| Year |
Citation |
Score |
| 2019 |
Shinn MK, Kozlov AG, Nguyen B, Bujalowski WM, Lohman TM. Are the intrinsically disordered linkers involved in SSB binding to accessory proteins? Nucleic Acids Research. PMID 31329947 DOI: 10.1093/nar/gkz606 |
0.827 |
|
| 2014 |
Bujalowski W, Jezewska MJ. Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves. Journal of Molecular Structure. 1077: 40-50. PMID 25284889 DOI: 10.1016/j.molstruc.2014.04.041 |
0.431 |
|
| 2013 |
Szymanski MR, Jezewska MJ, Bujalowski W. Energetics of the Escherichia coli DnaT protein trimerization reaction. Biochemistry. 52: 1858-73. PMID 23418702 DOI: 10.1021/Bi3015696 |
0.73 |
|
| 2013 |
Szymanski MR, Jezewska MJ, Bujalowski W. The Escherichia coli primosomal DnaT protein exists in solution as a monomer-trimer equilibrium system. Biochemistry. 52: 1845-57. PMID 23418648 DOI: 10.1021/Bi301568W |
0.677 |
|
| 2013 |
Szymanski MR, Jezewska MJ, Bujalowski WM. Unraveling the Mechanism of the Primosome Assembly Process Biophysical Journal. 104: 253a. DOI: 10.1016/J.Bpj.2012.11.1423 |
0.676 |
|
| 2012 |
Szymanski MR, Jezewska MJ, Bujalowski W. Helicase-Initiated Assembly of the Primosome Biophysical Journal. 102: 486a. DOI: 10.1016/J.Bpj.2011.11.2666 |
0.775 |
|
| 2011 |
Szymanski MR, Bujalowski PJ, Jezewska MJ, Gmyrek AM, Bujalowski W. The N-terminal domain of the Escherichia coli PriA helicase contains both the DNA- and nucleotide-binding sites. Energetics of domain--DNA interactions and allosteric effect of the nucleotide cofactors. Biochemistry. 50: 9167-83. PMID 21888358 DOI: 10.1021/Bi201100K |
0.774 |
|
| 2011 |
Szymanski MR, Jezewska MJ, Bujalowski PJ, Bussetta C, Ye M, Choi KH, Bujalowski W. Full-length Dengue virus RNA-dependent RNA polymerase-RNA/DNA complexes: stoichiometries, intrinsic affinities, cooperativities, base, and conformational specificities. The Journal of Biological Chemistry. 286: 33095-108. PMID 21725087 DOI: 10.1074/Jbc.M111.255034 |
0.758 |
|
| 2011 |
Szymanski MR, Jezewska MJ, Bujalowski W. Binding of two PriA-PriB complexes to the primosome assembly site initiates primosome formation. Journal of Molecular Biology. 411: 123-42. PMID 21641914 DOI: 10.1016/J.Jmb.2011.05.029 |
0.787 |
|
| 2011 |
Jezewska MJ, Szymanski MR, Bujalowski W. Kinetic mechanism of the ssDNA recognition by the polymerase X from African Swine Fever Virus. Dynamics and energetics of intermediate formations. Biophysical Chemistry. 158: 9-20. PMID 21605932 DOI: 10.1016/J.Bpc.2011.04.010 |
0.672 |
|
| 2011 |
Jezewska MJ, Szymanski MR, Bujalowski W. Interactions of the DNA polymerase X from African Swine Fever Virus with the ssDNA. Properties of the total DNA-binding site and the strong DNA-binding subsite. Biophysical Chemistry. 158: 26-37. PMID 21601347 DOI: 10.1016/J.Bpc.2011.04.012 |
0.791 |
|
| 2011 |
Jezewska MJ, Szymanski MR, Bujalowski W. The primary DNA-binding subsite of the rat pol β. Energetics of interactions of the 8-kDa domain of the enzyme with the ssDNA. Biophysical Chemistry. 156: 115-27. PMID 21382659 DOI: 10.1016/J.Bpj.2011.11.3277 |
0.706 |
|
| 2011 |
Bujalowski W, Jezewska MJ. Macromolecular competition titration method accessing thermodynamics of the unmodified macromolecule-ligand interactions through spectroscopic titrations of fluorescent analogs. Methods in Enzymology. 488: 17-57. PMID 21195223 DOI: 10.1016/B978-0-12-381268-1.00002-1 |
0.394 |
|
| 2011 |
Szymanski MR, Jezewska MJ, Bujalowski W. The Escherichia Coli PriA Helicase Specifically Recognizes Gapped DNA Substrates Biophysical Journal. 100: 73a. DOI: 10.1016/J.Bpj.2010.12.601 |
