Publications - Karl Maluf

Yang, T. C., Catalano, C. E., and Maluf, N. K. (2015). Analytical Ultracentrifugation as a Tool to Study Nonspecific Protein-DNA Interactions. Methods Enzymol. 562, 305-330.

Tarasevich, B. J., Philo, J. S., Maluf, N. K., Krueger, S., Buchko, G. W., Lin, G., and Shaw, W. J. (2015). The leucine-rich amelogenin protein (LRAP) is primarily monomeric and unstructured in physiological solution. J. Struct. Biol. 190, 81-91.

Yang, T. C and Maluf, N. K. (2014). Characterization of the non-specific DNA binding properties of the Adenoviral IVa2 protein. Biophys. Chem. 194, 1-8.

Rudolph, M. C., Wellberg, E. A., Lewis, A. S., Terrell, K. L., Merz, A. L., Maluf, N. K., Serkova, N. J., and Anderson, S. M. (2014). Thyroid Hormone Responsive Protein Spot14 Enhances Catalysis of Fatty Acid Synthase in Lactating Mammary Epithelium. J. Lipid Res. 55, 1052-1065.

Bain, D. L., Connaghan, K. D., Maluf, N. K., Yang, Q., Miura, M. T., De Angelis, R. W., Degala, G. D., and Lambert, J. R. (2013). Steroid receptor-DNA interactions: toward a quantitative connection between energetics and transcriptional regulation. Nucleic Acids Res. (epub ahead of print) [free full text]

Connaghan, K. D., Miura, M. T., Maluf, N. K., Lambert, J. R., and Bain, D. L. (2013). Analysis of a glucocorticoid-estrogen receptor chimera reveals that dimerization energetics are under ionic control. Biophys. Chem. 172, 8-17.

Bain, D. L., Yang, Q., Connaghan, K. D., Robblee, J. P., Miura, M. T., Degala, G. D., Lambert, J. R., and Maluf, N. K. (2012). Glucocorticoid receptor-DNA interactions: binding energetics are the primary determinant of sequence-specific transcriptional activity. J. Mol. Biol. 422, 18-32.

Yang, T. C. and Maluf, N. K. (2012). Cooperative heteroassembly of the adenoviral L4-22K and IVa2 proteins onto the viral packaging sequence DNA. Biochemistry 51, 1357-1368.

Jia, H., Korolev, S., Niedziela-Majka, A., Maluf, N. K., Gauss, G. H., Myong, S., Ha, T., Waksman, G., and Lohman, T. M. (2011). Rotations of the 2B sub-domain of E. coli UvrD helicase/translocase coupled to nucleotide and DNA binding. J. Mol. Biol. 411, 633-648.

Maluf, N. K. and Yang, T. C. (2011). Thermodynamic linkage of large-scale ligand aggregation with receptor binding. Biophys. Chem. 154, 82-89.

Niedziela-Majka, A., Maluf, N. K., Antony, E., and Lohman, T. M. (2011). Self-assembly of Escherichia coli MutL and its complexes with DNA. Biochemistry 50, 7868-7880.

Tomko, E. J., Jia, H., Park, J., Maluf, N. K., Ha, T., and Lohman, T. M. (2010). 5'-Single-stranded/duplex DNA junctions are loading sites for E. coli UvrD translocase. EMBO J. 29, 3826-3839. [free full text]

Yang, T. C. and Maluf, N. K. (2010). Self-association of the adenoviral L4-22K protein. Biochemistry 49, 9830-9838.

Yang, Q., Catalano, C. E., and Maluf, N. K. (2009). Kinetic analysis of the genome packaging reaction in bacteriophage lambda. Biochemistry 48, 10705-10715.

Yang, T. C., Yang, Q., and Maluf, N. K. (2009). Interaction of the adenoviral IVa2 protein with a truncated viral DNA packaging sequence. Biophys. Chem. 140, 78-90.

Townsend, H. L., Jha, B. K., Han, J. Q., Maluf, N. K., Silverman, R. H., and Barton, D. J. (2008). A viral RNA competitively inhibits the antiviral endoribonuclease domain of RNase L. RNA 14, 1026-1036.

Yang, Q., Maluf, N. K., and Catalano, C. E. (2008). Packaging of a unit-length viral genome: the role of nucleotides and the gpD decoration protein in stable nucleocapsid assembly in bacteriophage lambda. J. Mol. Biol. 383, 1037-1048.

Maluf, N. K. and Feiss, M. (2006). Virus DNA translocation: progress towards a first ascent of mount pretty difficult. Mol. Microbiol. 61, 1-4. [free PDF]

Maluf, N. K., Gaussier, H., Bogner, E., Feiss, M., and Catalano, C. E. (2006). Assembly of bacteriophage lambda terminase into a viral DNA maturation and packaging machine. Biochemistry 45, 15259-15268.

English, C. M., Maluf, N. K., Tripet, B., Churchill, M. E., and Tyler, J. K. (2005). ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA. Biochemistry 44, 13673-13682.

Gaussier, H., Ortega, M. E., Maluf, N. K., and Catalano, C. E. (2005). Nucleotides regulate the conformational state of the small terminase subunit from bacteriophage lambda: implications for the assembly of a viral genome-packaging motor. Biochemistry 44, 9645-9656.

Maluf, N. K., Yang, Q., and Catalano, C. E. (2005). Self-association properties of the bacteriophage lambda terminase holoenzyme: implications for the DNA packaging motor. J. Mol. Biol. 347, 523-542.

Fischer, C. J., Maluf, N. K., and Lohman, T. M. (2004). Mechanism of ATP-dependent translocation of E.coli UvrD monomers along single-stranded DNA. J. Mol. Biol. 344, 1287-1309.

Lucius, A. L., Maluf, N. K., Fischer, C. J., and Lohman, T. M. (2003). General methods for analysis of sequential "n-step" kinetic mechanisms: application to single turnover kinetics of helicase-catalyzed DNA unwinding. Biophys. J. 85, 2224-2239. [free full text]

Maluf, N. K., Fischer, C. J., and Lohman, T. M. (2003). A Dimer of Escherichia coli UvrD is the active form of the helicase in vitro. J. Mol. Biol. 325, 913-935.

Maluf, N. K., Ali, J. A., and Lohman, T. M. (2003). Kinetic mechanism for formation of the active, dimeric UvrD helicase-DNA complex. J. Biol. Chem. 278, 31930-31940. [free full text]

Maluf, N. K. and Lohman, T. M. (2003). Self-association equilibria of Escherichia coli UvrD helicase studied by analytical ultracentrifugation. J. Mol. Biol. 325, 889-912.

Ali, J. A., Maluf, N. K., and Lohman, T. M. (1999). An oligomeric form of E. coli UvrD is required for optimal helicase activity. J. Mol. Biol. 293, 815-834.

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