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Cam Patterson

Researcher at University of North Carolina at Chapel Hill

Publications -  201
Citations -  18436

Cam Patterson is an academic researcher from University of North Carolina at Chapel Hill. The author has contributed to research in topics: Ubiquitin ligase & Ubiquitin. The author has an hindex of 68, co-authored 200 publications receiving 17410 citations. Previous affiliations of Cam Patterson include NewYork–Presbyterian Hospital.

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The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

TL;DR: It is shown that CHIP functions with Hsc70 to sense the folded state of CFTR and targets aberrant forms for proteasomal degradation by promoting their ubiquitination.
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The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle.

TL;DR: The mechanism by which MYH is depleted under atrophy conditions is identified and it is demonstrated that inhibition of a single E3 ligase, MuRF1, is sufficient to maintain this important sarcomeric protein.
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The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins

TL;DR: It is reported that inhibition of Hsp90 led to decreases in p-tau levels independent of heat shock factor 1 (HSF1) activation, and this is the first demonstration to the authors' knowledge that blockade of the refolding pathway promotes p-Tau turnover through degradation.
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Targeted deletion of Dicer in the heart leads to dilated cardiomyopathy and heart failure.

TL;DR: It is reported that cardiac-specific knockout of Dicer, a gene encoding a RNase III endonuclease essential for microRNA (miRNA) processing, leads to rapidly progressive DCM, heart failure, and postnatal lethality and indicates that miRNAs play critical roles in normal cardiac function and under pathological conditions.
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p47phox is required for atherosclerotic lesion progression in ApoE–/– mice

TL;DR: These studies provide convincing support for the hypothesis that superoxide generation in general, and NADPH oxidase in particular, have a requisite role in atherosclerotic lesion formation, and they provide a rationale for further studies to dissect the contributions of ROS to vascular lesions formation.