Year |
Citation |
Score |
2023 |
Klontz E, Obi JO, Wang Y, Glendening G, Carr J, Tsibouris C, Buddula S, Nallar S, Soares AS, Beckett D, Redzic JS, Eisenmesser E, Palm C, Schmidt K, Scudder AH, et al. The structure of NAD consuming protein Acinetobacter baumannii TIR domain shows unique kinetics and conformations. The Journal of Biological Chemistry. 105290. PMID 37758001 DOI: 10.1016/j.jbc.2023.105290 |
0.403 |
|
2023 |
Samanta R, Sanghvi N, Beckett D, Matysiak S. Emergence of allostery through reorganization of protein residue network architecture. The Journal of Chemical Physics. 158: 085104. PMID 36859102 DOI: 10.1063/5.0136010 |
0.373 |
|
2020 |
Wang J, Samanta R, Custer GS, Look C, Matysiak S, Beckett D. Tuning Allostery through integration of Disorder-to-order with a Residue Network. Biochemistry. PMID 31899864 DOI: 10.1021/Acs.Biochem.9B01006 |
0.371 |
|
2020 |
Xu X, Godoy-Ruiz R, Adipietro KA, Peralta C, Ben-Hail D, Varney KM, Cook ME, Roth BM, Wilder PT, Cleveland T, Grishaev A, Neu HM, Michel SLJ, Yu W, Beckett D, et al. Structure of the cell-binding component of the binary toxin reveals a di-heptamer macromolecular assembly. Proceedings of the National Academy of Sciences of the United States of America. PMID 31896582 DOI: 10.1073/Pnas.1919490117 |
0.376 |
|
2020 |
He C, Beckett D. Plasticity in Protein Sequence-Function Relationships Biophysical Journal. 118. DOI: 10.1016/J.Bpj.2019.11.1210 |
0.398 |
|
2019 |
Samanta R, Wang J, Beckett D, Matysiak S. Integration of an Electrostatic Network and Disorder-to-Order Transitions in Protein Allostery Biophysical Journal. 116: 463a. DOI: 10.1016/J.Bpj.2018.11.2503 |
0.311 |
|
2018 |
Beckett D. Specificity and selectivity in post-translational biotin addition. Biochemical Society Transactions. PMID 30381340 DOI: 10.1042/Bst20180425 |
0.412 |
|
2018 |
Bonsor DA, Zhao Q, Schmidinger B, Weiss E, Wang J, Deredge D, Beadenkopf R, Dow B, Fischer W, Beckett D, Wintrode PL, Haas R, Sundberg EJ. The adhesin protein HopQ exploits the dimer interface of human CEACAMs to facilitate translocation of the oncoprotein CagA. The Embo Journal. PMID 29724755 DOI: 10.15252/Embj.201798664 |
0.397 |
|
2018 |
He C, Custer GS, Wang J, Matysiak S, Beckett D. Superrepression through Altered Corepressor-Activated Protein:protein Interactions. Biochemistry. PMID 29355305 DOI: 10.1021/Acs.Biochem.7B01122 |
0.486 |
|
2018 |
Bonsor DA, Zhao Q, Schmidinger B, Weiss E, Wang J, Deredge D, Beadenkopf R, Dow B, Fischer W, Beckett D, Wintrode PL, Haas R, Sundberg EJ. G-104 The Helicobacter pylori adhesin protein HopQ exploits the dimer interface of human CEACAMs for oncoprotein translocation Jaids Journal of Acquired Immune Deficiency Syndromes. 77: 45. DOI: 10.1097/01.Qai.0000532617.80271.6C |
0.356 |
|
2018 |
Beckett D, He C, Wang J, Custer G, Matysiak S. Protein:Protein Interactions Control Sensitivity of a Transcription Response to Input Signal Biophysical Journal. 114: 69a. DOI: 10.1016/J.Bpj.2017.11.426 |
0.443 |
|
2017 |
Wang J, Custer GS, Beckett D, Matysiak S. Long Distance Modulation of Disorder-to-Order in Protein Allostery. Biochemistry. PMID 28718281 DOI: 10.1021/Acs.Biochem.7B00496 |
0.434 |
|
2017 |
Beckett D. A conserved regulatory mechanism in bifunctional biotin protein ligases. Protein Science : a Publication of the Protein Society. PMID 28466579 DOI: 10.1002/Pro.3182 |
0.482 |
|
2016 |
