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Laura A. Lavery, Ph.D. - Publications

Affiliations: 
2013 Biophysics University of California, San Francisco, San Francisco, CA 
Area:
Structure, function, and folding of proteins, chromosomes, and centrosomes
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9 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
2015 Chen L, Chen K, Lavery LA, Baker SA, Shaw CA, Li W, Zoghbi HY. MeCP2 binds to non-CG methylated DNA as neurons mature, influencing transcription and the timing of onset for Rett syndrome. Proceedings of the National Academy of Sciences of the United States of America. 112: 5509-14. PMID 25870282 DOI: 10.1073/Pnas.1505909112  0.314
2014 Partridge JR, Lavery LA, Elnatan D, Naber N, Cooke R, Agard DA. A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity. Elife. 3. PMID 25531069 DOI: 10.7554/Elife.03487  0.613
2014 Prestegard JH, Agard DA, Moremen KW, Lavery LA, Morris LC, Pederson K. Sparse labeling of proteins: structural characterization from long range constraints. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 32-40. PMID 24656078 DOI: 10.1016/J.Jmr.2013.12.012  0.498
2014 Lavery LA, Partridge JR, Ramelot TA, Elnatan D, Kennedy MA, Agard DA. Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Molecular Cell. 53: 330-43. PMID 24462206 DOI: 10.1016/J.Molcel.2013.12.023  0.624
2014 Partridge JR, Lavery LA, Elnatan D, Naber N, Cooke R, Agard DA. Author response: A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity Elife. DOI: 10.7554/Elife.03487.021  0.488
2012 Street TO, Lavery LA, Verba KA, Lee CT, Mayer MP, Agard DA. Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity. Journal of Molecular Biology. 415: 3-15. PMID 22063096 DOI: 10.1016/J.Jmb.2011.10.038  0.67
2011 Street TO, Lavery LA, Agard DA. Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Molecular Cell. 42: 96-105. PMID 21474071 DOI: 10.1016/J.Molcel.2011.01.029  0.645
2011 Krukenberg KA, Street TO, Lavery LA, Agard DA. Conformational dynamics of the molecular chaperone Hsp90. Quarterly Reviews of Biophysics. 44: 229-55. PMID 21414251 DOI: 10.1017/S0033583510000314  0.672
2011 Street TO, Lavery L, Agard DA. Elucidating the Mechanism of Protein Remodeling by the Hsp90 Molecular Chaperone Biophysical Journal. 100: 390a. DOI: 10.1016/J.Bpj.2010.12.2318  0.645
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