0.784 |
|
| 2010 |
Szymanski MR, Jezewska MJ, Bujalowski W. The Escherichia coli PriA helicase-double-stranded DNA complex: location of the strong DNA-binding subsite on the helicase domain of the protein and the affinity control by the two nucleotide-binding sites of the enzyme. Journal of Molecular Biology. 402: 344-62. PMID 20624397 DOI: 10.1016/J.Jmb.2010.07.008 |
0.82 |
|
| 2010 |
Updegrove TB, Correia JJ, Galletto R, Bujalowski W, Wartell RM. E. coli DNA associated with isolated Hfq interacts with Hfq's distal surface and C-terminal domain. Biochimica Et Biophysica Acta. 1799: 588-96. PMID 20619373 DOI: 10.1016/J.Bbagrm.2010.06.007 |
0.578 |
|
| 2010 |
Kozlov AG, Jezewska MJ, Bujalowski W, Lohman TM. Binding specificity of Escherichia coli single-stranded DNA binding protein for the chi subunit of DNA pol III holoenzyme and PriA helicase. Biochemistry. 49: 3555-66. PMID 20329707 DOI: 10.1021/Bi100069S |
0.828 |
|
| 2010 |
Szymanski MR, Jezewska MJ, Bujalowski W. Interactions of the Escherichia coli primosomal PriB protein with the single-stranded DNA. Stoichiometries, intrinsic affinities, cooperativities, and base specificities. Journal of Molecular Biology. 398: 8-25. PMID 20156448 DOI: 10.1016/J.Jmb.2010.02.009 |
0.825 |
|
| 2010 |
Szymanski MR, Jezewska MJ, Bujalowski W. The Escherichia coli PriA helicase specifically recognizes gapped DNA substrates: effect of the two nucleotide-binding sites of the enzyme on the recognition process. The Journal of Biological Chemistry. 285: 9683-96. PMID 20089865 DOI: 10.1074/Jbc.M109.094789 |
0.798 |
|
| 2010 |
Jezewska MJ, Andreeva IE, Szymanski MR, Bujalowski W. Mechanisms of Nucleotide Cofactor Interactions with the RepA Protein of Plasmid RSF1010 Biophysical Journal. 98: 267a. DOI: 10.1016/J.Bpj.2009.12.1457 |
0.802 |
|
| 2009 |
Bujalowski W, Jezewska MJ. Thermodynamic analysis of the structure-function relationship in the total DNA-binding site of enzyme-DNA complexes. Methods in Enzymology. 466: 293-324. PMID 21603116 DOI: 10.1016/S0076-6879(09)66013-4 |
0.523 |
|
| 2009 |
Andreeva IE, Roychowdhury A, Szymanski MR, Jezewska MJ, Bujalowski W. Mechanisms of interactions of the nucleotide cofactor with the RepA protein of plasmid RSF1010. Binding dynamics studied using the fluorescence stopped-flow method. Biochemistry. 48: 10620-36. PMID 19747005 DOI: 10.1021/Bi900940Q |
0.795 |
|
| 2009 |
Roychowdhury A, Szymanski MR, Jezewska MJ, Bujalowski W. Interactions of the Escherichia coli DnaB-DnaC protein complex with nucleotide cofactors. 1. Allosteric conformational transitions of the complex. Biochemistry. 48: 6712-29. PMID 19569622 DOI: 10.1021/Bi900050X |
0.772 |
|
| 2009 |
Roychowdhury A, Szymanski MR, Jezewska MJ, Bujalowski W. Mechanism of NTP hydrolysis by the Escherichia coli primary replicative helicase DnaB protein. 2. Nucleotide and nucleic acid specificities. Biochemistry. 48: 6730-46. PMID 19435286 DOI: 10.1021/Bi9000529 |
0.763 |
|
| 2009 |
Roychowdhury A, Szymanski MR, Jezewska MJ, Bujalowski W. Escherichia coli DnaB helicase-DnaC protein complex: allosteric effects of the nucleotides on the nucleic acid binding and the kinetic mechanism of NTP hydrolysis. 3. Biochemistry. 48: 6747-63. PMID 19432487 DOI: 10.1021/Bi9000535 |
0.8 |
|
| 2009 |