Postel S, Deredge D, Bonsor DA, Yu X, Diederichs K, Helmsing S, Vromen A, Friedler A, Hust M, Egelman EH, Beckett D, Wintrode PL, Sundberg EJ. Bacterial flagellar capping proteins adopt diverse oligomeric states. Elife. 5. PMID 27664419 DOI: 10.7554/Elife.18857 |
0.444 |
|
2016 |
Postel S, Deredge D, Bonsor DA, Yu X, Diederichs K, Helmsing S, Vromen A, Friedler A, Hust M, Egelman EH, Beckett D, Wintrode PL, Sundberg EJ. Author response: Bacterial flagellar capping proteins adopt diverse oligomeric states Elife. DOI: 10.7554/Elife.18857.025 |
0.375 |
|
2015 |
Cressman WJ, Beckett D. Heat capacity changes and disorder-to-order in allosteric activation. Biochemistry. PMID 26678378 DOI: 10.1021/Acs.Biochem.5B00949 |
0.508 |
|
2015 |
Bonsor DA, Günther S, Beadenkopf R, Beckett D, Sundberg EJ. Diverse oligomeric states of CEACAM IgV domains. Proceedings of the National Academy of Sciences of the United States of America. 112: 13561-6. PMID 26483485 DOI: 10.1073/Pnas.1509511112 |
0.393 |
|
2015 |
Bonsor DA, Beckett D, Sundberg EJ. Structure of the N-terminal dimerization domain of CEACAM7. Acta Crystallographica. Section F, Structural Biology Communications. 71: 1169-75. PMID 26323304 DOI: 10.1107/S2053230X15013576 |
0.35 |
|
2015 |
Bonsor DA, Pham KT, Beadenkopf R, Diederichs K, Haas R, Beckett D, Fischer W, Sundberg EJ. Integrin Engagement by the Helical RGD Motif of the Helicobacter pylori CagL Protein Is Regulated by pH-induced Displacement of a Neighboring Helix. The Journal of Biological Chemistry. 290: 12929-40. PMID 25837254 DOI: 10.1074/Jbc.M115.641829 |
0.374 |
|
2015 |
Eginton C, Cressman WJ, Bachas S, Wade H, Beckett D. Allosteric coupling via distant disorder-to-order transitions. Journal of Molecular Biology. 427: 1695-704. PMID 25746672 DOI: 10.1016/J.Jmb.2015.02.021 |
0.482 |
|
2015 |
Eginton C, Naganathan S, Beckett D. Sequence-function relationships in folding upon binding. Protein Science : a Publication of the Protein Society. 24: 200-11. PMID 25407143 DOI: 10.1002/Pro.2605 |
0.727 |
|
2015 |
Beckett D, Cressman W. Critical Role of a Glycine Residue in an Allosteric Switch Biophysical Journal. 108: 531a. DOI: 10.1016/J.Bpj.2014.11.2909 |
0.441 |
|
2014 |
Beckett D, Eginton C, Bachas S, Wade H. Allosteric Coupling via Communication of Distal Disorder-To-Order Transitions Biophysical Journal. 106: 438a. DOI: 10.1016/J.Bpj.2013.11.2468 |
0.485 |
|
2014 |
Eginton C, Beckett D. Sequence-Function Relationships in Allostery Mediated by Disorder-To-Order Transitions Biophysical Journal. 106: 256a. DOI: 10.1016/J.Bpj.2013.11.1503 |
0.507 |
|
2013 |
Eginton C, Beckett D. A large solvent isotope effect on protein association thermodynamics. Biochemistry. 52: 6595-600. PMID 23984950 DOI: 10.1021/Bi400952M |
0.437 |
|
2013 |
Adikaram PR, Beckett D. Protein:protein interactions in control of a transcriptional switch. Journal of Molecular Biology. 425: 4584-94. PMID 23896299 DOI: 10.1016/J.Jmb.2013.07.029 |
0.812 |
|
2013 |
Beckett D, Adikaram P. Protein: Protein Interactions in Control of the Escherichia Coli Biotin Protein Ligase Functional Switch Biophysical Journal. 104: 660a-661a. DOI: 10.1016/J.Bpj.2012.11.3645 |
0.819 |
|
2013 |
Eginton C, Beckett D. The Sequence and Function Relationship in Ligand-Induced Folding Biophysical Journal. 104: 568a. DOI: 10.1016/J.Bpj.2012.11.3150 |
0.566 |
|
2012 |
Hondorp ER, Hou SC, Hempstead AD, Hause LL, Beckett DM, McIver KS. Characterization of the Group A Streptococcus Mga virulence regulator reveals a role for the C-terminal region in oligomerization and transcriptional activation. Molecular Microbiology. 83: 953-67. PMID 22468267 DOI: 10.1111/J.1365-2958.2012.07980.X |
