Parjit Kaur - Publications

Affiliations: 
Georgia State University, Atlanta, GA, United States 
Area:
Molecular Biology, Microbiology Biology

25 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2019 Peterson E, Shippee E, Brinton MA, Kaur P. Biochemical characterization of the mouse ABCF3 protein, a partner of the flavivirus-resistance protein OAS1B. The Journal of Biological Chemistry. PMID 31413116 DOI: 10.1074/Jbc.Ra119.008477  0.52
2018 Peterson E, Kaur P. Antibiotic Resistance Mechanisms in Bacteria: Relationships Between Resistance Determinants of Antibiotic Producers, Environmental Bacteria, and Clinical Pathogens. Frontiers in Microbiology. 9: 2928. PMID 30555448 DOI: 10.3389/Fmicb.2018.02928  0.309
2018 Rahman SJ, Kaur P. Conformational changes in a multidrug resistance ABC transporter DrrAB: Fluorescence-based approaches to study substrate binding. Archives of Biochemistry and Biophysics. PMID 30243711 DOI: 10.1016/J.Abb.2018.09.017  0.4
2017 Brown K, Li W, Kaur P. Role of aromatic and negatively-charged residues of DrrB in multi-substrate specificity conferred by the DrrAB system of Streptomyces peucetius. Biochemistry. PMID 28272881 DOI: 10.1021/Acs.Biochem.6B01155  0.459
2015 Zhang H, Rahman S, Li W, Fu G, Kaur P. Characterization of a novel domain 'GATE' in the ABC protein DrrA and its role in drug efflux by the DrrAB complex. Biochemical and Biophysical Research Communications. 459: 148-53. PMID 25721665 DOI: 10.1016/J.Bbrc.2015.02.086  0.496
2014 Li W, Sharma M, Kaur P. The DrrAB efflux system of Streptomyces peucetius is a multidrug transporter of broad substrate specificity. The Journal of Biological Chemistry. 289: 12633-46. PMID 24634217 DOI: 10.1074/Jbc.M113.536136  0.398
2013 Li W, Rao DK, Kaur P. Dual role of the metalloprotease FtsH in biogenesis of the DrrAB drug transporter. The Journal of Biological Chemistry. 288: 11854-64. PMID 23504316 DOI: 10.1074/Jbc.M112.441915  0.702
2010 Zhang H, Pradhan P, Kaur P. The extreme C terminus of the ABC protein DrrA contains unique motifs involved in function and assembly of the DrrAB complex. The Journal of Biological Chemistry. 285: 38324-36. PMID 20876527 DOI: 10.1074/Jbc.M110.131540  0.711
2009 Pradhan P, Li W, Kaur P. Translational coupling controls expression and function of the DrrAB drug efflux pump. Journal of Molecular Biology. 385: 831-42. PMID 19063901 DOI: 10.1016/J.Jmb.2008.11.027  0.635
2008 Rao DK, Kaur P. The Q-loop of DrrA is involved in producing the closed conformation of the nucleotide binding domains and in transduction of conformational changes between DrrA and DrrB. Biochemistry. 47: 3038-50. PMID 18237140 DOI: 10.1021/Bi701699A  0.69
2005 Kaur P, Rao DK, Gandlur SM. Biochemical characterization of domains in the membrane subunit DrrB that interact with the ABC subunit DrrA: identification of a conserved motif. Biochemistry. 44: 2661-70. PMID 15709779 DOI: 10.1021/Bi048959C  0.624
2004 Gandlur SM, Wei L, Levine J, Russell J, Kaur P. Membrane topology of the DrrB protein of the doxorubicin transporter of Streptomyces peucetius. The Journal of Biological Chemistry. 279: 27799-806. PMID 15090538 DOI: 10.1074/Jbc.M402898200  0.66
2003 Jia H, Kaur P. Biochemical evidence for interaction between the two nucleotide binding domains of ArsA. Insights from mutants and ATP analogs. The Journal of Biological Chemistry. 278: 6603-9. PMID 12488319 DOI: 10.1074/Jbc.M211845200  0.37
2002 Kaur P. Multidrug resistance: can different keys open the same lock? Drug Resistance Updates : Reviews and Commentaries in Antimicrobial and Anticancer Chemotherapy. 5: 61-4. PMID 12135581 DOI: 10.1016/S1368-7646(02)00020-1  0.468
2001 Jia H, Kaur P. Role of the linker region of the anion-stimulated ATPase ArsA. Effect of deletion and point mutations in the linker region Journal of Biological Chemistry. 276: 29582-29587. PMID 11389146 DOI: 10.1074/Jbc.M103042200  0.47
1999 Kaur P. The anion-stimulated ATPase ArsA shows unisite and multisite catalytic activity Journal of Biological Chemistry. 274: 25849-25854. PMID 10464326 DOI: 10.1074/Jbc.274.36.25849  0.422
1998 Kaur P, Russell J. Biochemical coupling between the DrrA and DrrB proteins of the doxorubicin efflux pump of Streptomyces peucetius Journal of Biological Chemistry. 273: 17933-17939. PMID 9651400 DOI: 10.1074/Jbc.273.28.17933  0.618
1998 Ramaswamy S, Kaur P. Nucleotide binding to the C-terminal nucleotide binding domain of ArsA: Studies with an ATP analogue, 5'-p-fluorosulfonylbenzoyladenosine (FSBA) Journal of Biological Chemistry. 273: 9243-9248. PMID 9535916 DOI: 10.1074/Jbc.273.15.9243  0.443
1997 Kaur P. Expression and characterization of DrrA and DrrB proteins of Streptomyces peucetius in Escherichia coli: DrrA is an ATP binding protein Journal of Bacteriology. 179: 569-575. PMID 9006006 DOI: 10.1128/Jb.179.3.569-575.1997  0.585
1994 Kaur P, Rosen BP. Identification of the site of [α-32P]ATP adduct formation in the ArsA protein Biochemistry®. 6456-6461. PMID 8204578 DOI: 10.1021/Bi00187A010  0.466
1994 Kaur P, Rosen BP. In vitro assembly of an anion-stimulated ATPase from peptide fragments Journal of Biological Chemistry. 269: 9698-9704. PMID 8144560  0.464
1993 Kaur P, Rosen BP. Complementation between nucleotide binding domains in an anion- translocating ATPase Journal of Bacteriology. 175: 351-357. PMID 8419286 DOI: 10.1128/Jb.175.2.351-357.1993  0.502
1992 Kaur P, Rosen BP. Plasmid-encoded resistance to arsenic and antimony Plasmid. 27: 29-40. PMID 1531541 DOI: 10.1016/0147-619X(92)90004-T  0.438
1992 Kaur P, Rosen BP. Mutagenesis of the C-terminal nucleotide-binding site of an anion- translocating ATPase Journal of Biological Chemistry. 267: 19272-19277. PMID 1388167  0.46
1990 Rosen BP, Hsu CM, Karkaria CE, Kaur P, Owolabi JB, Tisa LS. A plasmid-encoded anion-translocating ATPase Bba - Bioenergetics. 1018: 203-205. PMID 2144188 DOI: 10.1016/0005-2728(90)90249-4  0.369
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