Year |
Citation |
Score |
2023 |
Foroutannejad S, Good LL, Lin C, Carter ZI, Tadesse MG, Lucius AL, Crane BR, Maillard RA. The cofactor-dependent folding mechanism of Drosophila cryptochrome revealed by single-molecule pulling experiments. Nature Communications. 14: 1057. PMID 36828841 DOI: 10.1038/s41467-023-36701-y |
0.355 |
|
2022 |
Lin J, Shorter J, Lucius AL. AAA+ proteins: one motor, multiple ways to work. Biochemical Society Transactions. PMID 35356966 DOI: 10.1042/BST20200350 |
0.758 |
|
2020 |
Scull NW, Lucius AL. Kinetic Analysis of AAA+ Translocases by Combined Fluorescence and Anisotropy Methods. Biophysical Journal. 119: 1335-1350. PMID 32997959 DOI: 10.1016/J.Bpj.2020.08.018 |
0.394 |
|
2020 |
Lopez KE, Rizo AN, Tse E, Lin J, Scull NW, Thwin AC, Lucius AL, Shorter J, Southworth DR. Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis. Nature Structural & Molecular Biology. PMID 32313240 DOI: 10.1038/S41594-020-0409-5 |
0.778 |
|
2020 |
Lucius AL. Molecular Mechanisms of Enzyme Catalyzed Protein Unfolding and Translocation by Class 1 AAA+ Motor Biophysical Journal. 118: 319a. DOI: 10.1016/J.Bpj.2019.11.1793 |
0.367 |
|
2019 |
Scull CE, Clarke AM, Lucius AL, Schneider DA. Downstream sequence-dependent RNA cleavage and pausing by RNA polymerase I. The Journal of Biological Chemistry. PMID 31843971 DOI: 10.1074/Jbc.Ra119.011354 |
0.344 |
|
2019 |
Duran EC, Lucius AL. Examination of the nucleotide linked assembly mechanism of E. coli ClpA. Protein Science : a Publication of the Protein Society. PMID 31054177 DOI: 10.1002/Pro.3638 |
0.485 |
|
2019 |
Durie CL, Lin J, Scull NW, Mack KL, Jackrel ME, Sweeny EA, Castellano LM, Shorter J, Lucius AL. Hsp104 and Potentiated Variants Can Operate as Distinct Nonprocessive Translocases. Biophysical Journal. PMID 31027887 DOI: 10.1016/J.Bpj.2019.03.035 |
0.778 |
|
2019 |
Scull CE, Ingram ZM, Lucius AL, Schneider DA. A novel assay for RNA polymerase I transcription elongation sheds light on the evolutionary divergence of eukaryotic RNA polymerases. Biochemistry. PMID 30912638 DOI: 10.1021/Acs.Biochem.8B01256 |
0.306 |
|
2018 |
Duran EC, Lucius AL. ATP hydrolysis inactivating Walker B mutation perturbs E. coli ClpA self-assembly energetics in the absence of nucleotide. Biophysical Chemistry. 242: 6-14. PMID 30173103 DOI: 10.1016/J.Bpc.2018.08.005 |
0.408 |
|
2018 |
Durie CL, Duran EC, Lucius AL. Escherichia coli DnaK allosterically modulates ClpB between high and low peptide affinity states. Biochemistry. PMID 29812913 DOI: 10.1021/Acs.Biochem.8B00045 |
0.412 |
|
2018 |
Weaver CL, Jackrel ME, Lin J, Mack KL, Sweeny E, Duran EC, Shorter J, Lucius AL. Kinetic Mechanism of ATP-Dependent Disaggregating Motor Saccharomyces cerevisiae Hsp104 Biophysical Journal. 114: 553a. DOI: 10.1016/J.Bpj.2017.11.3021 |
0.756 |
|
2017 |
Duran EC, Weaver CL, Lucius AL. Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions. Frontiers in Molecular Biosciences. 4: 54. PMID 28824920 DOI: 10.3389/Fmolb.2017.00054 |
0.42 |
|
2017 |
