Patel S, Padilla-Benavides T, Collins JM and Argüello JM. Functional diversity of five homologous Cu+-ATPases present in Sinorhizobium meliloti. Microbiology in press (2014)
Raimunda D, Long, JE, Padilla-Benavides T, Sassetti CM and Argüello JM. Differential roles for the Co2+/Ni2+ transporting ATPases, CtpD and CtpJ, in Mycobacterium tuberculosis virulence. Mol. Microbiol. 91 (1):185-197 (2014)
Argüello JM, Raimunda D and Padilla-Benavides T. Mechanisms of Copper Homeostasis in Bacteria. Front. Cell. Infect. Microbiol. 3:(73)(2013)
Argüello JM, Padilla-Benavides T and Collins JM. Transport Mechanism and Cellular Functions of Bacterial Cu(I)-ATPases. Metals in Cells. Valeria Culotta (Editor). Wiley (2013)
Zielazinski EL, González-Guerrero M, Subramanian P, Stemmler TL, Argüello JM and Rosenzweig AC. Sinorhizobium meliloti Nia is a P1B-5-ATPase expressed in the nodule during plant symbiosis and is involved in Ni and Fe transport. Metallomics. 5: 1614-1623(2013)
Padilla-Benavides T, Long JE, Raimunda D, Sassetti CM and Argüello JM. PA novel P1B-type Mn2+ transporting ATPase is required for secreted protein metallation in mycobacteria. J Biol Chem 288(16):11334-11347 (2013)
Raimunda D, Padilla-Benavides T, Vogt S, Boutigny S, Tomkinson K, Finney L and Argüello JM. Periplasmic response upon disruption of transmembrane Cu transport in Pseudomonas aeruginosa. Metallomics 5(2): 144-151 (2013)
Padilla-Benavides T, McCann CJ, Argüello JM. The mechanism of Cu+ transport ATPases: Interaction with Cu+ chaperones and the role of transient metal binding sites. J Biol Chem 288 (1): 69–78 (2013)
Hernández-Montes G, Argüello JM, Valderrama B. Evolution and diversity of periplasmic proteins involved in copper homeostasis in gamma proteobacteria. BMC Microbiology 2012, 12:249.
Tonelli ML, Ibañez L, Taurian T, Argüello JM and Fabra A. Analysis of phenylalanine ammonia-lyase gene sequence from Arachis hypogeae L. and its transcript abundance in induced systemic resistance against Sclerotium rolfsii. The Journal of Plant Pathology (accepted for publication).
Rosenzweig AC, Argüello JM. Toward a Molecular Understanding of Metal Transport by P(1B)-Type ATPases. Curr Top Membr. 69:113-136 (2012).
Jayakanthan S, Roberts SA, Weichsel A, Argüello JM, McEvoy MM. Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle. Biosci Rep. 32(5):443-53 (2012).
Raimunda D, Khare T, Giometti C, Vogt S, Argüello JM, Finney L. Identifying metalloproteins through X-ray fluorescence mapping and mass spectrometry. Metallomics. 4(9):921-927 (2012).
Raimunda D, Long JE, Sassetti CM, Argüello JM. Role in metal homeostasis of CtpD, a Co2+ transporting P(1B4)-ATPase of Mycobacterium smegmatis. Mol Microbiol. 84 (6):1139-1149 (2012).
Raimunda D, Subramanian P, Stemmler T, Argüello JM. A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn(2+)-ATPases. Biochim Biophys Acta. 1818(5):1374-7 (2012).
Argüello JM, Raimunda D, González-Guerrero M. Metal transport across biomembranes: emerging models for a distinct chemistry. J Biol Chem. 287(17):13510-13517 (2012).
Argüello JM, González-Guerrero M, Raimunda D. Bacterial transition metal P(1B)-ATPases: transport mechanism and roles in virulence. Biochemistry. 50(46):9940-9999 (2011).
Rosadini CV, Gawronski JD, Raimunda D, Argüello JM, Akerley BJ. A novel zinc binding system, ZevAB, is critical for survival of nontypeable Haemophilus influenzae in a murine lung infection model. Infect Immun. 79(8):3366-76. (2011).
Raimunda D, González-Guerrero M, Leeber BW 3rd, Argüello JM. The transport mechanism of bacterial Cu+-ATPases: distinct efflux rates adapted to different function. Biometals. 24(3):467-475 (2011).
González-Guerrero M, Raimunda D, Cheng X, Argüello JM. Distinct functional roles of homologous Cu+ efflux ATPases in Pseudomonas aeruginosa. Mol Microbiol. 78(5):1246-58 (2010).
