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Lisa M. Gloss - Publications

Affiliations: 
Washington State University, Pullman, WA, United States 
Area:
Biochemistry
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35 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2018 Mauney AW, Tokuda JM, Gloss LM, Gonzalez O, Pollack L. Local DNA Sequence Controls Asymmetry of DNA Unwrapping from Nucleosome Core Particles. Biophysical Journal. PMID 30072033 DOI: 10.1016/J.Bpj.2018.07.009  0.4
2017 Hodges AJ, Gloss LM, Wyrick JJ. Residues in the Nucleosome Acidic Patch Regulate Histone Occupancy and Are Important for FACT Binding in Saccharomyces cerevisiae. Genetics. PMID 28468903 DOI: 10.1534/Genetics.117.201939  0.551
2017 Mauney A, Tokuda J, Chen Y, Gloss L, Topping T, Gonzalez O, Pollack L. Sequence Dependence in Salt Based Nucleosome Unwrapping Using Saxs Biophysical Journal. 112: 371a. DOI: 10.1016/J.Bpj.2016.11.2012  0.322
2017 Chen Y, Tokuda J, Topping T, Meisburger S, Pabit S, Gloss L, Pollack L. Asymmetric DNA Unwrapping Drives Sequential Dimer Release in Nucleosomes Biophysical Journal. 112: 370a-371a. DOI: 10.1016/J.Bpj.2016.11.2011  0.519
2016 Chen Y, Tokuda JM, Topping T, Meisburger SP, Pabit SA, Gloss LM, Pollack L. Asymmetric unwrapping of nucleosomal DNA propagates asymmetric opening and dissociation of the histone core. Proceedings of the National Academy of Sciences of the United States of America. PMID 28028239 DOI: 10.1073/Pnas.1611118114  0.503
2016 Mao P, Kyriss MN, Hodges AJ, Duan M, Morris RT, Lavine MD, Topping TB, Gloss LM, Wyrick JJ. A basic domain in the histone H2B N-terminal tail is important for nucleosome assembly by FACT. Nucleic Acids Research. PMID 27369377 DOI: 10.1093/Nar/Gkw588  0.529
2015 Tokuda JM, Chen Y, Topping T, Gloss LM, Pollack L. Using Contrast Variation with SAXS to Visualize DNA Dissociation from Nucleosome Core Particles Biophysical Journal. 108: 75a. DOI: 10.1016/J.Bpj.2014.11.442  0.467
2015 Chen Y, Tokuda JM, Topping T, Sutton JL, Meisburger SP, Pabit SA, Gloss LM, Pollack L. Asymmetric Nucleosome Disassembly with Disrupted Histones Revealed by Time Resolved Small Angle X-Ray Scattering with Contrast Variation Biophysical Journal. 108: 15a. DOI: 10.1016/J.Bpj.2014.11.108  0.429
2014 Chen Y, Tokuda JM, Topping T, Sutton JL, Meisburger SP, Pabit SA, Gloss LM, Pollack L. Revealing transient structures of nucleosomes as DNA unwinds. Nucleic Acids Research. 42: 8767-76. PMID 24990379 DOI: 10.1093/Nar/Gku562  0.436
2013 Tokuda J, Topping T, Gloss L, Pollack L. Visualizing DNA Disassociation from the Nucleosome Core Particle Biophysical Journal. 104: 198a. DOI: 10.1016/J.Bpj.2012.11.1116  0.438
2012 Guyett PJ, Gloss LM. The H2A-H2B dimeric kinetic intermediate is stabilized by widespread hydrophobic burial with few fully native interactions. Journal of Molecular Biology. 415: 600-14. PMID 22137897 DOI: 10.1016/J.Jmb.2011.11.032  0.831
2012 Guyett PJ, Gloss LM. Intermediates in protein folding Comprehensive Biophysics. 3: 43-71. DOI: 10.1016/B978-0-12-374920-8.00304-0  0.79
2011 Topping TB, Gloss LM. The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones. Protein Science : a Publication of the Protein Society. 20: 2060-73. PMID 21953551 DOI: 10.1002/Pro.743  0.562
2010 Stump MR, Gloss LM. Mutational studies uncover non-native structure in the dimeric kinetic intermediate of the H2A-H2B heterodimer. Journal of Molecular Biology. 401: 518-31. PMID 20600120 DOI: 10.1016/J.Jmb.2010.06.034  0.829
2009 Gloss LM. Equilibrium and kinetic approaches for studying oligomeric protein folding. Methods in Enzymology. 466: 325-57. PMID 21609867 DOI: 10.1016/S0076-6879(09)66014-6  0.463
2008 Stump MR, Gloss LM. Mutational analysis of the stability of the H2A and H2B histone monomers. Journal of Molecular Biology. 384: 1369-83. PMID 18976667 DOI: 10.1016/J.Jmb.2008.10.040  0.838
2008 Gloss LM, Topping TB, Binder AK, Lohman JR. Kinetic folding of Haloferax volcanii and Escherichia coli dihydrofolate reductases: haloadaptation by unfolded state destabilization at high ionic strength. Journal of Molecular Biology. 376: 1451-62. PMID 18207162 DOI: 10.1016/J.Jmb.2007.12.056  0.771
