Arabidopsis HMA2, a Divalent Heavy Metal-Transporting P(IB)-Type ATPase, Is Involved in Cytoplasmic Zn(2+) Homeostasis

Por Eren, Elif, Argüello, José M.
Publicado em 2004

Mechanism of Cu(+)-transporting ATPases: Soluble Cu(+) chaperones directly transfer Cu(+) to transmembrane transport sites

Por González-Guerrero, Manuel, Argüello, José M.
Publicado em 2008

Toward a Molecular Understanding of Metal Transport by P(1B)-Type ATPases

Por Rosenzweig, Amy C., Argüello, José M.
Publicado em 2012

Chaperone-mediated Cu(+) Delivery to Cu(+) Transport ATPases: REQUIREMENT OF NUCLEOTIDE BINDING

Por González-Guerrero, Manuel, Hong, Deli, Argüello, José M.
Publicado em 2009

Bacterial Transition Metal P(1B)-ATPases, Transport Mechanism and Roles in Virulence

Por Argüello, José M., González-Guerrero, Manuel, Raimunda, Daniel
Publicado em 2011

Metal Transport across Biomembranes: Emerging Models for a Distinct Chemistry

Por Argüello, José M., Raimunda, Daniel, González-Guerrero, Manuel
Publicado em 2012

Evolution and diversity of periplasmic proteins involved in copper homeostasis in gamma proteobacteria

Por Hernández-Montes, Georgina, Argüello, José M, Valderrama, Brenda
Publicado em 2012

Mechanisms of copper homeostasis in bacteria

Por Argüello, José M., Raimunda, Daniel, Padilla-Benavides, Teresita
Publicado em 2013

Bacterial Cu(+)-ATPases: Models for molecular structure-function studies

Por Argüello, José M., Patel, Sarju J., Quintana, Julia
Publicado no Metallomics (2016)

Copper homeostasis networks in the bacterium Pseudomonas aeruginosa

Por Quintana, Julia, Novoa-Aponte, Lorena, Argüello, José M.
Publicado no J Biol Chem (2017)

The Role of Na,k-Atpase α Subunit Serine 775 and Glutamate 779 in Determining the Extracellular K(+)And Membrane Potential–Dependent Properties of the Na,k -Pump

Por Peluffo, R. Daniel, Argüello, José M., Berlin, Joshua R.
Publicado em 2000

A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn(2+)-ATPases

Por Raimunda, Daniel, Subramanian, Poorna, Stemmler, Timothy, Argüello, José M.
Publicado em 2012

The Mechanism of Cu(+) Transport ATPases: INTERACTION WITH CU(+) CHAPERONES AND THE ROLE OF TRANSIENT METAL-BINDING SITES

Por Padilla-Benavides, Teresita, McCann, Courtney J., Argüello, José M.
Publicado em 2013

The transport mechanism of bacterial Cu(+)-ATPases: distinct efflux rates adapted to different function

Por Raimunda, Daniel, González-Guerrero, Manuel, Leeber, Blaise W., Argüello, José M.
Publicado em 2011

Role in metal homeostasis of CtpD, a Co(2+) transporting P(1B4)-ATPase of Mycobacterium smegmatis

Por Raimunda, Daniel, Long, Jarukit E., Sassetti, Christopher M., Argüello, José M.
Publicado em 2012

The Listeria monocytogenes Fur-regulated virulence protein FrvA is an Fe(II) efflux P(1B4)-type ATPase

Por Pi, Hualiang, Patel, Sarju J., Argüello, José M., Helmann, John D.
Publicado no Mol Microbiol (2016)

Electrogenic Sodium–Sodium Exchange Carried Out by Na,k -Atpase Containing the Amino Acid Substitution Glu779ala

Por Peluffo, R. Daniel, Argüello, José M., B Lingrel, Jerry, Berlin, Joshua R.
Publicado em 2000

Structure of the Two Transmembrane Cu(+) Transport Sites of the Cu(+)-ATPases

Por González-Guerrero, Manuel, Eren, Elif, Rawat, Swati, Stemmler, Timothy L., Argüello, José M.
Publicado em 2008

A Novel Zinc Binding System, ZevAB, Is Critical for Survival of Nontypeable Haemophilus influenzae in a Murine Lung Infection Model

Por Rosadini, Charles V., Gawronski, Jeffrey D., Raimunda, Daniel, Argüello, José M., Akerley, Brian J.
Publicado em 2011

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

Por Jayakanthan, Samuel, Roberts, Sue A., Weichsel, Andrzej, Argüello, José M., McEvoy, Megan M.
Publicado em 2012