Blaine H. Mooers, Ph.D.
Affiliations: | Biochemistry and Mol Biol | University of Oklahoma Health Sciences Center, Oklahoma City, OK, United States |
Area:
RNA structure, crystallographyWebsite:
http://www.oumedicine.com/department-of-biochemistry-and-molecular-biology/faculty/blaine-mooers-ph-d-Google:
"Blaine Mooers"Mean distance: 8.66 | S | N | B | C | P |
Cross-listing: Crystallography Tree
Parents
Sign in to add mentorP. Shing Ho | grad student | 1992-1997 | Oregon State |
Brian W. Matthews | post-doc | 1997-2006 | University of Oregon |
Collaborators
Sign in to add collaboratorJohn E. Hearst | collaborator | 1994-1997 | Oregon State |
Stephen L. Mayo | collaborator | 1999-2003 | University of Oregon |
John Andrew Berglund | collaborator | 2003-2005 | University of Oregon |
BETA: Related publications
See more...
Publications
You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect. |
Mooers B, Gulati S, Kumar V, et al. (2017) Atomic structures of kinetoplastid RNA editing sites Acta Crystallographica Section A. 73 |
Gu X, Mooers BH, Thomas LM, et al. (2015) Structures and Energetics of Four Adjacent G·U Pairs That Stabilize an RNA Helix. The Journal of Physical Chemistry. B. 119: 13252-61 |
Mooers BH, Baase WA, Wray JW, et al. (2009) Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. Protein Science : a Publication of the Protein Society. 18: 871-80 |
Mooers BH, Tronrud DE, Matthews BW. (2009) Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His. Protein Science : a Publication of the Protein Society. 18: 863-70 |
Mooers BH, Matthews BW. (2006) Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme. Acta Crystallographica. Section D, Biological Crystallography. 62: 165-76 |
Mooers BH, Logue JS, Berglund JA. (2005) The structural basis of myotonic dystrophy from the crystal structure of CUG repeats. Proceedings of the National Academy of Sciences of the United States of America. 102: 16626-31 |
Mooers BH, Matthews BW. (2004) Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods. Acta Crystallographica. Section D, Biological Crystallography. 60: 1726-37 |
Sagermann M, Baase WA, Mooers BH, et al. (2004) Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Biochemistry. 43: 1296-301 |
Mooers BH, Datta D, Baase WA, et al. (2003) Repacking the Core of T4 lysozyme by automated design. Journal of Molecular Biology. 332: 741-56 |
Gassner NC, Baase WA, Mooers BH, et al. (2003) Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability. Biophysical Chemistry. 100: 325-40 |