0.358 |
|
2012 |
Adikaram PR, Beckett D. Functional versatility of a single protein surface in two protein:protein interactions. Journal of Molecular Biology. 419: 223-33. PMID 22446587 DOI: 10.1016/J.Jmb.2012.03.010 |
0.828 |
|
2012 |
Ingaramo M, Beckett D. Selectivity in post-translational biotin addition to five human carboxylases. The Journal of Biological Chemistry. 287: 1813-22. PMID 22123817 DOI: 10.1074/Jbc.M111.275982 |
0.761 |
|
2012 |
Adikaram P, Beckett D. Surface Loops in Evolution of Bispecific Protein: Protein Interactions Biophysical Journal. 102: 258a. DOI: 10.1016/J.Bpj.2011.11.1421 |
0.831 |
|
2011 |
Tungtur S, Skinner H, Zhan H, Swint-Kruse L, Beckett D. In vivo tests of thermodynamic models of transcription repressor function. Biophysical Chemistry. 159: 142-51. PMID 21715082 DOI: 10.1016/J.Bpc.2011.06.005 |
0.406 |
|
2011 |
Ingaramo M, Beckett D. Biotinylation, a post-translational modification controlled by the rate of protein-protein association. The Journal of Biological Chemistry. 286: 13071-8. PMID 21343300 DOI: 10.1074/Jbc.M110.183624 |
0.785 |
|
2011 |
Beckett D. Measurement and analysis of equilibrium binding titrations: A beginner's guide. Methods in Enzymology. 488: 1-16. PMID 21195222 DOI: 10.1016/B978-0-12-381268-1.00001-X |
0.485 |
|
2011 |
Eginton C, Talbert C, Beckett D. Adaptative Ligand Induced Folding in an Allosteric Response Biophysical Journal. 100: 53a. DOI: 10.1016/J.Bpj.2010.12.485 |
0.49 |
|
2011 |
Beckett D. Folding and Dynamics in an Allosteric Response Biophysical Journal. 100: 27a. DOI: 10.1016/J.Bpj.2010.12.350 |
0.458 |
|
2011 |
Adikaram P, Beckett D. Structural Basis of Bispecific Protein:Protein Interactions Biophysical Journal. 100: 388a. DOI: 10.1016/J.Bpj.2010.12.2308 |
0.824 |
|
2010 |
Daniels KG, Beckett D. Biochemical properties and biological function of a monofunctional microbial biotin protein ligase. Biochemistry. 49: 5358-65. PMID 20499837 DOI: 10.1021/Bi1003958 |
0.491 |
|
2010 |
Ingaramo M, Beckett D. Reactivity of Human Holocarboxylase Synthetase Toward Biotin-Accepting Substrates Biophysical Journal. 98: 741a. DOI: 10.1016/J.Bpj.2009.12.4064 |
0.78 |
|
2010 |
Daniels K, Beckett D. Correlation Between Functionality and Biochemical Properties in Biotin Protein Ligases Biophysical Journal. 98: 38a. DOI: 10.1016/J.Bpj.2009.12.221 |
0.479 |
|
2009 |
Beckett D. Regulating transcription regulators via allostery and flexibility. Proceedings of the National Academy of Sciences of the United States of America. 106: 22035-6. PMID 20080782 DOI: 10.1073/Pnas.0912300107 |
0.45 |
|
2009 |
Ingaramo M, Beckett D. Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition. The Journal of Biological Chemistry. 284: 30862-70. PMID 19740736 DOI: 10.1074/Jbc.M109.046201 |
0.779 |
|
2009 |
Zhao H, Naganathan S, Beckett D. Thermodynamic and structural investigation of bispecificity in protein-protein interactions. Journal of Molecular Biology. 389: 336-48. PMID 19361526 DOI: 10.1016/J.Jmb.2009.04.009 |
0.744 |
|
2009 |
Beckett D. Biotin sensing at the molecular level. The Journal of Nutrition. 139: 167-70. PMID 19056812 DOI: 10.3945/Jn.108.095760 |
0.53 |
|
2008 |
Laine O, Streaker ED, Nabavi M, Fenselau CC, Beckett D. Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics. Journal of Molecular Biology. 381: 89-101. PMID 18586268 DOI: 10.1016/J.Jmb.2008.05.018 |
0.498 |
|
2008 |
Zhao H, Beckett D. Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch. Journal of Molecular Biology. 380: 223-36. PMID 18508076 DOI: 10.1016/J.Jmb.2008.04.068 |
