Results 21 to 30 of about 288,999 (305)

Phosphorylation at tyrosine 317 and 508 are crucial for PIK3CA/p110α to promote CRC tumorigenesis

open access: yesCell & Bioscience, 2023
Background PI3K/AKT signaling pathway plays important role in tumorigenesis of human cancer. Protein phosphorylation is crucial for signaling transduction of this pathway.
Ting Wang   +8 more
doaj   +1 more source

SH3 domain tyrosine phosphorylation--sites, role and evolution.

open access: yesPLoS ONE, 2012
BackgroundSH3 domains are eukaryotic protein domains that participate in a plethora of cellular processes including signal transduction, proliferation, and cellular movement. Several studies indicate that tyrosine phosphorylation could play a significant
Zuzana Tatárová   +3 more
doaj   +1 more source

The Genesis of Tyrosine Phosphorylation [PDF]

open access: yesCold Spring Harbor Perspectives in Biology, 2014
Tyrosine phosphorylation of proteins was discovered in 1979, but this posttranslational modification had been "invented" by evolution more than a billion years ago in single-celled eukaryotic organisms that were the antecedents of the first multicellular animals.
openaire   +2 more sources

Protein-tyrosine phosphorylation in the Archaea [PDF]

open access: yesJournal of Bacteriology, 1997
Sulfolobus sulfataricus ATCC 35091, Haloferax volcanii, and Methanosarcina thermophila TM-1, representing the Euryarchaeota and Crenarchaeota subdomains of the Archaea, contain proteins which are phosphorylated on tyrosine. These data raise fundamental questions as to the origin and evolution of tyrosine phosphorylation, a protein modification that is ...
S C, Smith, P J, Kennelly, M, Potts
openaire   +2 more sources

FLT3 and FLT3-ITD phosphorylate and inactivate the cyclin-dependent kinase inhibitor p27Kip1 in acute myeloid leukemia

open access: yesHaematologica, 2017
P27Kip1 (p27) can prevent cell proliferation by inactivating cyclin-dependent kinases. This function is impaired upon phosphorylation of p27 at tyrosine residue 88. We observed that FLT3 and FLT3-ITD can directly bind and selectively phosphorylate p27 on
Ines Peschel   +8 more
doaj   +1 more source

The Escherichia coli phosphotyrosine proteome relates to core pathways and virulence. [PDF]

open access: yesPLoS Pathogens, 2013
While phosphotyrosine modification is an established regulatory mechanism in eukaryotes, it is less well characterized in bacteria due to low prevalence. To gain insight into the extent and biological importance of tyrosine phosphorylation in Escherichia
Anne-Marie Hansen   +14 more
doaj   +1 more source

Tyrosine phosphorylation of myosin heavy chain during skeletal muscle differentiation: an integrated bioinformatics approach [PDF]

open access: yes, 2005
Background: Previously it has been shown that insulin-mediated tyrosine phosphorylation of myosin heavy chain is concomitant with enhanced association of C-terminal SRC kinase during skeletal muscle differentiation. We sought to identify putative site(s)
RJ Edwards   +8 more
core   +1 more source

EGF regulates tyrosine phosphorylation and membrane-translocation of the scaffold protein Tks5 [PDF]

open access: yes, 2013
Background: Tks5/FISH is a scaffold protein comprising of five SH3 domains and one PX domain. Tks5 is a substrate of the tyrosine kinase Src and is required for the organization of podosomes/invadopodia implicated in invasion of tumor cells.
Geiszt, Miklós   +5 more
core   +1 more source

3',5'-Cyclic Adenosine Monophosphate- and Ca2+-Calmodulin-Dependent Endogenous Protein Phosphorylation Activity in Membranes of the Bovine Chromaffin Secretory Vesicles: Identification of Two Phosphorylated Components as Tyrosine Hydroxylase and Protein Kinase Regulatory Subunit Type II [PDF]

open access: yes, 1983
: Membranes of the secretory vesicles from bovine adrenal medulla were investigated for the presence of the endogenous protein phosphorylation activity. Seven phosphoprotein bands in the molecular weight range of 250,000 to 30,000 were observed by means ...
Weber, W., Treiman, M., Gratzl, Manfred
core   +1 more source

Insulin Phosphorylates Tyrosine Residue 464 of Tub and Translocates Tubby into the Nucleus in HIRcB Cells [PDF]

open access: yesEndocrinology and Metabolism, 2014
BackgroundThe tubby protein has a motif that might be relevant for its action in the insulin signaling pathway. Previous studies have indicated that tubby undergoes phosphorylation on tyrosine residues in response to several stimuli and is known to ...
Jin Wook Kim   +3 more
doaj   +1 more source

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