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Interaction of a G-protein β-subunit with a conserved sequence in Ste20/PAK family protein kinases
Serine/threonine protein kinases of the Ste20/PAK family have been implicated in the signalling from heterotrimeric G proteins to mitogen-activated protein (MAP) kinase cascades,. In the yeastExpand
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The Structure of calnexin, an ER chaperone involved in quality control of protein folding.
The three-dimensional structure of the lumenal domain of the lectin-like chaperone calnexin determined to 2.9 A resolution reveals an extended 140 A arm inserted into a beta sandwich structureExpand
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Crystal structure of the bb' domains of the protein disulfide isomerase ERp57.
The synthesis of proteins in the endoplasmic reticulum (ER) is limited by the rate of correct disulfide bond formation. This process is carried out by protein disulfide isomerases, a family of ERExpand
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The alpha/beta hydrolase fold.
We have identified a new protein fold--the alpha/beta hydrolase fold--that is common to several hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of eachExpand
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Insights into interfacial activation from an open structure of Candida rugosa lipase.
The structure of the Candida rugosa lipase determined at 2.06-A resolution reveals a conformation with a solvent-accessible active site. Comparison with the crystal structure of the homologous lipaseExpand
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Relationship between sequence conservation and three‐dimensional structure in a large family of esterases, lipases, and related proteins
Based on the recently determined X‐ray structures of Torpedo californica acetylcholinesterase and Geotrichum candidum lipase and on their three‐dimensional superposition, an improved alignment of aExpand
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Two conformational states of Candida rugosa lipase
The structure of Candida rugosa lipase in a new crystal form has been determined and refined at 2.1 Å resolution. The lipase molecule was found in an inactive conformation, with the active siteExpand
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Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism.
2-Amino-3-ketobutyrate CoA ligase (KBL, EC 2.3.1.29) is a pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the second reaction step on the main metabolic degradation pathway for threonine.Expand
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Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72.
Protein disulfide isomerases are a family of proteins that catalyze the oxidation and isomerization of disulfide bonds in newly synthesized proteins in the endoplasmic reticulum. The family includesExpand
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Lipases and alpha/beta hydrolase fold.
Publisher Summary The three-dimensional structures of more than 20 representatives of the α/β hydrolase fold are now known and many more members have been identified by sequence and secondaryExpand
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