Marcelo R Pinto | Universidade de Uberaba (original) (raw)

Papers by Marcelo R Pinto

Data are the mean ± SEM (N = 3) obtained using duplicate aliquots con... more Data are the mean ± SEM (N = 3) obtained using duplicate aliquots containing 9.5 μg protein (juveniles) and 10.7 μg protein (adults) from three different gill homogenates. Activity was assayed at 25°C in 50 mmol L−1 triethanolamine buffer (pH 7.5), containing 2 mmol L−1 ATP, 5 mmol L−1 MgCl2, 1.0 mmol L−1 NAD+, 0.5 mmol L−1 sodium phosphate, 1.0 mmol L−1 G3P, 150 μg GAPDH (12 U), 20 μg PGK (9 U) and NaCl (50 mmol L−1 for juveniles and 20 mmol L−1 for adults), in a final volume of 1 mL. A- Juveniles. Inset: Variation in K0.5 with K+ concentration. B- Adults. Variation in VM (inset a) and K0.5 (inset b) with K+ concentration. K+ concentration (•) none, (○) 0.4 mmol L−1, (□) 0.5 mmol L−1, (▪) 2 mmol L−1, (▵) 5 mmol L−1, (▴) 10 mmol L−1, (▹) 20 mmol L−1.</p

Biochimica et Biophysica Acta (BBA) - Biomembranes

$Research paper thumbnail of Sucrose density gradient centrifugation of a microsomal fraction from gill tissue of juvenile and adult M. amazonicum$

Aliquots containing 4.5% (w/w) continuous sucrose density gradients. Fractions (0.5 mL) ... more Aliquots containing 4.5% (w/w) continuous sucrose density gradients. Fractions (0.5 mL) collected from the bottom of each gradient were analyzed for total ATPase activity (○), (Na+, K+)-ATPase activity (•), ouabain-insensitive ATPase activity (▵), protein concentration (▴) and sucrose concentration (□). Inset: Adult gill tissue.</p

Assays were performed continuously at 25°C in 50 mmol L−1 HEPES b... more Assays were performed continuously at 25°C in 50 mmol L−1 HEPES buffer, pH 7.5, containing 2 mmol L−1 ATP, 5 mmol L−1 MgCl2, 20 mmol L−1 KCl and 50 mmol L−1 NaCl for juveniles or 20 mmol L−1 NaCl for adults, in a final volume of 1.0 mL. Data are the mean ± SD from three (N = 3) different microsomal preparations. Oligomycin was prepared in ethanol. Bafilomycin and thapsigargin were prepared in dimethylsulfoxide.*Significantly different from respective value for juvenile (P≤0.05).</p

The Journal of Membrane Biology, 2020

We provide a kinetic characterization of (Na+, K+)-ATPase activity in a posterior gill microsomal... more We provide a kinetic characterization of (Na+, K+)-ATPase activity in a posterior gill microsomal fraction from the grapsid crab Goniopsis cruentata. (Na+, K+)-ATPase activity constitutes 95% of total ATPase activity, and sucrose density centrifugation reveals an ATPase activity peak between 25 and 35% sucrose, distributed into two, partially separated protein fractions. The (Na+, K+)-ATPase α-subunit is localized throughout the ionocyte cytoplasm and has an Mr of ≈ 10 kDa and hydrolyzes ATP obeying cooperative kinetics. Low (VM = 186.0 ± 9.3 nmol Pi min−1 mg−1 protein and K0.5 = 0.085 ± 0.004 mmol L−1) and high (VM = 153.4 ± 7.7 nmol Pi min−1 mg−1 protein and K0.5 = 0.013 ± 0.0006 mmol L−1) affinity ATP binding sites were characterized. At low ATP concentrations, excess Mg2+ stimulates the enzyme, triggering exposure of a high-affinity binding site that accounts for 50% of (Na+, K+)-ATPase activity. Stimulation by Mg2+ (VM = 425.9 ± 25.5 nmol Pi min−1 mg−1 protein, K0.5 = 0.16 ± 0.01 mmol L−1), K+ (VM = 485.3 ± 24.3 nmol Pi min−1 mg−1 protein, K0.5 = 0.9 ± 0.05 mmol L−1), Na+ (VM = 425.0 ± 23.4 nmol Pi min−1 mg−1 protein, K0.5 = 5.1 ± 0.3 mmol L−1) and NH4+ (VM = 497.9 ± 24.9 nmol Pi min−1 mg−1 protein, K0.5 = 9.7 ± 0.5 mmol L−1) obeys cooperative kinetics. Ouabain inhibits up to 95% of ATPase activity with KI = 196.6 ± 9.8 µmol L−1. This first kinetic characterization of the gill (Na+, K+)-ATPase in Goniopsis cruentata enables better comprehension of the biochemical underpinnings of osmoregulatory ability in this semi-terrestrial mangrove crab.

