoglobins for alleviation of nitrosative stress in Escherichia coli . Applied and
Environmental Microbiology , 68 , 4835-4840.
Frey, A. D., & Kallio, P. T. (2005). Nitric oxide detoxification—A new era for bacterial
globins in biotechnology? Trends in Biotechnology , 23 , 69-73.
Frey, A. D., Shepherd, M., Jokipii-Lukkari, S., Haggman, H., & Kallio, P. T. (2011). The
single-domain globin of Vitreoscilla : Augmentation of aerobic metabolism for biotechno-
logical applications. In R. K. Poole (Ed.), Advances in microbial physiology , Vol. 58 ,
(pp. 81-139). London: Academic Press.
Fridovich, I. (1999). Fundamental aspects of reactive oxygen species, or what's the matter
with oxygen? Annals of the New York Academy of Sciences , 893 , 13-18.
Friedman, C. R., Neimann, J., Wegener, H. C., & Tauxe, R. V. (2000). Epidemiology of
Campylobacter jejuni infections in the United States and other industrialized nations. In
I. Nachamkin & M. J. Blaser (Eds.), Campylobacter (pp. 121-138). Washington, DC:
ASM Press.
Gardner, P. R., Costantino, G., & Salzman, A. L. (1998). Constitutive and adaptive detox-
ification of nitric oxide in Escherichia coli . Role of nitric-oxide dioxygenase in the
protection of aconitase. The Journal of Biological Chemistry , 273 , 26528-26533.
Gardner, P. R., Costantino, G., Szabo, C., & Salzman, A. L. (1997). Nitric oxide sensitivity
of the aconitases. The Journal of Biological Chemistry , 272 , 25071-25076.
Gardner, A. M., & Gardner, P. R. (2002). Flavohemoglobin detoxifies nitric oxide in aer-
obic, but not anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic nitric
oxide-scavenging activity. The Journal of Biological Chemistry , 277 , 8166-8171.
Gardner, P. R., Gardner, A. M., Brashear, W. T., Suzuki, T., Hvitved, A. N.,
Setchell, K. D., et al. (2006). Hemoglobins dioxygenate nitric oxide with high fidelity.
Journal of Inorganic Biochemistry , 100 , 542-550.
Gardner, P. R., Gardner, A.M., Martin, L. A., Dou, Y., Li, T., Olson, J. S., et al. (2000). Nitric-
oxide dioxygenase activity and function of flavohemoglobins. sensitivity to nitric oxide and
carbon monoxide inhibition. The Journal of Biological Chemistry , 275 , 31581-31587.
Gardner, P. R., Gardner, A. M., Martin, L. A., & Salzman, A. L. (1998). Nitric oxide
dioxygenase: An enzymic function for flavohemoglobin. Proceedings of the National Acad-
emy of Sciences of the United States of America , 95 , 10378-10383.
Giardina, G., Rinaldo, S., Johnson, K. A., Di Matteo, A., Brunori, M., & Cutruzzola, F.
(2008). NO sensing in Pseudomonas aeruginosa : Structure of the transcriptional regulator
DNR. Journal of Molecular Biology , 378 , 1002-1015.
Gibson, Q. H., Olson, J. S., McKinnie, R. E., &Rohlfs, R. J. (1986). A kinetic description of
ligand binding to sperm whale myoglobin. The Journal of Biological Chemistry , 261 ,
10228-10239.
Green, J., Scott, C., & Guest, J. R. (2001). Functional versatility in the CRP-FNR super-
family of transcription factors: FNR and FLP. In R. K. Poole (Ed.), Advances in microbial
physiology , Vol. 44 , (pp. 1-34). London: Academic Press.
Greenberg, J. T., Monach, P., Chou, J. H., Josephy, P. D., & Demple, B. (1990). Positive
control of a global antioxidant defense regulon activated by superoxide-generating agents
Search WWH ::




Custom Search