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Benjamin A. Garcia

Researcher at University of Pennsylvania

Publications -  467
Citations -  40286

Benjamin A. Garcia is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Histone & Chromatin. The author has an hindex of 90, co-authored 425 publications receiving 31491 citations. Previous affiliations of Benjamin A. Garcia include Ludwig Maximilian University of Munich & Purdue University.

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SIRT6 mono-ADP ribosylates KDM2A to locally increase H3K36me2 at DNA damage sites to inhibit transcription and promote repair.

TL;DR: It is shown that the SIRT6 protein enhances non-homologous end joining (NHEJ) DNA repair by transiently repressing transcription and mediates a crosstalk between transcription and DNA repair machineries to promote DNA repair.
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Chromatin dysregulation associated with NSD1 mutation in head and neck squamous cell carcinoma

TL;DR: In this paper, the authors used genome-wide approaches and genome editing to dissect the downstream effects of loss of NSD1 in head and neck squamous cell carcinomas (HNSCCs).
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Stable Isotope Labeling of Phosphoproteins for Large-scale Phosphorylation Rate Determination

TL;DR: Stable isotope labeling of amino acids by phosphate is used to identify sites that have different phosphorylation kinetics during G1/S and M phase, and it is found that most sites had very similar phosphorylated rates under both conditions; however, a small subset of sites on proteins involved in the mitotic spindle were more activelyosphorylated during M phase.
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Sites Contributing to TRPA1 Activation by the Anesthetic Propofol Identified by Photoaffinity Labeling

TL;DR: It is confirmed that meta-azipropofol activates TRPA1 like the parent anesthetic, and two photolabeled residues (V954 and E969) in the S6 helix are identified, suggesting that the A-967079 cavity is a positive modulatory site for propofol.
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The nucleosomal surface is the main target of histone ADP-ribosylation in response to DNA damage.

TL;DR: The data suggest specific Asp/Glu residues are unlikely to be critical for DNA damage repair and rather that this process is likely dependent on ADP-ribosylation of the nucleosomal surface in general.