Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Maria L. McGlone"'
Autor:
Sulyman Barkho, Levi C T Pierce, Maria L McGlone, Sheng Li, Virgil L Woods, Ross C Walker, Joseph A Adams, Patricia A Jennings
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 9, p e1003188 (2013)
The Src family of tyrosine kinases (SFKs) regulate numerous aspects of cell growth and differentiation and are under the principal control of the C-terminal Src Kinase (Csk). Csk and SFKs share a modular design with the kinase domain downstream of th
Externí odkaz:
https://doaj.org/article/bfbd58ccdb684fed88493358920fc89e
Autor:
Ryan M. Plocinik, Chen-Ting Ma, Jonathan C. Hagopian, Joseph A. Adams, Brandon E. Aubol, Maria L. McGlone, Reeti Bandyopadhyay, Xiang-Dong Fu
Publikováno v:
Journal of Molecular Biology. 425:2894-2909
SR proteins are essential splicing factors whose biological function is regulated through phosphorylation of their C-terminal RS domains. Prior studies have shown that cytoplasmic-nuclear translocalization of the SR protein SRSF1 is regulated by mult
Autor:
Brandon E. Aubol, Malik M. Keshwani, Laurent Fattet, Joseph A. Adams, Kendra L. Hailey, Patricia A. Jennings, Maria L. McGlone
Publikováno v:
The Biochemical journal, vol 472, iss 3
Phosphorylation-dependent cell communication requires enzymes that specifically recognize key proteins in a sea of similar, competing substrates. The protein kinases achieve this goal by utilizing docking grooves in the kinase domain or heterologous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeaa8a69d402f3f16fc6822d04bb7abf
https://escholarship.org/uc/item/4mr327sw
https://escholarship.org/uc/item/4mr327sw
Autor:
Jonathan C. Hagopian, Ryan M. Plocinik, Brandon E. Aubol, Gourisankar Ghosh, Xiang-Dong Fu, Joseph A. Adams, Malik M. Keshwani, Maria L. McGlone
Publikováno v:
The Biochemical journal, vol 462, iss 1
SR proteins are essential splicing factors that are regulated through multisite phosphorylation of their RS (arginine/serine-rich) domains by two major families of protein kinases. The SRPKs (SR-specific protein kinases) efficiently phosphorylate the
Publikováno v:
Protein Engineering Design and Selection. 10:915-925
When the catalytic (rC) subunit of cAMP-dependent protein kinase (cAPK) is expressed in Escherichia coli, it is autophosphorylated at four sites, Ser10, Ser139, Ser338 and Thr197 (49). Three of these sites, Ser10, Ser338 and Thr197, are also found in
Publikováno v:
Journal of Biological Chemistry. 272:16946-16954
A glycine-rich loop in the ATP-binding site is one of the most highly conserved sequence motifs in protein kinases. Each conserved glycine (Gly-50, Gly-52, and Gly-55) in the catalytic (C) subunit of cAMP-dependent protein kinase (cAPK) was replaced
Publikováno v:
Protein Science. 6:569-579
All eukaryotic protein kinases share a conserved catalytic core. In the catalytic (C) subunit of cAMP-dependent protein kinase (cAPK) this core is preceded by a myristylation motif followed by a long helix with Trp 30 at the end of this A-helix filli
Recombinant Strategies for Rapid Purification of Catalytic Subunits of cAMP-Dependent Protein Kinase
Publikováno v:
Analytical Biochemistry. 245:115-122
Knowledge of the crystal structure of the catalytic subunit (C) of cAMP-dependent protein kinase provided for the first time a molecular basis for probing function by site-directed mutagenesis. The purification of mutant C-subunits, however, presente
The splicing function of SR proteins is regulated by multisite phosphorylation of their C-terminal RS (arginine-serine rich) domains. SRPK1 has been shown to phosphorylate the prototype SR protein SRSF1 using a directional mechanism in which 11 serin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6d0a57e27c26645a87437c5a41b9a37
https://europepmc.org/articles/PMC3865722/
https://europepmc.org/articles/PMC3865722/
Publikováno v:
Biochemistry. 34:2447-2454
Site-directed mutagenesis was used to remove a critical phosphorylation site, Thr-197, near the active site of the catalytic subunit of cAMP-dependent protein kinase. This residue is present in a number of protein kinases, and its phosphorylation lar