| Year |
Citation |
Score |
| 2024 |
Fleming PJ, Correia JJ, Fleming KG. The Molecular Basis for Hydrodynamic Properties of PEGylated Human Serum Albumin. Biophysical Journal. PMID 38778541 DOI: 10.1016/j.bpj.2024.05.019 |
0.604 |
|
| 2024 |
Devlin T, Fleming KG. A team of chaperones play to win in the bacterial periplasm. Trends in Biochemical Sciences. PMID 38677921 DOI: 10.1016/j.tibs.2024.03.015 |
0.47 |
|
| 2023 |
Fleming KG. Membrane defects as a generalized driving force for membrane protein interactions. Proceedings of the National Academy of Sciences of the United States of America. 120: e2315655120. PMID 37851703 DOI: 10.1073/pnas.2315655120 |
0.429 |
|
| 2023 |
Devlin T, Fleming PJ, Loza N, Fleming KG. Generation of unfolded outer membrane protein ensembles defined by hydrodynamic properties. European Biophysics Journal : Ebj. PMID 36899114 DOI: 10.1007/s00249-023-01639-y |
0.687 |
|
| 2023 |
Devlin T, Marx DC, Roskopf MA, Bubb QR, Plummer AM, Fleming KG. FkpA Enhances Membrane Protein Folding using an Extensive Interaction Surface. Protein Science : a Publication of the Protein Society. e4592. PMID 36775935 DOI: 10.1002/pro.4592 |
0.774 |
|
| 2023 |
Fleming PJ, Correia JJ, Fleming KG. Revisiting macromolecular hydration with HullRadSAS. European Biophysics Journal : Ebj. PMID 36602579 DOI: 10.1007/s00249-022-01627-8 |
0.523 |
|
| 2022 |
To P, Xia Y, Lee SO, Devlin T, Fleming KG, Fried SD. A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu. Proceedings of the National Academy of Sciences of the United States of America. 119: e2210536119. PMID 36417429 DOI: 10.1073/pnas.2210536119 |
0.387 |
|
| 2021 |
Alford RF, Fleming PJ, Fleming KG, Gray JJ. Protein Structure Prediction and Design in a Biologically Realistic Implicit Membrane. Biophysical Journal. 120: 4635. PMID 34534449 DOI: 10.1016/j.bpj.2021.09.019 |
0.676 |
|
| 2021 |
Marx DC, Fleming KG. Membrane proteins enter the fold. Current Opinion in Structural Biology. 69: 124-130. PMID 33975156 DOI: 10.1016/j.sbi.2021.03.006 |
0.825 |
|
| 2021 |
Vorobieva AA, White P, Liang B, Horne JE, Bera AK, Chow CM, Gerben S, Marx S, Kang A, Stiving AQ, Harvey SR, Marx DC, Khan GN, Fleming KG, Wysocki VH, et al. De novo design of transmembrane β barrels. Science (New York, N.Y.). 371. PMID 33602829 DOI: 10.1126/science.abc8182 |
0.751 |
|
| 2021 |
Marx DC, Fleming KG. Local Bilayer Hydrophobicity Modulates Membrane Protein Stability. Journal of the American Chemical Society. 143: 764-772. PMID 33412852 DOI: 10.1021/jacs.0c09412 |
0.814 |
|
| 2020 |
Huysmans GHM, Marx DC, Radford SE, Fleming KG. Determining the Free Energies of Outer Membrane Proteins in Lipid Bilayers. Methods in Molecular Biology (Clifton, N.J.). 2168: 217-232. PMID 33582994 DOI: 10.1007/978-1-0716-0724-4_10 |
0.831 |
|
| 2020 |
Marx DC, Plummer AM, Faustino AM, Devlin T, Roskopf MA, Leblanc MJ, Lessen HJ, Amann BT, Fleming PJ, Krueger S, Fried SD, Fleming KG. SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 33093201 DOI: 10.1073/pnas.2008175117 |
