George H. Lorimer
Affiliations: | Chemistry and Biochemistry | University of Maryland, College Park, College Park, MD |
Area:
photosynthesisWebsite:
http://www.biochem.umd.edu/faculty/lorimer.htmGoogle:
"George H. Lorimer"Bio:
http://www.nasonline.org/member-directory/members/3003896.html
http://chembio-newsarchive.umd.edu/about/circleofdiscovery/georgehlorimer
Mean distance: 8.96
Parents
Sign in to add mentor| N. Edward Tolbert | grad student | 1972 | Michigan State | |
| (The Role of Oxygen in Photorespiration) | ||||
| Birgit Vennesland | post-doc | 1972 | Forschungsstelle Vennesland der Max-Planck-Gesellschaft | |
Children
Sign in to add trainee| John P. Grason | grad student | 2003 | University of Maryland |
| Jennifer S. Gresham | grad student | 2004 | University of Maryland |
| Sarah C. Wehri | grad student | 2013 | University of Maryland |
| Nicholas C. Corsepius | grad student | 2014 | University of Maryland |
| Dong Yang | grad student | 2014 | University of Maryland |
| Xue Fei | grad student | 2009-2014 | NIH & University of Maryland College Park |
BETA: Related publications
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Publications
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| Stan G, Lorimer GH, Thirumalai D. (2022) Friends in need: How chaperonins recognize and remodel proteins that require folding assistance. Frontiers in Molecular Biosciences. 9: 1071168 |
| Thirumalai D, Lorimer GH, Hyeon C. (2019) Iterative Annealing Mechanism Explains the Functions of the GroEL and RNA Chaperones. Protein Science : a Publication of the Protein Society |
| Thirumalai D, Hyeon C, Zhuravlev PI, et al. (2019) Symmetry, Rigidity, and Allosteric Signaling: From Monomeric Proteins to Molecular Machines. Chemical Reviews |
| Lorimer GH, Fei X, Ye X. (2018) The GroEL chaperonin: a protein machine with pistons driven by ATP binding and hydrolysis. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 373 |
| Roh SH, Hryc CF, Jeong HH, et al. (2017) Subunit conformational variation within individual GroEL oligomers resolved by Cryo-EM. Proceedings of the National Academy of Sciences of the United States of America |
| Fei X, Ye X, LaRonde NA, et al. (2014) Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form Proceedings of the National Academy of Sciences of the United States of America. 111: 12775-12780 |
| Yang D, Ye X, Lorimer GH. (2013) Symmetric GroEL: GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine Proceedings of the National Academy of Sciences of the United States of America. 110: E4298-E4305 |
| Ye X, Lorimer GH. (2013) Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange Proceedings of the National Academy of Sciences of the United States of America. 110: E4289-E4297 |
| Fei X, Yang D, LaRonde-LeBlanc N, et al. (2013) Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution Proceedings of the National Academy of Sciences of the United States of America. 110: E2958-E2966 |
| Corsepius NC, Lorimer GH. (2013) Measuring how much work the chaperone GroEL can do Proceedings of the National Academy of Sciences of the United States of America. 110: E2451-E2459 |