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Development of biorational pest control formulation against longicorn beetles using a fungus, Beauveria brongniartii (Sacc.) Petch
Abstract Some basic experiments were performed in order to develop a biocidal formulation which is lethal to certain species of longicorn beetle. The entomopathogenic filamentous fungus, BeauveriaExpand
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Purification and cloning of a thermostable manganese catalase from a thermophilic bacterium.
We have purified a heat-stable catalase from a thermophilic bacterium, Thermus species strain YS 8-13. The enzyme was purified 160-fold from crude cellular extracts and possessed a specific activityExpand
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Hydrophilic Residues 526KNDAAD531 in the Flexible C-terminal Region of the Chaperonin GroEL Are Critical for Substrate Protein Folding within the Central Cavity*
The final 23 residues in the C-terminal region of Escherichia coli GroEL are invisible in crystallographic analyses due to high flexibility. To probe the functional role of these residues in theExpand
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Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases.
Alpha-synuclein is one of the causative proteins of familial Parkinson disease, which is characterized by neuronal inclusions named Lewy bodies. Lewy bodies include not only alpha-synuclein but alsoExpand
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Stopped-flow Fluorescence Analysis of the Conformational Changes in the GroEL Apical Domain
GroEL undergoes numerous conformational alterations in the course of facilitating the folding of various proteins, and the specific movements of the GroEL apical domain are of particular importanceExpand
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Amyloid-like fibril formation of co-chaperonin GroES: nucleation and extension prefer different degrees of molecular compactness.
The molecular chaperone GroES, together with GroEL from Escherichia coli, is the best characterized protein of the molecular chaperone family. Here, we report on the in vitro formation of GroESExpand
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Purification and characterization of a thermostable class II fumarase from Thermus thermophilus.
A thermostable fumarase was purified from a strain of Thermus thermophilus isolated from a Japanese hot spring. The maximum specific activity of the purified enzyme was 1740 units/mg at pH 8.0 and 85Expand
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Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model.
The guanidine-hydrochloride (Gdn-HCl) induced unfolding and refolding characteristics of the co-chaperonin GroES from Escherichia coli, a homoheptamer of subunit molecular mass 10,000 Da, wereExpand
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Overproduction of Thermus sp. YS 8-13 manganese catalase in Escherichia coli production of soluble apoenzyme and in vitro formation of active holoenzyme.
Overproduction of Thermus sp. YS 8-13 manganese catalase in Escherichia coli BL21(DE3) was accomplished by introducing a derivative of pET-23a(+) containing a copy of the coding gene into theExpand
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Structural stability of covalently linked GroES heptamer: advantages in the formation of oligomeric structure.
In order to understand how inter-subunit association stabilizes oligomeric proteins, a single polypeptide chain variant of heptameric co-chaperonin GroES (tandem GroES) was constructed fromExpand
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