Structural basis for virulence regulation in Vibrio cholerae by unsaturated fatty acid components of bile.Commun Biol.
A Modified ToxT Inhibitor Reduces Vibrio cholerae Virulence in Vivo. Biochemistry.
Privett BR, Pellegrini M, Kovacikova G, Taylor RK, Skorupski K, Mierke D, Kull FJ. (2017) Identification of a Small Molecule Activator for AphB, a LysR-Type Virulence Transcriptional Regulator in Vibrio cholerae. In preparation for Biochemistry.
Midgett CR, Almagro-Moreno S, Pellegrini M, Taylor RK, Skorupski S, and Kull FJ. (2017) Bile salts and alkaline pH reciprocally modulate the interaction between the periplasmic domains of Vibrio cholerae ToxR and ToxS. Molecular Microbiology, Under review.
Woodbrey AK, Onyango EO, Pellegrini M, Kovacikova G, Taylor RK, Gribble GW, Kull FJ. (2017) A new class of inhibitors of the AraC family virulence regulator Vibrio cholerae ToxT. Nature Scientific Reports, in press.
Shi W, Kovacikova G, Lin W, Taylor RK, Skorupski K, and Kull FJ. (2015) The 40-residue insertion in Vibrio cholerae FadR facilitates binding of an additional fatty acyl-CoA ligand. Nature Communications. 2015 Jan 21;6:6032. PMID: 25607896. PMCID: PMC4336772.
Kull FJ, Sloboda RD. (2014) A slow dance for microtubule acetylation. Cell. 2014 Jun 5;157(6):1255-6. doi: 10.1016/j.cell.2014.05.021. PMID: 24906144
Cochran JC, Thompson ME, Kull FJ. (2013) Metal Switch Controlled Myosin II from Dictyostelium discoideum Supports Closure of Nucleotide Pocket During ATP Binding is Coupled to Myosin Detachment from Actin Filaments. J Biol Chem. Sep 27;288(39):28312-23. PMID: 23960071. PMCID: PMC3784747.
Cochran JC, Kull FJ. (2013) “A molecular motor finds its track.” Nat Struct Mol Biol. Aug;20(8):920-1. PMID: 23912357
Kull FJ, Endow SA. (2013) “Force generation by kinesin and myosin cytoskeletal motor proteins.” J Cell Sci. Jan 1;126(Pt 1):9-19. doi: 10.1242/jcs.103911. Epub 2013 Mar 13. PMID: 23487037
Thompson ME, Heimsath EG, Gauvin TJ, Higgs HN, Kull FJ. (2013) “FMNL3 FH2-actin structure gives insight into formin-mediated actin nucleation and elongation.” Nat Struct Mol Biol. Jan;20(1):111-8. doi: 10.1038/nsmb.2462. Epub 2012 Dec 9. PMID: 23222643
Taylor JL, White SR, Lauring B, Kull FJ. (2012) “Crystal structure of the human spastin AAA domain.” Journal of Structural Biology. Aug;179(2):133-7. Epub 2012 Mar 14. PMID: 22446388. PMCID: PMC3411929
Taylor, J. L., R. S. De Silva, G. Kovacikova, W. Lin, R. K. Taylor, K. Skorupski and F. J. Kull (2011) “The crystal structure of AphB, a virulence gene activator from Vibrio cholerae, reveals residues that influence its response to oxygen and pH.” Molecular Microbiology. Feb;83(3):457-70. PMID:22053934. PMCID: PMC3262181. Note: Featured in a “MicroCommentary” in Molecular Microbiology.
Cochran, J. C., Y. C. Zhao, D. E. Wilcox, and F. J. Kull (2011) “A metal switch for controlling the activity of molecular motor proteins.” Nature Structural and Molecular Biology. Dec 25;19(1):122-7. PMID:22198464. PMCID: PMC3252401.
Waitzman, J. S., A. G. Larson, J. C. Cochran, N. Naber, R. Cooke, F. J. Kull, E. Pate and S. E. Rice (2011) “The loop 5 element structurally and kinetically coordinates dimers of the human kinesin-5, Eg5.” Biophysical Journal, Dec 7;101(11):2760-9. doi: 10.1016/j.bpj.2011.10.032. PMID: 22261065. PMCID: PMC3297777
Endow, S. A., F. J. Kull and H. Liu (2010) “Kinesins at a glance.” J Cell Sci. 123(Pt 20): 3420-3424. PMID: 20930137 PMCID: PMC2951464
Heuston, E., C. E. Bronner, F. J. Kull and S. A. Endow (2010) “A kinesin motor in a force-producing conformation.” BMC Struct Biol. 10: 19. PMID: 20602775 PMCID: PMC2906495 Note: Commentary in BMC Biology.
Lowden, M. J., K. Skorupski, M. Pellegrini, M. G. Chiorazzo, R. K. Taylor and F. J. Kull (2010) “Structure of Vibrio cholerae ToxT reveals a mechanism for fatty acid regulation of virulence genes.” Proc Natl Acad Sci USA. 107(7): 2860-2865. PMID: 20133655. PMCID: PMC2840316 Note: Selected as an Editors’ Choice in Science magazine.
Zhao, Y. C., F. J. Kull and J. C. Cochran (2010) “Modulation of the kinesin ATPase cycle by neck linker docking and microtubule binding.” J Biol Chem. 285(33): 25213-25220. PMID: 20558732. PMCID: PMC2919084
Cochran, J. C., C. V. Sindelar, N. K. Mulko, K. A. Collins, S. E. Kong, R. S. Hawley and F. J. Kull (2009) “ATPase cycle of the nonmotile kinesin NOD allows microtubule end tracking and drives chromosome movement.” Cell. 136(1): 110-122.
