Antibody Sampler Kit MAP Kinase Activation
... Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases that include three major MAPKs: p38, JNK, and ERK. These MAPKs are involved in many cellular programs such as cell proliferation, differentiation, motility, and death. Upon stimulation, the MA ...
... Mitogen-activated protein kinases (MAPKs) are a widely conserved family of serine/threonine protein kinases that include three major MAPKs: p38, JNK, and ERK. These MAPKs are involved in many cellular programs such as cell proliferation, differentiation, motility, and death. Upon stimulation, the MA ...
B Cell Receptor Complexes - Sigma
... B Cell Receptor Complexes Reversible tyrosine phosphorylation plays an important role in regulating B cell function. In particular, binding of antigen to the B cell receptor (BCR) promotes the activation of several protein tyrosine kinases that, in conjunction with protein tyrosine phosphatases, al ...
... B Cell Receptor Complexes Reversible tyrosine phosphorylation plays an important role in regulating B cell function. In particular, binding of antigen to the B cell receptor (BCR) promotes the activation of several protein tyrosine kinases that, in conjunction with protein tyrosine phosphatases, al ...
plasmodium protein kinases: from database mining to the search for
... that no malarial PK clustered with the tyrosine kinase (TK) group; and (iv) that no members of the dualspecificity protein kinase (MAPKK) family (a subgroup of the STE group) are present in the P. falciparum genome. In addition, a novel, apparently Plasmodium-specific family of 18 genes encoding pro ...
... that no malarial PK clustered with the tyrosine kinase (TK) group; and (iv) that no members of the dualspecificity protein kinase (MAPKK) family (a subgroup of the STE group) are present in the P. falciparum genome. In addition, a novel, apparently Plasmodium-specific family of 18 genes encoding pro ...
Abstract
... Protein kinases mediate most intracellular signal transduction via the reversible phosphorylation on serine, threonine, or tyrosine residue of specific protein/peptide substrates. Such phosphorylation is employed by all eukaryotes in regulation of enzyme activity, protein-protein interaction, subcel ...
... Protein kinases mediate most intracellular signal transduction via the reversible phosphorylation on serine, threonine, or tyrosine residue of specific protein/peptide substrates. Such phosphorylation is employed by all eukaryotes in regulation of enzyme activity, protein-protein interaction, subcel ...
Abstract
... Protein kinases mediate most intracellular signal transduction via the reversible phosphorylation on serine, threonine, or tyrosine residue of specific protein/peptide substrates. Such phosphorylation is employed by all eukaryotes in regulation of enzyme activity, protein-protein interaction, subcel ...
... Protein kinases mediate most intracellular signal transduction via the reversible phosphorylation on serine, threonine, or tyrosine residue of specific protein/peptide substrates. Such phosphorylation is employed by all eukaryotes in regulation of enzyme activity, protein-protein interaction, subcel ...