Cargando…
A Structure-Based Approach for Detection of Thiol Oxidoreductases and Their Catalytic Redox-Active Cysteine Residues
Cysteine (Cys) residues often play critical roles in proteins, for example, in the formation of structural disulfide bonds, metal binding, targeting proteins to the membranes, and various catalytic functions. However, the structural determinants for various Cys functions are not clear. Thiol oxidore...
Autores principales: | Marino, Stefano M., Gladyshev, Vadim N. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2673044/ https://www.ncbi.nlm.nih.gov/pubmed/19424433 http://dx.doi.org/10.1371/journal.pcbi.1000383 |
Ejemplares similares
-
Cysteine, Glutathione, and Thiol Redox Balance in Astrocytes
por: McBean, Gethin J.
Publicado: (2017) -
Catalytic Site Cysteines of Thiol Enzyme: Sulfurtransferases
por: Nagahara, Noriyuki
Publicado: (2011) -
Dynamic evolution of selenocysteine utilization in bacteria: a balance between selenoprotein loss and evolution of selenocysteine from redox active cysteine residues
por: Zhang, Yan, et al.
Publicado: (2006) -
Different Catalytic Mechanisms in Mammalian Selenocysteine- and Cysteine-Containing Methionine-R-Sulfoxide Reductases
por: Kim, Hwa-Young, et al.
Publicado: (2005) -
Structural insights into redox-active cysteine residues of the Src family kinases
por: Heppner, David E.
Publicado: (2021)