Revista Eletrônica de Farmácia, Dec 27, 2012

+)-ATPase was 60.66±1.6 mM, 38.22±3.6 mmol mM, 47.57±1.43 mM, 120.35±6.02 mM for zoeae I, decapod... more +)-ATPase was 60.66±1.6 mM, 38.22±3.6 mmol mM, 47.57±1.43 mM, 120.35±6.02 mM for zoeae I, decapodid III, juveniles and adults, respectively. Conclusion: Octopamine alters (Na + ,K +)-ATPase activity of the microsomal fraction of different ontogenetic stages of selected M. amazonicum and the different responses disclosed suggest that it may play an important role in the invasion of freshwater by this species.

Revista Eletrônica de Farmácia, Dec 27, 2012

Introduction: Macrobrachium rosenbergii is the species of freshwater shrimp more used in the comm... more Introduction: Macrobrachium rosenbergii is the species of freshwater shrimp more used in the commercial aquaculture. This freshwater prawn, also known as the giant Malaysian prawn, is native to the tropical Indo-Pacific region and has been introduced in several countries due to its economic interest. M. rosenbergii belongs to the family Palaemonidae which include the brackish and freshwater shrimps, where most species which comprise this family require brackish water to complete the early stages of their life cycle. The newly hatched larvae must reach brackish water with salinities of 10 to 14 parts per thousand (ppt) within two days or they will not survive. At this stage, they feed on zooplankton, worms and the larvae of other aquatic organisms and to reach the post-larval stage, the larvae undergo about 11 molts in approximately 35 days. During larval development many changes occur both in structure and physiology of the shrimp. The ability to survive in different salinities, until its complete establishment in freshwater, is dependent on enzymes that control and regulate the metabolism of the animal. Various enzymes are responsible for active ion transport in crustacean although their importance in osmoregulatory mechanisms differs among species. The (Na + ,K +)-ATPase and the V(H +)-ATPase are the two most important enzymes. Objective: Here, we examine the kinetic properties of the (Na + ,K +)-ATPase in whole larvae zoeae I from M. rosenbergii using ATP as a substrate. Methods: The whole individuals were rapidly homogenized in homogenization buffer (20 mL/g wet tissue). After centrifuging the crude extract at 20,000 × g for 35 min, at 4 °C, the supernatant was placed on crushed ice, and the pellet was re-suspended in an equal volume of homogenization buffer. After further centrifugation as above, the two supernatants were pooled and centrifuged at 100,000 × g for 3 h, at 4 °C. The resulting pellet was re-suspended in the homogenization buffer (10 mL/g wet tissue). Results: Our results showed that the (Na + ,K +)-ATPase hydrolyzes ATP at a rate of 207 U/mg and K 0.5 =0.05 mM, obeying cooperative kinetics. Similarly, stimulation by potassium (V 226 U/mg; K 0.5 =5.03 mM), magnesium (V 202 U/mg; K 0.5 =0.40 mM,), sodium (V 235; K 0.5 =5.39 mM) and ammonium ions (V 310; K 0.5 =3.10 mM) also was cooperative. In the presence of ammonium or potassium, ouabain inhibited activity at 73% (K i =50 μM) and 67% (K i =150 μM), respectively. Conclusion: The (Na + ,K +)-ATPase activity from larvae zoeae I was twice higher when compared with gills homogeneized from adult M. rosenbergii shrimp. This study reveals important findings concerning kinetic characterization of the (Na + ,K +)-ATPase in the shrimp M. rosenbergii.

