Year |
Citation |
Score |
2008 |
Li C, Rydberg E, Williams L, Zhang R, Begum A, Withers S, Brayer D. Mechanistic role of the catalytic residue D300 in human pancreatic alpha-amylase Acta Crystallographica Section a Foundations of Crystallography. 64: C263-C263. DOI: 10.1107/S0108767308091563 |
0.533 |
|
2006 |
Rydberg EH, Brumshtein B, Greenblatt HM, Wong DM, Shaya D, Williams LD, Carlier PR, Pang YP, Silman I, Sussman JL. Complexes of alkylene-linked tacrine dimers with Torpedo californica acetylcholinesterase: Binding of Bis5-tacrine produces a dramatic rearrangement in the active-site gorge. Journal of Medicinal Chemistry. 49: 5491-500. PMID 16942022 DOI: 10.1021/Jm060164B |
0.318 |
|
2003 |
Zeev-Ben-Mordehai T, Rydberg EH, Solomon A, Toker L, Auld VJ, Silman I, Botti S, Sussman JL. The intracellular domain of the Drosophila cholinesterase-like neural adhesion protein, gliotactin, is natively unfolded. Proteins. 53: 758-67. PMID 14579366 DOI: 10.1002/Prot.10471 |
0.341 |
|
2002 |
Rydberg EH, Li C, Maurus R, Overall CM, Brayer GD, Withers SG. Mechanistic analyses of catalysis in human pancreatic alpha-amylase: detailed kinetic and structural studies of mutants of three conserved carboxylic acids. Biochemistry. 41: 4492-502. PMID 11914097 DOI: 10.1021/Bi011821Z |
0.601 |
|
2000 |
Brayer GD, Sidhu G, Maurus R, Rydberg EH, Braun C, Wang Y, Nguyen NT, Overall CM, Withers SG. Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques. Biochemistry. 39: 4778-91. PMID 10769135 DOI: 10.1021/Bi9921182 |
0.568 |
|
1999 |
Rydberg EH, Sidhu G, Vo HC, Hewitt J, Côte HC, Wang Y, Numao S, MacGillivray RT, Overall CM, Brayer GD, Withers SG. Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris. Protein Science : a Publication of the Protein Society. 8: 635-43. PMID 10091666 DOI: 10.1110/Ps.8.3.635 |
0.4 |
|
1997 |
Rydberg EH, Overall CM, Withers SG. Mechanistic studies of human pancreatic o-amylase Faseb Journal. 11: A1311. |
0.426 |
|
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