Physical and Functional Interaction of the HECT Ubiquitin-protein Ligases E6AP and HERC2

E6-Associated Protein Is Required for Human Papillomavirus Type 16 E6 to Cause Cervical Cancer in Mice

(2010) Anny Shai et al.   CANCER RESEARCH

HERC2 Is an E3 Ligase That Targets BRCA1 for Degradation

(2010) W. Wu et al.   CANCER RESEARCH

The Angelman Syndrome Protein Ube3A Regulates Synapse Development by Ubiquitinating Arc

(2010) Paul L. Greer et al.   CELL

Regulation of the polycomb protein Ring1B by self-ubiquitination or by E6-AP may have implications to the pathogenesis of Angelman syndrome

(2010) D. Zaaroor-Regev et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Circadian control of XPA and excision repair of cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligase

(2010) T.-H. Kang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

RING Domain E3 Ubiquitin Ligases

(2009) Raymond J. Deshaies et al.   Annual Review of Biochemistry

E6AP promotes the degradation of the PML tumor suppressor

(2009) I Louria-Hayon et al.   CELL DEATH AND DIFFERENTIATION

The ubiquitin ligase E6-AP promotes degradation of α-synuclein

(2009) Shalaka A. Mulherkar et al.   JOURNAL OF NEUROCHEMISTRY

The Ubiquitin-Specific Peptidase USP15 Regulates Human Papillomavirus Type 16 E6 Protein Stability

(2009) R. M. Vos et al.   JOURNAL OF VIROLOGY

HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes

(2009) Simon Bekker-Jensen et al.   NATURE CELL BIOLOGY

Physiological functions of the HECT family of ubiquitin ligases

(2009) Daniela Rotin et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Ubiquitin-binding domains — from structures to functions

(2009) Ivan Dikic et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Ubiquitin ligase E6-AP and its role in human disease

(2008) Konstantin Matentzoglu et al.   BIOCHEMICAL SOCIETY TRANSACTIONS

HPV E6, E6AP and cervical cancer

(2008) Sylvie Beaudenon et al.   BMC BIOCHEMISTRY