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180 related items for PubMed ID: 19053245
1. Relative tolerance of an enzymatic molten globule and its thermostable counterpart to point mutation. Woycechowsky KJ, Choutko A, Vamvaca K, Hilvert D. Biochemistry; 2008 Dec 23; 47(51):13489-96. PubMed ID: 19053245 [Abstract] [Full Text] [Related]
2. Effects of point mutation on enzymatic activity: correlation between protein electronic structure and motion in chorismate mutase reaction. Ishida T. J Am Chem Soc; 2010 May 26; 132(20):7104-18. PubMed ID: 20426479 [Abstract] [Full Text] [Related]
3. Relative tolerance of mesostable and thermostable protein homologs to extensive mutation. Besenmatter W, Kast P, Hilvert D. Proteins; 2007 Feb 01; 66(2):500-6. PubMed ID: 17096428 [Abstract] [Full Text] [Related]
4. Exhaustive mutagenesis of six secondary active-site residues in Escherichia coli chorismate mutase shows the importance of hydrophobic side chains and a helix N-capping position for stability and catalysis. Lassila JK, Keeffe JR, Kast P, Mayo SL. Biochemistry; 2007 Jun 12; 46(23):6883-91. PubMed ID: 17506527 [Abstract] [Full Text] [Related]
5. Kinetics and thermodynamics of ligand binding to a molten globular enzyme and its native counterpart. Vamvaca K, Jelesarov I, Hilvert D. J Mol Biol; 2008 Oct 17; 382(4):971-7. PubMed ID: 18680748 [Abstract] [Full Text] [Related]
6. Structure and dynamics of a molten globular enzyme. Pervushin K, Vamvaca K, Vögeli B, Hilvert D. Nat Struct Mol Biol; 2007 Dec 17; 14(12):1202-6. PubMed ID: 17994104 [Abstract] [Full Text] [Related]
7. Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity. Lassila JK, Keeffe JR, Oelschlaeger P, Mayo SL. Protein Eng Des Sel; 2005 Apr 17; 18(4):161-3. PubMed ID: 15820980 [Abstract] [Full Text] [Related]
13. Predicting the effect of a point mutation on a protein fold: the villin and advillin headpieces and their Pro62Ala mutants. Piana S, Laio A, Marinelli F, Van Troys M, Bourry D, Ampe C, Martins JC. J Mol Biol; 2008 Jan 11; 375(2):460-70. PubMed ID: 18022635 [Abstract] [Full Text] [Related]