FET3/YMR058W Literature Guide Help

Other names published for FET3: YMR058W

FET3 - Protein Sequence Features (21)

ReferenceOther Genes Addressed
Breidenbach MA, et al.  (2012) Mapping yeast N-glycosites with isotopically recoded glycans. Mol Cell Proteomics 11(6):M111.015339
Spira F, et al.  (2012) Patchwork organization of the yeast plasma membrane into numerous coexisting domains.LID - 10.1038/ncb2487 [doi] Nat Cell Biol ()
Augustine AJ, et al.  (2010) Systematic perturbation of the trinuclear copper cluster in the multicopper oxidases: the role of active site asymmetry in its reduction of O2 to H2O. J Am Chem Soc 132(17):6057-67
Ziegler L, et al.  (2010) Core glycan in the yeast multicopper ferroxidase, Fet3p: A case study of N-linked glycosylation, protein maturation, and stability. Protein Sci 19(9):1739-50
Terzulli AJ and Kosman DJ  (2009) The Fox1 ferroxidase of Chlamydomonas reinhardtii: a new multicopper oxidase structural paradigm. J Biol Inorg Chem 14(2):315-25
Augustine AJ, et al.  (2008) Spectroscopic Studies of Perturbed T1 Cu Sites in the Multicopper Oxidases Saccharomyces cerevisiae Fet3p and Rhus vernicifera Laccase: Allosteric Coupling between the T1 and Trinuclear Cu Sites. Biochemistry 47(7):2036-2045
Stoj CS, et al.  (2007) Structure-function analysis of the cuprous oxidase activity in Fet3p from Saccharomyces cerevisiae. J Biol Chem 282(11):7862-8
Singh A, et al.  (2006) Assembly, activation, and trafficking of the Fet3p.Ftr1p high affinity iron permease complex in Saccharomyces cerevisiae. J Biol Chem 281(19):13355-64
Stoj CS, et al.  (2006) Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3p. Biochemistry 45(42):12741-9
Bonaccorsi di Patti MC, et al.  (2005) Specific aspartate residues in FET3 control high-affinity iron transport in Saccharomyces cerevisiae. Yeast 22(9):677-87
Quintanar L, et al.  (2005) Role of aspartate 94 in the decay of the peroxide intermediate in the multicopper oxidase Fet3p. Biochemistry 44(16):6081-91
Wang TP, et al.  (2003) Targeted suppression of the ferroxidase and iron trafficking activities of the multicopper oxidase Fet3p from Saccharomyces cerevisiae. J Biol Inorg Chem 8(6):611-20
Bonaccorsi di Patti MC, et al.  (2001) Mutational analysis of the iron binding site of Saccharomyces cerevisiae ferroxidase Fet3. An in vivo study. FEBS Lett 508(3):475-8
Bonaccorsi di Patti MC, et al.  (2000) The essential role of Glu-185 and Tyr-354 residues in the ferroxidase activity of Saccharomyces cerevisiae Fet3. FEBS Lett 472(2-3):283-6
Yun CW, et al.  (2000) Desferrioxamine-mediated iron uptake in Saccharomyces cerevisiae. Evidence for two pathways of iron uptake. J Biol Chem 275(14):10709-15
di Patti MC, et al.  (1999) Homology modeling of the multicopper oxidase Fet3 gives new insights in the mechanism of iron transport in yeast. Protein Eng 12(11):895-7
Hassett RF, et al.  (1998) Spectral and kinetic properties of the Fet3 protein from Saccharomyces cerevisiae, a multinuclear copper ferroxidase enzyme. J Biol Chem 273(36):23274-82
Murphy ME, et al.  (1997) Structural comparison of cupredoxin domains: domain recycling to construct proteins with novel functions. Protein Sci 6(4):761-70
de Silva D, et al.  (1997) Purification and characterization of Fet3 protein, a yeast homologue of ceruloplasmin. J Biol Chem 272(22):14208-13
Askwith C, et al.  (1994) The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76(2):403-10
Dancis A, et al.  (1994) Molecular characterization of a copper transport protein in S. cerevisiae: an unexpected role for copper in iron transport. Cell 76(2):393-402