Agarwal S, Hong D, Desai NK, Sazinsky MH, Argüello JM, Rosenzweig AC. Structure and interactions of the C-terminal metal binding domain of Archaeoglobus fulgidus CopA. Proteins. 78(11):2450-2458 (2010).
Roman EA, Argüello JM, González Flecha FL. Reversible unfolding of a thermophilic membrane protein in phospholipid/detergent mixed micelles. J Mol Biol. 397(2):550-559 (2010).
González-Guerrero M, Hong D, Argüello JM. Chaperone-mediated Cu+ delivery to Cu+ transport ATPases: requirement of nucleotide binding. J Biol Chem. 284(31):20804-20811 (2009).
González-Guerrero M, Eren E, Rawat S, Stemmler TL, Argüello JM. Structure of the two transmembrane Cu+ transport sites of the Cu+ -ATPases. J Biol Chem. 283(44):29753-29759 (2008).
González-Guerrero M, Argüello JM. Cu+ -ATPases brake system. Structure. 16(6):833-834 (2008).
González-Guerrero M, Argüello JM. Mechanism of Cu+-transporting ATPases: soluble Cu+ chaperones directly transfer Cu+ to transmembrane transport sites. Proc Natl Acad Sci U S A. 105(16):5992-5997 (2008).
Cattoni DI, González Flecha FL, Argüello JM. Thermal stability of CopA, a polytopic membrane protein from the hyperthermophile Archaeoglobus fulgidus. Arch Biochem Biophys. 471(2):198-206 (2008).
Sazinsky MH, LeMoine B, Orofino M, Davydov R, Bencze KZ, Stemmler TL, Hoffman BM, Argüello JM, Rosenzweig AC. Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus. J Biol Chem. 282(35):25950-25959 (2007).
Eren E, González-Guerrero M, Kaufman BM, Argüello JM. Novel Zn2+ coordination by the regulatory N-terminus metal binding domain of Arabidopsis thaliana Zn(2+)-ATPase HMA2. Biochemistry. 46(26):7754-64 (2007).
Argüello JM, Eren E, González-Guerrero M. The structure and function of heavy metal transport P1B-ATPases. Biometals. 20(3-4):233-248 (2007).
Yang Y, Mandal AK, Bredeston LM, González-Flecha FL, Argüello JM. Activation of Archaeoglobus fulgidus Cu(+)-ATPase CopA by cysteine. Biochim Biophys Acta. 1768(3):495-501 (2007).
Eren E, Kennedy DC, Maroney MJ, Argüello JM. A novel regulatory metal binding domain is present in the C terminus of Arabidopsis Zn2+-ATPase HMA2. J Biol Chem. 281(45):33881-33891 (2006).
Sazinsky MH, Agarwal S, Argüello JM, Rosenzweig AC. Structure of the actuator domain from the Archaeoglobus fulgidus Cu(+)-ATPase. Biochemistry. 45(33):9949-9955 (2006).
Sazinsky MH, Mandal AK, Argüello JM, Rosenzweig AC. Structure of the ATP binding domain from the Archaeoglobus fulgidus Cu+-ATPase. J Biol Chem. 281(16):11161-11166 (2006).
Mandal AK, Yang Y, Kertesz TM, Argüello JM. Identification of the transmembrane metal binding site in Cu+-transporting PIB-type ATPases. J Biol Chem. 279(52):54802-54807 (2004).
Eren E, Argüello JM. Arabidopsis HMA2, a divalent heavy metal-transporting P(IB)-type ATPase, is involved in cytoplasmic Zn2+ homeostasis. Plant Physiol. 136(3):3712-3723 (2004).
Argüello JM. Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases. J Membr Biol. 195(2):93-108 (2003).
Mandal AK, Argüello JM. Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu(+)-ATPase CopA. Biochemistry. 42(37):11040-11047 (2003).