Cochran, J. C. and F. J. Kull (2008) “Kinesin motors: no strain, no gain.” Cell. 134(6): 918-919.
De Silva, R. S., G. Kovacikova, W. Lin, R. K. Taylor, K. Skorupski and F. J. Kull (2007) “Crystal structure of the Vibrio cholerae quorum-sensing regulatory protein HapR.” J Bacteriol. 189(15): 5683-5691.
Durrwang, U., S. Fujita-Becker, M. Erent, F. J. Kull, G. Tsiavaliaris, M. A. Geeves and D. J. Manstein (2006) “Dictyostelium myosin-IE is a fast molecular motor involved in phagocytosis.” J Cell Sci. 119(Pt 3): 550-558.
Goetz, J. A., S. Singh, L. M. Suber, F. J. Kull and D. J. Robbins (2006) “A highly conserved amino-terminal region of sonic hedgehog is required for the formation of its freely diffusible multimeric form.” J Biol Chem. 281(7): 4087-4093.
De Silva, R. S., G. Kovacikova, W. Lin, R. K. Taylor, K. Skorupski and F. J. Kull (2005) “Crystal structure of the virulence gene activator AphA from Vibrio cholerae reveals it is a novel member of the winged helix transcription factor superfamily.” J Biol Chem. 280(14): 13779-13783.
Reubold, T. F., S. Eschenburg, A. Becker, M. Leonard, S. L. Schmid, R. B. Vallee, F. J. Kull and D. J. Manstein (2005) “Crystal structure of the GTPase domain of rat dynamin 1.” Proc Natl Acad Sci U S A. 102(37): 13093-13098.
Kull, F. J. and S. A. Endow (2004) “A new structural state of myosin.” Trends Biochem Sci. 29(3): 103-106.
Holmes, K. C., I. Angert, F. J. Kull, W. Jahn and R. R. Schroder (2003) “Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide.” Nature. 425(6956): 423-427.
Reubold, T. F., S. Eschenburg, A. Becker, F. J. Kull and D. J. Manstein (2003) “A structural model for actin-induced nucleotide release in myosin.” Nat Struct Biol. 10(10): 826-830.
Kollmar, M., U. Durrwang, W. Kliche, D. J. Manstein and F. J. Kull (2002) “Crystal structure of the motor domain of a class-I myosin.” EMBO J. 21(11): 2517-2525.
Kull, F. J. and S. A. Endow (2002) “Kinesin: switch I & II and the motor mechanism.” J Cell Sci. 115(Pt 1): 15-23.
Tsiavaliaris, G., S. Fujita-Becker, R. Batra, D. I. Levitsky, F. J. Kull, M. A. Geeves and D. J. Manstein (2002) “Mutations in the relay loop region result in dominant-negative inhibition of myosin II function in Dictyostelium.” EMBO Rep. 3(11): 1099-1105.
Kliche, W., S. Fujita-Becker, M. Kollmar, D. J. Manstein and F. J. Kull (2001) “Structure of a genetically engineered molecular motor.” EMBO J. 20(1-2): 40-46. PMCID: PMC140180.
Niemann, H. H., M. L. Knetsch, A. Scherer, D. J. Manstein and F. J. Kull (2001) “Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms.” EMBO J. 20(21): 5813-5821.
Kull, F. J. (2000) “Motor proteins of the kinesin superfamily: structure and mechanism.” Essays Biochem. 35: 61-73.
Sack, S., F. J. Kull and E. Mandelkow (1999) “Motor proteins of the kinesin family. Structures, variations, and nucleotide binding sites.” Eur J Biochem. 262(1): 1-11.
Kull, F. J. and R. J. Fletterick (1998) “Is the tubulin/FtsZ fold related to the G-protein fold?” Trends Cell Biol. 8(8): 306-307.
Kull, F. J., R. D. Vale and R. J. Fletterick (1998) “The case for a common ancestor: kinesin and myosin motor proteins and G proteins.” J Muscle Res Cell Motil. 19(8): 877-886.
Kull, F. J., E. P. Sablin, R. Lau, R. J. Fletterick and R. D. Vale (1996) “Crystal structure of the kinesin motor domain reveals a structural similarity to myosin.” Nature. 380(6574): 550-555.
Sablin, E. P., F. J. Kull, R. Cooke, R. D. Vale and R. J. Fletterick (1996) “Crystal structure of the motor domain of the kinesin-related motor ncd.” Nature. 380(6574): 555-559.
Eden, D., B. Q. Luu, D. J. Zapata, E. P. Sablin and F. J. Kull (1995) “Solution structure of two molecular motor domains: nonclaret disjunctional and kinesin.” Biophys J. 68(4 Suppl): 59S-64S; discussion 65S.
Fujiwara, S., F. J. Kull, E. P. Sablin, D. B. Stone and R. A. Mendelson (1995) “The shapes of the motor domains of two oppositely directed microtubule motors, ncd and kinesin: a neutron scattering study.” Biophys J. 69(4): 1563-1568. PMCID: PMC1236387.
Vale, R. D., C. M. Coppin, F. Malik, F. J. Kull and R. A. Milligan (1994) “Tubulin GTP hydrolysis influences the structure, mechanical properties, and kinesin-driven transport of microtubules.” J Biol Chem. 269(38): 23769-23775.
Kull, F.J., M. F. Reed, T. E. Elgren, T. L. Ciardelli and D. E. Wilcox (1990) Solid-Phase Peptide Synthesis of the alpha- and beta Domains of Human Liver Metallothionein 2 and the Metallothionein of Neurospora crassa. Journal of the American Chemical Society.