Andreeva IE, Szymanski MR, Jezewska MJ, Galletto R, Bujalowski W. Dynamics of the ssDNA recognition by the RepA hexameric helicase of plasmid RSF1010: analyses using fluorescence stopped-flow intensity and anisotropy methods. Journal of Molecular Biology. 388: 751-75. PMID 19289128 DOI: 10.1016/J.Jmb.2009.03.027 |
0.765 |
|
| 2008 |
Marcinowicz A, Jezewska MJ, Bujalowski W. Multiple global conformational states of the hexameric RepA helicase of plasmid RSF1010 with different ssDNA-binding capabilities are induced by different numbers of bound nucleotides. Analytical ultracentrifugation and dynamic light scattering studies. Journal of Molecular Biology. 375: 386-408. PMID 18022636 DOI: 10.1016/J.Jmb.2007.06.051 |
0.433 |
|
| 2007 |
Jezewska MJ, Bujalowski PJ, Bujalowski W. Interactions of the DNA polymerase X from African swine fever virus with gapped DNA substrates. Quantitative analysis of functional structures of the formed complexes. Biochemistry. 46: 12909-24. PMID 17941646 DOI: 10.1021/Bi700677J |
0.534 |
|
| 2007 |
Marcinowicz A, Jezewska MJ, Bujalowski PJ, Bujalowski W. Structure of the tertiary complex of the RepA hexameric helicase of plasmid RSF1010 with the ssDNA and nucleotide cofactors in solution. Biochemistry. 46: 13279-96. PMID 17939681 DOI: 10.1021/Bi700729K |
0.493 |
|
| 2007 |
Jezewska MJ, Bujalowski PJ, Bujalowski W. Interactions of the DNA polymerase X of African swine fever virus with double-stranded DNA. Functional structure of the complex. Journal of Molecular Biology. 373: 75-95. PMID 17765921 DOI: 10.1016/J.Jmb.2007.06.054 |
0.599 |
|
| 2006 |
Lucius AL, Jezewska MJ, Bujalowski W. Allosteric interactions between the nucleotide-binding sites and the ssDNA-binding site in the PriA helicase-ssDNA complex. 3. Biochemistry. 45: 7237-55. PMID 16752913 DOI: 10.1021/Bi0518287 |
0.809 |
|
| 2006 |
Lucius AL, Jezewska MJ, Roychowdhury A, Bujalowski W. Kinetic mechanisms of the nucleotide cofactor binding to the strong and weak nucleotide-binding site of the Escherichia coli PriA helicase. 2. Biochemistry. 45: 7217-36. PMID 16752912 DOI: 10.1021/Bi051827E |
0.707 |
|
| 2006 |
Lucius AL, Jezewska MJ, Bujalowski W. The Escherichia coli PriA helicase has two nucleotide-binding sites differing dramatically in their affinities for nucleotide cofactors. 1. Intrinsic affinities, cooperativities, and base specificity of nucleotide cofactor binding. Biochemistry. 45: 7202-16. PMID 16752911 DOI: 10.1021/Bi051826M |
0.782 |
|
| 2006 |
Jezewska MJ, Marcinowicz A, Lucius AL, Bujalowski W. DNA polymerase X from African swine fever virus: quantitative analysis of the enzyme-ssDNA interactions and the functional structure of the complex. Journal of Molecular Biology. 356: 121-41. PMID 16337650 DOI: 10.1016/J.Jmb.2005.10.061 |
0.807 |
|
| 2005 |
Galletto R, Jezewska MJ, Maillard R, Bujalowski W. The nucleotide-binding site of the Escherichia coli DnaC protein: molecular topography of DnaC protein-nucleotide cofactor complexes. Cell Biochemistry and Biophysics. 43: 331-53. PMID 16244362 DOI: 10.1385/Cbb:43:3:331 |
0.55 |
|
| 2005 |
Galletto R, Jezewska MJ, Bujalowski W. Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding: analysis of stopped-flow kinetic experiments. Cell Biochemistry and Biophysics. 42: 121-44. PMID 15858229 DOI: 10.1385/Cbb:42:2:121 |
0.434 |
|
| 2005 |
Jezewska MJ, Lucius AL, Bujalowski W. Binding of six nucleotide cofactors to the hexameric helicase RepA protein of plasmid RSF1010. 2. Base specificity, nucleotide structure, magnesium, and salt effect on the cooperative binding of the cofactors. Biochemistry. 44: 3877-90. PMID 15751963 DOI: 10.1021/Bi048036H |
