| pubmed-article:9660932 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9660932 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:9660932 | lifeskim:mentions | umls-concept:C0035711 | lld:lifeskim |
| pubmed-article:9660932 | lifeskim:mentions | umls-concept:C0079380 | lld:lifeskim |
| pubmed-article:9660932 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:9660932 | lifeskim:mentions | umls-concept:C1537998 | lld:lifeskim |
| pubmed-article:9660932 | lifeskim:mentions | umls-concept:C0301625 | lld:lifeskim |
| pubmed-article:9660932 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9660932 | pubmed:dateCreated | 1998-7-28 | lld:pubmed |
| pubmed-article:9660932 | pubmed:abstractText | According to the prevailing model, frameshift-suppressing tRNAs with an extra nucleotide in the anticodon loop suppress +1 frameshift mutations by recognizing a four-base codon and promoting quadruplet translocation. We present three sets of experiments that suggest a general alternative to this model. First, base modification should actually block such a four-base interaction by two classical frameshift suppressors. Second, for one Salmonella suppressor tRNA, it is not mutant tRNA but a structurally normal near cognate that causes the +1 shift in-frame. Finally, frameshifting occurs in competition with normal decoding of the next in-frame codon, consistent with an event that occurs in the ribosomal P site after the translocation step. These results suggest an alternative model involving peptidyl-tRNA slippage at the classical CCC-N and GGG-N frameshift suppression sites. | lld:pubmed |
| pubmed-article:9660932 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9660932 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9660932 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9660932 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9660932 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9660932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9660932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9660932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9660932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9660932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9660932 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9660932 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9660932 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9660932 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:9660932 | pubmed:author | pubmed-author:BjörkG RGR | lld:pubmed |
| pubmed-article:9660932 | pubmed:author | pubmed-author:FarabaughP... | lld:pubmed |
| pubmed-article:9660932 | pubmed:author | pubmed-author:ZhaoHH | lld:pubmed |
| pubmed-article:9660932 | pubmed:author | pubmed-author:LiJ NJN | lld:pubmed |
| pubmed-article:9660932 | pubmed:author | pubmed-author:HagervallT... | lld:pubmed |
| pubmed-article:9660932 | pubmed:author | pubmed-author:QianQQ | lld:pubmed |
| pubmed-article:9660932 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9660932 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:9660932 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9660932 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9660932 | pubmed:pagination | 471-82 | lld:pubmed |
| pubmed-article:9660932 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:meshHeading | pubmed-meshheading:9660932-... | lld:pubmed |
| pubmed-article:9660932 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9660932 | pubmed:articleTitle | A new model for phenotypic suppression of frameshift mutations by mutant tRNAs. | lld:pubmed |
| pubmed-article:9660932 | pubmed:affiliation | Department of Microbiology, Umeå University, Sweden. | lld:pubmed |
| pubmed-article:9660932 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9660932 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9660932 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9660932 | lld:pubmed |