0.595 |
|
2008 |
Beckett D. Linked equilibria in regulation of transcription initiation. Methods in Cell Biology. 84: 25-52. PMID 17964927 DOI: 10.1016/S0091-679X(07)84002-7 |
0.496 |
|
2008 |
Ingaramo M, Beckett D. Purification and characterization of human holocarboxylase synthetase The Faseb Journal. 22: 675-675. DOI: 10.1096/Fasebj.22.2_Supplement.675 |
0.698 |
|
2007 |
Zhao H, Streaker E, Pan W, Beckett D. Protein-protein interactions dominate the assembly thermodynamics of a transcription repression complex. Biochemistry. 46: 13667-76. PMID 17973495 DOI: 10.1021/Bi7013097 |
0.542 |
|
2007 |
Naganathan S, Beckett D. Nucleation of an allosteric response via ligand-induced loop folding. Journal of Molecular Biology. 373: 96-111. PMID 17765263 DOI: 10.1016/J.Jmb.2007.07.020 |
0.689 |
|
2007 |
Beckett D. Biotin sensing: universal influence of biotin status on transcription. Annual Review of Genetics. 41: 443-64. PMID 17669049 DOI: 10.1146/Annurev.Genet.41.042007.170450 |
0.481 |
|
2006 |
Semavina M, Beckett D, Logan TM. Metal-linked dimerization in the iron-dependent regulator from Mycobacterium tuberculosis. Biochemistry. 45: 12480-90. PMID 17029403 DOI: 10.1021/Bi060797S |
0.398 |
|
2006 |
Streaker ED, Beckett D. Nonenzymatic biotinylation of a biotin carboxyl carrier protein: unusual reactivity of the physiological target lysine. Protein Science : a Publication of the Protein Society. 15: 1928-35. PMID 16823034 DOI: 10.1110/Ps.062187306 |
0.525 |
|
2006 |
Streaker ED, Beckett D. The biotin regulatory system: kinetic control of a transcriptional switch. Biochemistry. 45: 6417-25. PMID 16700552 DOI: 10.1021/Bi052599R |
0.559 |
|
2006 |
Wood ZA, Weaver LH, Brown PH, Beckett D, Matthews BW. Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. Journal of Molecular Biology. 357: 509-23. PMID 16438984 DOI: 10.1016/J.Jmb.2005.12.066 |
0.477 |
|
2005 |
Beckett D. Multilevel regulation of protein-protein interactions in biological circuitry. Physical Biology. 2: S67-73. PMID 16204850 DOI: 10.1088/1478-3975/2/2/S07 |
0.5 |
|
2005 |
Beckett D. The Escherichia coli biotin regulatory system: a transcriptional switch. The Journal of Nutritional Biochemistry. 16: 411-5. PMID 15992680 DOI: 10.1016/J.Jnutbio.2005.03.019 |
0.467 |
|
2005 |
Brown PH, Beckett D. Use of binding enthalpy to drive an allosteric transition. Biochemistry. 44: 3112-21. PMID 15723556 DOI: 10.1021/Bi047792K |
0.466 |
|
2004 |
Beckett D. Functional switches in transcription regulation; molecular mimicry and plasticity in protein-protein interactions. Biochemistry. 43: 7983-91. PMID 15209493 DOI: 10.1021/Bi049890B |
0.525 |
|
2004 |
Beckett D. Linked equilibria in biotin repressor function: thermodynamic, structural, and kinetic analysis. Methods in Enzymology. 379: 209-34. PMID 15051360 DOI: 10.1016/S0076-6879(04)79012-6 |
0.528 |
|
2004 |
Brown PH, Cronan JE, Grøtli M, Beckett D. The biotin repressor: modulation of allostery by corepressor analogs. Journal of Molecular Biology. 337: 857-69. PMID 15033356 DOI: 10.1016/J.Jmb.2004.01.041 |
0.544 |
|
2004 |
Tang C, Loeliger E, Luncsford P, Kinde I, Beckett D, Summers MF. Entropic switch regulates myristate exposure in the HIV-1 matrix protein. Proceedings of the National Academy of Sciences of the United States of America. 101: 517-22. PMID 14699046 DOI: 10.1073/Pnas.0305665101 |
0.346 |
|
2003 |
