S
Sylvia E. Schwarz
Publications - 5
Citations - 1256
Sylvia E. Schwarz is an academic researcher. The author has contributed to research in topics: Ubiquitin-conjugating enzyme & Ubiquitin. The author has an hindex of 5, co-authored 5 publications receiving 1227 citations.
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Journal ArticleDOI
Activation of p53 by conjugation to the ubiquitin‐like protein SUMO‐1
Monica Gostissa,Arnd Hengstermann,Valentina Fogal,Peter Sandy,Sylvia E. Schwarz,Martin Scheffner,Giannino Del Sal,Giannino Del Sal +7 more
TL;DR: Evidence is provided that conjugation of SUMO‐1 to wild‐type p53 results in an increased transactivation ability of p53, suggesting that posttranslational modification of p51 by SUMO-1 conjugations provides a novel mechanism to regulate p53 activity.
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The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme
TL;DR: Yeast UBC9 functions as an E2 in a SMT3/SUMO-1 conjugation pathway analogous to ubiquitin-conjugating enzymes, which suggests that the role of yeast UBC 9 in cell cycle progression may be mediated through itsSMT3 conjugations activity.
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Characterization of Human hect Domain Family Members and Their Interaction with UbcH5 and UbcH7
TL;DR: It is shown that the hect domain of E6-AP is necessary and sufficient for ubiquitin thioester adduct formation, and in further support of the hypothesis that hect domain proteins represent a family of E3s, several of these are shown to formThioester complexes with UbcH7.
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Cloning of Human Ubiquitin-conjugating Enzymes UbcH6 and UbcH7 (E2-F1) and Characterization of Their Interaction with E6-AP and RSP5
TL;DR: Results indicate that E6-AP can interact with at least two species of E2 and that different hect proteins may interact with different E2s.
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The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate.
TL;DR: It is suggested that autoubiquitination and subsequent degradation of E6-AP represents a mechanism to control intracellular E 6-AP levels by inactivating E6 -AP molecules that are not bound to substrate proteins.