| pubmed-article:12659754 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12659754 | lifeskim:mentions | umls-concept:C0008109 | lld:lifeskim |
| pubmed-article:12659754 | lifeskim:mentions | umls-concept:C0017817 | lld:lifeskim |
| pubmed-article:12659754 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:12659754 | lifeskim:mentions | umls-concept:C0220825 | lld:lifeskim |
| pubmed-article:12659754 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:12659754 | lifeskim:mentions | umls-concept:C0443288 | lld:lifeskim |
| pubmed-article:12659754 | lifeskim:mentions | umls-concept:C0243071 | lld:lifeskim |
| pubmed-article:12659754 | lifeskim:mentions | umls-concept:C0205460 | lld:lifeskim |
| pubmed-article:12659754 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:12659754 | pubmed:dateCreated | 2003-3-27 | lld:pubmed |
| pubmed-article:12659754 | pubmed:abstractText | The two novel diastereoisomeric glutathione analogues 1 and 2 have been designed and synthesized by replacing the native gamma-glutamylic moiety with the conformational rigid skeleton of cis- or trans-4-carboxy-L-proline residue. Both analogues have been obtained by following the solution phase peptide chemistry methodologies and final reduction of the corresponding disulfide forms 13 and 14. The two analogues 1 and 2 have been tested towards gamma-glutamyltranspeptidase (gamma-GT) and human glutathione S-transferase (hGST P1-1). Both analogues 1 and 2 are completely resistant to enzymatic degradation by gamma-GT. The S-transferase utilizes the analogue 2 as a good substrate while is unable to bind the analogue 1. | lld:pubmed |
| pubmed-article:12659754 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12659754 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12659754 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12659754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12659754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12659754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12659754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12659754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12659754 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12659754 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12659754 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12659754 | pubmed:issn | 0968-0896 | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:LucenteGinoG | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:RicciGiorgioG | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:CaccuriAnna... | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:PinnenFrances... | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:Di... | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:CacciatoreIva... | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:ParadisiMario... | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:MollicaAdrian... | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:DuprèSilvestr... | lld:pubmed |
| pubmed-article:12659754 | pubmed:author | pubmed-author:SpiritoAlessa... | lld:pubmed |
| pubmed-article:12659754 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12659754 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:12659754 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:12659754 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12659754 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12659754 | pubmed:pagination | 1677-83 | lld:pubmed |
| pubmed-article:12659754 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:meshHeading | pubmed-meshheading:12659754... | lld:pubmed |
| pubmed-article:12659754 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12659754 | pubmed:articleTitle | Proline-glutamate chimeras in isopeptides. Synthesis and biological evaluation of conformationally restricted glutathione analogues. | lld:pubmed |
| pubmed-article:12659754 | pubmed:affiliation | Istituto di Chimica Biomolecolare, CNR Sezione di Roma, c/o Dipartimento di Studi Farmaceutici, Università di Roma La Sapienza, P.le A. Moro, 00185 Rome, Italy. | lld:pubmed |
| pubmed-article:12659754 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12659754 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