0.811 |
|
| 2020 |
Marx DC, Leblanc MJ, Plummer AM, Krueger S, Fleming KG. Domain Interactions Determine the Conformational Ensemble of the Periplasmic Chaperone SurA. Protein Science : a Publication of the Protein Society. PMID 32748422 DOI: 10.1002/Pro.3924 |
0.742 |
|
| 2020 |
O'Brien ES, Fuglestad B, Lessen HJ, Stetz MA, Lin DW, Marques BS, Gupta K, Fleming KG, Wand JJ. Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy. Angewandte Chemie (International Ed. in English). PMID 32277554 DOI: 10.1002/Anie.202003527 |
0.583 |
|
| 2020 |
Alford RF, Fleming PJ, Fleming KG, Gray JJ. Protein Structure Prediction and Design in a Biologically Realistic Implicit Membrane. Biophysical Journal. PMID 32224301 DOI: 10.1016/J.Bpj.2020.03.006 |
0.733 |
|
| 2020 |
Lessen HJ, Majumdar A, Fleming KG. Backbone hydrogen bond energies in membrane proteins are insensitive to large changes in local water concentration. Journal of the American Chemical Society. PMID 32134659 DOI: 10.1021/Jacs.0C00290 |
0.463 |
|
| 2020 |
Marx DC, Fleming KG. Towards Understanding How Water Modulates Membrane Protein Stability Biophysical Journal. 118: 26a-27a. DOI: 10.1016/J.Bpj.2019.11.325 |
0.799 |
|
| 2020 |
Roskopf MA, Marx DC, Fleming KG. Energetics of Dimeric FkpA Binding to a Native Unfolded Membrane Protein Client Biophysical Journal. 118: 366a. DOI: 10.1016/J.Bpj.2019.11.2101 |
0.822 |
|
| 2019 |
Chum AP, Shoemaker SR, Fleming PJ, Fleming KG. Plasticity and transient binding are key ingredients of the periplasmic chaperone network. Protein Science : a Publication of the Protein Society. PMID 31074917 DOI: 10.1002/Pro.3641 |
0.65 |
|
| 2019 |
Alford RF, Fleming P, Fleming KG, Gray JJ. A Thermodynamically-Rigorous, Biologically-Driven Energy Function for Membrane Protein Modeling and Design Biophysical Journal. 116: 58a. DOI: 10.1016/J.Bpj.2018.11.358 |
0.708 |
|
| 2019 |
Roskopf MA, Marx DC, Plummer AM, Bubb QR, Fleming KG. Dimeric FkpA Acts as an Anti-Aggregase on a Native Unfolded Membrane Protein Client Biophysical Journal. 116: 497a-498a. DOI: 10.1016/J.Bpj.2018.11.2683 |
0.822 |
|
| 2019 |
Marx DC, Fleming KG. Bilayer Depth Dependence of Hydrophobic Amino Acid Transfer Free Energies Biophysical Journal. 116: 497a. DOI: 10.1016/J.Bpj.2018.11.2680 |
0.721 |
|
| 2019 |
Lessen HJ, Fleming P, Fleming KG, Sodt AJ. Transmembrane Beta-Barrel Proteins Rigidify the Bacterial Outer Membrane Biophysical Journal. 116: 327a. DOI: 10.1016/J.Bpj.2018.11.1774 |
0.699 |
|
| 2018 |
Lessen HJ, Fleming PJ, Fleming KG, Sodt AJ. Building Blocks of the Outer Membrane: Calculating a general elastic energy model for β-barrel membrane proteins. Journal of Chemical Theory and Computation. PMID 29979594 DOI: 10.1021/Acs.Jctc.8B00377 |
0.732 |
|
| 2018 |
Fleming PJ, Fleming KG. HullRad: Fast Calculations of Folded and Disordered Protein and Nucleic Acid Hydrodynamic Properties. Biophysical Journal. 114: 856-869. PMID 29490246 DOI: 10.1016/J.Bpj.2018.01.002 |
0.624 |
|
| 2018 |