0.778 |
|
| 2005 |
Jezewska MJ, Lucius AL, Bujalowski W. Binding of six nucleotide cofactors to the hexameric helicase RepA protein of plasmid RSF1010. 1. Direct evidence of cooperative interactions between the nucleotide-binding sites of a hexameric helicase. Biochemistry. 44: 3865-76. PMID 15751962 DOI: 10.1021/Bi048037+ |
0.797 |
|
| 2005 |
Galletto R, Jezewska MJ, Bujalowski W. Kinetic mechanism of rat polymerase beta-dsDNA interactions. Fluorescence stopped-flow analysis of the cooperative ligand binding to a two-site one-dimensional lattice. Biochemistry. 44: 1251-67. PMID 15667219 DOI: 10.1021/Bi0487037 |
0.543 |
|
| 2004 |
Jezewska MJ, Galletto R, Bujalowski W. Interactions of the RepA helicase hexamer of plasmid RSF1010 with the ssDNA. Quantitative analysis of stoichiometries, intrinsic affinities, cooperativities, and heterogeneity of the total ssDNA-binding site. Journal of Molecular Biology. 343: 115-36. PMID 15381424 DOI: 10.1016/J.Jmb.2004.08.021 |
0.617 |
|
| 2004 |
Galletto R, Jezewska MJ, Bujalowski W. Unzipping mechanism of the double-stranded DNA unwinding by a hexameric helicase: the effect of the 3' arm and the stability of the dsDNA on the unwinding activity of the Escherichia coli DnaB helicase. Journal of Molecular Biology. 343: 101-14. PMID 15381423 DOI: 10.1016/J.Jmb.2004.07.056 |
0.432 |
|
| 2004 |
Galletto R, Jezewska MJ, Bujalowski W. Unzipping mechanism of the double-stranded DNA unwinding by a hexameric helicase: quantitative analysis of the rate of the dsDNA unwinding, processivity and kinetic step-size of the Escherichia coli DnaB helicase using rapid quench-flow method. Journal of Molecular Biology. 343: 83-99. PMID 15381422 DOI: 10.1016/J.Jmb.2004.07.055 |
0.412 |
|
| 2004 |
Galletto R, Jezewska MJ, Bujalowski W. Multistep sequential mechanism of Escherichia coli helicase PriA protein-ssDNA interactions. Kinetics and energetics of the active ssDNA-searching site of the enzyme. Biochemistry. 43: 11002-16. PMID 15323559 DOI: 10.1021/Bi049378Q |
0.592 |
|
| 2004 |
Galletto R, Maillard R, Jezewska MJ, Bujalowski W. Global conformation of the Escherichia coli replication factor DnaC protein in absence and presence of nucleotide cofactors. Biochemistry. 43: 10988-1001. PMID 15323558 DOI: 10.1021/Bi049377Y |
0.427 |
|
| 2003 |
Jezewska MJ, Galletto R, Bujalowski W. Tertiary conformation of the template-primer and gapped DNA substrates in complexes with rat polymerase beta. Fluorescence energy transfer studies using the multiple donor-acceptor approach. Biochemistry. 42: 11864-78. PMID 14529299 DOI: 10.1021/Bi030111L |
0.407 |
|
| 2003 |
Jezewska MJ, Galletto R, Bujalowski W. Rat polymerase beta gapped DNA interactions: antagonistic effects of the 5' terminal PO4 - group and magnesium on the enzyme binding to the gapped DNAs with different ssDNA gaps. Cell Biochemistry and Biophysics. 38: 125-60. PMID 12777712 DOI: 10.1385/Cbb:38:2:125 |
0.466 |
|
| 2003 |
Galletto R, Jezewska MJ, Bujalowski W. Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on protein-protein interactions and the topology of the complex. Journal of Molecular Biology. 329: 441-65. PMID 12767828 DOI: 10.1016/S0022-2836(03)00435-2 |
0.598 |
|
| 2003 |
Jezewska MJ, Galletto R, Bujalowski W. Rat polymerase beta binds double-stranded DNA using exclusively the 8-kDa domain. Stoichiometries, intrinsic affinities, and cooperativities. Biochemistry. 42: 5955-70. PMID 12741854 DOI: 10.1021/Bi030046F |
0.466 |
|
| 2003 |
