Herein we review all the currently available ATP‐site and non‐ATP‐site ligands bound to
p38α mitogen‐activated protein kinase (MAPK) available in the RCSB Protein Data Bank …

The p38α MAP Kinase has been an important target of drug design for treatment of
inflammatory diseases and cancers. This work applies multiple replica Gaussian …

The function of many protein kinases is controlled by the phosphorylation of a critical
tyrosine residue in the activation loop. Dual specificity tyrosine‐phosphorylation‐regulated …

Through a “tag-and-modify” protein chemical modification strategy, we site-selectively
phosphorylated the activation loop of protein kinase p38α. Phosphorylation at natural (180) …

PeBoW, a trimeric complex consisting of pescadillo (Pes1), block of proliferation (Bop1), and
the WD repeat protein 12 (WDR12), is essential for processing and maturation of …

Signaling processes are primarily promoted by molecular recognition and corresponding
protein-protein interactions. One of the key eukaryotic signaling pathways is the MAP kinase …

p38α is a key serine/threonine kinase that can enable atypical auto-activation through
Zap70 phosphorylation and initiate T cell receptor signaling. The auto-activation plays an …

We describe here for the first time a lipid‐binding‐domain (LBD) in p38γ mitogen‐activated
protein kinase (MAPK) involved in the response of T cells to a newly identified inhibitor …

The intramolecular network structure of a protein provides valuable insights into allosteric
sites and communication pathways. However, a straightforward method to comprehensively …

p38α mitogen-activated protein kinase (MAPK) is generally activated by dual
phosphorylation but has also been shown to exhibit alternative activation modes. One of …