Zobrazeno 1 - 5
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pro vyhledávání: '"Wade C. McGregor"'
Autor:
Maria T. Diaz-Meco, B. Douglas White, Wade C. McGregor, Jorge Moscat, Jeganathan Ramesh Babu, Thangiah Geetha, Chen Zheng
Publikováno v:
Neurochemistry International. 61:1289-1293
Amyloid β (Aβ) aggregates are the primary component of senile plaques in Alzheimer disease (AD) patient's brain. Aβ is known to bind p75 neurotrophin receptor (p75(NTR)) and mediates Aβ-induced neuronal death. Recently, we showed that NGF leads t
Publikováno v:
SpringerPlus
The H355A, H355K, H80A, and H80K mutant enzymes of the argE-encoded N-acetyl-L-ornithine deacetylase (ArgE) from Escherichia coli were prepared, however, only the H355A enzyme was found to be soluble. Kinetic analysis of the Co(II)-loaded H355A exhib
Publikováno v:
Journal of inorganic biochemistry. 111
The Zn, Co, and Mn K-edge extended X-ray absorption fine structure (EXAFS) spectra of the N-acetyl-l-ornithine deacetylase (ArgE) from Escherichia coli, loaded with one or two equivalents of divalent metal ions (i.e., [Zn(II)_(ArgE)], [Zn(II)Zn(II)(A
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 12(5)
The catalytically competent Mn(II)-loaded form of the argE-encoded N-acetyl-L-ornithine deacetylase from Escherichia coli (ArgE) was characterized by kinetic, thermodynamic, and spectroscopic methods. Maximum N-acetyl-L-ornithine (NAO) hydrolytic act
Publikováno v:
Journal of the American Chemical Society. 127(40)
The catalytic and structural properties of the argE-encoded N-acetyl-L-ornithine deacetylase (ArgE) from Escherichia coli were investigated. On the basis of kinetic and ITC (isothermal titration calorimetry) data, Zn(II) binds to ArgE with Kd values