Nedd4 Ubiquitin Protein Ligases
"Nedd4 Ubiquitin Protein Ligases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
E3 ubiquitin ligases that consist of four WW DOMAINS. They accept UBIQUITIN from E2 UBIQUITIN-CONJUGATING ENZYME as a thioester via their C-terminal HECT domains and transfer it specifically to the 63rd LYSINE residue (Lys-63) of target proteins. NEDD4 targets include many proteins and receptors with important functions for cell growth and homeostasis such as VEGFR-2; FGFR1 TYROSINE KINASE; and ERBB-4 RECEPTOR. They play a critical role in the internalization of these receptors, their degradation by LYSOSOMES, and also function as part of the ESCRT complex in VIRUS RELEASE.
Descriptor ID |
D000075702
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MeSH Number(s) |
D05.500.199.500 D08.811.464.938.750.257 D12.776.543.990.493.500
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Concept/Terms |
Nedd4 Ubiquitin Protein Ligases- Nedd4 Ubiquitin Protein Ligases
- Nedd4 Proteins
- Neuronal Precursor Cell-Expressed Developmentally Down-Regulated 4 Ligase
- Neuronal Precursor Cell Expressed Developmentally Down Regulated 4 Ligase
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Below are MeSH descriptors whose meaning is more general than "Nedd4 Ubiquitin Protein Ligases".
Below are MeSH descriptors whose meaning is more specific than "Nedd4 Ubiquitin Protein Ligases".
This graph shows the total number of publications written about "Nedd4 Ubiquitin Protein Ligases" by people in this website by year, and whether "Nedd4 Ubiquitin Protein Ligases" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2008 | 0 | 1 | 1 | 2015 | 0 | 3 | 3 | 2016 | 0 | 1 | 1 | 2018 | 1 | 0 | 1 |
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Below are the most recent publications written about "Nedd4 Ubiquitin Protein Ligases" by people in Profiles.
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Ziegler CM, Dang L, Eisenhauer P, Kelly JA, King BR, Klaus JP, Manuelyan I, Mattice EB, Shirley DJ, Weir ME, Bruce EA, Ballif BA, Botten J. NEDD4 family ubiquitin ligases associate with LCMV Z's PPXY domain and are required for virus budding, but not via direct ubiquitination of Z. PLoS Pathog. 2019 11; 15(11):e1008100.
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Guarnieri AL, Towers CG, Drasin DJ, Oliphant MUJ, Andrysik Z, Hotz TJ, Vartuli RL, Linklater ES, Pandey A, Khanal S, Espinosa JM, Ford HL. The miR-106b-25 cluster mediates breast tumor initiation through activation of NOTCH1 via direct repression of NEDD4L. Oncogene. 2018 07; 37(28):3879-3893.
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Rosario FJ, Powell TL, Jansson T. Mechanistic target of rapamycin (mTOR) regulates trophoblast folate uptake by modulating the cell surface expression of FR-a and the RFC. Sci Rep. 2016 08 26; 6:31705.
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Rosario FJ, Dimasuay KG, Kanai Y, Powell TL, Jansson T. Regulation of amino acid transporter trafficking by mTORC1 in primary human trophoblast cells is mediated by the ubiquitin ligase Nedd4-2. Clin Sci (Lond). 2016 Apr 01; 130(7):499-512.
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Chen YY, Rosario FJ, Shehab MA, Powell TL, Gupta MB, Jansson T. Increased ubiquitination and reduced plasma membrane trafficking of placental amino acid transporter SNAT-2 in human IUGR. Clin Sci (Lond). 2015 Dec; 129(12):1131-41.
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Bustos F, de la Vega E, Cabezas F, Thompson J, Cornelison DD, Olwin BB, Yates JR, Olgu?n HC. NEDD4 Regulates PAX7 Levels Promoting Activation of the Differentiation Program in Skeletal Muscle Precursors. Stem Cells. 2015 Oct; 33(10):3138-51.
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Yang B, Gay DL, MacLeod MK, Cao X, Hala T, Sweezer EM, Kappler J, Marrack P, Oliver PM. Nedd4 augments the adaptive immune response by promoting ubiquitin-mediated degradation of Cbl-b in activated T cells. Nat Immunol. 2008 Dec; 9(12):1356-63.
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