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Sensitivity of secondary structure propensities to sequence differences between α‐ and γ‐synuclein: Implications for fibrillation
The synucleins are a family of intrinsically disordered proteins involved in various human diseases. α‐Synuclein has been extensively characterized due to its role in Parkinson's disease where itExpand
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Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation.
The synucleins are a family of intrinsically disordered proteins involved in various human diseases. alpha-Synuclein has been extensively characterized due to its role in Parkinson's disease where itExpand
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Crystal structure of calpain reveals the structural basis for Ca2+‐dependent protease activity and a novel mode of enzyme activation
The combination of thiol protease activity and calmodulin‐like EF‐hands is a feature unique to the calpains. The regulatory mechanisms governing calpain activity are complex, and the nature of theExpand
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Antifreeze proteins: an unusual receptor-ligand interaction.
  • Z. Jia, P. Davies
  • Chemistry, Medicine
  • Trends in biochemical sciences
  • 1 February 2002
Antifreeze proteins (AFPs) help organisms to survive below 0 degrees C by inhibiting ice growth. Although AFPs are structurally diverse, they typically present a large proportion of their surfaceExpand
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Crystal structures of Escherichia coli phytase and its complex with phytate
Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets. Escherichia coli phytase, a member of the histidine acid phosphatase family has theExpand
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A Ca2+ Switch Aligns the Active Site of Calpain
Ca(2+) signaling by calpains leads to controlled proteolysis during processes ranging from cytoskeleton remodeling in mammals to sex determination in nematodes. Deregulated Ca(2+) levels result inExpand
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Mimicry of ice structure by surface hydroxyls and water of a β-helix antifreeze protein
Insect antifreeze proteins (AFP) are much more effective than fish AFPs at depressing solution freezing points by ice-growth inhibition. AFP from the beetle Tenebrio molitor is a small protein (8.4Expand
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Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats.
Heme oxygenases (HOs) catalyze the oxidation of heme to biliverdin, carbon monoxide (CO), and free iron. Iron acquisition is critical for invading microorganisms to enable survival and growth. HereExpand
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β-Helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
Insect antifreeze proteins (AFP) are considerably more active at inhibiting ice crystal growth than AFP from fish or plants. Several insect AFPs, also known as thermal hysteresis proteins, have beenExpand
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Novel structure of the conserved gram-negative lipopolysaccharide transport protein A and mutagenesis analysis.
Lipopolysaccharide (LPS) transport protein A (LptA) is an essential periplasmic localized transport protein that has been implicated together with MsbA, LptB, and the Imp/RlpB complex in LPSExpand
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