Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5704
pubmed:dateCreated
2004-12-17
pubmed:abstractText
The inositol pyrophosphates IP7 and IP8 contain highly energetic pyrophosphate bonds. Although implicated in various biologic functions, their molecular sites of action have not been clarified. Using radiolabeled IP7, we detected phosphorylation of multiple eukaryotic proteins. We also observed phosphorylation of endogenous proteins by endogenous IP7 in yeast. Phosphorylation by IP7 is nonenzymatic and may represent a novel intracellular signaling mechanism.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1-diphosphoinositol..., http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Magnesium, http://linkedlifedata.com/resource/pubmed/chemical/NSR1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Phosphate..., http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serine
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
17
pubmed:volume
306
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2101-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15604408-Adenosine Triphosphate, pubmed-meshheading:15604408-Amino Acid Sequence, pubmed-meshheading:15604408-Amino Acid Substitution, pubmed-meshheading:15604408-Animals, pubmed-meshheading:15604408-Drosophila Proteins, pubmed-meshheading:15604408-Drosophila melanogaster, pubmed-meshheading:15604408-Escherichia coli Proteins, pubmed-meshheading:15604408-Humans, pubmed-meshheading:15604408-Inositol Phosphates, pubmed-meshheading:15604408-Kinetics, pubmed-meshheading:15604408-Magnesium, pubmed-meshheading:15604408-Mice, pubmed-meshheading:15604408-Molecular Sequence Data, pubmed-meshheading:15604408-Mutation, pubmed-meshheading:15604408-Nuclear Proteins, pubmed-meshheading:15604408-Phosphates, pubmed-meshheading:15604408-Phosphorylation, pubmed-meshheading:15604408-Phosphotransferases (Phosphate Group Acceptor), pubmed-meshheading:15604408-Protein Kinases, pubmed-meshheading:15604408-Proteins, pubmed-meshheading:15604408-RNA-Binding Proteins, pubmed-meshheading:15604408-Saccharomyces cerevisiae, pubmed-meshheading:15604408-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15604408-Serine, pubmed-meshheading:15604408-Signal Transduction, pubmed-meshheading:15604408-Temperature
pubmed:year
2004
pubmed:articleTitle
Phosphorylation of proteins by inositol pyrophosphates.
pubmed:affiliation
Department of Neuroscience, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.