2008 Stump MR, Gloss LM. Unique fluorophores in the dimeric archaeal histones hMfB and hPyA1 reveal the impact of nonnative structure in a monomeric kinetic intermediate. Protein Science : a Publication of the Protein Society. 17: 322-32. PMID 18096639 DOI: 10.1110/Ps.073224308  0.828
2007 Hoch DA, Stratton JJ, Gloss LM. Protein-protein Förster resonance energy transfer analysis of nucleosome core particles containing H2A and H2A.Z. Journal of Molecular Biology. 371: 971-88. PMID 17597150 DOI: 10.1016/J.Jmb.2007.05.075  0.825
2007 Gloss LM. Tying the knot that binds. Structure (London, England : 1993). 15: 2-4. PMID 17223526 DOI: 10.1016/J.Str.2006.12.001  0.42
2005 Placek BJ, Harrison LN, Villers BM, Gloss LM. The H2A.Z/H2B dimer is unstable compared to the dimer containing the major H2A isoform. Protein Science : a Publication of the Protein Society. 14: 514-22. PMID 15632282 DOI: 10.1110/Ps.041026405  0.812
2005 Placek BJ, Gloss LM. 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 dimer. Journal of Molecular Biology. 345: 827-36. PMID 15588829 DOI: 10.1016/J.Jmb.2004.11.006  0.822
2004 Topping TB, Gloss LM. Stability and folding mechanism of mesophilic, thermophilic and hyperthermophilic archael histones: the importance of folding intermediates. Journal of Molecular Biology. 342: 247-60. PMID 15313621 DOI: 10.1016/J.Jmb.2004.07.045  0.679
2004 Banks DD, Gloss LM. Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome. Protein Science : a Publication of the Protein Society. 13: 1304-16. PMID 15096635 DOI: 10.1110/Ps.03535504  0.506
2004 Topping TB, Hoch DA, Gloss LM. Folding mechanism of FIS, the intertwined, dimeric factor for inversion stimulation. Journal of Molecular Biology. 335: 1065-81. PMID 14698300 DOI: 10.1016/J.Jmb.2003.11.013  0.801
2003 Banks DD, Gloss LM. Equilibrium folding of the core histones: the H3-H4 tetramer is less stable than the H2A-H2B dimer. Biochemistry. 42: 6827-39. PMID 12779337 DOI: 10.1021/Bi026957R  0.536
2002 Placek BJ, Gloss LM. The N-terminal tails of the H2A-H2B histones affect dimer structure and stability. Biochemistry. 41: 14960-8. PMID 12475245 DOI: 10.1021/Bi026283K  0.804
2002 Gloss LM, Placek BJ. The effect of salts on the stability of the H2A-H2B histone dimer. Biochemistry. 41: 14951-9. PMID 12475244 DOI: 10.1021/Bi026282S  0.818
2002 Wright DB, Banks DD, Lohman JR, Hilsenbeck JL, Gloss LM. The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases. Journal of Molecular Biology. 323: 327-44. PMID 12381324 DOI: 10.1016/S0022-2836(02)00916-6  0.733
2001 Gloss LM, Simler BR, Matthews CR. Rough energy landscapes in protein folding: dimeric E. coli Trp repressor folds through three parallel channels. Journal of Molecular Biology. 312: 1121-34. PMID 11580254 DOI: 10.1006/Jmbi.2001.4974  0.529
2000 Mevarech M, Frolow F, Gloss LM. Halophilic enzymes: Proteins with a grain of salt Biophysical Chemistry. 86: 155-164. PMID 11026680 DOI: 10.1016/S0301-4622(00)00126-5  0.442
2000 Jeffery CJ, Gloss LM, Petsko GA, Ringe D. The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase. Protein Engineering. 13: 105-12. PMID 10708649 DOI: 10.1093/Protein/13.2.105  0.319
1998 Gloss LM, Matthews CR. The barriers in the bimolecular and unimolecular folding reactions of the dimeric core domain of Escherichia coli Trp repressor are dominated by enthalpic contributions. Biochemistry. 37: 16000-10. PMID 9843407 DOI: 10.1021/bi981694f  0.393
1998 Gloss LM, Matthews CR. Mechanism of folding of the dimeric core domain of Escherichia coli trp repressor: a nearly diffusion-limited reaction leads to the formation of an on-pathway dimeric intermediate. Biochemistry. 37: 15990-9. PMID 9843406 DOI: 10.1021/bi981511p  0.419
1997 Gloss LM, Matthews CR. Urea and thermal equilibrium denaturation studies on the dimerization domain of Escherichia coli Trp repressor. Biochemistry. 36: 5612-23. PMID 9153401 DOI: 10.1021/bi970056e  0.498
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