Rolando Rossi

Research interests

Publications

• A kinetic comparison between E2P and the E2P-like state induced by a beryllium fluoride complex in the Na,K-ATPase. Interactions with Rb+

  Biochimica et Biophysica Acta (BBA) - Biomembranes · 2018 · 10.1016/j.bbamem.2018.10.020

• Aluminum inhibits the plasma membrane and sarcoplasmic reticulum Ca2+-ATPases by different mechanisms

  Biochimica et Biophysica Acta (BBA) - Biomembranes · 2018 · 10.1016/j.bbamem.2018.05.014

• Steady-state analysis of enzymes with non-Michaelis-Menten kinetics: The transport mechanism of Na+/K+-ATPase

  Journal of Biological Chemistry · 2017 · 10.1074/jbc.m117.799536

• Crystallographic and kinetic study of riboflavin synthase fromBrucella abortus, a chemotherapeutic target with an enhanced intrinsic flexibility

  Acta Crystallographica Section D Biological Crystallography · 2014 · 10.1107/s1399004714005161

• Conformational Changes Produced by ATP Binding to the Plasma Membrane Calcium Pump

  Journal of Biological Chemistry · 2013 · 10.1074/jbc.m113.494633

• Differential Effects of G- and F-Actin on the Plasma Membrane Calcium Pump Activity

  Cell Biochemistry and Biophysics · 2012 · 10.1007/s12013-012-9467-6

• Calcium Occlusion in Plasma Membrane Ca2+-ATPase

  Journal of Biological Chemistry · 2011 · 10.1074/jbc.m111.266650

• Rb+ occlusion stabilized by vanadate in gastric H+/K+-ATPase at 25°C

  Biochimica et Biophysica Acta (BBA) - Biomembranes · 2010 · 10.1016/j.bbamem.2010.08.022

• Quaternary Benzyltriethylammonium Ion Binding to the Na,K-ATPase: A Tool to Investigate Extracellular K+Binding Reactions

  Biochemistry · 2009 · 10.1021/bi900687u

• Phosphorylation of the Plasma Membrane Calcium Pump at High ATP Concentration. On the Mechanism of ATP Hydrolysis

  Biochemistry · 2007 · 10.1021/bi061857x

• Plasma membrane calcium pump activity is affected by the membrane protein concentration: Evidence for the involvement of the actin cytoskeleton

  Biochimica et Biophysica Acta (BBA) - Biomembranes · 2007 · 10.1016/j.bbamem.2007.03.012

• Eosin Fluorescence Changes during Rb+ Occlusion in the Na+/K+-ATPase

  Biochemistry · 2006 · 10.1021/bi060778i

• Binding of a Single Rb+ Increases Na+/K+-ATPase, Activating Dephosphorylation without Stoichiometric Occlusion

  Journal of Biological Chemistry · 2006 · 10.1074/jbc.m600953200

• Quantitative Analysis of the Interaction between the Fluorescent Probe Eosin and the Na+/K+-ATPase Studied through Rb+Occlusion

  Biochemistry · 2004 · 10.1021/bi0351763

• The Occlusion of Rb+ in the Na+/K+-ATPase

  Journal of Biological Chemistry · 2002 · 10.1074/jbc.m105886200

• The Occlusion of Rb+ in the Na+/K+-ATPase

  Journal of Biological Chemistry · 2002 · 10.1074/jbc.m105887200

• Quantitation of Plasma Membrane Calcium Pump Phosphorylated Intermediates by Electrophoresis

  Analytical Biochemistry · 2001 · 10.1006/abio.2000.4950

• Are the States That Occlude Rubidium Obligatory Intermediates of the Na+/K+-ATPase Reaction?

  Journal of Biological Chemistry · 1999 · 10.1074/jbc.274.30.20779

• An Attachment for Nondestructive, Fast Quenching of Samples in Rapid-Mixing Experiments

  Analytical Biochemistry · 1999 · 10.1006/abio.1999.4094

• Functional role of ecto-ATPase activity in goldfish hepatocytes

  American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · 1998 · 10.1152/ajpregu.1998.274.4.r1031

• An unexpected effect of ATP on the ratio between activity and phosphoenzyme level of Na+/K+-ATPase in steady state

  Biochimica et Biophysica Acta (BBA) - Biomembranes · 1995 · 10.1016/0005-2736(94)00229-i

• Kinetics of K(+)-stimulated dephosphorylation and simultaneous K+ occlusion by Na,K-ATPase, studied with the K+ congener Tl+. The possibility of differences between the first turnover and steady state

  Journal of Biological Chemistry · 1993 · 10.1016/s0021-9258(18)31428-5

• Steady-state kinetic analysis of the Na+/K+-ATPase. The inhibition by potassium and magnesium

  Biochimica et Biophysica Acta (BBA) - Biomembranes · 1989 · 10.1016/0005-2736(89)90087-4

• Steady-state kinetic analysis of the Na+/K+-ATPase. The effects of adenosine 5′-[ß, γ-methylene]triphosphate on substrate kinetics

  Biochimica et Biophysica Acta (BBA) - Biomembranes · 1989 · 10.1016/0005-2736(89)90085-0

• THE INTERACTION OF K+ Na+, Mg2+, AND ATP WITH THE (Na, K)‐ATPase*

  Annals of the New York Academy of Sciences · 1982 · 10.1111/j.1749-6632.1982.tb25745.x

Current projects

No projects listed.