-
1
-
-
0026584349
-
Solution studies of Staphylococcal nuclease H124L 2.1H, "C and "N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3',5'-bisphosphatecalcium ternary complex
-
1992 31:921-936.
-
Wang JF, Hinke AP, Loh SN, LeMaster DM, Markley JL. Solution studies of Staphylococcal nuclease H124L 2.1H, "C and "N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3',5'-bisphosphatecalcium ternary complex. Biochemistry(1992) 31:921-936.
-
Biochemistry
-
-
Wang, J.F.1
Hinke, A.P.2
Loh, S.N.3
Lemaster, D.M.4
Markley, J.L.5
-
3
-
-
16944365890
-
Discovery of potent non-peptide inhibitors of stromelysin using SAR by NMR
-
Sheppard G, Nettesheim DG, Olejiniczak ET, Shuker SB, Meadows RP, Steinman DH, Carrera GM Jr, Marcotte PA, Severin J, Walter K, Smith H, Gubbins E, Simmer R, Holzman TF, Morgan DW, Davidsen SK, Summers JB, Fesik SW. 1997 119:5818-5827.
-
Hajduk PJ, Sheppard G, Nettesheim DG, Olejiniczak ET, Shuker SB, Meadows RP, Steinman DH, Carrera GM Jr, Marcotte PA, Severin J, Walter K, Smith H, Gubbins E, Simmer R, Holzman TF, Morgan DW, Davidsen SK, Summers JB, Fesik SW. Discovery of potent non-peptide inhibitors of stromelysin using SAR by NMR. J Am Chem Soc (1997) 119:5818-5827.
-
J Am Chem Soc
-
-
Hajduk, P.J.1
-
5
-
-
33745994172
-
-
Used by permission from D Wiess, Schering-Plough Research Institute, USA.
-
Used by permission from D Wiess, Schering-Plough Research Institute, USA.
-
-
-
-
6
-
-
0001201663
-
Fast-HMQC using Ernst angle pulses: An efficient tool for screening of ligand binding to target proteins
-
1997 10:389-396.
-
Ross A, Salzmann M, Senn H. Fast-HMQC using Ernst angle pulses: An efficient tool for screening of ligand binding to target proteins. JBiomolNMR (1997) 10:389-396.
-
JBiomolNMR
-
-
Ross, A.1
Salzmann, M.2
Senn, H.3
-
7
-
-
0032126855
-
Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in "C-labeled proteins
-
1998 120:6394-6400.
-
Pervushin K, Riek R, Wider G, Wuthrich K. Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in "C-labeled proteins. J Am Chem Soc (1998) 120:6394-6400.
-
J Am Chem Soc
-
-
Pervushin, K.1
Riek, R.2
Wider, G.3
Wuthrich, K.4
-
8
-
-
0033518575
-
TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins
-
1999 121:844-848.
-
Salzmann M, Wider G, Pervushin K, Senn H, Wuthrich K. TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins. J Am Chem Soc (1999) 121:844-848.
-
J Am Chem Soc
-
-
Salzmann, M.1
Wider, G.2
Pervushin, K.3
Senn, H.4
Wuthrich, K.5
-
10
-
-
0030612833
-
Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
-
1997 94:12366-12371.
-
Pervushin K, Riek R, Wider G, Wuthrich K. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc NatlAcadSci USA (1997) 94:12366-12371.
-
Proc NatlAcadSci USA
-
-
Pervushin, K.1
Riek, R.2
Wider, G.3
Wuthrich, K.4
-
12
-
-
0032503612
-
Segmental isotope labeling for protein NMR using peptide splicing
-
1998 120:5591-5592.
-
Yamazaki T, Otomo T, Oda N, Kyogoku Y, Uegaki K, Ito N, Ishino Y, Nakamura H. Segmental isotope labeling for protein NMR using peptide splicing. JAm Chem Soc (1998) 120:5591-5592.
-
JAm Chem Soc
-
-
Yamazaki, T.1
Otomo, T.2
Oda, N.3
Kyogoku, Y.4
Uegaki, K.5
Ito, N.6
Ishino, Y.7
Nakamura, H.8
-
14
-
-
0033540665
-
Insertion of a synthetic peptide into a recombinant protein framework: A protein biosensor
-
1100-1101.
-
Cotton GJ, Ayers B, Xu R, Muir TW. Insertion of a synthetic peptide into a recombinant protein framework: A protein biosensor. JAm Chem Soc (1B99) 121:1100-1101.
-
JAm Chem Soc (1B99) 121
-
-
Cotton, G.J.1
Ayers, B.2
Xu, R.3
Muir, T.W.4
-
15
-
-
0033582287
-
Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies
-
1999 96:388-393.
-
Xu R, Ayers B, Cowbum D, Muir TW. Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies. Proc NatlAcad Sei USA (1999) 96:388-393.
-
Proc NatlAcad Sei USA
-
-
Xu, R.1
Ayers, B.2
Cowbum, D.3
Muir, T.W.4
-
16
-
-
0001364796
-
Screening mixtures by affinity NMR
-
Shapiro MJ, Wareing JR. 1997 62:8930-8931.
-
Lin M, Shapiro MJ, Wareing JR. Screening mixtures by affinity NMR. J Org Chem (1997) 62:8930-8931.
-
J Org Chem
-
-
Lin, M.1
-
17
-
-
33745986254
-
Diffusion-edited NMRaffinity NMR for direct observation of molecular interactions
-
1997 119:5249-5250.
-
Un M, Shapiro MJ, Wareing JR. Diffusion-edited NMRaffinity NMR for direct observation of molecular interactions. JAm Chem Soc (1997) 119:5249-5250.
