| Title : The active site of the SGNH hydrolase-like fold proteins: Nucleophile-oxyanion (Nuc-Oxy) and Acid-Base zones - Denessiouk_2024_Curr.Res.Struct.Biol_7_100123 |
| Author(s) : Denessiouk K , Denesyuk AI , Permyakov SE , Permyakov EA , Johnson MS , Uversky VN |
| Ref : Curr Res Struct Biol , 7 :100123 , 2024 |
| Abstract : Denessiouk_2024_Curr.Res.Struct.Biol_7_100123 |
| ESTHER : Denessiouk_2024_Curr.Res.Struct.Biol_7_100123 |
| PubMedSearch : Denessiouk_2024_Curr.Res.Struct.Biol_7_100123 |
| PubMedID: 38235349 |
| Title : The acid-base-nucleophile catalytic triad in ABH-fold enzymes is coordinated by a set of structural elements - Denesyuk_2020_PLoS.One_15_e0229376 |
| Author(s) : Denesyuk AI , Dimitriou PS , Johnson MS , Nakayama T , Denessiouk K |
| Ref : PLoS ONE , 15 :e0229376 , 2020 |
| Abstract : Denesyuk_2020_PLoS.One_15_e0229376 |
| ESTHER : Denesyuk_2020_PLoS.One_15_e0229376 |
| PubMedSearch : Denesyuk_2020_PLoS.One_15_e0229376 |
| PubMedID: 32084230 |
| Title : Distinctive structural motifs co-ordinate the catalytic nucleophile and the residues of the oxyanion hole in the alpha\/beta-hydrolase fold enzymes - Dimitriou_2019_Protein.Sci_28_344 |
| Author(s) : Dimitriou PS , Denesyuk AI , Nakayama T , Johnson MS , Denessiouk K |
| Ref : Protein Science , 28 :344 , 2019 |
| Abstract : Dimitriou_2019_Protein.Sci_28_344 |
| ESTHER : Dimitriou_2019_Protein.Sci_28_344 |
| PubMedSearch : Dimitriou_2019_Protein.Sci_28_344 |
| PubMedID: 30311984 |
| Title : Alpha\/beta-hydrolases: A unique structural motif coordinates catalytic acid residue in 40 protein fold families - Dimitriou_2017_Proteins_85_1845 |
| Author(s) : Dimitriou PS , Denesyuk AI , Takahashi S , Yamashita S , Johnson MS , Nakayama T , Denessiouk K |
| Ref : Proteins , 85 :1845 , 2017 |
| Abstract : Dimitriou_2017_Proteins_85_1845 |
| ESTHER : Dimitriou_2017_Proteins_85_1845 |
| PubMedSearch : Dimitriou_2017_Proteins_85_1845 |
| PubMedID: 28643343 |