Powers R - Search Results

1

The high-resolution, three-dimensional solution structure of human interleukin-4 determined by multidimensional heteronuclear magnetic resonance spectroscopy.

Powers R, Garrett DS, March CJ, Frieden EA, Gronenborn AM, Clore GM. Powers R, et al. Biochemistry. 1993 Jul 6;32(26):6744-62. doi: 10.1021/bi00077a030. Biochemistry. 1993. PMID: 8329398

2

Analysis of the backbone dynamics of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase using 15N relaxation measurements.

Powers R, Clore GM, Stahl SJ, Wingfield PT, Gronenborn A. Powers R, et al. Biochemistry. 1992 Sep 29;31(38):9150-7. doi: 10.1021/bi00153a006. Biochemistry. 1992. PMID: 1382587

3

1H, 15N, 13C, and 13CO assignments of human interleukin-4 using three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy.

Powers R, Garrett DS, March CJ, Frieden EA, Gronenborn AM, Clore GM. Powers R, et al. Biochemistry. 1992 May 5;31(17):4334-46. doi: 10.1021/bi00132a026. Biochemistry. 1992. PMID: 1567880

4

Determination of the secondary structure and folding topology of human interleukin-4 using three-dimensional heteronuclear magnetic resonance spectroscopy.

Garrett DS, Powers R, March CJ, Frieden EA, Clore GM, Gronenborn AM. Garrett DS, et al. Among authors: powers r. Biochemistry. 1992 May 5;31(17):4347-53. doi: 10.1021/bi00132a027. Biochemistry. 1992. PMID: 1567881

The secondary structure of human recombinant interleukin-4 (IL-4) has been investigated by three-dimensional (3D) 15N- and 13C-edited nuclear Overhauser (NOE) spectroscopy on the basis of the 1H, 15N, and 13C assignments presented in the preceding paper [Powers, R., …

The secondary structure of human recombinant interleukin-4 (IL-4) has been investigated by three-dimensional (3D) 15N- and 13C-edited nuclea …

5

Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy.

Powers R, Garrett DS, March CJ, Frieden EA, Gronenborn AM, Clore GM. Powers R, et al. Science. 1992 Jun 19;256(5064):1673-7. doi: 10.1126/science.256.5064.1673. Science. 1992. PMID: 1609277

6

Secondary structure of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy.

Powers R, Clore GM, Bax A, Garrett DS, Stahl SJ, Wingfield PT, Gronenborn AM. Powers R, et al. J Mol Biol. 1991 Oct 20;221(4):1081-90. doi: 10.1016/0022-2836(91)90920-2. J Mol Biol. 1991. PMID: 1719214

7

Resonance assignments for Oncostatin M, a 24-kDa alpha-helical protein.

Hoffman RC, Moy FJ, Price V, Richardson J, Kaubisch D, Frieden EA, Krakover JD, Castner BJ, King J, March CJ, Powers R. Hoffman RC, et al. Among authors: powers r. J Biomol NMR. 1996 Jun;7(4):273-82. doi: 10.1007/BF00200429. J Biomol NMR. 1996. PMID: 8765735

8

High-resolution solution structure of basic fibroblast growth factor determined by multidimensional heteronuclear magnetic resonance spectroscopy.

Moy FJ, Seddon AP, Böhlen P, Powers R. Moy FJ, et al. Among authors: powers r. Biochemistry. 1996 Oct 22;35(42):13552-61. doi: 10.1021/bi961260p. Biochemistry. 1996. PMID: 8885834

9

A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams. 1991.

Garrett DS, Powers R, Gronenborn AM, Clore GM. Garrett DS, et al. Among authors: powers r. J Magn Reson. 2011 Dec;213(2):357-63. doi: 10.1016/j.jmr.2011.09.007. J Magn Reson. 2011. PMID: 22152355 No abstract available.

10

High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR.

Moy FJ, Chanda PK, Cosmi S, Pisano MR, Urbano C, Wilhelm J, Powers R. Moy FJ, et al. Among authors: powers r. Biochemistry. 1998 Feb 10;37(6):1495-504. doi: 10.1021/bi972181w. Biochemistry. 1998. PMID: 9484219

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