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Methods in Enzymology|May 26, 2011
Equilibrium and kinetic approaches for studying oligomeric protein foldingLisa M GlossJournal of Molecular Biology|December 14, 2004
Three-state kinetic folding mechanism of the H2A/H2B histone heterodimer: the N-terminal tails affect the transition state between a dimeric intermediate and the native dimerBrandon J Placek, Lisa M GlossBiochemistry|December 12, 2002
The effect of salts on the stability of the H2A-H2B histone dimerLisa M Gloss, Brandon J PlacekJournal of Molecular Biology|December 6, 2011
The H2A-H2B dimeric kinetic intermediate is stabilized by widespread hydrophobic burial with few fully native interactionsPaul J Guyett, Lisa M GlossBiochemistry|June 5, 2003
Equilibrium folding of the core histones: the H3-H4 tetramer is less stable than the H2A-H2B dimerDouglas D Banks, Lisa M GlossProtein Science : a Publication of the Protein Society|December 22, 2007
Unique fluorophores in the dimeric archaeal histones hMfB and hPyA1 reveal the impact of nonnative structure in a monomeric kinetic intermediateMatthew R Stump, Lisa M GlossBiochemistry|December 12, 2002
The N-terminal tails of the H2A-H2B histones affect dimer structure and stabilityBrandon J Placek, Lisa M GlossProtein Science : a Publication of the Protein Society|April 21, 2004
Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosomeDouglas D Banks, Lisa M GlossProtein Science : a Publication of the Protein Society|September 29, 2011
The impact of solubility and electrostatics on fibril formation by the H3 and H4 histonesTraci B Topping, Lisa M GlossPageof 3