Fleming KG. Taking deterministic control of membrane protein monomer-dimer measurements. The Journal of General Physiology. PMID 29343502 DOI: 10.1085/Jgp.201711913 |
0.574 |
|
| 2018 |
Alford RF, Fleming P, Fleming KG, Gray JJ. Fast Implicit Potentials for Accurate Prediction and Design of Membrane Protein Structures Biophysical Journal. 114: 345a. DOI: 10.1016/J.Bpj.2017.11.1923 |
0.701 |
|
| 2017 |
Peterson JH, Plummer AM, Fleming KG, Bernstein HD. Selective pressure for rapid membrane integration constrains the sequence of bacterial outer membrane proteins. Molecular Microbiology. PMID 28941249 DOI: 10.1111/Mmi.13845 |
0.57 |
|
| 2017 |
Marx DC, Fleming KG. Influence of Protein Scaffold on Side-Chain Transfer Free Energies. Biophysical Journal. 113: 597-604. PMID 28793214 DOI: 10.1016/J.Bpj.2017.06.032 |
0.785 |
|
| 2017 |
Mo GC, Ross B, Hertel F, Manna P, Yang X, Greenwald E, Booth C, Plummer AM, Tenner B, Chen Z, Wang Y, Kennedy EJ, Cole PA, Fleming KG, Palmer A, et al. Genetically encoded biosensors for visualizing live-cell biochemical activity at super-resolution. Nature Methods. PMID 28288122 DOI: 10.1038/Nmeth.4221 |
0.381 |
|
| 2017 |
Marx D, Fleming K. Side Chain Hydrophobicity Scale using the Tilted Beta-Barrel Protein PagP Biophysical Journal. 112: 205a. DOI: 10.1016/J.Bpj.2016.11.1134 |
0.824 |
|
| 2017 |
Plummer AM, Krueger S, Fleming KG. Chaperone SurA Interacts with Unfolded Membrane Protein Clients via Delocalized Interface Biophysical Journal. 112: 205a. DOI: 10.1016/J.Bpj.2016.11.1132 |
0.607 |
|
| 2016 |
Danoff EJ, Fleming KG. Novel Kinetic Intermediates Populated along the Folding Pathway of the Transmembrane β-Barrel OmpA. Biochemistry. PMID 28001375 DOI: 10.1021/Acs.Biochem.6B00809 |
0.83 |
|
| 2016 |
McDonald SK, Fleming KG. Negative charge neutralization in the loops and turns of outer membrane phospholipase A impacts folding hysteresis at neutral pH. Biochemistry. PMID 27731977 DOI: 10.1021/Acs.Biochem.6B00652 |
0.475 |
|
| 2016 |
Costello SM, Plummer AM, Fleming PJ, Fleming KG. Dynamic periplasmic chaperone reservoir facilitates biogenesis of outer membrane proteins. Proceedings of the National Academy of Sciences of the United States of America. PMID 27482090 DOI: 10.1073/Pnas.1601002113 |
0.733 |
|
| 2016 |
Plummer AM, Fleming KG. From Chaperones to the Membrane with a BAM! Trends in Biochemical Sciences. PMID 27450425 DOI: 10.1016/J.Tibs.2016.06.005 |
0.539 |
|
| 2016 |
Fleming PJ, Patel DS, Wu EL, Qi Y, Yeom MS, Sousa MC, Fleming KG, Im W. BamA POTRA Domain Interacts with a Native Lipid Membrane Surface. Biophysical Journal. 110: 2698-709. PMID 27332128 DOI: 10.1016/J.Bpj.2016.05.010 |
0.746 |
|
| 2016 |
McDonald SK, Fleming KG. Aromatic side chain water-to-lipid transfer free energies show a depth-dependence across the membrane normal. Journal of the American Chemical Society. PMID 27254476 DOI: 10.1021/Jacs.6B03460 |
0.59 |
|
| 2016 |