Streaker ED, Beckett D. Coupling of protein assembly and DNA binding: biotin repressor dimerization precedes biotin operator binding. Journal of Molecular Biology. 325: 937-48. PMID 12527300 DOI: 10.1016/S0022-2836(02)01308-6 |
0.509 |
|
2002 |
Streaker ED, Gupta A, Beckett D. The biotin repressor: thermodynamic coupling of corepressor binding, protein assembly, and sequence-specific DNA binding. Biochemistry. 41: 14263-71. PMID 12450391 DOI: 10.1021/Bi0203839 |
0.542 |
|
2002 |
Kwon K, Streaker ED, Beckett D. Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase. Protein Science : a Publication of the Protein Society. 11: 558-70. PMID 11847279 DOI: 10.1110/Ps.33502 |
0.453 |
|
2001 |
Beckett D. Reduced-scale large-zone analytical gel-filtration chromatography for measurement of protein association equilibria. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit20.5. PMID 18429160 DOI: 10.1002/0471140864.Ps2005S18 |
0.413 |
|
2001 |
Beckett D. Regulated assembly of transcription factors and control of transcription initiation. Journal of Molecular Biology. 314: 335-52. PMID 11846548 DOI: 10.1006/Jmbi.2001.5134 |
0.422 |
|
2001 |
Weaver LH, Kwon K, Beckett D, Matthews BW. Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor. Protein Science : a Publication of the Protein Society. 10: 2618-22. PMID 11714930 DOI: 10.1110/Ps.32701 |
0.541 |
|
2001 |
Weaver LH, Kwon K, Beckett D, Matthews BW. Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator. Proceedings of the National Academy of Sciences of the United States of America. 98: 6045-50. PMID 11353844 DOI: 10.1073/Pnas.111128198 |
0.446 |
|
2000 |
Kwon K, Streaker ED, Ruparelia S, Beckett D. Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor. Journal of Molecular Biology. 304: 821-33. PMID 11124029 DOI: 10.1006/Jmbi.2000.4249 |
0.518 |
|
2000 |
Kwon K, Beckett D. Function of a conserved sequence motif in biotin holoenzyme synthetases. Protein Science : a Publication of the Protein Society. 9: 1530-9. PMID 10975574 DOI: 10.1110/Ps.9.8.1530 |
0.459 |
|
1999 |
Eisenstein E, Beckett D. Dimerization of the Escherichia coli biotin repressor: corepressor function in protein assembly. Biochemistry. 38: 13077-84. PMID 10529178 DOI: 10.1021/Bi991241Q |
0.523 |
|
1999 |
Streaker ED, Beckett D. Ligand-linked structural changes in the Escherichia coli biotin repressor: the significance of surface loops for binding and allostery. Journal of Molecular Biology. 292: 619-32. PMID 10497026 DOI: 10.1006/Jmbi.1999.3086 |
0.512 |
|
1999 |
Beckett D, Kovaleva E, Schatz PJ. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Science : a Publication of the Protein Society. 8: 921-9. PMID 10211839 DOI: 10.1110/Ps.8.4.921 |
0.386 |
|
1999 |
Yao X, Soden C, Summers MF, Beckett D. Comparison of the backbone dynamics of the apo- and holo-carboxy-terminal domain of the biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. Protein Science : a Publication of the Protein Society. 8: 307-17. PMID 10048324 DOI: 10.1110/Ps.8.2.307 |
0.57 |
|
1998 |
Beckett D. Energetic methods to study bifunctional biotin operon repressor. Methods in Enzymology. 295: 424-50. PMID 9750231 DOI: 10.1016/S0076-6879(98)95052-2 |
0.584 |
|
1998 |
Streaker ED, Beckett D. A map of the biotin repressor-biotin operator interface: binding of a winged helix-turn-helix protein dimer to a forty base-pair site. Journal of Molecular Biology. 278: 787-800. PMID 9614942 DOI: 10.1006/Jmbi.1998.1733 |
0.5 |
|
1998 |
Streaker ED, Beckett D. Coupling of site-specific DNA binding to protein dimerization in assembly of the biotin repressor-biotin operator complex. Biochemistry. 37: 3210-9. PMID 9485476 DOI: 10.1021/Bi9715019 |
