Year |
Citation |
Score |
2022 |
Al Adem K, Ferreira JC, Fadl S, Rabeh WM. pH profiles of 3-chymotrypsin-like protease (3CLpro) from SARS-CoV-2 elucidate its catalytic mechanism and a histidine residue critical for activity. The Journal of Biological Chemistry. 299: 102790. PMID 36509143 DOI: 10.1016/j.jbc.2022.102790 |
0.315 |
|
2021 |
Ferreira JC, Fadl S, Villanueva AJ, Rabeh WM. Catalytic Dyad Residues His41 and Cys145 Impact the Catalytic Activity and Overall Conformational Fold of the Main SARS-CoV-2 Protease 3-Chymotrypsin-Like Protease. Frontiers in Chemistry. 9: 692168. PMID 34249864 DOI: 10.3389/fchem.2021.692168 |
0.356 |
|
2018 |
Nawaz MH, Ferreira JC, Nedyalkova L, Zhu H, Carrasco-López C, Kirmizialtin S, Rabeh WM. The Catalytic Inactivation of the N-half of Human Hexokinase 2 and Structural and Biochemical Characterization of its Mitochondrial Conformation. Bioscience Reports. PMID 29298880 DOI: 10.1042/Bsr20171666 |
0.362 |
|
2016 |
Rabeh W. Abstract A32: Structural and molecular mechanisms of human hexokinase 2 in cancer metabolism and apoptosis Molecular Cancer Research. 14. DOI: 10.1158/1557-3125.Metca15-A32 |
0.331 |
|
2016 |
Conrado Ferreira J, Cardoso T, Nascimento O, Rabeh W, Nantes I. Reactivity of Recombinant Cytoglobin with Peroxides and Amyloid Structure in Peroxide-Activated Cytoglobin Free Radical Biology and Medicine. 100: S22. DOI: 10.1016/J.Freeradbiomed.2016.10.052 |
0.332 |
|
2013 |
Naumov P, Yasuda N, Rabeh WM, Bernstein J. The elusive crystal structure of the neuraminidase inhibitor Tamiflu (oseltamivir phosphate): molecular details of action. Chemical Communications (Cambridge, England). 49: 1948-50. PMID 23370708 DOI: 10.1039/C3Cc38801H |
0.314 |
|
2012 |
Rabeh WM, Bossard F, Xu H, Okiyoneda T, Bagdany M, Mulvihill CM, Du K, di Bernardo S, Liu Y, Konermann L, Roldan A, Lukacs GL. Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function. Cell. 148: 150-63. PMID 22265408 DOI: 10.1016/J.Cell.2011.11.024 |
0.307 |
|
2008 |
Tai CH, Rabeh WM, Guan R, Schnackerz KD, Cook PF. Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction. Archives of Biochemistry and Biophysics. 472: 115-25. PMID 18275838 DOI: 10.1016/J.Abb.2008.01.021 |
0.661 |
|
2008 |
Tai CH, Rabeh WM, Guan R, Schnackerz KD, Cook PF. Effect of mutation of lysine-120, located at the entry to the active site of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. Biochimica Et Biophysica Acta. 1784: 629-37. PMID 18243146 DOI: 10.1016/J.Bbapap.2007.12.017 |
0.663 |
|
2007 |
Tempel W, Rabeh WM, Bogan KL, Belenky P, Wojcik M, Seidle HF, Nedyalkova L, Yang T, Sauve AA, Park HW, Brenner C. Nicotinamide riboside kinase structures reveal new pathways to NAD+. Plos Biology. 5: e263. PMID 17914902 DOI: 10.1371/Journal.Pbio.0050263 |
0.415 |
|
2007 |
Bum SH, Senisterra G, Rabeh WM, Vedadi M, Leonardi R, Zhang YM, Rock CO, Jackowski S, Park HW. Crystal structures of human pantothenate kinases: Insights into allosteric regulation and mutations linked to a neurodegeneration disorder Journal of Biological Chemistry. 282: 27984-27993. PMID 17631502 DOI: 10.1074/Jbc.M701915200 |
0.364 |
|
2007 |
Chattopadhyay A, Meier M, Ivaninskii S, Burkhard P, Speroni F, Campanini B, Bettati S, Mozzarelli A, Rabeh WM, Li L, Cook PF. Structure, mechanism, and conformational dynamics of O-acetylserine sulfhydrylase from Salmonella typhimurium: comparison of A and B isozymes. Biochemistry. 46: 8315-30. PMID 17583914 DOI: 10.1021/Bi602603C |
0.612 |
|
2006 |
Rabeh WM, Mather T, Cook PF. A three-dimensional homology model of the O-acetylserine sulfhydrylase-B from Salmonella typhimurium. Protein and Peptide Letters. 13: 7-13. PMID 16454663 DOI: 10.2174/092986606774502126 |
0.553 |
|
2005 |
Rabeh WM, Alguindigue SS, Cook PF. Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction. Biochemistry. 44: 5541-50. PMID 15807548 DOI: 10.1021/Bi047479I |
0.586 |
|
2004 |
Rabeh WM, Cook PF. Structure and mechanism of O-acetylserine sulfhydrylase Journal of Biological Chemistry. 279: 26803-26806. PMID 15073190 DOI: 10.1074/Jbc.R400001200 |
0.627 |
|
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