Year |
Citation |
Score |
2023 |
Jensen D, Ruiz Manzano A, Rector M, Tomko EJ, Record MT, Galburt EA. High-throughput, fluorescent-aptamer-based measurements of steady-state transcription rates for the Mycobacterium tuberculosis RNA polymerase. Nucleic Acids Research. 51: e99. PMID 37739412 DOI: 10.1093/nar/gkad761 |
0.732 |
|
2023 |
Jensen D, Manzano AR, Rector M, Tomko EJ, Record MT, Galburt EA. High-throughput, fluorescent-aptamer-based measurements of steady-state transcription rates for RNA polymerase. Biorxiv : the Preprint Server For Biology. PMID 36993414 DOI: 10.1101/2023.03.13.532464 |
0.732 |
|
2022 |
Kozlov AG, Cheng X, Zhang H, Shinn MK, Weiland E, Nguyen B, Shkel IA, Zytkiewicz E, Finkelstein IJ, Record MT, Lohman TM. How Glutamate Promotes Liquid-liquid Phase Separation and DNA Binding Cooperativity of E. coli SSB Protein. Journal of Molecular Biology. 434: 167562. PMID 35351518 DOI: 10.1016/j.jmb.2022.167562 |
0.77 |
|
2021 |
Plaskon DM, Henderson KL, Felth LC, Molzahn CM, Evensen C, Dyke S, Shkel IA, Record MT. Temperature effects on RNA polymerase initiation kinetics reveal which open complex initiates and that bubble collapse is stepwise. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 34290140 DOI: 10.1073/pnas.2021941118 |
0.673 |
|
2020 |
Sreenivasan R, Shkel IA, Chhabra M, Drennan A, Heitkamp S, Wang HC, Sridevi MA, Plaskon D, McNerney C, Callies K, Cimperman CK, Record MT. Fluorescence-Detected Conformational Changes in Duplex DNA in Open Complex Formation by RNA Polymerase: Upstream Wrapping and Downstream Bending Precede Clamp Opening and Insertion of the Downstream Duplex. Biochemistry. 59: 1565-1581. PMID 32216369 DOI: 10.1021/Acs.Biochem.0C00098 |
0.449 |
|
2020 |
Doughty S, Plaskon D, Record MT. Effects of Discriminator Length on Transcription Initiation by
E. coli
RNA Polymerase The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.04428 |
0.337 |
|
2020 |
Evensen CE, Henderson K, Palatnik B, Ishikuri T, Plaskon D, Record MT. Differential Effects of Physiological Pyrophosphate on the Kinetics of Productive and Abortive Transcription Initiation The Faseb Journal. 34: 1-1. DOI: 10.1096/Fasebj.2020.34.S1.03079 |
0.616 |
|
2019 |
Henderson K, Evensen CE, Molzahn C, Felth LC, Dyke S, Liao G, Shkel IA, Record MT. RNA Polymerase: Step by Step Kinetics and Mechanism of Transcription Initiation. Biochemistry. PMID 30950601 DOI: 10.1021/Acs.Biochem.9B00049 |
0.684 |
|
2019 |
Evensen CE, Henderson K, Record MT. Characterizing Transient Intermediates in Productive RNAP Transcription Initiation Biophysical Journal. 116: 210a. DOI: 10.1016/J.Bpj.2018.11.1158 |
0.617 |
|
2018 |
Cheng X, Shkel IA, Molzahn C, Lambert D, Karim R, Record MT. Quantifying Interactions of Nucleobase Atoms with Model Compounds for the Peptide Backbone and Glutamine, Asparagine Side Chains in Water. Biochemistry. PMID 29533642 DOI: 10.1021/Acs.Biochem.8B00087 |
0.347 |
|
2018 |
Henderson K, Molzahn CM, Felth LC, Evensen C, Dyke S, Liao G, Prazich J, Record MT. Abortive and Productive Transcription Initiation by E. coli RNA Polymerase Biophysical Journal. 114: 246a-247a. DOI: 10.1016/J.Bpj.2017.11.1372 |
0.634 |
|
2017 |
Sengupta R, Capp MW, Shkel IA, Record MT. The mechanism and high-free-energy transition state of lac repressor-lac operator interaction. Nucleic Acids Research. PMID 29036376 DOI: 10.1093/Nar/Gkx862 |
0.381 |
|
2017 |
Cheng X, Shkel IA, Connor KO, Henrich J, Molzahn C, Lambert D, Record MT. Experimental Atom-by-Atom Dissection of Amide-Amide and Amide-Hydrocarbon Interactions in H2O. Journal of the American Chemical Society. PMID 28678492 DOI: 10.1021/Jacs.7B03261 |
0.358 |
|
2017 |
Henderson KL, Felth LC, Molzahn CM, Shkel I, Wang S, Chhabra M, Ruff EF, Bieter L, Kraft JE, Record MT. Mechanism of transcription initiation and promoter escape by E. coli RNA polymerase. Proceedings of the National Academy of Sciences of the United States of America. PMID 28348246 DOI: 10.1073/Pnas.1618675114 |
0.654 |
|
2016 |
Cheng X, Guinn EJ, Buechel E, Wong R, Sengupta R, Shkel IA, Record MT. Basis of Protein Stabilization by K Glutamate: Unfavorable Interactions with Carbon, Oxygen Groups. Biophysical Journal. 111: 1854-1865. PMID 27806267 DOI: 10.1016/J.Bpj.2016.08.050 |
0.388 |
|
2016 |
Sengupta R, Pantel A, Cheng X, Shkel I, Peran I, Stenzoski N, Raleigh DP, Record MT. Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9. Biochemistry. PMID 27054379 DOI: 10.1021/Acs.Biochem.6B00173 |
0.351 |
|
2016 |
Sreenivasan R, Heitkamp S, Chhabra M, Saecker RM, Lingeman E, Poulos M, McCaslin DR, Capp MW, Artsimovitch I, Record MT. FRET Characterization of DNA Wrapping in Closed and Open Escherichia coli RNA Polymerase - λPR Promoter Complexes. Biochemistry. PMID 26998673 DOI: 10.1021/Acs.Biochem.6B00125 |
0.457 |
|
2016 |
Culham DE, Shkel IA, Record MT, Wood JM. Contributions of Coulombic and Hofmeister Effects to the Osmotic Activation of Escherichia coli Transporter ProP. Biochemistry. 55: 1301-13. PMID 26871755 DOI: 10.1021/Acs.Biochem.5B01169 |
0.336 |
|
2016 |
