Scott C. Mohr - Publications

Affiliations: 
Boston University, Boston, MA, United States 
Area:
Biochemistry

14 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
2009 Kaya T, Swamy N, Persons KS, Ray S, Mohr SC, Ray R. Covalent labeling of nuclear vitamin D receptor with affinity labeling reagents containing a cross-linking probe at three different positions of the parent ligand: structural and biochemical implications. Bioorganic Chemistry. 37: 57-63. PMID 19223058 DOI: 10.1016/J.Bioorg.2009.01.001  0.579
2007 Aslan FM, Yu Y, Vajda S, Mohr SC, Cantor CR. Engineering a novel, stable dimeric streptavidin with lower isoelectric point. Journal of Biotechnology. 128: 213-25. PMID 17000019 DOI: 10.1016/J.Jbiotec.2006.08.014  0.377
2006 Kaya T, Mohr SC, Waxman DJ, Vajda S. Computational screening of phthalate monoesters for binding to PPARgamma. Chemical Research in Toxicology. 19: 999-1009. PMID 16918238 DOI: 10.1021/Tx050301S  0.55
2005 Aslan FM, Yu Y, Mohr SC, Cantor CR. Engineered single-chain dimeric streptavidins with an unexpected strong preference for biotin-4-fluorescein. Proceedings of the National Academy of Sciences of the United States of America. 102: 8507-12. PMID 15939877 DOI: 10.1073/Pnas.0503112102  0.378
2001 Mohr SC, Swamy N, Xu W, Ray R. Why do we need a three-dimensional architecture of the ligand-binding domain of the nuclear 1alpha,25-dihydroxyvitamin D(3) receptor? Steroids. 66: 189-201. PMID 11179726 DOI: 10.1016/S0039-128X(00)00134-3  0.555
2000 Swamy N, Xu W, Paz N, Hsieh JC, Haussler MR, Maalouf GJ, Mohr SC, Ray R. Molecular modeling, affinity labeling, and site-directed mutagenesis define the key points of interaction between the ligand-binding domain of the vitamin D nuclear receptor and 1 alpha,25-dihydroxyvitamin D3. Biochemistry. 39: 12162-71. PMID 11015194 DOI: 10.1021/Bi0002131  0.588
1999 Swamy N, Mohr SC, Xu W, Ray R. Vitamin D receptor interacts with DnaK/heat shock protein 70: identification of DnaK interaction site on vitamin D receptor. Archives of Biochemistry and Biophysics. 363: 219-26. PMID 10068443 DOI: 10.1006/Abbi.1998.1079  0.572
1998 Maalouf GJ, Xu W, Smith TF, Mohr SC. Homology model for the ligand-binding domain of the human estrogen receptor. Journal of Biomolecular Structure & Dynamics. 15: 841-51. PMID 9619507 DOI: 10.1080/07391102.1998.10508206  0.531
1991 Mohr SC, Sokolov NVHA, Chaomei H, Setlow P. Binding of small acid-soluble spore proteins from Bacillus subtilis changes the conformation of DNA from B to A Proceedings of the National Academy of Sciences of the United States of America. 88: 77-81. PMID 1898779 DOI: 10.1073/Pnas.88.1.77  0.322
1974 Gallopo AR, Kotsiopoulos PS, Mohr SC. Purification of tyrosine-sensitive 3-deoxy-D-arabinoheptulosonate-7-phosphate (DAHP) and tyrosyl-tRNA synthetases on agarose carrying carboxyl-linked tyrosine Advances in Experimental Medicine and Biology. 42: 157-163. PMID 4602167 DOI: 10.1007/978-1-4684-6982-0_12  0.422
1973 Steenbergen C, Mohr SC. A temperature jump kinetic study of the binding of proflavine to poly I. poly C Biopolymers. 12: 791-798. PMID 4695674 DOI: 10.1002/Bip.1973.360120408  0.325
1973 Tritton TR, Mohr SC. Kinetics of ethidium bromide binding as a probe of transfer ribonucleic acid structure Biochemistry. 12: 905-914. PMID 4568769 DOI: 10.1021/Bi00729A018  0.35
1971 Tritton TR, Mohr SC. Relaxation kinetics of the binding of ethidium bromide to unfractionated yeast tRNA at low dye/phosphate ratio Biochemical and Biophysical Research Communications. 45: 1240-1249. PMID 5135508 DOI: 10.1016/0006-291X(71)90151-3  0.369
1970 Eckfeldt J, Hammes GG, Mohr SC, Wu CW. Relaxation spectra of aspartate transcarbamylase. I. Interaction of 5-bromocytidine triphosphate with native enzyme and regulatory subunit Biochemistry. 9: 3353-3362. PMID 4941833 DOI: 10.1021/Bi00819A010  0.322
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