E6ap

Structure of E6AP in complex with HPV16E6 and p53 reveals a novel

Structure of E3 ligase E6AP with a proteasomebinding site provided by

Structure of E6AP in complex with HPV16E6 and p53 reveals a novel

Schematics of E6 binding motifs in IRF3 and E6AP to modulate cell

Structure of E6AP in complex with HPV16E6 and p53 reveals a novel

Proteomic Profiling of Potential E6AP Substrates via Ubiquitinbased

Structure of E3 ligase E6AP with a proteasomebinding site provided by

In vitro assays to test ubiquitination of E6AP substrates identified by

Structure of E3 ligase E6AP with a proteasomebinding site provided by

Reduced abundance of the E3 ubiquitin ligase E6AP contributes to

Structure of E3 ligase E6AP with a proteasomebinding site provided by

PDF Structure of E3 ligase E6AP with a proteasomebinding site

E3 Ubiquitin Ligase E6AP Negatively Regulates Adipogenesis by

Schematics of E6 binding motifs in IRF3 and E6AP to modulate cell

E3 Ubiquitin Ligase E6AP Negatively Regulates Adipogenesis by

The E6AP Binding Pocket of the HPV16 E6 Oncoprotein Provides a Docking

D The HECT E3 ligase E6AP does not repress transcription E6AP lanes

Structural and functional domains of E6AP and E6 The schematic of E6AP

The E6AP E3 ubiquitin ligase regulates the cellular response to

3D Molecular Interactions between E6 binding sites to E6AP A p53

Analysis of ubiquitin recognition by the HECT ligase E6AP provides

The E6AP E3 ubiquitin ligase regulates the cellular response to

E6AP AZUL interaction with UBQLN12 in cells condensates and an

2D Molecular Interactions between E6 binding sites to E6AP A p53

Schematic model illustrating the molecular mechanism proposed for E6AP

Schematics of E6 binding motifs in IRF3 and E6AP to modulate cell

E6AP Ubiquitin Ligase Mediates Ubiquitylation and Degradation of

Working models of how E6AP plays a role in normal neuronal physiology

2D Molecular Interactions between E6 binding sites to E6AP A p53

E6AP is essential for the proliferation of HPVpositive cancer cells by

E6AP over expression inhibits while E6APC843A promotes adipocyte

E6AP mediates MASTL degradation A HeLa cells were transfected with

E6AP AZUL interaction with UBQLN12 in cells condensates and an

Schematics of E6 binding motifs in IRF3 and E6AP to modulate cell

E6AP mediates MASTL degradation A HeLa cells were transfected with

E6AP is essential for the proliferation of HPVpositive cancer cells by

Analysis of ubiquitin recognition by the HECT ligase E6AP provides

Catalytically Important Residues of E6AP Ubiquitin Ligase Identified

Deciphering the mechanisms of HPV E6 mutations in the destabilization

Research Samy Meroueh Lab

Structural insights into the functional mechanism of the ubiquitin

Distinctive binding sites within the E6APE6p53 complex a Shown are

UBE3AE6AP General Information Sino Biological

The HECT E3 Ligase E6APUBE3A as a Therapeutic Target in Cancer and

Model of E6mediated ubiquitylation of p53 Model of E6mediated

Figure 1 from The Autism and Angelman Syndrome Protein Ube3AE6AP The

The HECT E3 Ligase E6APUBE3A as a Therapeutic Target in Cancer and

Structural dynamics of the E6APUBE3AE6p53 enzymesubstrate complex

Therapeutic potential of allosteric HECT E3 ligase inhibition Cell

A model for regulation of E6 protein function by E6I E6I protein

RCSB PDB 7QPB Catalytic Clobe of the HECTtype ubiquitin ligase

Pin1 Modulates ERα Levels in Breast Cancer through Inhibition of ...

