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Ryan C. Kunz

Researcher at Harvard University

Publications -  32
Citations -  1661

Ryan C. Kunz is an academic researcher from Harvard University. The author has contributed to research in topics: Active site & Phosphorylation. The author has an hindex of 19, co-authored 32 publications receiving 1410 citations. Previous affiliations of Ryan C. Kunz include Lawrence Berkeley National Laboratory & University of Nebraska–Lincoln.

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The membrane-associated methane monooxygenase (pMMO) and pMMO-NADH:quinone oxidoreductase complex from Methylococcus capsulatus bath

TL;DR: It is demonstrated that copper not only regulates the metabolic switch between the two methane monooxygenases but also regulates the level of expression of the pMMO and the development of internal membranes.
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S-Nitrosylation links obesity-associated inflammation to endoplasmic reticulum dysfunction

TL;DR: It is shown that, in the setting of obesity, inflammatory input through increased inducible nitric oxide synthase (iNOS) activity causes S-nitrosylation of a key UPR regulator, IRE1α, which leads to a progressive decline in hepatic I RE1α-mediated XBP1 splicing activity in both genetic and dietary models of obesity.
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Regulation of meiotic recombination via Mek1-mediated Rad54 phosphorylation

TL;DR: Mek1 phosphorylation provides a dynamic means of controlling recombination partner choice in meiosis in two ways: (1) it reduces Rad51 activity through inhibition of Rad51/Rad54 complex formation, and (2) it suppresses Rad51-mediated strand invasion of sister chromatids via a Rad54-independent mechanism.
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Evaluating multiplexed quantitative phosphopeptide analysis on a hybrid quadrupole mass filter/linear ion trap/orbitrap mass spectrometer

TL;DR: It is found that ratio distortion remained a problem for phosphopeptide analysis in multiplexed quantitative workflows, but the underlying cause of interference may not be due to coeluting and cofragmented peptides but instead from consistent, low level background fragmentation.
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Sensitive multiplexed analysis of kinase activities and activity-based kinase identification

TL;DR: An improved single-reaction strategy, which quantifies the phosphorylation of 90 synthetic peptides in a single mass spectrometry run, is compatible with nanogram to microgram amounts of cell lysate and enhances kinase monospecificity through substrate competition effects.