Report for Dimitriou PS

General

Full name :

First name :

Mail :

Zip Code :

City :

Country :

Email :

Phone :

Fax :

Website :

Directory :

References (3)

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