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785 related items for PubMed ID: 11945039
1. Complete relaxation and conformational exchange matrix (CORCEMA) analysis of intermolecular saturation transfer effects in reversibly forming ligand-receptor complexes. Jayalakshmi V, Krishna NR. J Magn Reson; 2002 Mar; 155(1):106-18. PubMed ID: 11945039 [Abstract] [Full Text] [Related]
3. CORCEMA refinement of the bound ligand conformation within the protein binding pocket in reversibly forming weak complexes using STD-NMR intensities. Jayalakshmi V, Rama Krishna N. J Magn Reson; 2004 May; 168(1):36-45. PubMed ID: 15082247 [Abstract] [Full Text] [Related]
4. Refinement of the conformation of UDP-galactose bound to galactosyltransferase using the STD NMR intensity-restrained CORCEMA optimization. Jayalakshmi V, Biet T, Peters T, Krishna NR. J Am Chem Soc; 2004 Jul 21; 126(28):8610-1. PubMed ID: 15250687 [Abstract] [Full Text] [Related]
5. A combined STD-NMR/molecular modeling protocol for predicting the binding modes of the glycosidase inhibitors kifunensine and salacinol to Golgi alpha-mannosidase II. Wen X, Yuan Y, Kuntz DA, Rose DR, Pinto BM. Biochemistry; 2005 May 10; 44(18):6729-37. PubMed ID: 15865418 [Abstract] [Full Text] [Related]
6. Quantitative Analysis of STD-NMR Spectra of Reversibly Forming Ligand-Receptor Complexes. Krishna NR, Jayalakshmi V. Top Curr Chem; 2008 May 10; 273():15-54. PubMed ID: 23605458 [Abstract] [Full Text] [Related]
12. Transient NOE-exchange-relay experiment: application to ligand-protein binding under slow exchange conditions. Podkorytov IS, Skrynnikov NR. J Magn Reson; 2007 Jul 10; 187(1):44-51. PubMed ID: 17449307 [Abstract] [Full Text] [Related]
13. Theoretical analysis of the inter-ligand overhauser effect: a new approach for mapping structural relationships of macromolecular ligands. London RE. J Magn Reson; 1999 Dec 10; 141(2):301-11. PubMed ID: 10579953 [Abstract] [Full Text] [Related]
14. Investigation of ligand binding and protein dynamics in Bacillus subtilis chorismate mutase by transverse relaxation optimized spectroscopy-nuclear magnetic resonance. Eletsky A, Kienhöfer A, Hilvert D, Pervushin K. Biochemistry; 2005 May 10; 44(18):6788-99. PubMed ID: 15865424 [Abstract] [Full Text] [Related]
15. Quantitative determination of conformational, dynamic, and kinetic parameters of a ligand-protein/DNA complex from a complete relaxation and conformational exchange matrix analysis of intermolecular transferred NOESY. Moseley HN, Lee W, Arrowsmith CH, Krishna NR. Biochemistry; 1997 May 06; 36(18):5293-9. PubMed ID: 9154911 [Abstract] [Full Text] [Related]
16. SOS-NMR: a saturation transfer NMR-based method for determining the structures of protein-ligand complexes. Hajduk PJ, Mack JC, Olejniczak ET, Park C, Dandliker PJ, Beutel BA. J Am Chem Soc; 2004 Mar 03; 126(8):2390-8. PubMed ID: 14982445 [Abstract] [Full Text] [Related]
17. Complete relaxation and conformational exchange matrix (CORCEMA) analysis of NOESY spectra of interacting systems; two-dimensional transferred NOESY. Moseley HN, Curto EV, Krishna NR. J Magn Reson B; 1995 Sep 03; 108(3):243-61. PubMed ID: 7670757 [Abstract] [Full Text] [Related]
18. Group epitope mapping considering relaxation of the ligand (GEM-CRL): including longitudinal relaxation rates in the analysis of saturation transfer difference (STD) experiments. Kemper S, Patel MK, Errey JC, Davis BG, Jones JA, Claridge TD. J Magn Reson; 2010 Mar 03; 203(1):1-10. PubMed ID: 20022272 [Abstract] [Full Text] [Related]