Identification of Phosphorylation Sites Altering Pollen Soluble Inorganic Pyrophosphatase Activity

Autor:	Deborah J, Eaves, Tamanna, Haque, Richard L, Tudor, Yoshimi, Barron, Cleidiane G, Zampronio, Nicholas P J, Cotton, Barend H J, de Graaf, Scott A, White, Helen J, Cooper, F Christopher H, Franklin, Jeffery F, Harper, Vernonica E, Franklin-Tong
Rok vydání:	2016
Předmět:	Substrate Specificity Tandem Mass Spectrometry Sequence Homology Nucleic Acid otorhinolaryngologic diseases Amino Acid Sequence Papaver Phosphorylation Phylogeny Plant Proteins Binding Sites Base Sequence Sequence Homology Amino Acid food and beverages Hydrogen Peroxide Articles Hydrogen-Ion Concentration Oxidants Isoenzymes Inorganic Pyrophosphatase Solubility Mutation Pollen Calcium Electrophoresis Polyacrylamide Gel Protein Kinases Chromatography Liquid
Zdroj:	Plant physiology. 173(3)
ISSN:	1532-2548
Popis:	Protein phosphorylation regulates numerous cellular processes. Identifying the substrates and protein kinases involved is vital to understand how these important posttranslational modifications modulate biological function in eukaryotic cells. Pyrophosphatases catalyze the hydrolysis of inorganic phosphate (PP
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::7004736ede7bd93ef9cae0603f6ab010 https://pubmed.ncbi.nlm.nih.gov/28126844 Zobrazit plný text záznamu