Trends in Comparative Biochemistry & Physiology

The kinetic properties of a microsomal gill (Na+, K+)-ATPase from juvenile and adult Amazon River... more The kinetic properties of a microsomal gill (Na+, K+)-ATPase from juvenile and adult Amazon River shrimp Macrobrachium amazonicum were characterized using the synthetic substrate p-nitrophenylphosphate. The substrate was hydrolyzed revealing cooperative kinetics at maximum rates of 71.3 ± 1.1 U mg-1 and 82.7 ± 2.3 U mg-1 with K 0.5 = 1.45 ± 0.02 mmol L-1 and 1.52 ± 0.04 mmol L-1 for juveniles and adults, respectively. Stimulation of K+ -phosphatase activity by Mg2+ and K+ also exhibited cooperative kinetics independently of ontogenetic stage. While the K0.5 values estimated for Mg2+ and K+ stimulation of K+ -phosphatase activity were very similar, maximum rates for adult shrimps were ≈1.8-fold greater than that for juveniles. NH4+ stimulation resulted in a ≈10-fold increase in K0.5 for both stages compared to Mg2+ and K+ . Further, when stimulated by NH4+ plus K+ , p-nitrophenylphosphate hydrolysis was mostly unchanged, suggesting that NH4+ and K+ bind to the same site. While K0.5 v...

In the transport ATPases like (Na+,K+)-ATPase, ATP is hydrolyzed via formation and hydrolysis of ... more In the transport ATPases like (Na+,K+)-ATPase, ATP is hydrolyzed via formation and hydrolysis of phosphorylated intermediates, where phosphate is bound to an aspartyl residue at the enzyme's substrate site. The resulting phosphorylated enzyme intermediates (EP) play a crucial role in the common reaction scheme for (Na+,K+)-ATPase where their formation, catalysed by Mg2+ and Na+, and breakdown, catalysed by K+, are important steps in the energy transduction and cation transport. The biologically active polyamines putrescine and spermidine are ubiquitous, small, positively charged molecules that are essential for normal cellular function and proliferation. Polyamines inhibit the (Na+,K+)-ATPase supposedly by binding to clusters of acidic residues at the enzyme. The goal of this work was to examine the effect of exogenously added polyamines on the activity and phosphorylation levels of the (Na+,K+)-ATPase from M. amazonicum gills in vitro. Total ATPase activity was notably inhibite...

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 2015

We evaluate (Na(+), K(+))-ATPase activity, and protein and gene expression of the α-subunit in po... more We evaluate (Na(+), K(+))-ATPase activity, and protein and gene expression of the α-subunit in posterior gills 6 and 7 of Callinectes ornatus, a euryhaline crab, during a 10-day acclimation period from seawater (33‰ S) to low salinity (21‰ S). (Na(+), K(+))-ATPase activity decreased within 1h after transfer to 21‰ S, values recovering by 24h and attaining a maximum of ≈180nmolPimin(-1)mg(-1) after 10days (≈2.5-fold increase). (Na(+), K(+))-ATPase activity is ≈1.5-fold greater in gill 6 than in gill 7, independently of salinity. Relative expression of (Na(+), K(+))-ATPase α-subunit mRNA increased in both gills within 1- to 2-h exposure to low salinity, reaching an ≈8-fold maximum after 24-h exposure, decreasing slightly by 10 days acclimation to low salinity. This increase in α-subunit mRNA expression may underpin the increased (Na(+), K(+))-ATPase activity seen after 10 days acclimation to low salinity. Enzyme affinity for ATP was greater in gill 6 than in gill 7, in contrast to oua...

