Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:10983406rdf:typepubmed:Citationlld:pubmed
pubmed-article:10983406lifeskim:mentionsumls-concept:C0140649lld:lifeskim
pubmed-article:10983406lifeskim:mentionsumls-concept:C0449438lld:lifeskim
pubmed-article:10983406lifeskim:mentionsumls-concept:C0521116lld:lifeskim
pubmed-article:10983406pubmed:issue1lld:pubmed
pubmed-article:10983406pubmed:dateCreated2000-11-15lld:pubmed
pubmed-article:10983406pubmed:abstractTextRibosome inactivating proteins (RIPs) are a group of naturally occurring plant proteins with a RNA-N-glycosidases activity which depurinate rRNA at a specific universally conserved position (i.e. cleavage of N-glycosidic bond of a specific adenine of 28S rRNA). These proteins are found in different parts of plants, in concentrations ranging from a few micrograms to several hundred mg per 100 g of plant tissues. RIPs exist in two forms, type 1 having a single polypeptide chain with a molecular mass of approximately 30 kDa possessing N-glycosidase activity; and type 2 with two or four polypeptide chains having a molecular mass of approximately 60 kDa and approximately 120 kDa respectively showing lectin activity along with N-glycosidase moiety. Such biomolecules causing cytotoxicity are being exploited for designing immunotoxins/hormonotoxins using heterobifunctional conjugates. These carrier conjugates with the RIPs can influence cellular trafficking and inhibition of protein synthesis. We are witnessing a novel protein from plants that can be utilised for various therapeutical treatments ranging from cancers, AIDS and other viral diseases of present times.lld:pubmed
pubmed-article:10983406pubmed:languageenglld:pubmed
pubmed-article:10983406pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10983406pubmed:citationSubsetIMlld:pubmed
pubmed-article:10983406pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:10983406pubmed:statusMEDLINElld:pubmed
pubmed-article:10983406pubmed:monthFeblld:pubmed
pubmed-article:10983406pubmed:issn0301-1208lld:pubmed
pubmed-article:10983406pubmed:authorpubmed-author:SinghVVlld:pubmed
pubmed-article:10983406pubmed:authorpubmed-author:SinghR CRClld:pubmed
pubmed-article:10983406pubmed:issnTypePrintlld:pubmed
pubmed-article:10983406pubmed:volume37lld:pubmed
pubmed-article:10983406pubmed:ownerNLMlld:pubmed
pubmed-article:10983406pubmed:authorsCompleteYlld:pubmed
pubmed-article:10983406pubmed:pagination1-5lld:pubmed
pubmed-article:10983406pubmed:dateRevised2005-11-16lld:pubmed
pubmed-article:10983406pubmed:meshHeadingpubmed-meshheading:10983406...lld:pubmed
pubmed-article:10983406pubmed:meshHeadingpubmed-meshheading:10983406...lld:pubmed
pubmed-article:10983406pubmed:year2000lld:pubmed
pubmed-article:10983406pubmed:articleTitleCurrent status of ribosome inactivating proteins.lld:pubmed
pubmed-article:10983406pubmed:affiliationHormone Biochemistry Laboratory, North-Eastern Hill University, Meghalaya, India.lld:pubmed
pubmed-article:10983406pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10983406pubmed:publicationTypeReviewlld:pubmed