pubmed-article:2048935 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2048935 | lifeskim:mentions | umls-concept:C0036025 | lld:lifeskim |
pubmed-article:2048935 | lifeskim:mentions | umls-concept:C0031165 | lld:lifeskim |
pubmed-article:2048935 | lifeskim:mentions | umls-concept:C0001128 | lld:lifeskim |
pubmed-article:2048935 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:2048935 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:2048935 | lifeskim:mentions | umls-concept:C0205246 | lld:lifeskim |
pubmed-article:2048935 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:2048935 | pubmed:dateCreated | 1991-7-15 | lld:pubmed |
pubmed-article:2048935 | pubmed:abstractText | Addition of the L-proline analogue L-azetidine 2-carboxylic acid to growing cultures of Saccharomyces cerevisiae var. ellipsoideus promoted fast deactivation of the general aminoacid permease, measured as L-valine uptake, without an immediate decrease in the growth rate. Cells preincubated with the analogue for 3 h were unable to restore either growth ability or general aminoacid permease activity in analogue-free medium. Eadie-Hofstee plots of L-valine uptake in the presence of the analogue are consistent with a strong reduction in the number of active molecules of the general amino-acid permease located in the plasma membrane. Inhibitory effects on protein synthesis were seen after preincubations of the yeast with the analogue for 3 h although a 30 min preincubation had no effect. | lld:pubmed |
pubmed-article:2048935 | pubmed:language | eng | lld:pubmed |
pubmed-article:2048935 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2048935 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2048935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2048935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2048935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2048935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2048935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2048935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2048935 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2048935 | pubmed:issn | 0302-8933 | lld:pubmed |
pubmed-article:2048935 | pubmed:author | pubmed-author:MuñozRR | lld:pubmed |
pubmed-article:2048935 | pubmed:author | pubmed-author:GirbésTT | lld:pubmed |
pubmed-article:2048935 | pubmed:author | pubmed-author:IglesiasRR | lld:pubmed |
pubmed-article:2048935 | pubmed:author | pubmed-author:FerrerasJ MJM | lld:pubmed |
pubmed-article:2048935 | pubmed:author | pubmed-author:AriasF JFJ | lld:pubmed |
pubmed-article:2048935 | pubmed:author | pubmed-author:RojoM AMA | lld:pubmed |
pubmed-article:2048935 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2048935 | pubmed:volume | 155 | lld:pubmed |
pubmed-article:2048935 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2048935 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2048935 | pubmed:pagination | 320-4 | lld:pubmed |
pubmed-article:2048935 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:2048935 | pubmed:meshHeading | pubmed-meshheading:2048935-... | lld:pubmed |
pubmed-article:2048935 | pubmed:meshHeading | pubmed-meshheading:2048935-... | lld:pubmed |
pubmed-article:2048935 | pubmed:meshHeading | pubmed-meshheading:2048935-... | lld:pubmed |
pubmed-article:2048935 | pubmed:meshHeading | pubmed-meshheading:2048935-... | lld:pubmed |
pubmed-article:2048935 | pubmed:meshHeading | pubmed-meshheading:2048935-... | lld:pubmed |
pubmed-article:2048935 | pubmed:meshHeading | pubmed-meshheading:2048935-... | lld:pubmed |
pubmed-article:2048935 | pubmed:meshHeading | pubmed-meshheading:2048935-... | lld:pubmed |
pubmed-article:2048935 | pubmed:meshHeading | pubmed-meshheading:2048935-... | lld:pubmed |
pubmed-article:2048935 | pubmed:meshHeading | pubmed-meshheading:2048935-... | lld:pubmed |
pubmed-article:2048935 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:2048935 | pubmed:articleTitle | Effect of L-azetidine 2-carboxilic acid on the activity of the general amino-acid permease from Saccharomyces cerevisiae var. ellipsoideus. | lld:pubmed |
pubmed-article:2048935 | pubmed:affiliation | Departamento de Bioquímica, Biología Molecular y Fisiología, Facultad de Ciencias, Universidad de Valladolid, Spain. | lld:pubmed |
pubmed-article:2048935 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2048935 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2048935 | lld:pubmed |