Source:http://linkedlifedata.com/resource/pubmed/id/21518817
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rdf:type | |
lifeskim:mentions |
umls-concept:C0003732,
umls-concept:C0012899,
umls-concept:C0015161,
umls-concept:C0015219,
umls-concept:C0018270,
umls-concept:C0035552,
umls-concept:C0035820,
umls-concept:C0040711,
umls-concept:C0042774,
umls-concept:C0439855,
umls-concept:C0851285,
umls-concept:C1335642,
umls-concept:C1554080,
umls-concept:C1706198,
umls-concept:C2347858
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pubmed:issue |
3
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pubmed:dateCreated |
2011-4-26
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pubmed:abstractText |
When the functions of a protein serve a useful survival and unique purpose, the selective pressures of evolutionary laws of nature conserve the DNA sequences encoding such proteins. In many instances, the conservation of these sequences has occurred since the inception of life on earth to the present in phylogenetically related species. The unique function(s) of metallopanstimulin (MPS-1/RPS27) ribosomal protein (RP) and a limited number of other RPs, in growth regulation, and viral infection is further documented here. Based on the correlation of information concerning Genome Context Analysis, and new information presented here, the author proposes that neutralization or elimination of ribosomal MPS-1/S27 DNA, mRNA or translated protein in eukaryote cells, initiated in the process of chemical, viral or radiation carcinogenesis can result in control of most carcinogenic processes by selective elimination of transformed cells which display overexpression of RPMPS-1/S27, and/or non-lethal pathogenic mutations of RPMPS-1/S27 gene. Recently, critical interactions were reported between RPMPS-1/S27 and p53 induced by DNA damage such as ionizing radiation, or chemotherapy drugs, that result in the activation of p53 which in turn represses RPMPS-1/S27 actions. Thus, p53, RPS27L, and RPS27/MPS-1) regulate growth and survival.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Metalloproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RPS27 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ribosomal Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
1790-6295
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
105-26
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pubmed:meshHeading |
pubmed-meshheading:21518817-Archaea,
pubmed-meshheading:21518817-Cell Division,
pubmed-meshheading:21518817-DNA Repair,
pubmed-meshheading:21518817-Eukaryotic Cells,
pubmed-meshheading:21518817-Herpesvirus 1, Human,
pubmed-meshheading:21518817-Herpesvirus 2, Human,
pubmed-meshheading:21518817-Humans,
pubmed-meshheading:21518817-Metalloproteins,
pubmed-meshheading:21518817-Nuclear Proteins,
pubmed-meshheading:21518817-Protein Biosynthesis,
pubmed-meshheading:21518817-RNA-Binding Proteins,
pubmed-meshheading:21518817-Ribosomal Proteins,
pubmed-meshheading:21518817-Virus Replication
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pubmed:articleTitle |
Conservation of multifunctional ribosomal protein metallopanstimulin-1 (RPS27) through complex evolution demonstrates its key role in growth regulation in Archaea, eukaryotic cells, DNA repair, translation and viral replication.
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pubmed:affiliation |
Antagoras Agrobusiness, LLC., Biotechnology, Chesterfield, MO 63017-3446, USA. fernandezpol@earthlink.net
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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