Publications by authors named "E M WORDEN"

Histone H3K9 methylation (H3K9me) by Setdb1 silences retrotransposons (rTE) by sequestering them in constitutive heterochromatin. Atf7IP is a constitutive binding partner of Setdb1 and is responsible for Setdb1 nuclear localization, activation and chromatin recruitment. However, structural details of the Setdb1/Atf7IP interaction have not been evaluated.

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Mono-ubiquitination of lysine 18 on histone H3 (H3K18ub), catalyzed by UHRF1, is a DNMT1 docking site that facilitates replication-coupled DNA methylation maintenance. Its functions beyond this are unknown. Here, we genomically map simultaneous increases in UHRF1-dependent H3K18ub and SUV39H1/H2-dependent H3K9me3 following DNMT1 inhibition.

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Article Synopsis
  • Surgical assessment tools are crucial for evaluating the performance of surgical trainees, and this study focused on a 12-item tool specifically for Roux-en-Y Gastric Bypass (RYGB) procedures.
  • The study assessed the performance of a surgical fellow over 17 surgeries using various evaluation methods, including the Global Operative Assessment of Laparoscopic Skills (GOALS) and the General Assessment of Surgical Skill (GASS).
  • Findings showed significant improvements in overall surgical skills, specifically in tasks like jejunojejunostomy creation and stapler use, indicating that trainees can enhance their capabilities through hands-on surgical experience.
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Background: Broad implementation of the American Board of Surgery's entrustable professional activities initiative will require assessment instruments that are reliable and easy to use. Existing assessment instruments of general laparoscopic surgical skills have limited reliability, efficiency, and validity across the spectrum of formative (low-stakes) and summative (high-stakes) assessments. A novel six-item global assessment of surgical skills (GASS) instrument was developed and evaluated with a focus upon safe versus unsafe surgical practice scoring rubric.

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Rpn11 is an essential metalloprotease responsible for the en bloc removal of ubiquitin chains from protein substrates that are targeted for degradation by the 26S proteasome. A unique feature of Rpn11 is that its deubiquitinase (DUB) activity is greatly stimulated by the mechanical translocation of the substrate into the proteasomal AAA+ (ATPase Associated with diverse cellular Activities) motor, which delivers the scissile isopeptide bond between a substrate lysine and the proximal moiety of an attached ubiquitin chain to the DUB catalytic active site. As a consequence, Rpn11 cleaves at the base of ubiquitin chains and lacks selectivity towards specific ubiquitin-chain linkage types, which is in contrast to other DUBs, including the related AMSH that selectively cleaves Lys63-linked chains.

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