Phosphatase-dependent regulation of epithelial mitogen-activated protein kinase responses to toxin-induced membrane pores. [PDF]
PLoS ONE, 2009 Diverse bacterial species produce pore-forming toxins (PFT) that can puncture eukaryotic cell membranes. Host cells respond to sublytic concentrations of PFT through conserved intracellular signaling pathways, including activation of mitogen-activated ...
Jorge L Aguilar +6 more
doaj +1 more source
c-Jun N-Terminal Kinase in Inflammation and Rheumatic Diseases. [PDF]
, 2012 The c-Jun N-terminal kinases (JNKs) are members of the mitogen-activated protein kinase (MAPK) family and are activated by environmental stress. JNK is also activated by proinflammatory cytokines, such as TNF and IL-1, and Toll-like receptor ligands ...
Firestein, Gary S, Guma, Monica
core +1 more source
Integration of a Phosphatase Cascade with the MAP Kinase Pathway provides for a Novel Signal Processing Function [PDF]
, 2009 We mathematically modeled the receptor-activated MAP kinase signaling by incorporating the regulation through cellular phosphatases. Activation induced the alignment of a phosphatase cascade in parallel with the MAP kinase pathway.
Alon +54 more
core +3 more sources
Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments [PDF]
, 2018 Reversible phosphorylation is a key mechanism that regulates many cellular processes in prokaryotes and eukaryotes. In prokaryotes, signal transduction includes two-component signaling systems, which involve a membrane sensor histidine kinase and a ...
Janczarek, Monika +3 more
core +1 more source
Rule-based Modelling and Tunable Resolution [PDF]
, 2009 We investigate the use of an extension of rule-based modelling for cellular signalling to create a structured space of model variants. This enables the incremental development of rule sets that start from simple mechanisms and which, by a gradual ...
Russ Harmer +2 more
core +5 more sources
Critical Role of the Secondary Binding Pocket in Modulating the Enzymatic Activity of DUSP5 toward Phosphorylated ERKs [PDF]
, 2016 DUSP5 is an inducible nuclear dual-specificity phosphatase that specifically interacts with and deactivates extracellular signal-regulated kinases ERK1 and ERK2, which are responsible for cell proliferation, differentiation, and survival. The phosphatase
Bongard, Robert D +6 more
core +3 more sources
Research advances of dual-specificity phosphatases in kidney disease
Linchuang shenzangbing zazhi, 2021 Belonging to the family of protein tyrosine phosphatases,DUSPs（dual-specificity phosphatases）can dephosphorylate both serine/threonine and tyrosine residues concurrently.In recent years,with the in-depth study of DUSPs,they have been implicated as major ...
杜宇, 章波, 赵景宏
doaj
Structural and biochemical analysis of atypically low dephosphorylating activity of human dual-specificity phosphatase 28. [PDF]
PLoS ONE, 2017 Dual-specificity phosphatases (DUSPs) constitute a subfamily of protein tyrosine phosphatases, and are intimately involved in the regulation of diverse parameters of cellular signaling and essential biological processes.
Bonsu Ku +9 more
doaj +1 more source
Protein Expression, Characterization and Activity Comparisons of Wild Type and Mutant DUSP5 Proteins [PDF]
, 2014 Background The mitogen-activated protein kinases (MAPKs) pathway is critical for cellular signaling, and proteins such as phosphatases that regulate this pathway are important for normal tissue development.
Gastonguay, Adam J. +11 more
core +2 more sources
Expression Profile of Tyrosine Phosphatases in HER2 Breast Cancer Cells and Tumors
Cellular Oncology, 2010 Background: HER2-overexpression promotes malignancy by modulating signalling molecules, which include PTPs/DSPs (protein tyrosine and dual-specificity phosphatases). Our aim was to identify PTPs/DSPs displaying HER2-associated expression alterations.
Maria Antonietta Lucci +5 more
doaj +1 more source