Zaccai NR, Sandlin CW, Hoopes JT, Curtis JE, Fleming PJ, Fleming KG, Krueger S. Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane Proteins. Methods in Enzymology. 566: 159-210. PMID 26791979 DOI: 10.1016/Bs.Mie.2015.06.041 |
0.71 |
|
| 2016 |
Costello SM, Plummer AM, Fleming PJ, Fleming KG. A Computational Model for Membrane Protein Flux across the Bacterial Periplasm Biophysical Journal. 110: 58a. DOI: 10.1016/J.Bpj.2015.11.379 |
0.721 |
|
| 2016 |
Fleming KG. The Versatile Beta-Barrel Gives Up Secrets of the Membrane Biophysical Journal. 110: 5a. DOI: 10.1016/J.Bpj.2015.11.074 |
0.572 |
|
| 2015 |
Plummer AM, Gessmann D, Fleming KG. Erratum to: The Role of a Destabilized Membrane for OMP Insertion. Methods in Molecular Biology (Clifton, N.J.). 1329: E1. PMID 27914068 DOI: 10.1007/978-1-4939-2871-2_23 |
0.493 |
|
| 2015 |
Sandlin CW, Zaccai NR, Fleming KG. Skp Trimer Formation Is Insensitive to Salts in the Physiological Range. Biochemistry. 54: 7059-62. PMID 26579730 DOI: 10.1021/Acs.Biochem.5B00806 |
0.533 |
|
| 2015 |
Plummer AM, Gessmann D, Fleming KG. The Role of a Destabilized Membrane for OMP Insertion. Methods in Molecular Biology (Clifton, N.J.). 1329: 57-65. PMID 26427676 DOI: 10.1007/978-1-4939-2871-2_5 |
0.499 |
|
| 2015 |
Plummer AM, Fleming KG. BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism. Biochemistry. PMID 26394056 DOI: 10.1021/Acs.Biochem.5B00950 |
0.548 |
|
| 2015 |
Fleming KG. A combined kinetic push and thermodynamic pull as driving forces for outer membrane protein sorting and folding in bacteria. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 370. PMID 26370938 DOI: 10.1098/Rstb.2015.0026 |
0.525 |
|
| 2015 |
Danoff EJ, Fleming KG. Aqueous, Unfolded OmpA Forms Amyloid-Like Fibrils upon Self-Association. Plos One. 10: e0132301. PMID 26196893 DOI: 10.1371/Journal.Pone.0132301 |
0.816 |
|
| 2015 |
Danoff EJ, Fleming KG. Membrane defects accelerate outer membrane β-barrel protein folding. Biochemistry. 54: 97-9. PMID 25513891 DOI: 10.1021/Bi501443P |
0.846 |
|
| 2015 |
Costello SM, Plummer AM, Fleming KG. Identifying the Oligomerization State of DegP in the Absence and Presence of Substrate Biophysical Journal. 108: 92a. DOI: 10.1016/J.Bpj.2014.11.535 |
0.503 |
|
| 2015 |
Plummer AM, Bernstein HD, Fleming KG. Evolutionary Avoidance of Transmembrane Embedded Arginines is due to Slowed Folding Kinetics Biophysical Journal. 108: 559a. DOI: 10.1016/J.Bpj.2014.11.3062 |
0.489 |
|
| 2015 |
Zaccai NR, Sandlin CW, Hoopes JT, Curtis JE, Fleming PJ, Fleming KG, Krueger S. Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane Proteins Methods in Enzymology. DOI: 10.1016/bs.mie.2015.06.041 |
0.63 |
|
| 2014 |
Wu EL, Fleming PJ, Yeom MS, Widmalm G, Klauda JB, Fleming KG, Im W. E. coli outer membrane and interactions with OmpLA. Biophysical Journal. 106: 2493-502. PMID 24896129 DOI: 10.1016/J.Bpj.2014.04.024 |
0.703 |
|
| 2014 |
Fleming KG. Energetics of membrane protein folding. Annual Review of Biophysics. 43: 233-55. PMID 24895854 DOI: 10.1146/Annurev-Biophys-051013-022926 |
0.616 |
|
| 2014 |
