Swati Rawat, Ph.D.
Affiliations: | 2011 | Biochemistry and Molecular Biology | Wayne State University, Detroit, MI, United States |
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Biochemistry, Molecular BiologyGoogle:
"Swati Rawat"Parents
Sign in to add mentorTimothy L. Stemmler | grad student | 2011 | Wayne State | |
(Molecular details of the mitochondrial iron sulfur cluster assembly pathway.) |
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Publications
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Rawat S, Kondapalli KC, Rodrigues AV, et al. (2019) Backbone resonance assignments and secondary structure of the apo-Drosophila melanogaster frataxin homolog (Dfh). Biomolecular Nmr Assignments. 13: 377-381 |
Dzul SP, Rocha AG, Rawat S, et al. (2016) In vitro characterization of a novel Isu homologue from Drosophila melanogaster for de novo FeS-cluster formation. Metallomics : Integrated Biometal Science |
Kumar NV, Yang J, Pillai JK, et al. (2015) Arsenic directly binds to and activates the yeast AP-1-like transcription factor Yap8. Molecular and Cellular Biology |
Rawat S, Zhu L, Lindner E, et al. (2015) SecA drives transmembrane insertion of RodZ, an unusual single-span membrane protein. Journal of Molecular Biology. 427: 1023-37 |
Rawat S, Lindner E, White SH. (2013) Insertion Mechanism in E. Coli of Single-Span Membrane Proteins with Far-Downstream Transmembrane Segments Biophysical Journal. 104: 410a |
Smith SM, Rawat S, Telser J, et al. (2011) Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M. Biochemistry. 50: 10231-40 |
Rawat S, Stemmler TL. (2011) Key players and their role during mitochondrial iron-sulfur cluster biosynthesis. Chemistry (Weinheim An Der Bergstrasse, Germany). 17: 746-53 |
Cook JD, Kondapalli KC, Rawat S, et al. (2010) Molecular details of the yeast frataxin-Isu1 interaction during mitochondrial Fe-S cluster assembly. Biochemistry. 49: 8756-65 |
Balasubramanian R, Smith SM, Rawat S, et al. (2010) Oxidation of methane by a biological dicopper centre. Nature. 465: 115-9 |
Yang J, Rawat S, Stemmler TL, et al. (2010) Arsenic binding and transfer by the ArsD As(III) metallochaperone. Biochemistry. 49: 3658-66 |