8736867

Source:http://linkedlifedata.com/resource/pubmed/id/8736867

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0086418, umls-concept:C0106453, umls-concept:C1514562
pubmed:issue	2
pubmed:dateCreated	1996-12-16
pubmed:databankReference	http://linkedlifedata.com/resource/pubmed/xref/GENBANK/U30313
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/7506897
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Acid Anhydride Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Pyrophosphatases, http://linkedlifedata.com/resource/pubmed/chemical/bis(5'-nucleosyl)tetraphosphatase..., http://linkedlifedata.com/resource/pubmed/chemical/mutT protein, E coli
pubmed:status	MEDLINE
pubmed:month	May
pubmed:issn	0300-5127
pubmed:author	pubmed-author:BarracloughRR, pubmed-author:HankinSS, pubmed-author:McLennanA GAG, pubmed-author:NuñezCC, pubmed-author:ThorneN MNM, pubmed-author:WilkinsonM CMC
pubmed:issnType	Print
pubmed:volume	24
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	209S
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:8736867-Acid Anhydride Hydrolases, pubmed-meshheading:8736867-Amino Acid Sequence, pubmed-meshheading:8736867-Bacterial Proteins, pubmed-meshheading:8736867-Conserved Sequence, pubmed-meshheading:8736867-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:8736867-Escherichia coli Proteins, pubmed-meshheading:8736867-Female, pubmed-meshheading:8736867-Humans, pubmed-meshheading:8736867-Molecular Sequence Data, pubmed-meshheading:8736867-Peptide Fragments, pubmed-meshheading:8736867-Phosphoric Monoester Hydrolases, pubmed-meshheading:8736867-Placenta, pubmed-meshheading:8736867-Pregnancy, pubmed-meshheading:8736867-Protein Structure, Secondary, pubmed-meshheading:8736867-Pyrophosphatases, pubmed-meshheading:8736867-Saccharomyces cerevisiae, pubmed-meshheading:8736867-Sequence Homology, Amino Acid
pubmed:year	1996
pubmed:articleTitle	Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase (Ap4A hydrolase) possesses a MutT motif.
pubmed:affiliation	Department of Biochemistry, University of Liverpool, UK.
pubmed:publicationType	Journal Article, Comparative Study, Research Support, Non-U.S. Gov't