Henderson K, Felth L, Wang S, Molzahn C, Chhabra M, Poulos M, Ruff E, Bieter L, Record MT. Large Effects of Discriminator Exchanges on the RNA Polymerase-Promoter Open Complex Structure, Lifetime and Transcription Initiation Patterns Biophysical Journal. 110: 233a. DOI: 10.1016/J.Bpj.2015.11.1284 |
0.695 |
|
2015 |
Ruff EF, Drennan AC, Capp MW, Poulos MA, Artsimovitch I, Record MT. E. coli RNA Polymerase Determinants of Open Complex Lifetime and Structure. Journal of Molecular Biology. 427: 2435-50. PMID 26055538 DOI: 10.1016/J.Jmb.2015.05.024 |
0.462 |
|
2015 |
Ruff EF, Record MT, Artsimovitch I. Initial events in bacterial transcription initiation. Biomolecules. 5: 1035-62. PMID 26023916 DOI: 10.3390/biom5021035 |
0.332 |
|
2015 |
Knowles DB, Shkel IA, Phan NM, Sternke M, Lingeman E, Cheng X, Cheng L, O'Connor K, Record MT. Chemical Interactions of Polyethylene Glycols (PEGs) and Glycerol with Protein Functional Groups: Applications to Effects of PEG and Glycerol on Protein Processes. Biochemistry. 54: 3528-42. PMID 25962980 DOI: 10.1021/Acs.Biochem.5B00246 |
0.398 |
|
2015 |
Shkel IA, Knowles DB, Record MT. Separating chemical and excluded volume interactions of polyethylene glycols with native proteins: Comparison with PEG effects on DNA helix formation. Biopolymers. 103: 517-27. PMID 25924886 DOI: 10.1002/Bip.22662 |
0.402 |
|
2015 |
Ruff EF, Kontur WS, Record MT. Using solutes and kinetics to probe large conformational changes in the steps of transcription initiation. Methods in Molecular Biology (Clifton, N.J.). 1276: 241-61. PMID 25665568 DOI: 10.1007/978-1-4939-2392-2_14 |
0.434 |
|
2014 |
Ruff E, Svetlov D, Bown N, Persing T, Chong-Macias S, Drennan A, Artsimovitch I, Record MT. Toward a General Mechanism for Transcription Initiation Biophysical Journal. 106: 488a. DOI: 10.1016/J.Bpj.2013.11.4480 |
0.454 |
|
2014 |
Sengupta R, Guinn EJ, Kontur WS, Tsodikov OV, Shkel I, Record MT. Denaturant Probes Quantify the Preferential Burial of Amide Surface in Forming the Key Transition State and Early Intermediates in Protein Folding Biophysical Journal. 106: 469a. DOI: 10.1016/J.Bpj.2013.11.2655 |
0.327 |
|
2013 |
Diehl RC, Guinn EJ, Capp MW, Tsodikov OV, Record MT. Quantifying additive interactions of the osmolyte proline with individual functional groups of proteins: comparisons with urea and glycine betaine, interpretation of m-values. Biochemistry. 52: 5997-6010. PMID 23909383 DOI: 10.1021/Bi400683Y |
0.378 |
|
2013 |
Record MT, Guinn E, Pegram L, Capp M. Introductory lecture: interpreting and predicting Hofmeister salt ion and solute effects on biopolymer and model processes using the solute partitioning model. Faraday Discussions. 160: 9-44; discussion 103. PMID 23795491 DOI: 10.1039/C2Fd20128C |
0.385 |
|
2013 |
Guinn EJ, Schwinefus JJ, Cha HK, McDevitt JL, Merker WE, Ritzer R, Muth GW, Engelsgjerd SW, Mangold KE, Thompson PJ, Kerins MJ, Record MT. Quantifying functional group interactions that determine urea effects on nucleic acid helix formation. Journal of the American Chemical Society. 135: 5828-38. PMID 23510511 DOI: 10.1021/Ja400965N |
0.437 |
|
2012 |
Shkel IA, Record MT. Coulombic free energy and salt ion association per phosphate of all-atom models of DNA oligomer: dependence on oligomer size. Soft Matter. 8: 9345-9355. PMID 26005495 DOI: 10.1039/C2Sm25607J |
0.451 |
|
2012 |
Drennan A, Kraemer M, Capp M, Gries T, Ruff E, Sheppard C, Wigneshweraraj S, Artsimovitch I, Record MT. Key roles of the downstream mobile jaw of Escherichia coli RNA polymerase in transcription initiation. Biochemistry. 51: 9447-59. PMID 23116321 DOI: 10.1021/Bi301260U |
0.498 |
|
2012 |
Drennan A, Saecker R, Heitkamp S, Capp M, Kraemer M, Bellissimo D, Gries T, Ruff E, Sheppard C, Wigneshweraraj S, Artsimovitch I, Record MT. E. Coli RNA Polymerase: A Molecular DNA Opening Machine Biophysical Journal. 102: 286a. DOI: 10.1016/J.Bpj.2011.11.1583 |
0.43 |
|
2012 |
Heitkamp S, Lingeman E, Capp M, Saecker R, Record MT. Use of Fast DNA Footprinting and Real-Time Fluorescence Spectroscopy to Characterize Novel, Biologically Revlevant Transcription Initiation Intermediates for E. Coli RNA Polymerase Biophysical Journal. 102: 286a. DOI: 10.1016/J.Bpj.2011.11.1581 |
0.467 |
|
2012 |
Record MT, Knowles DB. Separating Excluded Volume and Chemical Effects of PEG on DNA Helix Formation Biophysical Journal. 102: 3a. DOI: 10.1016/J.Bpj.2011.11.032 |
0.448 |
|
2011 |
Guinn EJ, Pegram LM, Capp MW, Pollock MN, Record MT. Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer. Proceedings of the National Academy of Sciences of the United States of America. 108: 16932-7. PMID 21930943 DOI: 10.1073/Pnas.1109372108 |
0.363 |
|
2011 |
Knowles DB, LaCroix AS, Deines NF, Shkel I, Record MT. Separation of preferential interaction and excluded volume effects on DNA duplex and hairpin stability. Proceedings of the National Academy of Sciences of the United States of America. 108: 12699-704. PMID 21742980 DOI: 10.1073/Pnas.1103382108 |
0.46 |
|
2011 |
Koh J, Shkel I, Saecker RM, Record MT. Nonspecific DNA binding and bending by HUαβ: interfaces of the three binding modes characterized by salt-dependent thermodynamics. Journal of Molecular Biology. 410: 241-67. PMID 21513716 DOI: 10.1016/J.Jmb.2011.04.001 |
0.425 |
|
2011 |