Pin1 Modulates ER Levels in Breast Cancer through Inhibition of

E6AP an E3 ubiquitin ligase negatively regulates granulopoiesis by

Therapeutic potential of allosteric HECT E3 ligase inhibition Cell

Potential Therapeutic Targets for the Treatment of HPVAssociated

The HECT E3 Ligase E6APUBE3A as a Therapeutic Target in Cancer and

Nucleosomes specify cofactor access to p53 Molecular Cell

Model of E6mediated ubiquitylation of p53 Model of E6mediated

A schematic diagram illustrating the proposed antifibrotic mechanism

Researchers observe what ubiquitination hinges on EurekAlert

Solution Structure Analysis of the HPV16 E6 Oncoprotein Reveals a Self

Structure of the ternary complex of HPV16 E6 p53 and a E6APderived

A timer model for the role of the ATME6APMASTL axis in cell cycle

Research NewsShanghai Institute of Material Medical Chinese Academy

Schematic representation of the functional domains of E6AP E6AP

Structural dynamics of the E6APUBE3AE6p53 enzymesubstrate complex

Structure of HighRisk Papillomavirus 31 E6 Oncogenic Protein and

UBE3A and MCM6 synergistically regulate the proliferation and migration

Structural insights into the functional mechanism of the ubiquitin

Identification of SmallMolecule Activators of the Ubiquitin Ligase

Some of the known functions of HPV 16E6 HPV 16E6 partners with the

Protein Domain UBE3A Angelman Syndrome

Schematic representation of E6mediated tumor suppressor p53 protein

Activation of E6APUBE3AMediated Protein Ubiquitination and

Proteomic discovery of MNT as a novel interacting partner of E3

MNT expression is upregulated during myeloid differentiation a HL60

E6AP an E3 ubiquitin ligase negatively regulates granulopoiesis by

Structure of the E6E6APp53 complex required for HPVmediated

Figure 2 from The Autism Protein Ube3AE6AP Remodels Neuronal Dendritic

Structure of the E6E6APp53 complex required for HPVmediated

Proteotranscriptomic Measurements of E6Associated Protein E6AP

Rational Design of Stapled Covalent Peptide Modifiers of Oncoprotein E6

Frontiers Ubiquitination of the HPV Oncoprotein E6 Is Critical for E6

Deciphering the mechanisms of HPV E6 mutations in the destabilization

Figure 1 from The Autism Protein Ube3AE6AP Remodels Neuronal Dendritic

HPV E6E6APp53 Complex Juno Shemano

Identification of SmallMolecule Activators of the Ubiquitin Ligase

RCSB PDB 7QPB Catalytic Clobe of the HECTtype ubiquitin ligase

Figure 3 from The Autism Protein Ube3AE6AP Remodels Neuronal Dendritic

Identification of SmallMolecule Activators of the Ubiquitin Ligase

Nat Commun | 上海药物所揭示E6AP活性动态调控分子机制医药新闻-ByDrug-一站式医药资源共享中心-医药魔方

Nat Commun E6APByDrug

Deciphering the mechanisms of HPV E6 mutations in the destabilization

Identification of SmallMolecule Activators of the Ubiquitin Ligase

Molecular modeling of the E6peptide 13 conjugate A Structural

The Active Form of E6associated protein E6APUBE3A Ubiquitin Ligase

Proteotranscriptomic Measurements of E6Associated Protein E6AP

Structure of the E6E6APp53 complex required for HPVmediated

HPV16 E6 induces chromosomal instability due to polar chromosomes

Deciphering the mechanisms of HPV E6 mutations in the destabilization

Association strength of E6 to E6APp53 complex correlates with HPV

Stepwise multipolyubiquitination of p53 by the E6APE6 ubiquitin ligase

E6AP an E3 ubiquitin ligase negatively regulates granulopoiesis by

The Active Form of E6associated protein E6APUBE3A Ubiquitin Ligase

HPV E6E6APp53 Complex Juno Shemano

Deciphering the mechanisms of HPV E6 mutations in the destabilization

RCSB PDB 8JRQ Structure of E6APE6 complex in Det1 state

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