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2015

Novel kinetic properties of a microsomal gill V(H +)-ATPase from juvenile and adult Amazon River ... more Novel kinetic properties of a microsomal gill V(H +)-ATPase from juvenile and adult Amazon River shrimp, Macrobrachium amazonicum, are described. While protein expression patterns are markedly different, Western blot analysis reveals a sole immunoreactive band, suggesting a single V(H +)-ATPase subunit isoform, distributed in membrane fractions of similar density in both ontogenetic stages. Immunofluorescence labeling locates the V(H +)-ATPase in the apical regions of the lamellar pillar cells in both stages in which mRNA expression of the V(H +)-ATPase B-subunit is identical. Juvenile (36.6 ± 3.3 nmol Pi min −1 mg −1) and adult (41.6 ± 1.3 nmol P i min −1 mg −1) V(H +)-ATPase activities are similar, the apparent affinity for ATP of the adult enzyme (K 0.5 = 0.21 ± 0.02 mmol L −1) being 3-fold greater than for juveniles (K 0.5 = 0.61 ± 0.01 mmol L −1). The K 0.5 for Mg 2+ interaction with the juvenile V(H +)-ATPase (1.40 ± 0.07 mmol L −1) is ≈6-fold greater than for adults (0.26 ± 0.02 mmol L −1) while the bafilomycin A1 inhibition constant (K I) is 45.0 ± 2.3 nmol L −1 and 24.2 ± 1.2 nmol L −1 , for juveniles and adults, respectively. Both stages exhibited residual bafilomycin-insensitive ATPase activity of ≈25 nmol P i min −1 mg −1 , suggesting the presence of ATPases other than the V(H +)-ATPase. These differences may reflect a long-term regulatory mechanism of V(H +)-ATPase activity, and suggest stage-specific enzyme modulation. This is the first kinetic analysis of V(H +)-ATPase activity in different ontogenetic stages of a freshwater shrimp and allows better comprehension of the biochemical adaptations underpinning the establishment of palaemonid shrimps in fresh water.

The Journal of Membrane Biology, 2014

We characterize the kinetic properties of a gill (Na(+), K(+))-ATPase from the pelagic marine sea... more We characterize the kinetic properties of a gill (Na(+), K(+))-ATPase from the pelagic marine seabob Xiphopenaeus kroyeri. Sucrose density gradient centrifugation revealed membrane fractions distributed mainly into a heavy fraction showing considerable (Na(+), K(+))-ATPase activity, but also containing mitochondrial F0F1- and Na(+)- and V-ATPases. Western blot analysis identified a single immunoreactive band against the (Na(+), K(+))-ATPase α-subunit with an Mr of ≈110 kDa. The α-subunit was immunolocalized to the intralamellar septum of the gill lamellae. The (Na(+), K(+))-ATPase hydrolyzed ATP obeying Michaelis-Menten kinetics with VM = 109.5 ± 3.2 nmol Pi min(-1 )mg(-1) and KM = 0.03 ± 0.003 mmol L(-1). Mg(2+) (VM = 109.8 ± 2.1 nmol Pi min(-1 )mg(-1), K0.5 = 0.60 ± 0.03 mmol L(-1)), Na(+) (VM = 117.6 ± 3.5 nmol Pi min(-1 )mg(-1), K0.5 = 5.36 ± 0.14 mmol L(-1)), K(+) (VM = 112.9 ± 1.4 nmol Pi min(-1 )mg(-1), K0.5 = 1.32 ± 0.08 mmol L(-1)), and NH4 (+) (VM = 200.8 ± 7.1 nmol Pi min(-1 )mg(-1), K0.5 = 2.70 ± 0.04 mmol L(-1)) stimulated (Na(+), K(+))-ATPase activity following site-site interactions. K(+) plus NH4 (+) does not synergistically stimulate (Na(+), K(+))-ATPase activity, although each ion modulates affinity of the other. The enzyme exhibits a single site for K(+) binding that can be occupied by NH4 (+), stimulating the enzyme. Ouabain (KI = 84.0 ± 2.1 µmol L(-1)) and orthovanadate (KI = 0.157 ± 0.001 µmol L(-1)) inhibited total ATPase activity by ≈50 and ≈44 %, respectively. Ouabain inhibition increases ≈80 % in the presence of NH4 (+) with a threefold lower KI, suggesting that NH4 (+) is likely transported as a K(+) congener.

PLoS ONE, 2014

We investigate the synergistic stimulation by K + plus NH 4 + of (Na + , K +)-ATPase activity in ... more We investigate the synergistic stimulation by K + plus NH 4 + of (Na + , K +)-ATPase activity in microsomal preparations of whole zoea I and decapodid III, and in juvenile and adult river shrimp gills. Modulation of (Na + , K +)-ATPase activity is ontogenetic stage-specific, and particularly distinct between juveniles and adults. Although both gill enzymes exhibit two different sites for K + and NH 4 + binding, in the juvenile enzyme, these two sites are equivalent: binding by both ions results in slightly stimulated activity compared to that of a single ionic species. In the adult enzyme, the sites are not equivalent: when one ion occupies its specific binding site, (Na + , K +)-ATPase activity is stimulated synergistically by <50% on binding of the complementary ion. Immunolocalization reveals the enzyme to be distributed predominantly throughout the intralamellar septum in the gill lamellae of juveniles and adults. Western blot analyses demonstrate a single immunoreactive band, suggesting a single (Na + , K +)-ATPase a-subunit isoform that is distributed into different density membrane fractions, independently of ontogenetic stage. We propose a model for the modulation by K + and NH 4 + of gill (Na + , K +)-ATPase activity. These findings suggest that the gill enzyme may be regulated by NH 4 + during ontogenetic development in M. amazonicum.