Saecker RM, Record MT, Dehaseth PL. Mechanism of bacterial transcription initiation: RNA polymerase - promoter binding, isomerization to initiation-competent open complexes, and initiation of RNA synthesis. Journal of Molecular Biology. 412: 754-71. PMID 21371479 DOI: 10.1016/J.Jmb.2011.01.018 |
0.457 |
|
2011 |
Drennan A, Gries T, Heitkamp S, Ruff E, Saecker R, Record MT. Probing DNA Binding, DNA Opening and Assembly of a Downstream Clamp During Transcription Initiation by E. coli RNA Polymerase at the λPR Promoter Biophysical Journal. 100: 66a. DOI: 10.1016/J.Bpj.2010.12.557 |
0.48 |
|
2011 |
Knowles D, Deines N, Lacroix A, Record MT. Separation of Preferential Interaction and Crowding Effects on DNA Hairpin and Duplex Formation Biophysical Journal. 100: 57a-58a. DOI: 10.1016/J.Bpj.2010.12.511 |
0.464 |
|
2010 |
Gries TJ, Kontur WS, Capp MW, Saecker RM, Record MT. One-step DNA melting in the RNA polymerase cleft opens the initiation bubble to form an unstable open complex. Proceedings of the National Academy of Sciences of the United States of America. 107: 10418-23. PMID 20483995 DOI: 10.1073/Pnas.1000967107 |
0.444 |
|
2010 |
Pegram LM, Wendorff T, Erdmann R, Shkel I, Bellissimo D, Felitsky DJ, Record MT. Why Hofmeister effects of many salts favor protein folding but not DNA helix formation. Proceedings of the National Academy of Sciences of the United States of America. 107: 7716-21. PMID 20385834 DOI: 10.1073/Pnas.0913376107 |
0.439 |
|
2010 |
Kontur WS, Capp MW, Gries TJ, Saecker RM, Record MT. Probing DNA binding, DNA opening, and assembly of a downstream clamp/jaw in Escherichia coli RNA polymerase-lambdaP(R) promoter complexes using salt and the physiological anion glutamate. Biochemistry. 49: 4361-73. PMID 20201585 DOI: 10.1021/Bi100092A |
0.479 |
|
2010 |
Ballin JD, Prevas JP, Ross CR, Toth EA, Wilson GM, Record MT. Contributions of the histidine side chain and the N-terminal alpha-amino group to the binding thermodynamics of oligopeptides to nucleic acids as a function of pH. Biochemistry. 49: 2018-30. PMID 20108951 DOI: 10.1021/Bi902027Z |
0.386 |
|
2010 |
Bleam ML, Anderson CF, Record MT. Relative binding affinities of monovalent cations for double-stranded DNA. Proceedings of the National Academy of Sciences of the United States of America. 77: 3085-9. PMID 16592827 DOI: 10.1073/Pnas.77.6.3085 |
0.435 |
|
2009 |
Capp MW, Pegram LM, Saecker RM, Kratz M, Riccardi D, Wendorff T, Cannon JG, Record MT. Interactions of the osmolyte glycine betaine with molecular surfaces in water: thermodynamics, structural interpretation, and prediction of m-values. Biochemistry. 48: 10372-9. PMID 19757837 DOI: 10.1021/Bi901273R |
0.398 |
|
2009 |
Pegram LM, Record MT. Using surface tension data to predict differences in surface and bulk concentrations of nonelectrolytes in water. The Journal of Physical Chemistry. C, Nanomaterials and Interfaces. 113: 2171-2174. PMID 19436772 DOI: 10.1021/Jp8073305 |
0.322 |
|
2009 |
Pegram LM, Record MT. Quantifying the roles of water and solutes (denaturants, osmolytes, and Hofmeister salts) in protein and model processes using the solute partitioning model. Methods in Molecular Biology (Clifton, N.J.). 490: 179-93. PMID 19157084 DOI: 10.1007/978-1-59745-367-7_8 |
0.314 |
|
2009 |
Schroeder LA, Gries TJ, Saecker RM, Record MT, Harris ME, DeHaseth PL. Evidence for a tyrosine-adenine stacking interaction and for a short-lived open intermediate subsequent to initial binding of Escherichia coli RNA polymerase to promoter DNA. Journal of Molecular Biology. 385: 339-49. PMID 18976666 DOI: 10.1016/J.Jmb.2008.10.023 |
0.48 |
|
2009 |
Koh J, Saecker RM, Record MT. Thermodynamics of Interactions between Histone-like Proteins from Escherichia coli (HU and IHF) and Intact Duplex DNA Biophysical Journal. 96: 59a. DOI: 10.1016/J.Bpj.2008.12.205 |
0.441 |
|
2009 |
Gries TJ, Kontur WS, Capp MW, Davis CA, Drennan AC, Saecker RM, Record MT. Rapid-Quench Mixing and Use of Fast Footprinting to Characterize DNA Opening in the Late Steps of Open Complex Formation at λPR by E. coli RNA Polymerase Biophysical Journal. 96: 55a. DOI: 10.1016/J.Bpj.2008.12.182 |
0.469 |
|
2008 |
Vander Meulen KA, Davis JH, Foster TR, Record MT, Butcher SE. Thermodynamics and folding pathway of tetraloop receptor-mediated RNA helical packing. Journal of Molecular Biology. 384: 702-17. PMID 18845162 DOI: 10.1016/J.Jmb.2008.09.049 |
0.77 |
|
2008 |
Koh J, Saecker RM, Record MT. DNA binding mode transitions of Escherichia coli HU(alphabeta): evidence for formation of a bent DNA--protein complex on intact, linear duplex DNA. Journal of Molecular Biology. 383: 324-46. PMID 18657548 DOI: 10.1016/J.Jmb.2008.07.024 |
0.426 |
|
2008 |
Pegram LM, Record MT. Thermodynamic origin of hofmeister ion effects. The Journal of Physical Chemistry. B. 112: 9428-36. PMID 18630860 DOI: 10.1021/Jp800816A |
0.335 |
|
2008 |
Vander Meulen KA, Saecker RM, Record MT. Formation of a wrapped DNA-protein interface: experimental characterization and analysis of the large contributions of ions and water to the thermodynamics of binding IHF to H' DNA. Journal of Molecular Biology. 377: 9-27. PMID 18237740 DOI: 10.1016/J.Jmb.2007.11.104 |
0.789 |
|
2008 |
