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Valina L. Dawson

Researcher at Johns Hopkins University School of Medicine

Publications -  477
Citations -  88024

Valina L. Dawson is an academic researcher from Johns Hopkins University School of Medicine. The author has contributed to research in topics: Neurodegeneration & Parkin. The author has an hindex of 136, co-authored 451 publications receiving 76986 citations. Previous affiliations of Valina L. Dawson include University of Baltimore & Hospital of the University of Pennsylvania.

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Neuronal NOS and cyclooxygenase-2 contribute to DNA damage in a mouse model of Parkinson disease.

TL;DR: It is found that not only nuclear, but also mitochondrial, DNA is a target for the MPTP insult and this results suggest that the loss of genomic integrity can be triggered by the concerted actions of nNOS and Cox-2 and provide further support to the view that DNA damage may contribute to the neurodegenerative process in Parkinson disease.
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Role for the ubiquitin-proteasome system in Parkinson's disease and other neurodegenerative brain amyloidoses.

TL;DR: An overview of the key genes / proteins implicated in the abnormal UPS-mediated proteolytic processing of unwanted proteins observed in neurodegenerative brain amyloidoses is provided and the mechanisms by which UPS dysfunction can compromise neuronal integrity are discussed.
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Differential Effect of PARP-2 Deletion on Brain Injury after Focal and Global Cerebral Ischemia

TL;DR: In this paper, the authors evaluated the impact of PARP-2 deletion on histopathological outcome from two different experimental models of cerebral ischemia and found that PARP deletion significantly increased neuronal cell loss in the hippocampal CA1 field (65%736% ischemic neurons) when compared with WT mice (31%733%).
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Protein microarray characterization of the S-nitrosoproteome

TL;DR: The S-nitrosoproteome is described using a high-density protein microarray chip containing 16,368 unique human proteins, and eight ubiquitin E3 ligases are identified, whose activities are modulated by S-Nitrosylation, providing a unique regulatory mechanism of the ubiquit in proteasome system.
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New insights into Parkinson's disease.

TL;DR: Findings in parkin function as well as mutations in UCH-L1 fit with the notion that derangements in the ubiquitin proteasomal pathway (UPP) may play important roles in the demise of dopamine neurons in PD.