Gessmann D, Chung YH, Danoff EJ, Plummer AM, Sandlin CW, Zaccai NR, Fleming KG. Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA. Proceedings of the National Academy of Sciences of the United States of America. 111: 5878-83. PMID 24715731 DOI: 10.1073/Pnas.1322473111 |
0.851 |
|
| 2014 |
Wu EL, Fleming PJ, Klauda JB, Fleming KG, Im W. A Molecular Dynamics Simulation Study of Outer Membrane Phospholipase a (OMPLA) Structure and Dynamics in an Asymmetric Lipopolysaccharide Membrane Biophysical Journal. 106: 656a. DOI: 10.1016/J.Bpj.2013.11.3632 |
0.707 |
|
| 2013 |
Moon CP, Zaccai NR, Fleming PJ, Gessmann D, Fleming KG. Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm. Proceedings of the National Academy of Sciences of the United States of America. 110: 4285-90. PMID 23440211 DOI: 10.1073/Pnas.1212527110 |
0.86 |
|
| 2012 |
Lees JP, Manlandro CM, Picton LK, Tan AZ, Casares S, Flanagan JM, Fleming KG, Hill RB. A designed point mutant in Fis1 disrupts dimerization and mitochondrial fission. Journal of Molecular Biology. 423: 143-58. PMID 22789569 DOI: 10.1016/J.Jmb.2012.06.042 |
0.381 |
|
| 2012 |
O'Neill MJ, Bhakta MN, Fleming KG, Wilks A. Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO). Proceedings of the National Academy of Sciences of the United States of America. 109: 5639-44. PMID 22451925 DOI: 10.1073/Pnas.1121549109 |
0.399 |
|
| 2012 |
Fleming PJ, Freites JA, Moon CP, Tobias DJ, Fleming KG. Outer membrane phospholipase A in phospholipid bilayers: a model system for concerted computational and experimental investigations of amino acid side chain partitioning into lipid bilayers. Biochimica Et Biophysica Acta. 1818: 126-34. PMID 21816133 DOI: 10.1016/J.Bbamem.2011.07.016 |
0.831 |
|
| 2012 |
Moon CP, Fleming KG. Membrane Protein Stabilities and M-Values Biophysical Journal. 102: 218a. DOI: 10.1016/J.Bpj.2011.11.1196 |
0.825 |
|
| 2012 |
Buchanan SK, Yamashita S, Fleming KG. Structure and folding of outer membrane proteins Comprehensive Biophysics. 5: 139-163. DOI: 10.1016/B978-0-12-374920-8.00514-2 |
0.412 |
|
| 2011 |
Moon CP, Kwon S, Fleming KG. Overcoming hysteresis to attain reversible equilibrium folding for outer membrane phospholipase A in phospholipid bilayers. Journal of Molecular Biology. 413: 484-94. PMID 21888919 DOI: 10.1016/J.Jmb.2011.08.041 |
0.819 |
|
| 2011 |
Danoff EJ, Fleming KG. The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel. Biophysical Chemistry. 159: 194-204. PMID 21782315 DOI: 10.1016/J.Bpc.2011.06.013 |
0.824 |
|
| 2011 |
Moon CP, Fleming KG. Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers. Proceedings of the National Academy of Sciences of the United States of America. 108: 10174-7. PMID 21606332 DOI: 10.1073/pnas.1103979108 |
0.798 |
|
| 2011 |
Moon CP, Fleming KG. Using tryptophan fluorescence to measure the stability of membrane proteins folded in liposomes. Methods in Enzymology. 492: 189-211. PMID 21333792 DOI: 10.1016/B978-0-12-381268-1.00018-5 |
0.787 |
|
| 2011 |