Mana-Capelli S, Mandal AK, Argüello JM. Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase: functional role of its histidine-rich-N-terminal metal binding domain. J Biol Chem. 278(42):40534-40541 (2003)
Mandal AK, Mikhailova L, Argüello JM. The Na,K-ATPase S5-H5 helix: structural link between phosphorylation and cation-binding sites. Ann N Y Acad Sci. 986:224-225 (2003)
Argüello JM, Mandal AK, Mana-Capelli S. Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus. Ann N Y Acad Sci. 986:212-218 (2003)
Argüello JM, Mandal AK, Mana-Capelli S. Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus. Ann N Y Acad Sci. 986:212-218 (2003)
Mikhailova L, Mandal AK, Argüello JM. Catalytic phosphorylation of Na,K-ATPase drives the outward movement of its cation-binding H5-H6 hairpin. Biochemistry. 41(25):8195-202 (2002)
Mandal AK, Cheung WD, Argüello JM. Characterization of a thermophilic P-type Ag+/Cu+-ATPase from the extremophile Archaeoglobus fulgidus. J Biol Chem. 277(9):7201-7208 (2002)
Zichittella AE, Shi HG, Argüello JM. Reactivity of cysteines in the transmembrane region of the Na, K-ATPase alpha subunit probed with Hg(2+). J Membr Biol. 177(3):187-197 (2000)
Peluffo RD, Argüello JM, Lingrel JB, Berlin JR. Electrogenic sodium-sodium exchange carried out by Na,K-ATPase containing the amino acid substitution Glu779Ala. J Gen Physiol. 116(1):61-73 (2000)
Peluffo RD, Argüello JM, Berlin JR. The role of Na,K-ATPase alpha subunit serine 775 and glutamate 779 in determining the extracellular K+ and membrane potential-dependent properties of the Na,K-pump. J Gen Physiol. 116(1):47-59.(2000)
Shi HG, Mikhaylova L, Zichittella AE, Argüello JM. Functional role of cysteine residues in the (Na,K)-ATPase alpha subunit. Biochim Biophys Acta. 1464(2):177-187 (2000).
Argüello JM, Whitis J, Lingrel JB. Alanine scanning mutagenesis of oxygen-containing amino acids in the transmembrane region of the Na,K-ATPase. Arch Biochem Biophys. 367(2):341-347 (1999).
Argüello JM, Whitis J, Cheung MC, Lingrel JB. Functional role of oxygen-containing residues in the fifth transmembrane segment of the Na,K-ATPase alpha subunit. Arch Biochem Biophys. 364(2):254-263. (1999).
Blostein R, Daly SE, Boxenbaum N, Lane LK, Arguello JM, Lingrel JB, Karlish SJ, Caplan MJ, Dunbar L. Conformational alterations resulting from mutations in cytoplasmic domains of the alpha subunit of the Na,K-ATPase. Acta Physiol Scand Suppl. 643:275-81 (1998).
Lingrel JB, Croyle ML, Woo AL, Argüello JM. Ligand binding sites of Na,K-ATPase. Acta Physiol Scand Suppl. 643:69-77 (1998).
Peluffo RD, Lingrel JB, Argüello JM, Berlin JR. Changes to Na,K-ATPase alpha-subunit E779 separate the structural basis for VM and ion dependence of Na,K-pump current. Ann N Y Acad Sci. 834:339-342 (1997).
Lingrel JB, Argüello JM, Van Huysse J, Kuntzweiler TA. Cation and cardiac glycoside binding sites of the Na,K-ATPase. Ann N Y Acad Sci. 1997 Nov 3;834:194-206 (1997).
Blostein R, Wilczynska A, Karlish SJ, Argüello JM, Lingrel JB. Evidence that Ser775 in the alpha subunit of the Na,K-ATPase is a residue in the cation binding pocket. J Biol Chem. 1997 272(40):24987-24993 (1997).
Kuntzweiler TA, Argüello JM, Lingrel JB. Asp804 and Asp808 in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues. J Biol Chem. 271(47):29682-29687 (1996).
Argüello JM, Peluffo RD, Feng J, Lingrel JB, Berlin JR. Substitution of glutamic 779 with alanine in the Na,K-ATPase alpha subunit removes voltage dependence of ion transport. J Biol Chem. 271(40):24610-24616 (1996).
Palasis M, Kuntzweiler TA, Argüello JM, Lingrel JB. Ouabain interactions with the H5-H6 hairpin of the Na,K-ATPase reveal a possible inhibition mechanism via the cation binding domain. J Biol Chem. 271(24):14176-14182 (1996).
Argüello JM, Lingrel JB. Substitutions of serine 775 in the alpha subunit of the Na,K-ATPase selectively disrupt K+ high affinity activation without affecting Na+ interaction. J Biol Chem. 270(39):22764-22771 (1995).
Shin JM, Kajimura M, Argüello JM, Kaplan JH, Sachs G. Biochemical identification of transmembrane segments of the Ca(2+)-ATPase of sarcoplasmic reticulum. J Biol Chem. 269(36):22533-22537 (1994).
Argüello JM, Kaplan JH. Glutamate 779, an intramembrane carboxyl, is essential for monovalent cation binding by the Na,K-ATPase. J Biol Chem. 269(9):6892-6899 (1994).
Arguello JM, Kaplan JH. Evidence for essential carboxyls in the cation-binding domain of the Na,K-ATPase. J Biol Chem. 266(22):14627-14635 (1991).
Arguello JM, Kaplan JH. N-acetylimidazole inactivates renal Na,K-ATPase by disrupting ATP binding to the catalytic site. Biochemistry. 29(24):5775-82 (1990).