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2012

We examine hemolymph ion regulation and the kinetic properties of a gill microsomal (Na(+), K(+))... more We examine hemolymph ion regulation and the kinetic properties of a gill microsomal (Na(+), K(+))-ATPase from the intertidal hermit crab, Clibanarius vittatus, acclimated to 45‰ salinity for 10 days. Hemolymph osmolality is hypo-regulated (1102.5 ± 22.1 mOsm kg(-1) H(2)O) at 45‰ but elevated compared to fresh-caught crabs (801.0 ± 40.1 mOsm kg(-1) H(2)O). Hemolymph [Na(+)] (323.0 ± 2.5 mmol L(-1)) and [Mg(2+)] (34.6 ± 1.0 mmol L(-1)) are hypo-regulated while [Ca(2+)] (22.5 ± 0.7 mmol L(-1)) is hyper-regulated; [K(+)] is hyper-regulated in fresh-caught crabs (17.4 ± 0.5 mmol L(-1)) but hypo-regulated (6.2 ± 0.7 mmol L(-1)) at 45‰. Protein expression patterns are altered in the 45‰-acclimated crabs, although Western blot analyses reveal just a single immunoreactive band, suggesting a single (Na(+), K(+))-ATPase α-subunit isoform, distributed in different density membrane fractions. A high-affinity (Vm=46.5 ± 3.5 Umg(-1); K(0.5)=7.07 ± 0.01 μmol L(-1)) and a low-affinity ATP binding site (Vm=108.1 ± 2.5 U mg(-1); K(0.5)=0.11 ± 0.3 mmol L(-1)), both obeying cooperative kinetics, were disclosed. Modulation of (Na(+), K(+))-ATPase activity by Mg(2+), K(+) and NH(4)(+) also exhibits site-site interactions, but modulation by Na(+) shows Michaelis-Menten kinetics. (Na(+), K(+))-ATPase activity is synergistically stimulated up to 45% by NH(4)(+) plus K(+). Enzyme catalytic efficiency for variable [K(+)] and fixed [NH(4)(+)] is 10-fold greater than for variable [NH(4)(+)] and fixed [K(+)]. Ouabain inhibited ≈80% of total ATPase activity (K(I)=464.7 ± 23.2 μmol L(-1)), suggesting that ATPases other than (Na(+), K(+))-ATPase are present. While (Na(+), K(+))-ATPase activities are similar in fresh-caught (around 142 nmol Pi min(-1)mg(-1)) and 45‰-acclimated crabs (around 154 nmol Pi min(-1)mg(-1)), ATP affinity decreases 110-fold and Na(+) and K(+) affinities increase 2-3-fold in 45‰-acclimated crabs.