Bujalowski W. Expanding the physiological role of the hexameric DnaB helicase. Trends in Biochemical Sciences. 28: 116-8. PMID 12633988 DOI: 10.1016/S0968-0004(03)00034-3 |
0.386 |
|
| 2002 |
Galletto R, Bujalowski W. Kinetics of the E. coli replication factor DnaC protein-nucleotide interactions. II. Fluorescence anisotropy and transient, dynamic quenching stopped-flow studies of the reaction intermediates. Biochemistry. 41: 8921-34. PMID 12102634 DOI: 10.1021/Bi020127W |
0.518 |
|
| 2002 |
Galletto R, Bujalowski W. The E. coli replication factor DnaC protein exists in two conformations with different nucleotide binding capabilities. I. Determination of the binding mechanism using ATP and ADP fluorescent analogues. Biochemistry. 41: 8907-20. PMID 12102633 DOI: 10.1021/Bi0201264 |
0.546 |
|
| 2002 |
Jezewska MJ, Galletto R, Bujalowski W. Dynamics of gapped DNA recognition by human polymerase beta. The Journal of Biological Chemistry. 277: 20316-27. PMID 11912205 DOI: 10.1074/Jbc.M200918200 |
0.447 |
|
| 2001 |
Jezewska MJ, Rajendran S, Galletto R, Bujalowski W. Kinetic mechanisms of rat polymerase beta-ssDNA interactions. Quantitative fluorescence stopped-flow analysis of the formation of the (Pol beta)(16) and (Pol beta)(5) ssDNA binding mode. Journal of Molecular Biology. 313: 977-1002. PMID 11700054 DOI: 10.1006/Jmbi.2001.5042 |
0.511 |
|
| 2001 |
Rajendran S, Jezewska MJ, Bujalowski W. Multiple-step kinetic mechanisms of the ssDNA recognition process by human polymerase β in its different ssDNA binding modes Biochemistry. 40: 11794-11810. PMID 11570880 DOI: 10.1021/Bi011173J |
0.527 |
|
| 2001 |
Rajendran S, Jezewska MJ, Bujalowski W. Recognition of template-primer and gapped DNA substrates by the human DNA polymerase β Journal of Molecular Biology. 308: 477-500. PMID 11327782 DOI: 10.1006/Jmbi.2001.4571 |
0.526 |
|
| 2001 |
Jezewska MJ, Rajendran S, Bujalowski W. Energetics and Specificity of Rat DNA Polymerase β Interactions with Template-primer and Gapped DNA Substrates Journal of Biological Chemistry. 276: 16123-16136. PMID 11278675 DOI: 10.1074/Jbc.M010434200 |
0.458 |
|
| 2001 |
Jezewska MJ, Rajendran S, Bujalowski W. Interactions of the 8-kDa domain of rat DNA polymerase β with DNA Biochemistry. 40: 3295-3307. PMID 11258949 DOI: 10.1021/Bi002749S |
0.542 |
|
| 2000 |
Rajendran S, Jezewska MJ, Bujalowski W. Multiple-step kinetic mechanism of DNA-independent ATP binding and hydrolysis by Escherichia coli replicative helicase DnaB protein: Quantitative analysis using the rapid quench-flow method Journal of Molecular Biology. 303: 773-795. PMID 11061975 DOI: 10.1006/Jmbi.2000.4124 |
0.465 |
|
| 2000 |
Galletto R, Rajendran S, Bujalowski W. Interactions of nucleotide cofactors with the Escherichia coli replication factor DnaC protein. Biochemistry. 39: 12959-69. PMID 11041861 DOI: 10.1021/Bi0012484 |
0.589 |
|
| 2000 |
Jezewska MJ, Bujalowski W. Interactions of Escherichia coli replicative helicase PriA protein with single-stranded DNA Biochemistry. 39: 10454-10467. PMID 10956036 DOI: 10.1021/Bi001113Y |
0.648 |
|
| 2000 |
Jezewska MJ, Rajendran S, Bujalowski W. Escherichia coli replicative helicase PriA protein-single-stranded DNA complex: Stoichiometries, free energy of binding, and cooperativities Journal of Biological Chemistry. 275: 27865-27873. PMID 10875934 DOI: 10.1074/Jbc.M004104200 |
0.654 |
|
| 2000 |
