Wadih Ghattas
Bât. 420 – LCBB – ICMMO
Université Paris-Saclay
Rue du doyen Georges Poitou
91405 Orsay Cedex
FRANCE
+33 1 69 15 47 23
wadih.ghattas@u-psud.fr
https://orcid.org/0000-0001-6743-6253
An artificial metalloprotein with metal-adaptive coordination sites and Ni-dependent quercetinase activity. M. Beaumet, A. Dose, A. Bräuer, J.-P. Mahy, W. Ghattas, M. Groll, C. R. Hess, J. Inorg. Biochem., 2022, 235, 111914
Antimicrobial Activity of Cationic Poly(3-hexylthiophene) Nanoparticles Coupled with Dual Fluorescent and Electrochemical Sensing: Theragnostic Prospect. N. Elgiddawy, S. Ren, W. Ghattas, W. M. A. E. Rouby, A. O. El-Gendy, A. A. Farghali, A. Yassar, H. Korri-Youssoufi, Sensors, 2021, 21, 1715
Artificial enzymes for Diels-Alder reactions. W. Ghattas, J.-P. Mahy, M. Réglier, A. J. Simaan, ChemBioChem, 2021, 22, 443-459
Artificial iron hydrogenase made by covalent grafting of Knölker's complex into xylanase: Application in asymmetric hydrogenation of an aryl ketone in water. K. Kariyawasam, W. Ghattas, Y. L. D. L. Santos, N. Doucet, S. Gaillard, J.-L. Renaud, F. Avenier, J.-P. Mahy, R. Ricoux, Biotechnol. Appl. Biochem., 2020, 67, 563-573
CuII-Containing 1-Aminocyclopropane Carboxylic Acid Oxidase Is an Efficient Stereospecific Diels–Alderase. W. Ghattas, V. Dubosclard, S. Tachon, M. Beaumet, R. Guillot, M. Réglier, A. J. Simaan, J.-P. Mahy, Angew. Chem. Int. Ed., 2019, 58, 14605-14609
Functionalized Artificial Bidomain Proteins Based on an α-Solenoid Protein Repeat Scaffold: A New Class of Artificial Diels–Alderases. T. Di Meo, K. Kariyawasam, W. Ghattas, M. Valerio-Lepiniec, G. Sciortino, J.-D. Maréchal, P. Minard, J.-P. Mahy, A. Urvoas, R. Ricoux, ACS Omega, 2019, 4, 4437-4447
Receptor-based artificial metalloenzymes on living human cells. W. Ghattas, V. Dubosclard, A. Wick, A. Bendelac, R. Guillot, R. Ricoux, J.-P. Mahy, J. Am. Chem. Soc., 2018, 140, 8756-8762
Crystal Structure of Phosphomannose Isomerase from Candida albicans Complexed with 5‐Phospho‐D‐Arabinonhydrazide. L. Ahmad, S. Plancqueel, V. Dubosclard, N. Lazar, W. Ghattas, I. Li De La Sierra‐gallay, H. Van Tilbeurgh, L. Salmon, FEBS Lett., 2018, 592, 1667-1680
αRep A3: A versatile artificial scaffold for metalloenzyme design. T. Di Meo, W. Ghattas, C. Herrero, C. Velours, P. Minard, J.-P. Mahy, R. Ricoux, A. Urvoas, Chem. Eur. J., 2017, 23, 10156-10166
Artificial Metalloenzymes with the Neocarzinostatin Scaffold: Toward a Biocatalyst for the Diels–Alder Reaction. W. Ghattas, L. Cotchico-Alonso, J.-D. Maréchal, A. Urvoas, M. Rousseau, J.-P. Mahy, R. Ricoux, ChemBioChem, 2016, 17, 433-440
Synthesis and characterization of [Fe(BPMEN)ACC]SbF₆: a structural and functional mimic of ACC-oxidase. Y. Roux, W. Ghattas, F. Avenier, R. Guillot, A. J. Simaan, J.-P. Mahy, Dalton Trans., 2015, 44, 5966-5968
Neocarzinostatin-based hybrid biocatalysts with a RNase like activity. A. Urvoas, W. Ghattas, J.-D. Maréchal, F. Avenier, F. Bellande, W. Mao, R. Ricoux, J.-P. Mahy, Bioorg. Med. Chem., 2014, 22, 5678-5686
Neocarzinostatin-based hybrid biocatalysts for oxidation reactions. E. Sansiaume-Dagousset, A. Urvoas, K. Chelly, W. Ghattas, J.-D. Maréchal, J.-P. Mahy, R. Ricoux, Dalton Trans., 2014, 43, 8344-8354
A unique 1-amino-1-cyclopropane carboxylate cupric-cryptate hosting sodium. W. Ghattas, R. Ricoux, H. Korri-Youssoufi, R. Guillot, E. Riviere, J.-P. Mahy, Dalton Trans., 2014, 43, 7708-7711