Results 11 to 20 of about 327,500 (191)

UBE3A/E6-AP regulates cell proliferation by promoting proteasomal degradation of p27

open access: yesNeurobiology of Disease, 2009
The UBE3A/E6-AP is known to function both as an E3 ubiquitin ligase of the ubiquitin proteasome system and as a transcriptional coactivator. E6-AP shows brain-specific imprinting and loss of function of maternally inherited E6-AP causes Angelman syndrome.
Amit Mishra   +2 more
doaj   +3 more sources

Ubiquitin ligase E6-AP and its role in human disease [PDF]

open access: yesBiochemical Society Transactions, 2008
The ubiquitin ligase E6-AP (E6-associated protein) represents a prime example for the notion that deregulated modification of proteins with ubiquitin contributes to the development of human disease: loss of E6-AP function by mutation is responsible for ...
Matentzoglu, Konstantin   +1 more
core   +4 more sources

E6-associated protein (E6-AP) is a dual function coactivator of steroid hormone receptors [PDF]

open access: yesNuclear Receptor Signaling, 2008
Steroid hormone receptors (SHR) belong to a large family of ligand-activated transcription factors that perform their biological functions by enhancing the transcription of specific target genes.
Nawaz, Zafar, Ramamoorthy, Sivapriya
core   +3 more sources

Overexpression of ligase defective E6-associated protein, E6-AP, results in mammary tumorigenesis

open access: yesBreast Cancer Research and Treatment, 2011
E6-associated protein (E6-AP) is a dual function protein. It acts as an E3 ubiquitin-protein ligase enzyme and coactivator of steroid hormone receptors such as estrogen (ERα) and progesterone (PR) receptors.
Sivapriya Ramamoorthy   +13 more
core   +3 more sources

The Angelman Syndrome-Associated Protein, E6-AP, Is a Coactivator for the Nuclear Hormone Receptor Superfamily [PDF]

open access: yesMolecular and Cellular Biology, 1999
In this study, we found that the E6-associated protein (E6-AP/UBE3A) directly interacts with and coactivates the transcriptional activity of the human progesterone receptor (PR) in a hormone-dependent manner.
Tsai, Sophia Y   +6 more
core   +3 more sources

The role of the ubiquitin ligase E6-AP in human papillomavirus E6-mediated degradation of PDZ domain-containing proteins [PDF]

open access: yesJournal of Biological Chemistry, 2007
The E6 oncoprotein of human papillomaviruses associated with cervical cancer targets the tumor suppressor p53 and several other cellular proteins including the human homologs of Dlg and Scribble for degradation via the ubiquitin-proteasome system ...
Matentzoglu, Konstantin   +2 more
core   +4 more sources

E6-AP facilitates efficient transcription at estrogen responsive promoters through recruitment of chromatin modifiers

open access: yesSteroids, 2011
E6-AP is a known coactivator of the estrogen receptor alpha (ERα), however the coactivation mechanism of E6-AP is not clear. This work was undertaken to elucidate the coactivation mechanism of E6-AP. In order to examine the role of E6-AP in ERα signaling,
Zafar Nawaz   +3 more
core   +3 more sources

Ubiquitin-dependent proteolysis of trihydrophobin 1 (TH1) by the human papilloma virus E6-associated protein (E6-AP).

open access: yesJournal of Cellular Biochemistry, 2007
Human Papilloma virus E6-associated protein (E6-AP), which is known as an E3 ubiquitin ligase, mediates ubiquitination and subsequent degradation of a series of cellular proteins.
Zong, Hongliang
core   +4 more sources

E6-Associated Protein (E6-AP): A Potential Tumor Suppressor Protein for Non-Hodgkin Lymphoma

open access: yesBlood, 2006
Over the past decade considerable progress has been made in cloning and characterization of potential tumor suppressor genes. Tumor suppressors have a repressive effect on the regulation of the cell cycle or promote apoptosis and sometimes do both.
Zafar, Shazia   +2 more
core   +2 more sources

E6-AP/UBE3A protein acts as a ubiquitin ligase toward SOX9 protein. [PDF]

open access: yesJ Biol Chem, 2013
SOX9 is a transcription factor that acts as a key regulator at various stages of cartilage differentiation. There is ample evidence that intracellular SOX9 protein levels are tightly regulated both by sumoylation and by degradation through the ubiquitin-proteasome pathway. Using a proteomics approach, here we report the identification of a SOX9-binding
Hattori T   +7 more
europepmc   +4 more sources

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