• inhibitors
  • p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors. (uniprot.org)
  • residue
  • This induces long-range allostery via protein domain dynamics, causing the structure to be destabilized, resulting in the opening up of the SH3, SH2 and kinase domains and the autophosphorylation of the residue tyrosine 416. (wikipedia.org)
  • induces
  • Binding of neuregulin to the ligand binding subdomains (I and III) induces a conformational change in ErbB3 that causes the protrusion of the dimerization loop in subdomain II, activating the protein for dimerization. (wikipedia.org)
  • cytokine
  • Jennifer C. C. Neale, Thomas P. Kenny, Ronald S. Tjeerdema, and M. Eric Gershwin, "PAH- and PCB-induced Alterations of Protein Tyrosine Kinase and Cytokine Gene Transcription in Harbor Seal ( Phoca Vitulina ) PBMC," Clinical and Developmental Immunology , vol. 12, no. 2, pp. 91-97, 2005. (hindawi.com)
  • Interacts
  • When Src is inactive, the phosphorylated tyrosine group at the 527 position interacts with the SH2 domain which helps the SH3 domain interact with the flexible linker domain and thereby keeps the inactive unit tightly bound. (wikipedia.org)
  • enzyme
  • Antibodies raised against a peptide corresponding to amino acids 39-64 of p56lck, a sequence found near the N-terminus, recognized the slower-migrating, but not the faster-migrating, form of the enzyme, indicating that a fraction of the protein had been proteolysed near the N-terminus during purification. (biochemj.org)
  • Non-receptor tyrosine-protein kinase TYK2 is an enzyme that in humans is encoded by the TYK2 gene. (wikipedia.org)
  • subunit
  • ErbB3 binding causes the allosteric activation of p110[disambiguation needed], the lipid kinase subunit of PI3K, a function not found in either EGFR or ErbB2. (wikipedia.org)