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James J. Pesavento

Researcher at Saint Mary's College of California

Publications -  26
Citations -  3621

James J. Pesavento is an academic researcher from Saint Mary's College of California. The author has contributed to research in topics: Histone & Histone H4. The author has an hindex of 22, co-authored 26 publications receiving 3245 citations. Previous affiliations of James J. Pesavento include University of California, Berkeley & University of Illinois at Urbana–Champaign.

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Activation of the MCM2-7 helicase by association with Cdc45 and GINS proteins.

TL;DR: Biochemical activities of the MCM AAA+ motor are altered and enhanced through such associations: ATP hydrolysis rates are elevated by two orders of magnitude, helicase activity is robust on circular templates, and affinity for DNA substrates is improved.
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How many human proteoforms are there

Ruedi Aebersold, +53 more
TL;DR: This work frames central issues regarding determination of protein-level variation and PTMs, including some paradoxes present in the field today, and uses this framework to assess existing data and ask the question, "How many distinct primary structures of proteins (proteoforms) are created from the 20,300 human genes?"
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Certain and progressive methylation of histone H4 at lysine 20 during the cell cycle.

TL;DR: Metabolic labeling and top-down mass spectrometry reveal that newly synthesized H4 is progressively methylated at K20 during the G2, M, and G1 phases of the cell cycle in a process that is largely inescapable and irreversible.
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Pervasive combinatorial modification of histone H3 in human cells.

TL;DR: A platform using hydrophilic interaction chromatography and high-resolution tandem mass spectrometry for analyses of histone H3 that allows comprehensive characterization of 'histone codes' at the molecular level is developed, revealing pervasive combinatorial modification previously unaccounted for by other techniques.
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Quantitative analysis of modified proteins and their positional isomers by tandem mass spectrometry: human histone H4.

TL;DR: The ion fragmentation methods validated here are directly extensible to intact human proteins to derive quantitative information on the highly related and often isomeric protein forms created by combinatorial arrays of posttranslational modifications.