Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
By A. Salmeen, J. Andersen, M. Myers, T. Meng, J. Hinks, N. Tonks, D. Barford. Nature, 2003
929 citations recorded by the source corpus.
Subfields: Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/3fe048dd1476adf60461e9260c41a6a894d47503
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In Immunology
In Molecular Biology
- Navdeep S. Chandel
- Dean P. Jones
- N. Tonks
- Lucas B. Sullivan
- S. Rhee
- B. D'Autréaux
- M. Tolédano
- H. Forman
Citations in the corpus
- ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis (2007, background): “The -SOH is highly reactive, its stability being influenced by the availability of a proximal -SH with which it condenses to form a disulphide bond, or by availability of a proximal nitrogen to form a sulphenamide 115,116 or by the presence of H 2 O 2 , which further oxidizes it to form sulphinic (-”
- Radical-free biology of oxidative stress. (2008, background): “In certain protein structures, they can be stabilized as sulfenamides (150, 185).”
- Cadmium stress: an oxidative challenge (2010, positive): “Hyperoxidation of the sulphenic acid to sulphinic acid was thought to be an irreversible modification until the discovery of the sulphinic acid reductase sulfiredoxin was discovered (Biteau et al. 2003; Salmeen et al. 2003; van Montfort et al. 2003; Barranco-Medina et al. 2009).”
- Signal transduction by reactive oxygen species (2011, background): “These initial reports speculated that the intracellular target of oxidants might be the family of tyrosine and dual specific phosphatases, a hypothesis that was subsequently elegantly established (Lee et al., 1998; Salmeen et al., 2003).”
- Selenoproteins: molecular pathways and physiological roles. (2014, background): “This mode of regulation is observed, for example, in tyrosine protein phosphatase 1B (300) and PTEN (194).”
- Mitochondrial reactive oxygen species and cancer (2014, background): “PTP1B also suppresses Akt activity by dephosphorylation but, like PP2A, ROS inhibit PTP1B activity and increase Akt activity resulting in increased anchorage-independent growth [42,43].”
- Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. (2005, background): “Recently, however, the highly unstable Cys–SOH of PTP1B was shown to form a five-membered cyclic sulfenyl amide species, in which the sulfur atom of the active site cysteine is covalently linked to the nitrogen of a neighboring serine residue [15,16].”
- Hydrogen peroxide sensing, signaling and regulation of transcription factors (2014, background): “If these enzymes had only an antioxidant function, why is there such a variety? For all these reasons, it was concluded that a signaling protein like PTP1B that is redox regulated by H2O2 [16][17][18] but has a low reactivity towards H2O2 [19], could not be a direct sensor of H2O2 [20][21][22][13].”
- Mechanisms of Cell Death in Oxidative Stress (2007, neutral): “UVC radiation which selectively promotes direct”
- Signaling Functions of Reactive Oxygen Species (2010, background): “Thus, while it has been demonstrated that PTP1B can react in vitro with H2O2 to form a sulfenic acid that goes on to form a sulfenyl-amide intermediate (85, 86), this is rather unlikely to occur in a cell where it would be in competition with Prxs and Sec-GPxs, which are abundant in the cytosol and ”