Archives of Biochemistry and Biophysics, 2013

We provide an extensive characterization of the modulation by p-nitrophenylphosphate, Mg 2+ , Na ... more We provide an extensive characterization of the modulation by p-nitrophenylphosphate, Mg 2+ , Na + , K + , Rb + , NH þ 4 and pH of gill microsomal K +-phosphatase activity in the posterior gills of Callinectes ornatus acclimated to low salinity (21‰). The synergistic stimulation by K + and NH þ 4 of the K +-phosphatase activity is a novel finding, and may constitute a species-specific feature of K + /NH þ 4 interplay that regulates crustacean gill (Na + , K +)-ATPase activity. p-Nitrophenylphosphate was hydrolyzed at a maximum rate (V) of 69.2 ± 2.8 nmol Pi min À1 mg À1 with K 0.5 = 2.3 ± 0.1 mmol L À1 , obeying cooperative kinetics (n H = 1.7). Stimulation by Mg 2+ (V = 70.1 ± 3.0 nmol Pi min À1 mg À1 , K 0.5 = 0.88 ± 0.04 mmol L À1), K + (V = 69.6 ± 2.7 nmol Pi min À1 mg À1 , K 0.5 = 1.60 ± 0.07 mmol L À1) and NH þ 4 (V = 90.8 ± 4.0 nmol Pi min À1mg À1 , K 0.5 = 9.2 ± 0.3 mmol L À1) all displayed site-site interaction kinetics. In the presence of NH þ 4 , enzyme affinity for K + unexpectedly increased by 7-fold, while affinity for NH þ 4 was 28-fold greater in the presence than absence of K +. Ouabain partially inhibited K +-phosphatase activity (K I = 320 ± 14.0lmol L À1), more effectively when NH þ 4 was present (K I = 240 ± 12.0 lmol L À1). We propose a model for the synergistic stimulation by K + and NH þ 4 of the K +-phosphatase activity of the (Na + , K +)-ATPase from C. ornatus posterior gill tissue.

Acid-Base Balance and Nitrogen Excretion in Invertebrates, 2016

Crustaceans inhabit diverse biotopes, often subject to alterations that constitute a severe chall... more Crustaceans inhabit diverse biotopes, often subject to alterations that constitute a severe challenge to their homeostatic mechanisms. These challenges have driven the evolution of biochemical and physiological processes that have enabled their survival in such niches. Ion-transporting enzymes like the (Na+, K+)-ATPase and V(H+)-ATPase present in the gill epithelia underpin the ion regulatory abilities of these highly diversified organisms. The present chapter examines the structure and function of these two gill ATPases that also participate actively in ammonia excretion. We summarize current knowledge on their role in osmotic and ionic regulation and associated with ontogenetic changes. We analyze the effects of polyamines on (Na+, K+)-ATPase activity and phosphoenzyme formation, aiming to provide insights into the biochemical bases of physiological homeostasis in crustaceans. We examine future perspectives that should provide a better understanding of the role of gill ATPases in active ammonia excretion.

Journal of Magnetism and Magnetic Materials, 2015

Revista Brasileira de Cardiologia Invasiva, 2013

Clopidogrel and aspirin are the most commonly used medications worldwide for dual antiplatelet th... more Clopidogrel and aspirin are the most commonly used medications worldwide for dual antiplatelet therapy after percutaneous coronary intervention. However, clopidogrel hyporesponsiveness related to gene polymorphisms is a concern. Populations with higher degrees of genetic admixture may have increased prevalence of clopidogrel hyporesponsiveness. To assess this, we genotyped CYP2C19, ABCB1, and PON1 in 187 patients who underwent percutaneous coronary intervention. Race was self-defined by patients. We also performed light transmission aggregometry with adenosine diphosphate (ADP) and arachidonic acid during dual antiplatelet therapy. We found a significant difference for presence of the CYP2C19*2 polymorphism between white and non-white patients. Although 7% of patients had platelet resistance to clopidogrel, this did not correlate with any of the tested genetic polymorphisms. We did not find platelet resistance to aspirin in this cohort. Multivariate analysis showed that patients with PON1 and CYP2C19 polymorphisms had higher light transmission after ADP aggregometry than patients with native alleles. There was no preponderance of any race in patients with higher light transmission aggregometry. In brief, PON1 and CYP2C19 polymorphisms were associated with lower clopidogrel responsiveness in this sample. Despite differences in CYP2C19 polymorphisms across white and non-white patients, genetic admixture by itself was not able to identify clopidogrel hyporesponsiveness.

Biochimica et Biophysica Acta (BBA) - Biomembranes

$Research paper thumbnail of Sucrose density gradient centrifugation of a microsomal fraction from gill tissue of juvenile and adult M. amazonicum$

The Journal of Membrane Biology, 2020

Revista Eletrônica de Farmácia, Dec 27, 2012

Trends in Comparative Biochemistry & Physiology

Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 2015

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2015

The Journal of Membrane Biology, 2014

PLoS ONE, 2014

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2012

Archives of Biochemistry and Biophysics, 2013

Acid-Base Balance and Nitrogen Excretion in Invertebrates, 2016

Journal of Magnetism and Magnetic Materials, 2015

Revista Brasileira de Cardiologia Invasiva, 2013