18235846

Source:http://linkedlifedata.com/resource/pubmed/id/18235846

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0014323, umls-concept:C0014442, umls-concept:C0029277, umls-concept:C1880022
pubmed:issue	1
pubmed:dateCreated	2008-1-31
pubmed:databankReference	http://linkedlifedata.com/resource/pubmed/xref/GENBANK/AAX35675
pubmed:abstractText	The polyamines putrescine, spermidine, and spermine are organic cations that are required for cell growth and differentiation. Ornithine decarboxylase (ODC), the first and rate-limiting enzyme in the polyamine biosynthetic pathway, is a highly regulated enzyme.
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101291488
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Eflornithine, http://linkedlifedata.com/resource/pubmed/chemical/Ornithine, http://linkedlifedata.com/resource/pubmed/chemical/Ornithine Decarboxylase, http://linkedlifedata.com/resource/pubmed/chemical/Polyamines, http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
pubmed:status	MEDLINE
pubmed:issn	1935-2735
pubmed:author	pubmed-author:AnamikaKrishanpalK, pubmed-author:BakreAbhijeet AAA, pubmed-author:BhattacharyaAlokA, pubmed-author:BhattacharyaSudhaS, pubmed-author:JhingranAnupamA, pubmed-author:MadhubalaRentalaR, pubmed-author:PadmanabhanPrasad KPK, pubmed-author:SinghSushmaS, pubmed-author:SrinivasanNarayanaswamyN
pubmed:issnType	Electronic
pubmed:volume	2
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	e115
pubmed:meshHeading	pubmed-meshheading:18235846-Amino Acid Sequence, pubmed-meshheading:18235846-Blotting, Northern, pubmed-meshheading:18235846-Cloning, Molecular, pubmed-meshheading:18235846-Eflornithine, pubmed-meshheading:18235846-Electrophoresis, Gel, Pulsed-Field, pubmed-meshheading:18235846-Entamoeba histolytica, pubmed-meshheading:18235846-Enzyme Activation, pubmed-meshheading:18235846-Humans, pubmed-meshheading:18235846-Molecular Sequence Data, pubmed-meshheading:18235846-Open Reading Frames, pubmed-meshheading:18235846-Ornithine, pubmed-meshheading:18235846-Ornithine Decarboxylase, pubmed-meshheading:18235846-Phylogeny, pubmed-meshheading:18235846-Polyamines, pubmed-meshheading:18235846-Protozoan Proteins, pubmed-meshheading:18235846-Recombinant Proteins, pubmed-meshheading:18235846-Sequence Homology, Amino Acid, pubmed-meshheading:18235846-Substrate Specificity
pubmed:year	2008
pubmed:articleTitle	Characterization of the Entamoeba histolytica ornithine decarboxylase-like enzyme.
pubmed:affiliation	School of Life Sciences, Jawaharlal Nehru University, New Delhi, India.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't