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C. Cristina Osuna-Martínez

Researcher at Autonomous University of Sinaloa

Publications -  22
Citations -  320

C. Cristina Osuna-Martínez is an academic researcher from Autonomous University of Sinaloa. The author has contributed to research in topics: Chemistry & Shrimp. The author has an hindex of 6, co-authored 18 publications receiving 176 citations. Previous affiliations of C. Cristina Osuna-Martínez include National Autonomous University of Mexico.

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Arsenic in waters, soils, sediments, and biota from Mexico: An environmental review

TL;DR: In contaminated arid and semi-arid areas, the plants P. laevigata and A. farnesiana exhibit the highest As levels, and the human and environmental risks associated with the presence of As in such regions are emphasized.
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Bioavailability of Cadmium, Copper, Mercury, Lead, and Zinc in Subtropical Coastal Lagoons from the Southeast Gulf of California Using Mangrove Oysters (Crassostrea corteziensis and Crassostrea palmula)

TL;DR: Metal concentrations in edible tissues of Crassrotrea corteziensis oysters collected during the rainy and dry seasons and correlation analyses showed a high and significant (P < 0.05) correlation between metal concentrations in both species are needed to compare results from distinct regions.
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Mercury in cultured oysters (Crassostrea gigas Thunberg, 1793 and C. corteziensis Hertlein, 1951) from four coastal lagoons of the SE Gulf of California, Mexico.

TL;DR: Elevated mercury contents in cultured oysters from coastal lagoons (SE Gulf of California) are apparently related to terrigen transport from the watershed, while during the dry season, the moderate levels are related to upwellings.
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Metals and oxidative stress in aquatic decapod crustaceans: A review with special reference to shrimp and crabs.

TL;DR: In this paper, the relationship between metals and oxidative stress in aquatic crustaceans (mainly shrimp and crabs) was synthetized to analyze antioxidant responses when organisms are exposed to metals because the direct metal binding to the active site of enzymes inactivates most of the antioxidant systems.