Kontur WS, Saecker RM, Capp MW, Record MT. Late steps in the formation of E. coli RNA polymerase-lambda P R promoter open complexes: characterization of conformational changes by rapid [perturbant] upshift experiments. Journal of Molecular Biology. 376: 1034-47. PMID 18191943 DOI: 10.1016/J.Jmb.2007.11.064 |
0.387 |
|
2008 |
Anderson CF, Record MT. The relationship between the poisson-boltzmann model and the condensation hypothesis: an analysis based on the low salt form of the Donnan coefficient. Biophysical Chemistry. 11: 353-60. PMID 16997254 DOI: 10.1016/0301-4622(80)87008-6 |
0.317 |
|
2007 |
Konopka MC, Weisshaar JC, Record MT. Methods of changing biopolymer volume fraction and cytoplasmic solute concentrations for in vivo biophysical studies. Methods in Enzymology. 428: 487-504. PMID 17875435 DOI: 10.1016/S0076-6879(07)28027-9 |
0.329 |
|
2007 |
Cannon JG, Anderson CF, Record MT. Urea-amide preferential interactions in water: quantitative comparison of model compound data with biopolymer results using water accessible surface areas. The Journal of Physical Chemistry. B. 111: 9675-85. PMID 17658791 DOI: 10.1021/Jp072037C |
0.373 |
|
2007 |
Davis CA, Bingman CA, Landick R, Record MT, Saecker RM. Real-time footprinting of DNA in the first kinetically significant intermediate in open complex formation by Escherichia coli RNA polymerase. Proceedings of the National Academy of Sciences of the United States of America. 104: 7833-8. PMID 17470797 DOI: 10.1073/Pnas.0609888104 |
0.443 |
|
2006 |
Konopka MC, Shkel IA, Cayley S, Record MT, Weisshaar JC. Crowding and confinement effects on protein diffusion in vivo. Journal of Bacteriology. 188: 6115-23. PMID 16923878 DOI: 10.1128/Jb.01982-05 |
0.302 |
|
2006 |
Shkel IA, Ballin JD, Record MT. Interactions of cationic ligands and proteins with small nucleic acids: analytic treatment of the large coulombic end effect on binding free energy as a function of salt concentration. Biochemistry. 45: 8411-26. PMID 16819840 DOI: 10.1021/Bi0520434 |
0.44 |
|
2006 |
Kontur WS, Saecker RM, Davis CA, Capp MW, Record MT. Solute probes of conformational changes in open complex (RPo) formation by Escherichia coli RNA polymerase at the lambdaPR promoter: evidence for unmasking of the active site in the isomerization step and for large-scale coupled folding in the subsequent conversion to RPo. Biochemistry. 45: 2161-77. PMID 16475805 DOI: 10.1021/Bi051835V |
0.438 |
|
2005 |
Hong J, Capp MW, Saecker RM, Record MT. Use of urea and glycine betaine to quantify coupled folding and probe the burial of DNA phosphates in lac repressor-lac operator binding. Biochemistry. 44: 16896-911. PMID 16363803 DOI: 10.1021/Bi0515218 |
0.405 |
|
2005 |
Davis CA, Capp MW, Record MT, Saecker RM. The effects of upstream DNA on open complex formation by Escherichia coli RNA polymerase. Proceedings of the National Academy of Sciences of the United States of America. 102: 285-90. PMID 15626761 DOI: 10.1073/Pnas.0405779102 |
0.497 |
|
2004 |
Hong J, Capp MW, Anderson CF, Saecker RM, Felitsky DJ, Anderson MW, Record MT. Preferential interactions of glycine betaine and of urea with DNA: implications for DNA hydration and for effects of these solutes on DNA stability. Biochemistry. 43: 14744-58. PMID 15544345 DOI: 10.1021/Bi049096Q |
0.481 |
|
2004 |
Felitsky DJ, Cannon JG, Capp MW, Hong J, Van Wynsberghe AW, Anderson CF, Record MT. The exclusion of glycine betaine from anionic biopolymer surface: why glycine betaine is an effective osmoprotectant but also a compatible solute. Biochemistry. 43: 14732-43. PMID 15544344 DOI: 10.1021/Bi049115W |
0.375 |
|
2004 |
Cayley S, Record MT. Large changes in cytoplasmic biopolymer concentration with osmolality indicate that macromolecular crowding may regulate protein-DNA interactions and growth rate in osmotically stressed Escherichia coli K-12. Journal of Molecular Recognition : Jmr. 17: 488-96. PMID 15362109 DOI: 10.1002/Jmr.695 |
0.338 |
|
2004 |
Felitsky DJ, Record MT. Application of the local-bulk partitioning and competitive binding models to interpret preferential interactions of glycine betaine and urea with protein surface. Biochemistry. 43: 9276-88. PMID 15248785 DOI: 10.1021/Bi049862T |
0.37 |
|
2004 |
Ballin JD, Shkel IA, Record MT. Interactions of the KWK6 cationic peptide with short nucleic acid oligomers: demonstration of large Coulombic end effects on binding at 0.1-0.2 M salt. Nucleic Acids Research. 32: 3271-81. PMID 15205469 DOI: 10.1093/Nar/Gkh646 |
0.435 |
|
2004 |
Shkel IA, Record MT. Effect of the number of nucleic acid oligomer charges on the salt dependence of stability (DeltaG 37degrees) and melting temperature (Tm): NLPB analysis of experimental data. Biochemistry. 43: 7090-101. PMID 15170346 DOI: 10.1021/Bi036225E |
0.386 |
|
2003 |
Saecker RM, Tsodikov OV, Capp MW, Record MT. Rapid quench mixing to quantify kinetics of steps in association of Escherichia coli RNA polymerase with promoter DNA. Methods in Enzymology. 370: 535-46. PMID 14712673 DOI: 10.1016/S0076-6879(03)70045-7 |
0.463 |
|
2003 |
Cayley S, Record MT. Roles of cytoplasmic osmolytes, water, and crowding in the response of Escherichia coli to osmotic stress: biophysical basis of osmoprotection by glycine betaine. Biochemistry. 42: 12596-609. PMID 14580206 DOI: 10.1021/Bi0347297 |
