Cargando…
Structures of human PKG reveal cGMP-selectived activation mechanisms
Autores principales: | Huang, Gilbert Y, Kim, Jeong J, Reger, Albert S, Lorenz, Robin, Moon, Eui-Whan, Zhao, Chi, Casteel, Darren E, Bertinetti, Daniela, VanSchouwen, Bryan, Selvaratnam, Rajeevan, Pflugrath, James W, Sankaran, Banumathi, Melacini, Giuseppe, Herberg, Friedrich W, Kim, Choel |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3765643/ http://dx.doi.org/10.1186/2050-6511-14-S1-O16 |
Ejemplares similares
-
Transforming PKA into PKG – a structure-function approach to understand cyclic nucleotide selectivity
por: Lorenz, Robin, et al.
Publicado: (2013) -
Crystal structures of the carboxyl cGMP binding domain of plasmodium falciparum cGMP-dependent protein kinase reveals a novel salt bridge crucial for activation
por: Kim, Jeong Joo, et al.
Publicado: (2013) -
An auto-inhibited state of protein kinase G and implications for selective activation
por: Sharma, Rajesh, et al.
Publicado: (2022) -
The role of cGMP and PKG in cardioprotection
por: Downey, James M, et al.
Publicado: (2009) -
Neutron Diffraction Reveals Hydrogen Bonds Critical
for cGMP-Selective Activation: Insights for cGMP-Dependent Protein
Kinase Agonist Design
por: Huang, Gilbert Y., et al.
Publicado: (2014)