Bujalowski W, Jezewska MJ. Kinetic mechanism of nucleotide cofactor binding to Escherichia coli replicative helicase DnaB protein. Stopped-flow kinetic studies using fluorescent, ribose-, and base-modified nucleotide analogues Biochemistry. 39: 2106-2122. PMID 10684661 DOI: 10.1021/Bi992413M |
0.487 |
|
| 2000 |
Bujalowski W, Jezewska MJ. Kinetic mechanism of the single-stranded DNA recognition by Escherichia coli replicative helicase DnaB protein. Application of the matrix projection operator technique to analyze stopped-flow kinetics Journal of Molecular Biology. 295: 831-852. PMID 10656794 DOI: 10.1006/Jmbi.1999.3378 |
0.596 |
|
| 1998 |
Jezewska MJ, Rajendran S, Bujalowski W. Transition between different binding modes in rat DNA polymerase β-ssDNA complexes Journal of Molecular Biology. 284: 1113-1131. PMID 9837730 DOI: 10.1006/Jmbi.1998.2252 |
0.415 |
|
| 1998 |
Rajendran S, Jezewska MJ, Bujalowski W. Human DNA polymerase β recognizes single-stranded DNA using two different binding modes Journal of Biological Chemistry. 273: 31021-31031. PMID 9813000 DOI: 10.1074/Jbc.273.47.31021 |
0.496 |
|
| 1998 |
Jezewska MJ, Rajendran S, Bujalowska D, Bujalowski W. Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB helicase? Fluorescence energy transfer studies Journal of Biological Chemistry. 273: 10515-10529. PMID 9553111 DOI: 10.1074/Jbc.273.17.10515 |
0.527 |
|
| 1998 |
Jezewska MJ, Rajendran S, Bujalowski W. Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein Journal of Biological Chemistry. 273: 9058-9069. PMID 9535894 DOI: 10.1074/Jbc.273.15.9058 |
0.636 |
|
| 1998 |
Jezewska MJ, Rajendran S, Bujalowski W. Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: Recognition and structure Biochemistry. 37: 3116-3136. PMID 9485465 DOI: 10.1021/Bi972564U |
0.51 |
|
| 1997 |
Jezewska MJ, Rajendran S, Bujalowski W. Strand specificity in the interactions of Escherichia coli primary replicative helicase DnaB protein with a replication fork Biochemistry. 36: 10320-10326. PMID 9254631 DOI: 10.1021/Bi970712A |
0.598 |
|
| 1997 |
Jezewska MJ, Bujalowski W. Quantitative analysis of ligand-macromolecule interactions using differential dynamic quenching of the ligand fluorescence to monitor the binding Biophysical Chemistry. 64: 253-269. PMID 9127949 DOI: 10.1016/S0301-4622(96)02221-1 |
0.422 |
|
| 1997 |
Jezewska MJ, Bujalowski W. A general method of analysis of ligand binding to competing macromolecules. Application to the E. coli DnaB helicase-nucleic acid interactions Faseb Journal. 11. |
0.445 |
|
| 1996 |
Jezewska MJ, Kim US, Bujalowski W. Interactions of Escherichia coli primary replicative helicase DnaB protein with nucleotide cofactors Biophysical Journal. 71: 2075-2086. PMID 8889182 DOI: 10.1016/S0006-3495(96)79406-7 |
0.54 |
|
| 1996 |
Jezewska MJ, Kim US, Bujalowski W. Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer Biochemistry. 35: 2129-2145. PMID 8652555 DOI: 10.1021/Bi952345D |
0.617 |
|
| 1996 |
Jezewska MJ, Bujalowski W. A general method of analysis of ligand binding to competing macromolecules using the spectroscopic signal originating from a reference macromolecule. Application to Escherichia coli replicative helicase DnaB protein-nucleic acid interactions Biochemistry. 35: 2117-2128. PMID 8652554 DOI: 10.1021/Bi952344L |
0.488 |
|
| 1996 |
Jezewska MJ, Bujalowski W. Global conformational transitions in Escherichia coli primary replicative helicase DnaB protein induced by ATP, ADP, and single-stranded DNA binding: Multiple conformational states of the helicase hexamer Journal of Biological Chemistry. 271: 4261-4265. PMID 8626772 DOI: 10.1074/Jbc.271.8.4261 |