0.31 |
|
2003 |
Hong J, Capp MW, Anderson CF, Record MT. Preferential interactions in aqueous solutions of urea and KCl. Biophysical Chemistry. 105: 517-32. PMID 14499915 DOI: 10.1016/S0301-4622(03)00112-1 |
0.337 |
|
2003 |
Felitsky DJ, Record MT. Thermal and urea-induced unfolding of the marginally stable lac repressor DNA-binding domain: a model system for analysis of solute effects on protein processes. Biochemistry. 42: 2202-17. PMID 12590610 DOI: 10.1021/Bi0270992 |
0.337 |
|
2002 |
Anderson CF, Felitsky DJ, Hong J, Record MT. Generalized derivation of an exact relationship linking different coefficients that characterize thermodynamic effects of preferential interactions. Biophysical Chemistry. 101: 497-511. PMID 12488023 DOI: 10.1016/S0301-4622(02)00159-X |
0.325 |
|
2002 |
Saecker RM, Record MT. Protein surface salt bridges and paths for DNA wrapping. Current Opinion in Structural Biology. 12: 311-9. PMID 12127449 DOI: 10.1016/S0959-440X(02)00326-3 |
0.475 |
|
2002 |
Saecker RM, Tsodikov OV, McQuade KL, Schlax PE, Capp MW, Record MT. Kinetic studies and structural models of the association of E. coli sigma(70) RNA polymerase with the lambdaP(R) promoter: large scale conformational changes in forming the kinetically significant intermediates. Journal of Molecular Biology. 319: 649-71. PMID 12054861 DOI: 10.1016/S0022-2836(02)00293-0 |
0.428 |
|
2002 |
Shkel IA, Tsodikov OV, Record MT. Asymptotic solution of the cylindrical nonlinear Poisson-Boltzmann equation at low salt concentration: analytic expressions for surface potential and preferential interaction coefficient. Proceedings of the National Academy of Sciences of the United States of America. 99: 2597-602. PMID 11880615 DOI: 10.1073/Pnas.032480699 |
0.355 |
|
2001 |
Courtenay ES, Capp MW, Record MT. Thermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein processes and changes in water-accessible surface area. Protein Science : a Publication of the Protein Society. 10: 2485-97. PMID 11714916 DOI: 10.1110/Ps.Ps.20801 |
0.315 |
|
2001 |
Tsodikov OV, Holbrook JA, Shkel IA, Record MT. Analytic binding isotherms describing competitive interactions of a protein ligand with specific and nonspecific sites on the same DNA oligomer. Biophysical Journal. 81: 1960-9. PMID 11566770 DOI: 10.1016/S0006-3495(01)75847-X |
0.439 |
|
2001 |
Holbrook JA, Tsodikov OV, Saecker RM, Record MT. Specific and non-specific interactions of integration host factor with DNA: thermodynamic evidence for disruption of multiple IHF surface salt-bridges coupled to DNA binding. Journal of Molecular Biology. 310: 379-401. PMID 11428896 DOI: 10.1006/Jmbi.2001.4768 |
0.499 |
|
1999 |
Tsodikov OV, Saecker RM, Melcher SE, Levandoski MM, Frank DE, Capp MW, Record MT. Wrapping of flanking non-operator DNA in lac repressor-operator complexes: implications for DNA looping. Journal of Molecular Biology. 294: 639-55. PMID 10610786 DOI: 10.1006/Jmbi.1999.3283 |
0.494 |
|
1999 |
Tsodikov OV, Record MT. General method of analysis of kinetic equations for multistep reversible mechanisms in the single-exponential regime: application to kinetics of open complex formation between Esigma70 RNA polymerase and lambdaP(R) promoter DNA. Biophysical Journal. 76: 1320-9. PMID 10049315 DOI: 10.1016/S0006-3495(99)77294-2 |
0.363 |
|
1999 |
Zhang W, Ni H, Capp MW, Anderson CF, Lohman TM, Record MT. The importance of coulombic end effects: experimental characterization of the effects of oligonucleotide flanking charges on the strength and salt dependence of oligocation (L8+) binding to single-stranded DNA oligomers. Biophysical Journal. 76: 1008-17. PMID 9916032 DOI: 10.1016/S0006-3495(99)77265-6 |
0.726 |
|
1998 |
Tsodikov OV, Craig ML, Saecker RM, Record MT. Quantitative analysis of multiple-hit footprinting studies to characterize DNA conformational changes in protein-DNA complexes: application to DNA opening by Esigma70 RNA polymerase. Journal of Molecular Biology. 283: 757-69. PMID 9790838 DOI: 10.1006/Jmbi.1998.2130 |
0.473 |
|
1998 |
Craig ML, Tsodikov OV, McQuade KL, Schlax PE, Capp MW, Saecker RM, Record MT. DNA footprints of the two kinetically significant intermediates in formation of an RNA polymerase-promoter open complex: evidence that interactions with start site and downstream DNA induce sequential conformational changes in polymerase and DNA. Journal of Molecular Biology. 283: 741-56. PMID 9790837 DOI: 10.1006/Jmbi.1998.2129 |
0.482 |
|
1998 |
DeHaseth PL, Zupancic ML, Record MT. RNA polymerase-promoter interactions: The comings and goings of RNA polymerase Journal of Bacteriology. 180: 3019-3025. PMID 9620948 DOI: 10.1128/Jb.180.12.3019-3025.1998 |
0.352 |
|
1998 |
Record MT, Courtenay ES, Cayley S, Guttman HJ. Biophysical compensation mechanisms buffering E. coli protein-nucleic acid interactions against changing environments. Trends in Biochemical Sciences. 23: 190-4. PMID 9612084 DOI: 10.1016/S0968-0004(98)01207-9 |
0.361 |
|
1997 |
Frank DE, Saecker RM, Bond JP, Capp MW, Tsodikov OV, Melcher SE, Levandoski MM, Record MT. Thermodynamics of the interactions of lac repressor with variants of the symmetric lac operator: effects of converting a consensus site to a non-specific site. Journal of Molecular Biology. 267: 1186-206. PMID 9150406 DOI: 10.1006/Jmbi.1997.0920 |
