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David Bulkley, Ph.D.

Affiliations: 
2013 Yale University, New Haven, CT 
Area:
Biochemistry, structural chemistry
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"David Bulkley"
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Thomas A. Steitz grad student 2013 Yale
 (Structural Studies of the Inhibition of Bacterial Translation.)

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Publications

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Lin J, Gagnon MG, Bulkley D, et al. (2015) Conformational changes of elongation factor G on the ribosome during tRNA translocation. Cell. 160: 219-27
Polikanov YS, Osterman IA, Szal T, et al. (2014) Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome. Molecular Cell. 56: 531-40
Gagnon MG, Lin J, Bulkley D, et al. (2014) Crystal structure of elongation factor 4 bound to a clockwise ratcheted ribosome. Science (New York, N.Y.). 345: 684-7
Brown JA, Bulkley D, Wang J, et al. (2014) Structural insights into the stabilization of MALAT1 noncoding RNA by a bipartite triple helix. Nature Structural & Molecular Biology. 21: 633-40
Bulkley D, Brandi L, Polikanov YS, et al. (2014) The antibiotics dityromycin and GE82832 bind protein S12 and block EF-G-catalyzed translocation. Cell Reports. 6: 357-65
Xia S, Vashishtha A, Bulkley D, et al. (2012) Contribution of partial charge interactions and base stacking to the efficiency of primer extension at and beyond abasic sites in DNA. Biochemistry. 51: 4922-31
Gagnon MG, Seetharaman SV, Bulkley D, et al. (2012) Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome. Science (New York, N.Y.). 335: 1370-2
Bulkley D, Johnson F, Steitz TA. (2012) The antibiotic thermorubin inhibits protein synthesis by binding to inter-subunit bridge B2a of the ribosome. Journal of Molecular Biology. 416: 571-8
Steitz TA, Blaha G, Innis CA, et al. (2012) Structural studies of the functional complexes of the 50s and 70s ribosome, a major antibiotic target Nato Science For Peace and Security Series a: Chemistry and Biology. 135-148
Bulkley D, Innis CA, Blaha G, et al. (2010) Revisiting the structures of several antibiotics bound to the bacterial ribosome. Proceedings of the National Academy of Sciences of the United States of America. 107: 17158-63
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