Cargando…
Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases
Cysteine-based protein tyrosine phosphatases (Cys-based PTPs) perform dephosphorylation to regulate signaling pathways in cellular responses. The hydrogen bonding network in their active site plays an important conformational role and supports the phosphatase activity. Nearly half of dual-specificit...
Autores principales: | Lai, Chih-Hsuan, Chang, Co-Chih, Chuang, Huai-Chia, Tan, Tse-Hua, Lyu, Ping-Chiang |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7589817/ https://www.ncbi.nlm.nih.gov/pubmed/33053837 http://dx.doi.org/10.3390/ijms21207515 |
Ejemplares similares
-
Regulation of Dual-Specificity Phosphatase (DUSP) Ubiquitination and Protein Stability
por: Chen, Hsueh-Fen, et al.
Publicado: (2019) -
MAP4K Family Kinases and DUSP Family Phosphatases in T-Cell Signaling and Systemic Lupus Erythematosus
por: Chuang, Huai-Chia, et al.
Publicado: (2019) -
Downregulation of the phosphatase JKAP/DUSP22 in T cells as a potential new biomarker of systemic lupus erythematosus nephritis
por: Chuang, Huai-Chia, et al.
Publicado: (2016) -
Induction of DUSP14 ubiquitination by PRMT5-mediated arginine methylation
por: Yang, Chia-Yu, et al.
Publicado: (2018) -
Hepatocyte phosphatase DUSP22 mitigates NASH-HCC progression by targeting FAK
por: Ge, Chenxu, et al.
Publicado: (2022)