0.471 |
|
1997 |
Padmanabhan S, Zhang W, Capp MW, Anderson CF, Record MT. Binding of cationic (+4) alanine- and glycine-containing oligopeptides to double-stranded DNA: thermodynamic analysis of effects of coulombic interactions and alpha-helix induction. Biochemistry. 36: 5193-206. PMID 9136881 DOI: 10.1021/bi962927a |
0.375 |
|
1996 |
Levandoski MM, Tsodikov OV, Frank DE, Melcher SE, Saecker RM, Record MT. Cooperative and anticooperative effects in binding of the first and second plasmid Osym operators to a LacI tetramer: evidence for contributions of non-operator DNA binding by wrapping and looping. Journal of Molecular Biology. 260: 697-717. PMID 8709149 DOI: 10.1006/jmbi.1996.0431 |
0.373 |
|
1996 |
Zhang W, Bond JP, Anderson CF, Lohman TM, Record MT. Large electrostatic differences in the binding thermodynamics of a cationic peptide to oligomeric and polymeric DNA. Proceedings of the National Academy of Sciences of the United States of America. 93: 2511-6. PMID 8637905 DOI: 10.1073/pnas.93.6.2511 |
0.702 |
|
1996 |
Capp MW, Cayley DS, Zhang W, Guttman HJ, Melcher SE, Saecker RM, Anderson CF, Record MT. Compensating effects of opposing changes in putrescine (2+) and K+ concentrations on lac repressor-lac operator binding: in vitro thermodynamic analysis and in vivo relevance. Journal of Molecular Biology. 258: 25-36. PMID 8613989 DOI: 10.1006/jmbi.1996.0231 |
0.316 |
|
1995 |
Stein VM, Bond JP, Capp MW, Anderson CF, Record MT. Importance of coulombic end effects on cation accumulation near oligoelectrolyte B-DNA: a demonstration using 23Na NMR. Biophysical Journal. 68: 1063-72. PMID 7756526 DOI: 10.1016/S0006-3495(95)80281-X |
0.315 |
|
1995 |
Craig ML, Suh WC, Record MT. HO· and DNase I probing of Eσ70 RNA polymerase-λPR promoter open complexes: Mg2+ binding and its structural consequences at the transcription start site Biochemistry. 34: 15624-15632. PMID 7495790 DOI: 10.1021/bi00048a004 |
0.341 |
|
1994 |
Rao L, Ross W, Appleman JA, Gaal T, Leirmo S, Schlax PJ, Record MT, Gourse RL. Factor independent activation of rrnB p1. An 'Extended' promoter with an upstream element that dramatically increases promoter strength Journal of Molecular Biology. 235: 1421-1435. PMID 8107083 DOI: 10.1006/Jmbi.1994.1098 |
0.321 |
|
1994 |
Bond JP, Anderson CF, Record MT. Conformational transitions of duplex and triplex nucleic acid helices: thermodynamic analysis of effects of salt concentration on stability using preferential interaction coefficients. Biophysical Journal. 67: 825-36. PMID 7948695 DOI: 10.1016/S0006-3495(94)80542-9 |
0.32 |
|
1993 |
Law SM, Bellomy GR, Schlax PJ, Record MT. In vivo thermodynamic analysis of repression with and without looping in lac constructs. Estimates of free and local lac repressor concentrations and of physical properties of a region of supercoiled plasmid DNA in vivo. Journal of Molecular Biology. 230: 161-73. PMID 8450533 DOI: 10.1006/Jmbi.1993.1133 |
0.445 |
|
1993 |
Anderson CF, Record MT. Salt dependence of oligoion-polyion binding: a thermodynamic description based on preferential interaction coefficients The Journal of Physical Chemistry. 97: 7116-7126. DOI: 10.1021/J100129A032 |
0.386 |
|
1992 |
Dombroski AJ, Walter WA, Record MT, Siegele DA, Gross CA. Polypeptides containing highly conserved regions of transcription initiation factor sigma 70 exhibit specificity of binding to promoter DNA. Cell. 70: 501-12. PMID 1643661 DOI: 10.1016/0092-8674(92)90174-B |
0.47 |
|
1992 |
Ha JH, Capp MW, Hohenwalter MD, Baskerville M, Record MT. Thermodynamic stoichiometries of participation of water, cations and anions in specific and non-specific binding of lac repressor to DNA. Possible thermodynamic origins of the "glutamate effect" on protein-DNA interactions. Journal of Molecular Biology. 228: 252-64. PMID 1447786 DOI: 10.1016/0022-2836(92)90504-D |
0.485 |
|
1992 |
Suh WC, Leirmo S, Record MT. Roles of Mg2+ in the mechanism of formation and dissociation of open complexes between Escherichia coli RNA polymerase and the lambda PR promoter: kinetic evidence for a second open complex requiring Mg2+. Biochemistry. 31: 7815-25. PMID 1387321 DOI: 10.1021/Bi00149A011 |
0.429 |
|
1991 |
Cayley S, Lewis BA, Guttman HJ, Record MT. Characterization of the cytoplasm of Escherichia coli K-12 as a function of external osmolarity. Implications for protein-DNA interactions in vivo Journal of Molecular Biology. 222: 281-300. PMID 1960728 DOI: 10.1016/0022-2836(91)90212-O |
0.327 |
|
1991 |
Record MT, Ha JH, Fisher MA. Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA. Methods in Enzymology. 208: 291-343. PMID 1779839 DOI: 10.1016/0076-6879(91)08018-D |
0.522 |
|
1989 |
Paulsen MD, Anderson CF, Record MT. Counterion exchange reactions on DNA: Monte Carlo and Poisson-Boltzmann analysis. Biopolymers. 27: 1249-65. PMID 3219396 DOI: 10.1002/Bip.360270806 |
0.424 |
|
1989 |
Mazur SJ, Record MT. Association kinetics of site-specific protein-DNA interactions: roles of nonspecific DNA sites and of the molecular location of the specific site. Biopolymers. 28: 929-53. PMID 2742985 DOI: 10.1002/Bip.360280503 |
