Zobrazeno 1 - 10
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pro vyhledávání: '"David Kerk"'
Autor:
David Kerk, Jordan F. Mattice, Mario E. Valdés-Tresanco, Sergei Yu Noskov, Kenneth K.-S. Ng, Greg B. Moorhead
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
Abstract Phosphoprotein phosphatase (PPP) enzymes are ubiquitous proteins involved in cellular signaling pathways and other functions. Here we have traced the origin of the PPP sequences of Eukaryotes and their radiation. Using a bacterial PPP Hidden
Externí odkaz:
https://doaj.org/article/3b06f50c4dba434391b0f94c6280040b
Autor:
David Kerk, Mario E. Valdés-Tresanco, Ryan Toth, Sergei Yu. Noskov, Kenneth K.-S. Ng, Greg B. Moorhead
Publikováno v:
BBA Advances, Vol 1, Iss , Pp 100005- (2021)
Background: Phosphoprotein phosphatases (PPP) belong to the PPP Sequence family, which in turn belongs to the broader metallophosphoesterase (MPE) superfamily. The relationship between the PPP Sequence family and other members of the MPE superfamily
Externí odkaz:
https://doaj.org/article/de6d77dcf5ea48508a1691d8b862e2d7
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0132863 (2015)
Mg+2/Mn+2-dependent type 2C protein phosphatases (PP2Cs) are ubiquitous in eukaryotes, mediating diverse cellular signaling processes through metal ion catalyzed dephosphorylation of target proteins. We have identified a distinct PP2C sequence class
Externí odkaz:
https://doaj.org/article/ae3f086ac00f4d6eaaf04463a78eef6c
Publikováno v:
Bioscience Reports. 43
Phosphoprotein phosphatases (PPPs) are a ubiquitous class of enzymes which dephosphorylate serine and threonine residues on substrate proteins involved in a wide variety of cellular processes. The active site of PPP enzymes are highly conserved with
Autor:
Sergei Y. Noskov, Kenneth K.-S. Ng, David Kerk, Jordan F. Mattice, Greg B. G. Moorhead, Mario E. Valdés-Tresanco
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
Scientific Reports
Scientific Reports
Phosphoprotein phosphatase (PPP) enzymes are ubiquitous proteins involved in cellular signaling pathways and other functions. Here we have traced the origin of the PPP sequences of Eukaryotes and their radiation. Using a bacterial PPP Hidden Markov M
Publikováno v:
Biochemical and Biophysical Research Communications. 458:739-744
Protein phosphatase 2A (PP2A) is a major serine/threonine phosphatase of eukaryotes. PP2A containing the B55 subunit is a key regulator of mitosis and must be inhibited by phosphorylated α–endosulfine (ENSA) or cyclic AMP-regulated 19 kDa phosphop
Publikováno v:
Plant Physiology. 163:1829-1843
Protein phosphorylation is a reversible regulatory process catalyzed by the opposing reactions of protein kinases and phosphatases, which are central to the proper functioning of the cell. Dysfunction of members in either the protein kinase or phosph
Publikováno v:
PLoS ONE, Vol 10, Iss 8, p e0132863 (2015)
PLoS ONE
PLoS ONE
Mg+2/Mn+2-dependent type 2C protein phosphatases (PP2Cs) are ubiquitous in eukaryotes, mediating diverse cellular signaling processes through metal ion catalyzed dephosphorylation of target proteins. We have identified a distinct PP2C sequence class
Autor:
David Kerk, Terry Conley, Douglas G. Muench, Flor A. Rodriguez, Hue T. Tran, Greg B. G. Moorhead, Mhairi Nimick
Publikováno v:
The Plant Journal. 46:400-413
Dual-specificity protein phosphatases (DSPs) are important regulators of a wide variety of protein kinase signaling cascades in animals, fungi and plants. We previously identified a cluster of putative DSPs in Arabidopsis (including At3g52180 and At3
Publikováno v:
Plant Physiology. 131:1209-1219
We have collected a set of 44 Arabidopsis proteins with similarity to the USPA (universal stress protein A ofEscherichia coli) domain of bacteria. The USPA domain is found either in small proteins, or it makes up the N-terminal portion of a larger pr