Laura A. Lavery, Ph.D.

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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"Laura Lavery"
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David A. Agard grad student 2013 UCSF
 (Structure and Function of the Mitochondrial Hsp90, TRAPl.)
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Publications

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Chen L, Chen K, Lavery LA, et al. (2015) 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
Partridge JR, Lavery LA, Elnatan D, et al. (2014) A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity. Elife. 3
Prestegard JH, Agard DA, Moremen KW, et al. (2014) Sparse labeling of proteins: structural characterization from long range constraints. Journal of Magnetic Resonance (San Diego, Calif. : 1997). 241: 32-40
Lavery LA, Partridge JR, Ramelot TA, et al. (2014) Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism. Molecular Cell. 53: 330-43
Partridge JR, Lavery LA, Elnatan D, et al. (2014) Author response: A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity Elife
Street TO, Lavery LA, Verba KA, et al. (2012) Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity. Journal of Molecular Biology. 415: 3-15
Street TO, Lavery LA, Agard DA. (2011) Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone. Molecular Cell. 42: 96-105
Krukenberg KA, Street TO, Lavery LA, et al. (2011) Conformational dynamics of the molecular chaperone Hsp90. Quarterly Reviews of Biophysics. 44: 229-55
Street TO, Lavery L, Agard DA. (2011) Elucidating the Mechanism of Protein Remodeling by the Hsp90 Molecular Chaperone Biophysical Journal. 100: 390a
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