0.415 |
|
1989 |
Cowing DW, Mecsas J, Record MT, Gross CA. Intermediates in the formation of the open complex by RNA polymerase holoenzyme containing the sigma factor σ32 at the groE promoter Journal of Molecular Biology. 210: 521-530. PMID 2693737 DOI: 10.1016/0022-2836(89)90128-9 |
0.416 |
|
1989 |
Ha JH, Spolar RS, Record MT. Role of the hydrophobic effect in stability of site-specific protein-DNA complexes. Journal of Molecular Biology. 209: 801-16. PMID 2585510 DOI: 10.1016/0022-2836(89)90608-6 |
0.426 |
|
1988 |
Braunlin WH, Anderson CF, Record MT. Competitive interactions of Co(NH3)6(3+) and Na+ with helical B-DNA probed by 59Co and 23Na NMR. Biochemistry. 26: 7724-31. PMID 3427101 DOI: 10.1021/bi00398a028 |
0.357 |
|
1988 |
Bellomy GR, Mossing MC, Record MT. Physical properties of DNA in vivo as probed by the length dependence of the lac operator looping process. Biochemistry. 27: 3900-6. PMID 3046661 |
0.76 |
|
1988 |
Padmanabhan S, Richey B, Anderson CF, Record MT. Interaction of an N-methylated polyamine analogue, hexamethonium(2+), with NaDNA: quantitative 14N and 23Na NMR relaxation rate studies of the cation-exchange process. Biochemistry. 27: 4367-76. PMID 2901852 DOI: 10.1021/bi00412a025 |
0.32 |
|
1987 |
Richey B, Cayley DS, Mossing MC, Kolka C, Anderson CF, Farrar TC, Record MT. Variability of the intracellular ionic environment of Escherichia coli. Differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene expression. The Journal of Biological Chemistry. 262: 7157-64. PMID 3108249 |
0.361 |
|
1987 |
Leirmo S, Harrison C, Cayley DS, Burgess RR, Record MT. Replacement of potassium chloride by potassium glutamate dramatically enhances protein-DNA interactions in vitro Biochemistry. 26: 2095-2101. PMID 2887198 DOI: 10.1021/bi00382a006 |
0.349 |
|
1987 |
Paulsen MD, Richey B, Anderson CF, Record M. The salt dependence of the preferential interaction coefficient in dna solutions as determined by grand canonical monte carlo simulations Chemical Physics Letters. 139: 448-452. DOI: 10.1016/0009-2614(87)80589-4 |
0.424 |
|
1986 |
Mazur SJ, Record MT. Kinetics of nonspecific binding reactions of proteins with DNA flexible coils: site-based and molecule-based association reactions. Biopolymers. 25: 985-1008. PMID 3730520 DOI: 10.1002/Bip.360250603 |
0.363 |
|
1986 |
Mossing MC, Record MT. Upstream operators enhance repression of the lac promoter. Science (New York, N.Y.). 233: 889-92. PMID 3090685 DOI: 10.1126/Science.3090685 |
0.76 |
|
1986 |
Roe JH, Record MT. Regulation of the kinetics of the interaction of Escherichia coli RNA polymerase with the lambda PR promoter by salt concentration. Biochemistry. 24: 4721-6. PMID 2934084 DOI: 10.1021/bi00339a002 |
0.347 |
|
1986 |
Mills P, Anderson CF, Record MT. Grand canonical Monte Carlo calculations of thermodynamic coefficients for a primitive model of DNA-salt solutions The Journal of Physical Chemistry. 90: 6541-6548. DOI: 10.1021/J100282A025 |
0.773 |
|
1986 |
Mills P, Paulsen MD, Anderson CF, Record M. Monte carlo simulations of counterion accumulation near helical DNA Chemical Physics Letters. 129: 155-158. DOI: 10.1016/0009-2614(86)80188-9 |
0.763 |
|
1985 |
Mossing MC, Record MT. Thermodynamic origins of specificity in the lac repressor-operator interaction. Adaptability in the recognition of mutant operator sites. Journal of Molecular Biology. 186: 295-305. PMID 4087296 DOI: 10.1016/0022-2836(85)90106-8 |
0.753 |
|
1985 |
Record MT, Anderson CF, Mills P, Mossing M, Roe JH. Ions as regulators of protein-nucleic acid interactions in vitro and in vivo. Advances in Biophysics. 20: 109-35. PMID 3914831 DOI: 10.1016/0065-227X(85)90033-4 |
0.747 |
|
1985 |
Roe JH, Burgess RR, Record MT. Temperature dependence of the rate constants of the Escherichia coli RNA polymerase-λPR promoter interaction. Assignment of the kinetic steps corresponding to protein conformational change and DNA opening Journal of Molecular Biology. 184: 441-453. PMID 3900414 DOI: 10.1016/0022-2836(85)90293-1 |
0.386 |
|
1985 |
Mills P, Anderson CF, Record MT. Monte Carlo studies of counterion-DNA interactions. Comparison of the radial distribution of counterions with predictions of other polyelectrolyte theories The Journal of Physical Chemistry. 89: 3984-3994. DOI: 10.1021/J100265A012 |
0.776 |
|
1984 |
Roe JH, Burgess RR, Record MT. Kinetics and mechanism of the interaction of Escherichia coli RNA polymerase with the λPR promoter Journal of Molecular Biology. 176: 495-522. PMID 6235375 DOI: 10.1016/0022-2836(84)90174-8 |
0.397 |
|
1983 |
Melançon P, Burgess RR, Record MT. Direct evidence for the preferential binding of Escherichia coli RNA polymerase holoenzyme to the ends of deoxyribonucleic acid restriction fragments. Biochemistry. 22: 5169-76. PMID 6317017 DOI: 10.1021/bi00291a017 |
0.369 |
|
1982 |
Braunlin WH, Strick TJ, Record MT. Equilibrium dialysis studies of polyamine binding to DNA. Biopolymers. 21: 1301-14. PMID 7115891 DOI: 10.1002/bip.360210704 |
0.322 |
|
1982 |
Shaner SL, Melancon P, Lee KS, Burgess RR, Record MT. Ion effects on the aggregation and DNA-binding reactions of Escherichia coli RNA polymerase Cold Spring Harbor Symposia On Quantitative Biology. 47: 463-472. PMID 6345063 DOI: 10.1101/Sqb.1983.047.01.055 |