0.491 |
|
| 1996 |
Jezewska MJ, Bujalowski W. Structure and conformational transitions of the of E. Coureplicative helicase DnaB protein hexamer - SsDNA complex Faseb Journal. 10. |
0.592 |
|
| 1995 |
Bujalowski W, Jezewska MJ. Interactions of escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. the nucleic acid does not wrap around the protein hexamer Biochemistry®. 34: 8513-8519. PMID 7612593 DOI: 10.1021/Bi00027A001 |
0.667 |
|
| 1994 |
Lohman TM, Bujalowski W. Effects of base composition on the negative cooperativity and binding mode transitions of Escherichia coli SSB-single-stranded DNA complexes. Biochemistry. 33: 6167-76. PMID 8193130 DOI: 10.1021/Bi00186A016 |
0.704 |
|
| 1994 |
Bujalowski W. Structural characteristics of the nucleotide-binding site of escherichia coli primary replicative helicase DnaB protein. studies with ribose and base-modified fluorescent nucleotide analogs Biochemistry. 33: 4682-4694. PMID 8161526 DOI: 10.1021/Bi00181A028 |
0.47 |
|
| 1994 |
Ferrari ME, Bujalowski W, Lohman TM. Co-operative binding of Escherichia coli SSB tetramers to single-stranded DNA in the (SSB)35 binding mode. Journal of Molecular Biology. 236: 106-23. PMID 8107097 DOI: 10.1006/jmbi.1994.1122 |
0.708 |
|
| 1994 |
Bujalowski W, Klonowska MM. Close proximity of tryptophan residues and ATP-binding site in Escherichia coli primary replicative helicase DnaB protein: Molecular topography of the enzyme Journal of Biological Chemistry. 269: 31359-31371. PMID 7989300 |
0.542 |
|
| 1993 |
Bujalowski W, Klonowska MM. Negative cooperativity in the binding of nucleotides to Escherichia coli replicative helicase DnaB protein. Interactions with fluorescent nucleotide analogs Biochemistry. 32: 5888-5900. PMID 8504109 DOI: 10.1021/Bi00073A023 |
0.562 |
|
| 1992 |
Wei TF, Bujalowski W, Lohman TM. Cooperative binding of polyamines induces the Escherichia coli single-strand binding protein-DNA binding mode transitions. Biochemistry. 31: 6166-74. PMID 1627560 |
0.733 |
|
| 1992 |
Wong I, Chao KL, Bujalowski W, Lohman TM. DNA-induced dimerization of the Escherichia coli rep helicase. Allosteric effects of single-stranded and duplex DNA. The Journal of Biological Chemistry. 267: 7596-610. PMID 1313807 |
0.839 |
|
| 1991 |
Bujalowski W, Lohman TM. Monomers of the Escherichia coli SSB-1 mutant protein bind single-stranded DNA. Journal of Molecular Biology. 217: 63-74. PMID 1988680 DOI: 10.1016/0022-2836(91)90611-9 |
0.77 |
|
| 1991 |
Bujalowski W, Lohman TM. Monomer-tetramer equilibrium of the Escherichia coli ssb-1 mutant single strand binding protein. The Journal of Biological Chemistry. 266: 1616-26. PMID 1988441 |
0.637 |
|
| 1991 |
Lohman TM, Bujalowski W. Thermodynamic methods for model-independent determination of equilibrium binding isotherms for protein-DNA interactions: spectroscopic approaches to monitor binding. Methods in Enzymology. 208: 258-90. PMID 1779838 DOI: 10.1016/0076-6879(91)08017-C |
0.671 |
|
| 1989 |
Bujalowski W, Lohman TM, Anderson CF. On the cooperative binding of large ligands to a one-dimensional homogeneous lattice: the generalized three-state lattice model. Biopolymers. 28: 1637-43. PMID 2775853 DOI: 10.1002/bip.360280912 |
0.557 |
|
| 1989 |
Bujalowski W, Lohman TM. Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. II. Salt, temperature and oligonucleotide length effects Journal of Molecular Biology. 207: 269-288. PMID 2661833 DOI: 10.1016/0022-2836(89)90455-5 |
