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Wael Rabeh is Associate Professor of Chemistry in the Division of Science at New York University Abu Dhabi. He received his BS from Damascus University and PhD in Biochemistry from the University of Oklahoma, where he worked in Professor Paul F. Cook's laboratory characterizing the final enzymatic step of the cysteine biosynthetic pathway in Salmonella typhimurium. In 2005, Rabeh joined the Structural Genomic Consortium at the University of Toronto as a postdoctoral fellow, determining three-dimensional structures of medically relevant human proteins via X-ray crystallography. In 2007, he moved to Dr. Gergely Lukacs' laboratory at McGill University to investigate the cystic fibrosis transmembrane conductance regulator (CFTR) membrane channel. His research program at NYU Abu Dhabi elucidates protein structures and mechanisms to comprehend biological functions, with a focus on disease-related proteins to facilitate therapeutic development using structural data and simulations. Primary targets encompass human Hexokinase 2, critical for tumor initiation and proliferation, alongside bioluminescent luciferases from diverse species to decode light-emitting color mechanisms.
Rabeh has published extensively in premier journals, including Cell on correcting ΔF508 CFTR folding and function (2012), Science on peripheral quality control of unfolded CFTR (2010), and PLoS Biology on nicotinamide riboside kinase structures revealing NAD+ pathways (2007). Additional key works cover O-acetylserine sulfhydrylase mechanisms (Biochemistry, 2005 and 2007), SARS-CoV-2 main protease catalytic dyad (2021), and structural analyses of neuraminidase inhibitors Zanamivir and Tamiflu (Crystal Growth & Design and Chemical Communications, 2013). His contributions exhibit substantial academic impact, evidenced by highly cited papers such as the 2010 Science article (515 citations) and 2012 Cell paper (381 citations) per Google Scholar, advancing fields of enzymology, protein folding, and drug design.
