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Carla D. Fultz

Researcher at Indiana University – Purdue University Columbus

Publications -  9
Citations -  187

Carla D. Fultz is an academic researcher from Indiana University – Purdue University Columbus. The author has contributed to research in topics: Hsp70 & Polyacrylamide gel electrophoresis. The author has an hindex of 8, co-authored 9 publications receiving 187 citations. Previous affiliations of Carla D. Fultz include Indiana University.

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Regional protein alterations in rat kidneys induced by lead exposure

TL;DR: Observations reflect the complexity of lead's nephrotoxicity and endorse the application of proteomics in mechanistic studies as well as biomarker development in a variety of toxicologic paradigms.
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Differential expression of cytosolic proteins in the rat kidney cortex and medulla: preliminary proteomics.

TL;DR: The results both confirm and expand the understanding of the molecular heterogeneity characterizing structurally and functionally distinct regions of the kidney and serve as a useful foundation for future nephrotoxicologic studies.
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Two‐dimensional electrophoretic mapping of hepatic and renal stress proteins

TL;DR: The results suggest that this group of proteins has significant responsibilities in normal, unstressed cells, due to their constitutive abundance, and the 2‐DE stress protein pattern established in this study may be very useful in toxicologic screening as well as describing a broad range of molecular effects of xenobiotic exposure.
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Toxicant-induced alterations in two-dimensional electrophoretic patterns of hepatic and renal stress proteins

TL;DR: The stress response to perfluorocarboxylic acids is tissue‐, toxicant‐, and stress protein class‐specific and dose‐related and the 2‐DE stress protein pattern may be suitable to future toxicologic screening applications.
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Glutathione S‐transferases: Two‐dimensional electrophoretic protein markers of lead exposure

TL;DR: Preliminary data confirm the utility of 2‐D electrophoretic GST analysis as indicative of lead exposure and toxicity and support its use for further elaboration of lead's effects on renal protein expression.