Moon P, Fleming K. Measuring Side-Chain Hydrophobicity using a Whole Transmembrane Protein in Lipid Bilayers Biophysical Journal. 100: 206a-207a. DOI: 10.1016/J.Bpj.2010.12.1339 |
0.619 |
|
| 2010 |
Ebie Tan A, Burgess NK, DeAndrade DS, Marold JD, Fleming KG. Self-association of unfolded outer membrane proteins. Macromolecular Bioscience. 10: 763-7. PMID 20491126 DOI: 10.1002/Mabi.200900479 |
0.759 |
|
| 2009 |
Pang T, Savva CG, Fleming KG, Struck DK, Young R. Structure of the lethal phage pinhole. Proceedings of the National Academy of Sciences of the United States of America. 106: 18966-71. PMID 19861547 DOI: 10.1073/Pnas.0907941106 |
0.479 |
|
| 2009 |
Burgess NK, Fleming KG. Beta-barrel Proteins that Reside in the E. coli Outer Membrane In Vivo Demonstrate Varied Folding Behavior In Vitro Biophysical Journal. 96: 79a. DOI: 10.1016/J.Bpj.2008.12.308 |
0.838 |
|
| 2009 |
Moon P, Fleming KG. Measuring The Energetic Cost Of Burying An Arginine Sidechain Into A Lipid Bilayer Using A Transmembrane Protein Biophysical Journal. 96: 350a-351a. DOI: 10.1016/J.Bpj.2008.12.1766 |
0.558 |
|
| 2008 |
Ebie Tan A, Fleming KG. Outer membrane phospholipase a dimer stability does not correlate to occluded surface area. Biochemistry. 47: 12095-103. PMID 18939857 DOI: 10.1021/Bi801436A |
0.806 |
|
| 2008 |
Fleming KG. Determination of membrane protein molecular weight using sedimentation equilibrium analytical ultracentrifugation. Current Protocols in Protein Science / Editorial Board, John E. Coligan ... [Et Al.]. Unit 7.12.1-7.12.13. PMID 18729051 DOI: 10.1002/0471140864.Ps0712S53 |
0.569 |
|
| 2008 |
Burgess NK, Dao TP, Stanley AM, Fleming KG. Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro. The Journal of Biological Chemistry. 283: 26748-58. PMID 18641391 DOI: 10.1074/Jbc.M802754200 |
0.848 |
|
| 2008 |
MacKenzie KR, Fleming KG. Association energetics of membrane spanning alpha-helices. Current Opinion in Structural Biology. 18: 412-9. PMID 18539023 DOI: 10.1016/J.Sbi.2008.04.007 |
0.592 |
|
| 2008 |
Stanley AM, Fleming KG. The process of folding proteins into membranes: challenges and progress. Archives of Biochemistry and Biophysics. 469: 46-66. PMID 17971290 DOI: 10.1016/J.Abb.2007.09.024 |
0.82 |
|
| 2008 |
Burgess NK, Stanley AM, Fleming KG. Determination of membrane protein molecular weights and association equilibrium constants using sedimentation equilibrium and sedimentation velocity. Methods in Cell Biology. 84: 181-211. PMID 17964932 DOI: 10.1016/S0091-679X(07)84007-6 |
0.835 |
|
| 2007 |
Duong MT, Jaszewski TM, Fleming KG, MacKenzie KR. Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations. Journal of Molecular Biology. 371: 422-34. PMID 17570394 DOI: 10.1016/J.Jmb.2007.05.026 |
0.56 |
|
| 2007 |
Stanley AM, Fleming KG. The role of a hydrogen bonding network in the transmembrane beta-barrel OMPLA. Journal of Molecular Biology. 370: 912-24. PMID 17555765 DOI: 10.1016/J.Jmb.2007.05.009 |
0.712 |
|
| 2007 |
Stanley AM, Treubrodt AM, Chuawong P, Hendrickson TL, Fleming KG. Lipid chain selectivity by outer membrane phospholipase A. Journal of Molecular Biology. 366: 461-8. PMID 17174333 DOI: 10.1016/J.Jmb.2006.10.055 |
