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Journal Abstract Search
631 related items for PubMed ID: 18164033
1. Crystal structure of the GluR0 ligand-binding core from Nostoc punctiforme in complex with L-glutamate: structural dissection of the ligand interaction and subunit interface. Lee JH, Kang GB, Lim HH, Jin KS, Kim SH, Ree M, Park CS, Kim SJ, Eom SH. J Mol Biol; 2008 Feb 15; 376(2):308-16. PubMed ID: 18164033 [Abstract] [Full Text] [Related]
8. On the binding determinants of the glutamate agonist with the glutamate receptor ligand binding domain. Speranskiy K, Kurnikova M. Biochemistry; 2005 Aug 30; 44(34):11508-17. PubMed ID: 16114887 [Abstract] [Full Text] [Related]
10. Crystal structure of the second PDZ domain of SAP97 in complex with a GluR-A C-terminal peptide. von Ossowski I, Oksanen E, von Ossowski L, Cai C, Sundberg M, Goldman A, Keinänen K. FEBS J; 2006 Nov 30; 273(22):5219-29. PubMed ID: 17069616 [Abstract] [Full Text] [Related]
11. Crystal structure of the kainate receptor GluR5 ligand-binding core in complex with (S)-glutamate. Naur P, Vestergaard B, Skov LK, Egebjerg J, Gajhede M, Kastrup JS. FEBS Lett; 2005 Feb 14; 579(5):1154-60. PubMed ID: 15710405 [Abstract] [Full Text] [Related]
15. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Brejc K, van Dijk WJ, Klaassen RV, Schuurmans M, van Der Oost J, Smit AB, Sixma TK. Nature; 2001 May 17; 411(6835):269-76. PubMed ID: 11357122 [Abstract] [Full Text] [Related]
16. Molecular interaction between the Strep-tag affinity peptide and its cognate target, streptavidin. Schmidt TG, Koepke J, Frank R, Skerra A. J Mol Biol; 1996 Feb 09; 255(5):753-66. PubMed ID: 8636976 [Abstract] [Full Text] [Related]
17. Compromise and accommodation in ecotin, a dimeric macromolecular inhibitor of serine proteases. Gillmor SA, Takeuchi T, Yang SQ, Craik CS, Fletterick RJ. J Mol Biol; 2000 Jun 16; 299(4):993-1003. PubMed ID: 10843853 [Abstract] [Full Text] [Related]
19. Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis. Vévodová J, Graham RM, Raux E, Schubert HL, Roper DI, Brindley AA, Ian Scott A, Roessner CA, Stamford NP, Elizabeth Stroupe M, Getzoff ED, Warren MJ, Wilson KS. J Mol Biol; 2004 Nov 19; 344(2):419-33. PubMed ID: 15522295 [Abstract] [Full Text] [Related]