0.456 |
|
1997 |
Yao X, Wei D, Soden C, Summers MF, Beckett D. Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. Biochemistry. 36: 15089-100. PMID 9398236 DOI: 10.1021/Bi971485F |
0.565 |
|
1997 |
Xu Y, Beckett D. Biotinyl-5'-adenylate synthesis catalyzed by Escherichia coli repressor of biotin biosynthesis. Methods in Enzymology. 279: 405-21. PMID 9211293 DOI: 10.1016/S0076-6879(97)79045-1 |
0.47 |
|
1997 |
Beckett D, Matthews BW. Escherichia coli repressor of biotin biosynthesis. Methods in Enzymology. 279: 362-76. PMID 9211289 DOI: 10.1016/S0076-6879(97)79041-4 |
0.571 |
|
1996 |
Xu Y, Beckett D. Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant. Biochemistry. 35: 1783-92. PMID 8639659 DOI: 10.1021/Bi952269E |
0.493 |
|
1996 |
Nenortas E, Beckett D. Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase. The Journal of Biological Chemistry. 271: 7559-67. PMID 8631788 DOI: 10.1074/Jbc.271.13.7559 |
0.535 |
|
1996 |
Xu Y, Johnson CR, Beckett D. Thermodynamic analysis of small ligand binding to the Escherichia coli repressor of biotin biosynthesis. Biochemistry. 35: 5509-17. PMID 8611542 DOI: 10.1021/Bi9600658 |
0.458 |
|
1995 |
Xu Y, Nenortas E, Beckett D. Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis. Biochemistry. 34: 16624-31. PMID 8527435 DOI: 10.1021/Bi00051A010 |
0.467 |
|
1994 |
Burz DS, Beckett D, Benson N, Ackers GK. Self-assembly of bacteriophage lambda cI repressor: effects of single-site mutations on the monomer-dimer equilibrium. Biochemistry. 33: 8399-405. PMID 8031775 DOI: 10.1021/Bi00194A003 |
0.68 |
|
1994 |
Xu Y, Beckett D. Kinetics of biotinyl-5'-adenylate synthesis catalyzed by the Escherichia coli repressor of biotin biosynthesis and the stability of the enzyme-product complex. Biochemistry. 33: 7354-60. PMID 8003500 DOI: 10.1021/Bi00189A041 |
0.411 |
|
1993 |
Abbott J, Beckett D. Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator sequence. Biochemistry. 32: 9649-56. PMID 8373769 DOI: 10.1021/Bi00088A017 |
0.56 |
|
1993 |
Beckett D, Burz DS, Ackers GK, Sauer RT. Isolation of lambda repressor mutants with defects in cooperative operator binding. Biochemistry. 32: 9073-9. PMID 8369279 DOI: 10.1021/Bi00086A012 |
0.712 |
|
1992 |
Koblan KS, Bain DL, Beckett D, Shea MA, Ackers GK. Analysis of site-specific interaction parameters in protein-DNA complexes Methods in Enzymology. 210: 405-425. PMID 1584044 DOI: 10.1016/0076-6879(92)10021-5 |
0.735 |
|
1991 |
Beckett D, Koblan KS, Ackers GK. Quantitative study of protein association at picomolar concentrations: The λ phage cl repressor Analytical Biochemistry. 196: 69-75. PMID 1888038 DOI: 10.1016/0003-2697(91)90118-D |
0.656 |
|
1988 |
Beckett D, Wu HN, Uhlenbeck OC. Roles of operator and non-operator RNA sequences in bacteriophage R17 capsid assembly. Journal of Molecular Biology. 204: 939-47. PMID 3221401 DOI: 10.1016/0022-2836(88)90053-8 |
0.53 |
|
1988 |
Beckett D, Uhlenbeck OC. Ribonucleoprotein complexes of R17 coat protein and a translational operator analog Journal of Molecular Biology. 204: 927-938. PMID 3221400 DOI: 10.1016/0022-2836(88)90052-6 |
0.584 |
|
1983 |
Uhlenbeck OC, Carey J, Romaniuk PJ, Lowary PT, Beckett D. Interaction of r17 coat protein with its rna binding site for translational repression Journal of Biomolecular Structure and Dynamics. 1: 539-552. PMID 6401118 DOI: 10.1080/07391102.1983.10507460 |
0.723 |
|
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