-
JAm Chem Soc
-
-
Un, M.1
Shapiro, M.J.2
Wareing, J.R.3
-
19
-
-
0032514975
-
Diffusion edited NMR: Screening compound mixtures by affinity NMR to detect binding hgands to vancomycin
-
1998 63:8486-8490.
-
Bleicher K, Un M, Shapiro MJ, Wareing JR. Diffusion edited NMR: Screening compound mixtures by affinity NMR to detect binding hgands to vancomycin. J Org Chem (1998) 63:8486-8490.
-
J Org Chem
-
-
Bleicher, K.1
Un, M.2
Shapiro, M.J.3
Wareing, J.R.4
-
20
-
-
0030965629
-
Otting G. Organic solvents identify specific ligand binding sites on protein surfaces
-
199715:264-268.
-
Liepinsh E, Otting G. Organic solvents identify specific ligand binding sites on protein surfaces. Nat Biotechnot (1997)15:264-268.
-
Nat Biotechnot
-
-
Liepinsh, E.1
-
22
-
-
0031576702
-
One-dimensional relaxation- And diffusion-edited NMR methods for screening compounds that bind to macromolecules
-
1997 119:12257-12261.
-
Hajduk PJ, Olejniczak ET, Fesik SW. One-dimensional relaxation- and diffusion-edited NMR methods for screening compounds that bind to macromolecules. J Am Chem Soc (1997) 119:12257-12261.
-
J Am Chem Soc
-
-
Hajduk, P.J.1
Olejniczak, E.T.2
Fesik, S.W.3
-
24
-
-
0000265755
-
Otting G. Detection of protein-ligand NOEs with small, weakly binding ligands by combined relaxation and diffusion filtering
-
1997 9:441-444.
-
Ponstingl H, Otting G. Detection of protein-ligand NOEs with small, weakly binding ligands by combined relaxation and diffusion filtering. JBiomolNMR (1997) 9:441-444.
-
JBiomolNMR
-
-
Ponstingl, H.1
-
25
-
-
0030997805
-
Probing protein structure by solvent perturbation of NMR spectra: The surface accessibility of bovine pancreatic trypsin inhibitor
-
1997 73:382-396.
-
Molinari H, Esposito G, Ragona L, Pegna M, Niccolai N, Brunne RM, task AM, Zetta L. Probing protein structure by solvent perturbation of NMR spectra: the surface accessibility of bovine pancreatic trypsin inhibitor. Biophys J (1997) 73:382-396.
-
Biophys J
-
-
Molinari, H.1
Esposito, G.2
Ragona, L.3
Pegna, M.4
Niccolai, N.5
Brunne, R.M.6
Task, A.M.7
Zetta, L.8
-
26
-
-
0033136831
-
Use of organic solvents and small molecules for locating binding sites on proteins in solution
-
1999 in press.
-
Dalvit C, Roersheim P, Zurini M, Widmer A. Use of organic solvents and small molecules for locating binding sites on proteins in solution. JBiomolNMR (1999) in press.
-
JBiomolNMR
-
-
Dalvit, C.1
Roersheim, P.2
Zurini, M.3
Widmer, A.4
-
27
-
-
0029868304
-
Ringe D. Locating and characterizing binding sites on proteins
-
1996 14:595-599.
-
Mattos C, Ringe D. Locating and characterizing binding sites on proteins. Nat Biotechnol (1996) 14:595-599.
-
Nat Biotechnol
-
-
Mattos, C.1
-
28
-
-
0030917461
-
Screening mixtures for biological activity by NMR
-
1997 246:705709.
-
Meyer B, Weimar T, Peters T. Screening mixtures for biological activity by NMR. Eur J Biochem (1997) 246:705709.
-
Eur J Biochem
-
-
Meyer, B.1
Weimar, T.2
Peters, T.3
-
29
-
-
0032494393
-
Shapiro MJ. NOE pumping: A novel NMR technique for identification of compounds with binding affinity to macromolecules
-
•• The NOE pumping experiment only detects binding ligand signals transferred from target macromolecules by NOE without regard to size of the macromolecule. Because the ligand signals observed are transferred from the macromolecule target, this method should not be subject to false positives.
-
Chen A, Shapiro MJ. NOE pumping: A novel NMR technique for identification of compounds with binding affinity to macromolecules. JAm Chem Soc (1998) 120:10258-10259. •• The NOE pumping experiment only detects binding ligand signals transferred from target macromolecules by NOE without regard to size of the macromolecule. Because the ligand signals observed are transferred from the macromolecule target, this method should not be subject to false positives.
-
JAm Chem Soc (1998) 120:10258-10259.
-
-
Chen, A.1
-
31
-
-
33746028060
-
-
1999. http-J/www.enc-conference.org
-
Fesik S. Impact of the Cryoprobe on drug discovery. 4Cf Experimental NMR Conference, Orlando, Florida, USA, 28 February - 5 March, 1999. http-J/www.enc-conference.org
-
Impact of the Cryoprobe on Drug Discovery. 4Cf Experimental NMR Conference, Orlando, Florida, USA, 28 February - 5 March
-
-
Fesik, S.1
-
32
-
-
0031989836
-
High-resolution microcoil NMR for analysis of mass-limited, nanoliter samples
-
1998 70:645-650.
-
Oison DL, Lacey ME, Sweedler JV. High-resolution microcoil NMR for analysis of mass-limited, nanoliter samples. Anal Chem (1998) 70:645-650.
-
Anal Chem
-
-
Oison, D.L.1
Lacey, M.E.2
Sweedler, J.V.3
|