@article{park_liu_gardner_johnson_keeler_ortiz_rabah_ford_2020, title={Biohybrid nanofibers containing manganese oxide-forming fungi for heavy metal removal from water}, volume={15}, ISSN={["1558-9250"]}, DOI={10.1177/1558925019898954}, abstractNote={Manganese-oxidizing fungi support bioremediation through the conversion of manganese ions into manganese oxide deposits that in turn adsorb manganese and other heavy metal ions from the environment. Manganese-oxidizing fungi were immobilized onto nanofiber surfaces to assist remediation of heavy metal–contaminated water. Two fungal isolates, Coniothyrium sp. and Coprinellus sp., from a Superfund site (Lot 86, Farm Unit #1) water treatment system were incubated in the presence of nanofibers. Fungal hyphae had strong association with nanofiber surfaces. Upon fungal attachment to manganese chloride–seeded nanofibers, Coniothyrium sp. catalyzed the conformal deposition of manganese oxide along hyphae and nanofibers, but Coprinellus sp. catalyzed manganese oxide only along its hyphae. Fungi–nanofiber hybrids removed various heavy metals from the water. Heavy metal ions were adsorbed into manganese oxide crystalline structure, possibly by ion exchange with manganese within the manganese oxide. Hybrid materials of fungal hyphae and manganese oxides confined to nanofiber-adsorbed heavy metal ions from water.}, journal={JOURNAL OF ENGINEERED FIBERS AND FABRICS}, author={Park, Yaewon and Liu, Shuang and Gardner, Terrence and Johnson, Drake and Keeler, Aaron and Ortiz, Nathalia and Rabah, Ghada and Ford, Ericka}, year={2020}, month={Jan} }
 @article{rabah_2018, title={Determination of the Acid Dissociation Constant of a Phenolic Acid by High Performance Liquid Chromatography: An Experiment for the Upper Level Analytical Chemistry laboratory}, volume={95}, url={https://doi.org/10.1021/acs.jchemed.7b00647}, DOI={10.1021/acs.jchemed.7b00647}, abstractNote={A high performance liquid chromatography (HPLC) experiment for the upper level analytical chemistry laboratory is described. The students consider the effect of mobile-phase composition and pH on the retention times of ionizable compounds in order to determine the acid dissociation constant, Ka, of a phenolic acid. Results are analyzed using nonlinear regression.}, number={2}, journal={Journal of Chemical Education}, publisher={American Chemical Society (ACS)}, author={Rabah, Ghada}, year={2018}, month={Feb}, pages={310–314} }
 @article{chadwick_rabah_davies_smirnova_2009, title={Membrane insertion of peptides mimicking E2 domain of Sindbis virus is modulated by cholesterol}, volume={96}, ISSN={0006-3495}, url={http://dx.doi.org/10.1016/j.bpj.2008.12.2910}, DOI={10.1016/j.bpj.2008.12.2910}, abstractNote={In the process of assembly Sindbis enveloped virus uses a host-derived membrane bilayer that is “sandwiched” between the concentric protein shells. The transmembrane domains of three glycoproteins penetrate the bilayer and are capable of assembling in two strikingly different membranes: mammalian membranes that contain up to 40% of cholesterol and insects membranes that contain larger fraction of shorter unsaturated lipids and no cholesterol. Recently, it was shown that mutations in the transmembrane domain of the Sindbis virus E2 protein produce deferential alterations in the protein association with the lipid bilayer: some mutants were able to grow in insect cells, but not in mammalian cells [1,2]. The Sindbis virus with STM-16 deletion mutation of the E2 transmembrane domain shows the most pronounced differential growth in mammal and insect cells while STM-18 shows almost wild-type behaviour. We have investigated the interaction of synthetic peptides mimicking E2 domain mutants with lipid bilayers with the goal to understand constraints placed upon membrane spanning domains for correct integration into the bilayer. The phospholipid composition was chosen to represent mammalian and insects' membranes. Results of EPR spin-labeling experiments show that both STM-16 and STM-18 peptides adopt a transmembrane configuration in bilayers with lipid composition mimicking that of insects. In mammalian cell mimicking membranes and containing cholesterol the STM-16 peptide aggregates at the surface of the bilayer. Both peptides exhibit transmembrane orientation in bilayers consisting of “mammalian” lipid mixture but without cholesterol. Thus, we show that cholesterol content of the lipid mixture modulates insertion of the peptides into bilayer mimicking mammalian cell membrane. Supported by NSF grant MCB-0451510 to TIS.[1] Hernandez, R., et. al. J Virol 2003 77(23), 12710-9.[2] West, J., et. al. J. Virol., 2006 80:4458-4468.}, number={3}, journal={Biophysical Journal}, publisher={Elsevier BV}, author={Chadwick, Thomas G. and Rabah, Ghada A. and Davies, Brian R. and Smirnova, Tatyana I.}, year={2009}, month={Feb}, pages={389a–390a} }
 @article{rabah_popescu_cox_engelborghs_craescu_2004, title={Solution structure and dynamics of Nereis sarcoplasmic calcium binding protein}, DOI={10.2210/pdb1q80/pdb}, publisher={Worldwide Protein Data Bank}, author={Rabah, G. and Popescu, R. and Cox, J.A. and Engelborghs, Y. and Craescu, C.T.}, year={2004}, month={Sep} }
 @article{rabah_koser_1996, title={Facile synthetic entry into the 1,3-dihydro-3-methyl-3-phenyl-1,2-benziodoxole family of λ3-lodanes}, volume={37}, DOI={10.1016/0040-4039(96)01436-0}, abstractNote={The synthesis of series of 1,3-dihydro-3-methyl-3-phenyl-1,2-benziodoxoles, 7, containing chloro, tosyloxy, acetoxy, trifluoroacetoxy and azido ligands and the optical resolution of 2-iodo-α-methylbenzhydrol, the starting material for the synthesis of 7, are reported.}, number={36}, journal={Tetrahedron Letters}, publisher={Elsevier BV}, author={Rabah, Ghada A. and Koser, Gerald F.}, year={1996}, month={Sep}, pages={6453–6456} }
 @article{koser_mcconville_rabah_youngs_1995, title={Crystal and molecular structure of 1-chloro-1,2-benziodoxolin-3(1H)-one·tetra-n-butylammonium chloride}, volume={25}, DOI={10.1007/bf01671083}, number={12}, journal={Journal of Chemical Crystallography}, publisher={Springer Science and Business Media LLC}, author={Koser, Gerald F. and McConville, David B. and Rabah, Ghada A. and Youngs, Wiley J.}, year={1995}, pages={857–862} }