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Nicolas L. Young

Researcher at Baylor College of Medicine

Publications -  64
Citations -  3810

Nicolas L. Young is an academic researcher from Baylor College of Medicine. The author has contributed to research in topics: Histone & Chromatin. The author has an hindex of 24, co-authored 58 publications receiving 3189 citations. Previous affiliations of Nicolas L. Young include Florida State University & Purdue University.

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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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SIRT7 links H3K18 deacetylation to maintenance of oncogenic transformation

TL;DR: It is shown that SIRT7 is an NAD+-dependent H3K18Ac (acetylated lysine 18 of histone H3) deacetylase that stabilizes the transformed state of cancer cells and demonstrates a pivotal role for Sirt7 in chromatin regulation, cellular transformation programs and tumour formation in vivo.
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Asymmetrically Modified Nucleosomes

TL;DR: It is demonstrated that nucleosomes in embryonic stem cells, fibroblasts, and cancer cells exist in both symmetrically and asymmetrically modified populations for histone H3 lysine 27 di/trimethylation (H3K27me2/3).
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High-throughput characterization of combinatorial histone codes

TL;DR: A novel method utilizing “saltless” pH gradient weak cation exchange-hydrophilic interaction liquid chromatography directly coupled to electron transfer dissociation (ETD) mass spectrometry for the automated on-line high throughput characterization of hypermodified combinatorial histone codes is presented.
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Histone H3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells

TL;DR: The results suggest that K56Ac is involved in the human core transcriptional network of pluripotency, and more accurately reflects the epigenetic differences between hESCs and somatic cells than other active histone marks such as H3 K4 trimethylation and K9 acetylation.