0.708 |
|
| 1989 |
Bujalowski W, Lohman TM. Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative model Journal of Molecular Biology. 207: 249-268. PMID 2661832 DOI: 10.1016/0022-2836(89)90454-3 |
0.738 |
|
| 1989 |
Jezewska MJ, Bujalowski W, Lohman TM. Iron(II)-ethylenediaminetetraacetic acid catalyzed cleavage of DNA is highly specific for duplex DNA. Biochemistry. 28: 6161-4. PMID 2506924 |
0.579 |
|
| 1988 |
Bujalowski W, Porschke D. Contributions to selective binding of aromatic amino acid residues to tRNAPhe Biophysical Chemistry. 30: 151-157. PMID 3416041 DOI: 10.1016/0301-4622(88)85012-9 |
0.496 |
|
| 1988 |
Lohman TM, Bujalowski W. Negative cooperativity within individual tetramers of Escherichia coli single strand binding protein is responsible for the transition between the (SSB)35 and (SSB)56 DNA binding modes Biochemistry®. 27: 2260-2265. PMID 3289611 |
0.773 |
|
| 1988 |
Lohman TM, Bujalowski W, Overman LB, Wei TF. Interactions of the E. coli Single Strand Binding (SSB) protein with ss nucleic acids. Binding mode transitions and equilibrium binding studies Biochemical Pharmacology. 37: 1781-1782. PMID 3288214 DOI: 10.1016/0006-2952(88)90443-1 |
0.837 |
|
| 1988 |
Bujalowski W, Porschke D. Fluorescence temperature jump Zeitschrift Fur Naturforschung - Section C Journal of Biosciences. 43: 91-98. PMID 3287785 DOI: 10.1515/znc-1988-1-218 |
0.486 |
|
| 1988 |
Bujalowski W, Overman LB, Lohman TM. Binding mode transitions of Escherichia coli single strand binding protein-single-stranded DNA complexes Journal of Biological Chemistry. 263: 4629-4640. PMID 3280566 |
0.829 |
|
| 1988 |
Overman LB, Bujalowski W, Lohman TM. Equilibrium binding of Escherichia coli single-strand binding protein to single-stranded nucleic acids in the (SSB)65 binding mode. Cation and anion effects and polynucleotide specificity Biochemistry. 27: 456-471. PMID 3280021 DOI: 10.1021/Bi00401A067 |
0.819 |
|
| 1988 |
Lohman TM, Bujalowski W, Overman LB. E. coli single strand binding protein: a new look at helix-destabilizing proteins Trends in Biochemical Sciences. 13: 250-255. PMID 2855682 |
0.802 |
|
| 1987 |
Bujalowski W, Lohman TM. Limited co-operativity in protein-nucleic acid interactions. A thermodynamic model for the interactions of Escherichia coli single strand binding protein with single-stranded nucleic acids in the "beaded", (SSB)65 mode Journal of Molecular Biology. 195: 897-907. PMID 3309344 DOI: 10.1016/0022-2836(87)90493-1 |
0.745 |
|
| 1987 |
Bujalowski W. A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to escherichia coli single-strand binding protein-nucleic acid interactions Biochemistry. 26: 3099-3106. PMID 3300771 DOI: 10.1021/BI00385A023 |
0.51 |
|
| 1986 |
Bujalowski W, Lohman TM. Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNA Biochemistry. 25: 7799-7802. PMID 3542037 |
0.762 |
|
| 1986 |
Bujalowski W, Jung M, McLaughlin LW, Porschke D. Codon-induced association of the isolated anticodon loop of tRNAPhe. Biochemistry. 25: 6372-8. PMID 3539190 DOI: 10.1021/Bi00369A005 |
0.337 |
|
| 1986 |
Bujalowski W, Graeser E, McLaughlin LW, Proschke D. Anticodon loop of tRNAPhe: structure, dynamics, and Mg2+ binding. Biochemistry. 25: 6365-71. PMID 3539189 DOI: 10.1021/Bi00369A004 |
0.407 |
|
| 1984 |
Bujalowski W, Porschke D. Selective binding of amino add residues to tRNAPhe Nucleic Acids Research. 12: 7549-7563. PMID 6387624 DOI: 10.1093/nar/12.19.7549 |
0.506 |
|
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