0.752 |
|
| 2007 |
Ebie AZ, Fleming KG. Dimerization of the erythropoietin receptor transmembrane domain in micelles. Journal of Molecular Biology. 366: 517-24. PMID 17173930 DOI: 10.1016/J.Jmb.2006.11.035 |
0.415 |
|
| 2006 |
Stanley AM, Chuawong P, Hendrickson TL, Fleming KG. Energetics of outer membrane phospholipase A (OMPLA) dimerization. Journal of Molecular Biology. 358: 120-31. PMID 16497324 DOI: 10.1016/J.Jmb.2006.01.033 |
0.799 |
|
| 2006 |
Kroch AE, Fleming KG. Alternate interfaces may mediate homomeric and heteromeric assembly in the transmembrane domains of SNARE proteins. Journal of Molecular Biology. 357: 184-94. PMID 16427079 DOI: 10.1016/J.Jmb.2005.12.060 |
0.797 |
|
| 2005 |
Stanley AM, Fleming KG. The transmembrane domains of ErbB receptors do not dimerize strongly in micelles. Journal of Molecular Biology. 347: 759-72. PMID 15769468 DOI: 10.1016/J.Jmb.2005.01.059 |
0.71 |
|
| 2005 |
Kobus FJ, Fleming KG. The GxxxG-containing transmembrane domain of the CCK4 oncogene does not encode preferential self-interactions. Biochemistry. 44: 1464-70. PMID 15683231 DOI: 10.1021/Bi048076L |
0.518 |
|
| 2004 |
Doura AK, Fleming KG. Complex interactions at the helix-helix interface stabilize the glycophorin A transmembrane dimer. Journal of Molecular Biology. 343: 1487-97. PMID 15491626 DOI: 10.1016/J.Jmb.2004.09.011 |
0.349 |
|
| 2004 |
Raasi S, Orlov I, Fleming KG, Pickart CM. Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A. Journal of Molecular Biology. 341: 1367-79. PMID 15321727 DOI: 10.1016/J.Jmb.2004.06.057 |
0.397 |
|
| 2004 |
Doura AK, Kobus FJ, Dubrovsky L, Hibbard E, Fleming KG. Sequence context modulates the stability of a GxxxG-mediated transmembrane helix-helix dimer. Journal of Molecular Biology. 341: 991-8. PMID 15289100 DOI: 10.1016/J.Jmb.2004.06.042 |
0.43 |
|
| 2004 |
Fleming KG, Ren CC, Doura AK, Eisley ME, Kobus FJ, Stanley AM. Thermodynamics of glycophorin A transmembrane helix dimerization in C14 betaine micelles. Biophysical Chemistry. 108: 43-9. PMID 15043920 DOI: 10.1016/J.Bpc.2003.10.008 |
0.696 |
|
| 2002 |
Fleming KG. Standardizing the free energy change of transmembrane helix-helix interactions. Journal of Molecular Biology. 323: 563-71. PMID 12381309 DOI: 10.1016/S0022-2836(02)00920-8 |
0.409 |
|
| 2001 |
Fleming KG, Engelman DM. Computation and mutagenesis suggest a right-handed structure for the synaptobrevin transmembrane dimer. Proteins. 45: 313-7. PMID 11746678 DOI: 10.1002/Prot.1151 |
0.621 |
|
| 2001 |
Fleming KG, Engelman DM. Specificity in transmembrane helix-helix interactions can define a hierarchy of stability for sequence variants. Proceedings of the National Academy of Sciences of the United States of America. 98: 14340-4. PMID 11724930 DOI: 10.1073/Pnas.251367498 |
0.69 |
|
| 2001 |
Vergis JM, Bulock KG, Fleming KG, Beardsley GP. Human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity. The Journal of Biological Chemistry. 276: 7727-33. PMID 11096114 DOI: 10.1074/Jbc.M009940200 |
