19 results for author:"Rodgers D.W." in Literature citations
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| Active site mutations change the cleavage specificity of neprilysin. Sexton T., Hitchcook L.J., Rodgers D.W., Bradley L.H., Hersh L.B. PLoS ONE 7:e32343-e32343(2012) · Mapped (3) |
| Anion activation site of insulin-degrading enzyme. Noinaj N., Song E.S., Bhasin S., Alper B.J., Schmidt W.K., Hersh L.B., Rodgers D.W. J. Biol. Chem. 287:48-57(2012) · UniProtKB (1) |
| Identification of the allosteric regulatory site of insulysin. Noinaj N., Bhasin S.K., Song E.S., Scoggin K.E., Juliano M.A., Juliano L., Hersh L.B., Rodgers D.W. PLoS ONE 6:E20864-E20864(2011) · UniProtKB (1) |
| Mixed dimers of insulin-degrading enzyme reveal a cis activation mechanism. Song E.S., Rodgers D.W., Hersh L.B. J. Biol. Chem. 286:13852-13858(2011) · Mapped (4) |
| Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes. Kessler J.H., Khan S., Seifert U., Le Gall S., Chow K.M., Paschen A., Bres-Vloemans S.A., de Ru A., van Montfoort N., Franken K.L. et al. Nat. Immunol. 12:45-53(2011) · Mapped (8) |
| The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes. Cai Y., Chin H.F., Lazarova D., Menon S., Fu C., Cai H., Sclafani A., Rodgers D.W., De La Cruz E.M., Ferro-Novick S. et al. Cell 133:1202-1213(2008) · Mapped (7) |
| Insights into the substrate specificity of plant peptide deformylase, an essential enzyme with potential for the development of novel biotechnology applications in agriculture. Dirk L.M., Schmidt J.J., Cai Y., Barnes J.C., Hanger K.M., Nayak N.R., Williams M.A., Grossman R.B., Houtz R.L., Rodgers D.W. Biochem. J. 413:417-427(2008) · UniProtKB (1) |
| Neprilysin and amyloid beta peptide degradation. Hersh L.B., Rodgers D.W. Curr Alzheimer Res 5:225-231(2008) · Mapped (3) |
| Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase. Lim E.J., Sampath S., Coll-Rodriguez J., Schmidt J., Ray K., Rodgers D.W. J. Biol. Chem. 282:9722-9732(2007) · UniProtKB (1) · Mapped (7) |
| The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase. Yikilmaz E., Rodgers D.W., Miller A.F. Biochemistry 45:1151-1161(2006) · Mapped (1) |
| Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders. Cai Y., Cronin C.N., Engel A.G., Ohno K., Hersh L.B., Rodgers D.W. EMBO J. 23:2047-2058(2004) · UniProtKB (1) |
| Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization. Ray K., Hines C.S., Coll-Rodriguez J., Rodgers D.W. J. Biol. Chem. 279:20480-20489(2004) · Mapped (1) |
| Mapping sequence differences between thimet oligopeptidase and neurolysin implicates key residues in substrate recognition. Ray K., Hines C.S., Rodgers D.W. Protein Sci. 11:2237-2246(2002) · Mapped (4) |
| Structures of nitroreductase in three states: effects of inhibitor binding and reduction. Haynes C.A., Koder R.L., Miller A.-F., Rodgers D.W. J. Biol. Chem. 277:11513-11520(2002) · UniProtKB (1) |
| Structure of neurolysin reveals a deep channel that limits substrate access. Brown C.K., Madauss K., Lian W., Beck M.R., Tolbert W.D., Rodgers D.W. Proc. Natl. Acad. Sci. U.S.A. 98:3127-3132(2001) · UniProtKB (1) |
| The complex between phage 434 repressor DNA-binding domain and operator site OR3: structural differences between consensus and non-consensus half-sites. Rodgers D.W., Harrison S.C. Structure 1:227-240(1993) · Mapped (1) |
| The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1. Rodgers D.W., Gamblin S.J., Harris B.A., Ray S., Culp J.S., Hellmig B., Woolf D.J., Debouck C., Harrison S.C. Proc. Natl. Acad. Sci. U.S.A. 92:1222-1226(1995) · UniProtKB (1) |
| Recognition of a DNA operator by the repressor of phage 434: a view at high resolution. Aggarwal A.K., Rodgers D.W., Drottar M., Ptashne M., Harrison S.C. Science 242:899-907(1988) · UniProtKB (1) |
| Atomic structure of a fragment of human CD4 containing two immunoglobulin-like domains. Wang J., Yan Y., Garrett T.P., Liu J., Rodgers D.W., Garlick R.L., Tarr G.E., Husain Y., Reinherz E.L., Harrison S.C. Nature 348:411-418(1990) · UniProtKB (1) |