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| Title : Identification of lipases with activity towards monoacylglycerol by criterion of conserved cap architectures - Riegler-Berket_2018_Biochim.Biophys.Acta_1863_679 |
| Author(s) : Riegler-Berket L , Leitmeier A , Aschauer P , Dreveny I , Oberer M |
| Ref : Biochimica & Biophysica Acta , 1863 :679 , 2018 |
| Abstract : Riegler-Berket_2018_Biochim.Biophys.Acta_1863_679 |
| ESTHER : Riegler-Berket_2018_Biochim.Biophys.Acta_1863_679 |
| PubMedSearch : Riegler-Berket_2018_Biochim.Biophys.Acta_1863_679 |
| PubMedID: 29627382 |
| Gene_locus related to this paper: 9bact-TtEst , agrvs-b9jym4 , bac25-mglp , bacsu-cbxnp , human-MGLL , symth-q67mr3 , vibch-VC1974 , yeast-mgll |
| Title : Conformational plasticity and ligand binding of bacterial monoacylglycerol lipase - Rengachari_2013_J.Biol.Chem_288_31093 |
| Author(s) : Rengachari S , Aschauer P , Schittmayer M , Mayer N , Gruber K , Breinbauer R , Birner-Gruenberger R , Dreveny I , Oberer M |
| Ref : Journal of Biological Chemistry , 288 :31093 , 2013 |
| Abstract : Rengachari_2013_J.Biol.Chem_288_31093 |
| ESTHER : Rengachari_2013_J.Biol.Chem_288_31093 |
| PubMedSearch : Rengachari_2013_J.Biol.Chem_288_31093 |
| PubMedID: 24014019 |
| Gene_locus related to this paper: bac25-mglp |
| Title : The structure of monoacylglycerol lipase from Bacillus sp. H257 reveals unexpected conservation of the cap architecture between bacterial and human enzymes - Rengachari_2012_Biochim.Biophys.Acta_1821_1012 |
| Author(s) : Rengachari S , Bezerra GA , Riegler-Berket L , Gruber CC , Sturm C , Taschler U , Boeszoermenyi A , Dreveny I , Zimmermann R , Gruber K , Oberer M |
| Ref : Biochimica & Biophysica Acta , 1821 :1012 , 2012 |
| Abstract : Rengachari_2012_Biochim.Biophys.Acta_1821_1012 |
| ESTHER : Rengachari_2012_Biochim.Biophys.Acta_1821_1012 |
| PubMedSearch : Rengachari_2012_Biochim.Biophys.Acta_1821_1012 |
| PubMedID: 22561231 |
| Gene_locus related to this paper: bac25-mglp |
| Title : Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity - Dreveny_2009_Biochemistry_48_3370 |
| Author(s) : Dreveny I , Andryushkova AS , Glieder A , Gruber K , Kratky C |
| Ref : Biochemistry , 48 :3370 , 2009 |
| Abstract : Dreveny_2009_Biochemistry_48_3370 |
| ESTHER : Dreveny_2009_Biochemistry_48_3370 |
| PubMedSearch : Dreveny_2009_Biochemistry_48_3370 |
| PubMedID: 19256550 |
| Title : Comprehensive step-by-step engineering of an (R)-hydroxynitrile lyase for large-scale asymmetric synthesis - |
| Author(s) : Glieder A , Weis R , Skranc W , Poechlauer P , Dreveny I , Majer S , Wubbolts M , Schwab H , Gruber K |
| Ref : Angew Chem Int Ed Engl , 42 :4815 , 2003 |
| PubMedID: 14562357 |
| Title : The active site of hydroxynitrile lyase from Prunus amygdalus: modeling studies provide new insights into the mechanism of cyanogenesis - Dreveny_2002_Protein.Sci_11_292 |
| Author(s) : Dreveny I , Kratky C , Gruber K |
| Ref : Protein Science , 11 :292 , 2002 |
| Abstract : Dreveny_2002_Protein.Sci_11_292 |
| ESTHER : Dreveny_2002_Protein.Sci_11_292 |
| PubMedSearch : Dreveny_2002_Protein.Sci_11_292 |
| PubMedID: 11790839 |
| Title : The hydroxynitrile lyase from almond: a lyase that looks like an oxidoreductase - Dreveny_2001_Structure_9_803 |
| Author(s) : Dreveny I , Gruber K , Glieder A , Thompson A , Kratky C |
| Ref : Structure , 9 :803 , 2001 |
| Abstract : Dreveny_2001_Structure_9_803 |
| ESTHER : Dreveny_2001_Structure_9_803 |
| PubMedSearch : Dreveny_2001_Structure_9_803 |
| PubMedID: 11566130 |