0.337 |
|
| 2000 |
Fleming KG. Probing stability of helical transmembrane proteins Methods in Enzymology. 323: 63-77. PMID 10944747 DOI: 10.1016/S0076-6879(00)23361-2 |
0.495 |
|
| 2000 |
Fleming KG. Riding the wave: Structural and energetic principles of helical membrane proteins Current Opinion in Biotechnology. 11: 67-71. PMID 10679347 DOI: 10.1016/S0958-1669(99)00056-7 |
0.578 |
|
| 1999 |
Biswas I, Ban C, Fleming KG, Qin J, Lary JW, Yphantis DA, Yang W, Hsieh P. Oligomerization of a MutS mismatch repair protein from Thermus aquaticus Journal of Biological Chemistry. 274: 23673-23678. PMID 10438551 DOI: 10.1074/Jbc.274.33.23673 |
0.379 |
|
| 1999 |
Schubert C, Hirsch JA, Gurevich VV, Engelman DM, Sigler PB, Fleming KG. Visual arrestin activity may be regulated by self-association. The Journal of Biological Chemistry. 274: 21186-90. PMID 10409673 DOI: 10.1074/Jbc.274.30.21186 |
0.568 |
|
| 1998 |
O'Brien R, DeDecker B, Fleming KG, Sigler PB, Ladbury JE. The effects of salt on the TATA binding protein-DNA interaction from a hyperthermophilic archaeon. Journal of Molecular Biology. 279: 117-25. PMID 9636704 DOI: 10.1006/Jmbi.1998.1743 |
0.368 |
|
| 1998 |
Fleming KG, Hohl TM, Yu RC, Müller SA, Wolpensinger B, Engel A, Engelhardt H, Brünger AT, Söllner TH, Hanson PI. A revised model for the oligomeric state of the N-ethylmaleimide-sensitive fusion protein, NSF. The Journal of Biological Chemistry. 273: 15675-81. PMID 9624162 DOI: 10.1074/Jbc.273.25.15675 |
0.456 |
|
| 1998 |
Beardsley GP, Rayl EA, Gunn K, Moroson BA, Seow H, Anderson KS, Vergis J, Fleming K, Worland S, Condon B, Davies J. Structure and functional relationships in human pur H. Advances in Experimental Medicine and Biology. 431: 221-6. PMID 9598063 DOI: 10.1007/978-1-4615-5381-6_43 |
0.349 |
|
| 1998 |
Fleming KG, Ackerman AL, Engelman DM. Free energy measurements of transmembrane helix-helix interactions Chemtracts. 11: 985-990. |
0.499 |
|
| 1997 |
Fleming KG, Ackerman AL, Engelman DM. The effect of point mutations on the free energy of transmembrane alpha-helix dimerization. Journal of Molecular Biology. 272: 266-75. PMID 9299353 DOI: 10.1006/Jmbi.1997.1236 |
0.635 |
|
| 1997 |
Rodgers KK, Fleming KG. Metal-dependent structure and self association of the RAG1 zinc-binding domain Techniques in Protein Chemistry. 8: 573-584. DOI: 10.1016/S1080-8914(97)80057-9 |
0.373 |
|
| 1996 |
Munson M, Balasubramanian S, Fleming KG, Nagi AD, O'Brien R, Sturtevant JM, Regan L. What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties. Protein Science : a Publication of the Protein Society. 5: 1584-93. PMID 8844848 DOI: 10.1002/Pro.5560050813 |
0.46 |
|
| 1996 |
Rodgers KK, Bu Z, Fleming KG, Schatz DG, Engelman DM, Coleman JE. A zinc-binding domain involved in the dimerization of RAG1. Journal of Molecular Biology. 260: 70-84. PMID 8676393 DOI: 10.1006/Jmbi.1996.0382 |
0.582 |
|
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