Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers CP Moon, KG Fleming Proceedings of the National Academy of Sciences 108 (25), 10174-10177, 2011 | 356 | 2011 |
What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties M Munson, S Balasubramanian, KG Fleming, AD Nagi, R O'Brien, ... Protein Science 5 (8), 1584-1593, 1996 | 305 | 1996 |
The effect of point mutations on the free energy of transmembrane α-helix dimerization KG Fleming, AL Ackerman, DM Engelman Journal of molecular biology 272 (2), 266-275, 1997 | 297 | 1997 |
β-Barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro NK Burgess, TP Dao, AM Stanley, KG Fleming Journal of Biological Chemistry 283 (39), 26748-26758, 2008 | 278 | 2008 |
Specificity in transmembrane helix–helix interactions can define a hierarchy of stability for sequence variants KG Fleming, DM Engelman Proceedings of the National Academy of Sciences 98 (25), 14340-14344, 2001 | 227 | 2001 |
Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA D Gessmann, YH Chung, EJ Danoff, AM Plummer, CW Sandlin, ... Proceedings of the National Academy of Sciences 111 (16), 5878-5883, 2014 | 208 | 2014 |
Binding of polyubiquitin chains to ubiquitin-associated (UBA) domains of HHR23A S Raasi, I Orlov, KG Fleming, CM Pickart Journal of molecular biology 341 (5), 1367-1379, 2004 | 198 | 2004 |
HullRad: fast calculations of folded and disordered protein and nucleic acid hydrodynamic properties PJ Fleming, KG Fleming Biophysical journal 114 (4), 856-869, 2018 | 185 | 2018 |
E. coli outer membrane and interactions with OmpLA EL Wu, PJ Fleming, MS Yeom, G Widmalm, JB Klauda, KG Fleming, W Im Biophysical journal 106 (11), 2493-2502, 2014 | 175 | 2014 |
Genetically encoded biosensors for visualizing live-cell biochemical activity at super-resolution GCH Mo, B Ross, F Hertel, P Manna, X Yang, E Greenwald, C Booth, ... Nature methods 14 (4), 427-434, 2017 | 165 | 2017 |
Standardizing the free energy change of transmembrane helix–helix interactions KG Fleming Journal of molecular biology 323 (3), 563-571, 2002 | 140 | 2002 |
The effects of salt on the TATA binding protein-DNA interaction from a hyperthermophilic archaeon R O’Brien, B DeDecker, KG Fleming, PB Sigler, JE Ladbury Journal of molecular biology 279 (1), 117-125, 1998 | 139 | 1998 |
Sequence context modulates the stability of a GxxxG-mediated transmembrane helix–helix dimer AK Doura, FJ Kobus, L Dubrovsky, E Hibbard, KG Fleming Journal of molecular biology 341 (4), 991-998, 2004 | 131 | 2004 |
Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm CP Moon, NR Zaccai, PJ Fleming, D Gessmann, KG Fleming Proceedings of the National Academy of Sciences 110 (11), 4285-4290, 2013 | 129 | 2013 |
A zinc-binding domain involved in the dimerization of RAG1 KK Rodgers, Z Bu, KG Fleming, DG Schatz, DM Engelman, JE Coleman Journal of molecular biology 260 (1), 70-84, 1996 | 129 | 1996 |
Complex interactions at the helix–helix interface stabilize the glycophorin A transmembrane dimer AK Doura, KG Fleming Journal of molecular biology 343 (5), 1487-1497, 2004 | 124 | 2004 |
De novo design of transmembrane β barrels AA Vorobieva, P White, B Liang, JE Horne, AK Bera, CM Chow, S Gerben, ... Science 371 (6531), eabc8182, 2021 | 121 | 2021 |
The process of folding proteins into membranes: challenges and progress AM Stanley, KG Fleming Archives of biochemistry and biophysics 469 (1), 46-66, 2008 | 120 | 2008 |
Structure of the lethal phage pinhole T Pang, CG Savva, KG Fleming, DK Struck, R Young Proceedings of the National Academy of Sciences 106 (45), 18966-18971, 2009 | 116 | 2009 |
A revised model for the oligomeric state of the N-ethylmaleimide-sensitive fusion protein, NSF KG Fleming, TM Hohl, CY Richard, SA Muller, B Wolpensinger, A Engel, ... Journal of Biological Chemistry 273 (25), 15675-15681, 1998 | 113 | 1998 |