0.336 |
|
1982 |
Melançon P, Burgess RR, Record MT. Nitrocellulose filter binding studies of the interactions of Escherichia coli RNA polymerase holoenzyme with deoxyribonucleic acid restriction fragments: Evidence for multiple classes of nonpromoter interactions, some of which display promoter-like properties Biochemistry. 21: 4318-4331. PMID 6289878 DOI: 10.1021/bi00261a022 |
0.333 |
|
1981 |
Strauss HS, Boston RS, Record MT, Burgess RR. Variables affecting the selectivity and efficiency of retention of DNA fragments by E. coli RNA polymerase in the nitrocellulose-filter-binding assay Gene. 13: 75-87. PMID 7016668 DOI: 10.1016/0378-1119(81)90045-7 |
0.481 |
|
1980 |
Lohman TM, DeHaseth PL, Record MT. Pentalysine-deoxyribonucleic acid interactions: A model for the general effects of ion concentrations on the interactions of proteins with nucleic acids Biochemistry. 19: 3522-3530. PMID 7407056 DOI: 10.1021/Bi00556A017 |
0.679 |
|
1980 |
Strauss HS, Burgess RR, Record MT. Binding of Escherichia coli ribonucleic acid polymerase holoenzyme to a bacteriophage T7 promoter-containing fragment: Evaluation of promoter binding constants as a function of solution conditions Biochemistry. 19: 3504-3515. PMID 6996705 DOI: 10.1021/bi00556a015 |
0.318 |
|
1980 |
Lohman TM, Wensley CG, Cina J, Burgess RR, Record MT. Use of difference boundary sedimentation velocity to investigate nonspecific protein-nucleic acid interactions Biochemistry. 19: 3516-3522. PMID 6250571 DOI: 10.1021/Bi00556A016 |
0.746 |
|
1980 |
Strauss HS, Burgess RR, Record MT. Binding of Escherichia coli ribonucleic acid polymerase holoenzyme to a bacteriophage T7 promoter-containing fragment: Selectivity exists over a wide range of solution conditions Biochemistry. 19: 3496-3504. PMID 6250570 DOI: 10.1021/Bi00556A014 |
0.404 |
|
1978 |
Lohman TM, DeHaseth PL, Record MT. Analysis of ion concentration effects on the kinetics of protein-nucleic acid interactions. Application to lac repressor-operator interactions Biophysical Chemistry. 8: 281-294. PMID 728535 DOI: 10.1016/0301-4622(78)80011-8 |
0.721 |
|
1978 |
Anderson CF, Record MT, Hart PA. Sodium-23 NMR studies of cation-DNA interactions. Biophysical Chemistry. 7: 301-16. PMID 623871 DOI: 10.1016/0301-4622(78)85007-8 |
0.356 |
|
1978 |
Record MT, Anderson CF, Lohman TM. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity Quarterly Reviews of Biophysics. 11: 103-178. PMID 353875 DOI: 10.1017/S003358350000202X |
0.687 |
|
1978 |
DeHaseth PL, Lohman TM, Burgess RR, Record MT. Nonspecific interactions of Escherichia coli RNA polymerase with native and denatured DNA: Differences in the binding behavior of core and holoenzyme Biochemistry. 17: 1612-1622. PMID 350271 |
0.744 |
|
1978 |
Record MT, Lohman TM. A semiempirical extension of polyelectrolyte theory to the treatment of oligoelectrolytes: Application to oligonucleotide helix-coil transitions Biopolymers. 17: 159-166. DOI: 10.1002/Bip.1978.360170112 |
0.691 |
|
1977 |
Record MT, DeHaseth PL, Lohman TM. Interpretation of monovalent and divalent cation effects on the lac repressor-operator interaction Biochemistry. 16: 4791-4796. PMID 911790 DOI: 10.1021/Bi00641A005 |
0.726 |
|
1977 |
DeHaseth PL, Lohman TM, Record MT. Nonspecific interaction of lac repressor with DNA: An association reaction driven by counterion release Biochemistry. 16: 4783-4790. PMID 911789 DOI: 10.1021/Bi00641A004 |
0.733 |
|
1977 |
DeHaseth PL, Gross CA, Burgess RR, Record MT. Measurement of binding constants for protein-DNA interactions by DNA-cellulose chromatography Biochemistry. 16: 4777-4783. PMID 911788 DOI: 10.1021/Bi00641A003 |
0.486 |
|
1976 |
Wensley CG, Record MT. Intermediates in the strand-separation transition of T7 DNA. Biopolymers. 15: 717-28. PMID 1252605 DOI: 10.1002/Bip.1976.360150410 |
0.382 |
|
1976 |
Record MT, Lohman TM, Haseth Pd. Ion effects on ligand-nucleic acid interactions Journal of Molecular Biology. 107: 145-158. PMID 1003464 DOI: 10.1016/S0022-2836(76)80023-X |
0.697 |
|
1976 |
Record MT, Woodbury CP, Lohman TM. Na+ effects on transitions of DNA and polynucleotides of variable linear charge density Biopolymers. 15: 893-915. PMID 4169 DOI: 10.1002/Bip.1976.360150507 |
0.702 |
|
1975 |
Record MT. Effects of Na+ and Mg++ ions on the helix-coil transition of DNA Biopolymers. 14: 2137-2158. DOI: 10.1002/Bip.1975.360141012 |
0.379 |
|
1974 |
Kallay M, Record MT. The strand-separation transition of T7 DNA. Biopolymers. 13: 825-41. PMID 4847588 DOI: 10.1002/Bip.1974.360130416 |
0.39 |
|
1974 |
Elson EL, Record MT. The strand‐separation transition of T2 bacteriophage DNA Biopolymers. 13: 797-824. PMID 4847587 DOI: 10.1002/Bip.1974.360130415 |
0.602 |
|
1972 |
Record MT. Kinetics of the helix-coil transition in DNA. Biopolymers. 11: 1435-84. PMID 5042850 DOI: 10.1002/Bip.1972.360110711 |
0.396 |
|
1968 |
Record MT. Electrostatic effects on polynucleotide transitions. I. Behavior at neutral pH. Biopolymers. 5: 975-92. PMID 6078884 DOI: 10.1002/Bip.1967.360051010 |
0.315 |
|
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