Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Claire Y Chiang"'
Autor:
Herschel S Dhekne, Francesca Tonelli, Wondwossen M Yeshaw, Claire Y Chiang, Charles Limouse, Ebsy Jaimon, Elena Purlyte, Dario R Alessi, Suzanne R Pfeffer
Publikováno v:
eLife, Vol 12 (2023)
Activating mutations in the leucine-rich repeat kinase 2 (LRRK2) cause Parkinson’s disease. LRRK2 phosphorylates a subset of Rab GTPases, particularly Rab10 and Rab8A, and we showed previously that these phosphoRabs play an important role in LRRK2
Externí odkaz:
https://doaj.org/article/3565c7f6dcf745449d8d8cc68bd1cf97
Autor:
Edmundo G Vides, Ayan Adhikari, Claire Y Chiang, Pawel Lis, Elena Purlyte, Charles Limouse, Justin L Shumate, Elena Spínola-Lasso, Herschel S Dhekne, Dario R Alessi, Suzanne R Pfeffer
Publikováno v:
eLife, Vol 11 (2022)
Activating mutations in the leucine-rich repeat kinase 2 (LRRK2) cause Parkinson’s disease, and previously we showed that activated LRRK2 phosphorylates a subset of Rab GTPases (Steger et al., 2017). Moreover, Golgi-associated Rab29 can recruit LRR
Externí odkaz:
https://doaj.org/article/3925beaf71f0417ebbc0fd002e21efb5
Autor:
Herschel S. Dhekne, Francesca Tonelli, Wondwossen M. Yeshaw, Claire Y. Chiang, Charles Limouse, Ebsy Jaimon, Elena Purlyte, Dario R. Alessi, Suzanne R. Pfeffer
Activating mutations in the Leucine Rich Repeat Kinase 2 (LRRK2) cause Parkinson’s disease. LRRK2 phosphorylates a subset of Rab GTPases, particularly Rab10 and Rab8A, and we showed previously that phosphoRabs play an important role in LRRK2 membra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3257f216220943444e2beacd3afcc126
https://doi.org/10.1101/2023.02.17.529028
https://doi.org/10.1101/2023.02.17.529028
Autor:
Edmundo G Vides, Ayan Adhikari, Claire Y Chiang, Pawel Lis, Elena Purlyte, Charles Limouse, Justin L Shumate, Elena Spínola-Lasso, Herschel S Dhekne, Dario R Alessi, Suzanne R Pfeffer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d5529d608bd60d4f0daa33683392c225
https://doi.org/10.7554/elife.79771.sa2
https://doi.org/10.7554/elife.79771.sa2
Autor:
Hanjie Jiang, Claire Y. Chiang, Zan Chen, Sara Nathan, Gabriel D’Agostino, Joao A. Paulo, Guang Song, Heng Zhu, Sandra B. Gabelli, Philip A. Cole
Publikováno v:
The Journal of biological chemistry. 298(5)
WWP2 is a HECT E3 ligase that targets protein Lys residues for ubiquitination and is comprised of an N-terminal C2 domain, four central WW domains, and a C-terminal catalytic HECT domain. The peptide segment between the middle WW domains, the 2,3-lin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78680d80efd9b3d58c5013eb0d236a94
https://pubmed.ncbi.nlm.nih.gov/35331737
https://pubmed.ncbi.nlm.nih.gov/35331737
Publikováno v:
J Biol Chem
NEDD4-1 E3 ubiquitin protein ligase (NEDD4-1) and WW domain-containing E3 ubiquitin ligase (WWP2) are HECT family ubiquitin E3 ligases. They catalyze Lys ubiquitination of themselves and other proteins and are important in cell growth and differentia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dce8f422ee1a47eeff485dcb2042a608
https://doi.org/10.1074/jbc.ra119.009211
https://doi.org/10.1074/jbc.ra119.009211