Weaver CL, Duran EC, Mack KL, Lin J, Jackrel ME, Sweeny EA, Shorter J, Lucius AL. Avidity for polypeptide binding by nucleotide-bound Hsp104 structures. Biochemistry. PMID 28379007 DOI: 10.1021/Acs.Biochem.7B00225 |
0.774 |
|
2016 |
Lin J, Lucius AL. Examination of ClpB quaternary structure and linkage to nucleotide binding. Biochemistry. PMID 26891079 DOI: 10.1016/J.Bpj.2015.11.1129 |
0.789 |
|
2015 |
Appling FD, Lucius AL, Schneider DA. Transient-State Kinetic Analysis of the RNA Polymerase I Nucleotide Incorporation Mechanism. Biophysical Journal. 109: 2382-2393. PMID 26636949 DOI: 10.1016/J.Bpj.2015.10.037 |
0.329 |
|
2015 |
Lin J, Lucius AL. Analysis of Linked Equilibria. Methods in Enzymology. 562: 161-86. PMID 26412651 DOI: 10.1016/Bs.Mie.2015.07.003 |
0.775 |
|
2015 |
Lin J, Lucius AL. Examination of the dynamic assembly equilibrium for E. coli ClpB. Proteins. PMID 26313457 DOI: 10.1002/Prot.24914 |
0.766 |
|
2015 |
Li T, Weaver CL, Lin J, Duran EC, Miller JM, Lucius AL. Escherichia coli ClpB is a non-processive polypeptide translocase. The Biochemical Journal. 470: 39-52. PMID 26251445 DOI: 10.1042/Bj20141457 |
0.752 |
|
2015 |
Li T, Lin J, Lucius AL. Examination of polypeptide substrate specificity for Escherichia coli ClpB. Proteins. 83: 117-34. PMID 25363713 DOI: 10.1002/Prot.24710 |
0.764 |
|
2015 |
Stafford RP, Lucius AL. Using Sedimentation Velocity to Investigate the Nucleotide-Linked Assembly of E. coli ClpA Biophysical Journal. 108: 56a. DOI: 10.1016/J.Bpj.2014.11.341 |
0.471 |
|
2015 |
Lin J, Lucius AL. Thermodynamic and Hydrodynamic Examination of ClpB Assembly Biophysical Journal. 108: 222a. DOI: 10.1016/J.Bpj.2014.11.1224 |
0.769 |
|
2014 |
Fancy RM, Wang L, Napier T, Lin J, Jing G, Lucius AL, McDonald JM, Zhou T, Song Y. Characterization of calmodulin-Fas death domain interaction: an integrated experimental and computational study. Biochemistry. 53: 2680-8. PMID 24702583 DOI: 10.1021/Bi500228H |
0.707 |
|
2014 |
Miller JM, Lucius AL. ATPγS competes with ATP for binding at Domain 1 but not Domain 2 during ClpA catalyzed polypeptide translocation. Biophysical Chemistry. 185: 58-69. PMID 24362308 DOI: 10.1016/J.Bpc.2013.11.002 |
0.395 |
|
2013 |
Li T, Lucius AL. Examination of the polypeptide substrate specificity for Escherichia coli ClpA. Biochemistry. 52: 4941-54. PMID 23773038 DOI: 10.1021/Bi400178Q |
0.502 |
|
2013 |
Miller JM, Lin J, Li T, Lucius AL. E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP. Journal of Molecular Biology. 425: 2795-812. PMID 23639359 DOI: 10.1016/J.Jmb.2013.04.019 |
0.78 |
|
2012 |
Lucius AL, Veronese PK, Stafford RP. Dynamic light scattering to study allosteric regulation. Methods in Molecular Biology (Clifton, N.J.). 796: 175-86. PMID 22052490 DOI: 10.1007/978-1-61779-334-9_9 |
0.381 |
|
2011 |
Veronese PK, Rajendar B, Lucius AL. Activity of E. coli ClpA bound by nucleoside diphosphates and triphosphates. Journal of Molecular Biology. 409: 333-47. PMID 21376057 DOI: 10.1016/J.Jmb.2011.02.018 |
0.486 |
|
2011 |
Lucius AL, Miller JM, Rajendar B. Application of the sequential n-step kinetic mechanism to polypeptide translocases. Methods in Enzymology. 488: 239-64. PMID 21195231 DOI: 10.1016/B978-0-12-381268-1.00010-0 |
0.456 |
|
2011 |
Miller JM, Lucius AL. An Examination of the Kinetic Mechanism of the ATP-Dependent Protease ClpAP Biophysical Journal. 100: 392a. DOI: 10.1016/J.Bpj.2010.12.2326 |
0.457 |
|
2011 |
Lucius AL. Structural and Functional Studies of the E. Coli ClpA Molecular Motor Biophysical Journal. 100: 390a-391a. DOI: 10.1016/J.Bpj.2010.12.2320 |
0.456 |
|
2010 |
Veronese PK, Lucius AL. Effect of temperature on the self-assembly of the Escherichia coli ClpA molecular chaperone. Biochemistry. 49: 9820-9. PMID 20964444 DOI: 10.1021/Bi101136D |
0.391 |
|
2010 |
Rajendar B, Lucius AL. Molecular mechanism of polypeptide translocation catalyzed by the Escherichia coli ClpA protein translocase. Journal of Molecular Biology. 399: 665-79. PMID 20380838 DOI: 10.1016/J.Jmb.2010.03.061 |
0.436 |
|
2009 |
Veronese PK, Stafford RP, Lucius AL. The Escherichia coli ClpA molecular chaperone self-assembles into tetramers. Biochemistry. 48: 9221-33. PMID 19650643 DOI: 10.1021/Bi900935Q |
0.498 |
|
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 |
0.705 |
|
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 |
0.653 |
|
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 |
0.68 |
|
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 |
0.703 |
|
2005 |
Wong CJ, Lucius AL, Lohman TM. Energetics of DNA end binding by E.coli RecBC and RecBCD helicases indicate loop formation in the 3'-single-stranded DNA tail. Journal of Molecular Biology. 352: 765-82. PMID 16126227 DOI: 10.1016/J.Jmb.2005.07.056 |
0.657 |
|
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 |
0.667 |
|
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+ |
0.688 |
|
2004 |
Lucius AL, Lohman TM. Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E.coli RecBCD helicase-catalyzed DNA unwinding. Journal of Molecular Biology. 339: 751-71. PMID 15165848 DOI: 10.1016/J.Jmb.2004.04.010 |
0.643 |
|
2004 |
Lucius AL, Wong CJ, Lohman TM. Fluorescence stopped-flow studies of single turnover kinetics of E.coli RecBCD helicase-catalyzed DNA unwinding. Journal of Molecular Biology. 339: 731-50. PMID 15165847 DOI: 10.1016/J.Jmb.2004.04.009 |
0.617 |
|
2003 |
Lucius AL, Maluf NK, Fischer CJ, Lohman TM. General methods for analysis of sequential "n-step" kinetic mechanisms: application to single turnover kinetics of helicase-catalyzed DNA unwinding. Biophysical Journal. 85: 2224-39. PMID 14507688 DOI: 10.1016/S0006-3495(03)74648-7 |
0.765 |
|
2003 |
Lohman TM, Hsieh J, Maluf NK, Cheng W, Lucius AL, Fischer CJ, Brendza KM, Korolev S, Waksman G. DNA helicases, motors that move along nucleic acids: Lessons from the SF1 helicase superfamily Enzymes. 23: 303-369,III-VII. DOI: 10.1016/S1874-6047(04)80008-8 |
0.733 |
|
2002 |
Lucius AL, Vindigni A, Gregorian R, Ali JA, Taylor AF, Smith GR, Lohman TM. DNA unwinding step-size of E. coli RecBCD helicase determined from single turnover chemical quenched-flow kinetic studies. Journal of Molecular Biology. 324: 409-28. PMID 12445778 DOI: 10.1016/S0022-2836(02)01067-7 |
0.78 |
|
Show low-probability matches. |