Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Chris W. Cody"'
Autor:
P. C. Huang, Chris W. Cody
Publikováno v:
Biochemical and Biophysical Research Communications. 202:954-959
Mammalian metallothioneins (MTs) possess eight highly conserved lysine residues, including three in each of two metal binding domains. We used site-directed mutagenesis to replace these intradomain lysines in Chinese hamster ovary MT2 with glutamic a
Publikováno v:
Biochemical and Biophysical Research Communications. 202:621-628
Lysine residues are highly conserved in mammalian metallothioneins (MTs). Recombinant mutant Chinese hamster MT2 in which all of the lysines (K) in the alpha-domain were substituted by glutamic acids (E) was assayed with, expressed in and purified fr
Autor:
Ethylin Wang Jabs, Carrie L. Hayes, William F. Greenlee, Yu Yuan P Wo, Hong Yin, Thomas R. Sutter, Xiang Li, Yong Ming Tang, Chris W. Cody
Publikováno v:
Journal of Biological Chemistry. 269:13092-13099
Previously, levels of a novel human mRNA, detected by a recombinant cDNA designated clone 1, were shown to be increased 50-fold in response to treatment of a keratinocyte cell line with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), in part as a functio
Autor:
Jonathan A. Gastel, Nigel J. Walker, Chris W. Cody, Hong Yin, Ying Li, Carrie L. Hayes, Thomas R. Sutter
Publikováno v:
Modulation of Cellular Responses in Toxicity ISBN: 9783642798740
During the past decade tremendous advances have been made in understanding the role of receptors as signal transducers, linking cells and their environment in a carefully orchestrated symphony of multicellular life. Through changes in gene expression
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dfe5d820a6e2af1e8d92ffbf75b1f4ec
https://doi.org/10.1007/978-3-642-79872-6_3
https://doi.org/10.1007/978-3-642-79872-6_3
Autor:
P. C. Huang, Chris W. Cody
Publikováno v:
Biochemistry. 32(19)
Mammalian metallothioneins (MTs) possess eight highly conserved lysine residues, two of which constitute the hinge between two metal binding domains. By site-directed mutagenesis and recombinant DNA techniques, we replaced the interdomain lysines in
Publikováno v:
Biochemistry. 32(5)
The green-fluorescent proteins (GFP) are a unique class of proteins involved in bioluminescence of many cnidaria. The GFPs serve as energy-transfer acceptors, receiving energy from either a luciferase-oxyluciferin complex or a Ca(2+)-activated photop
Publikováno v:
Photochemistry and Photobiology. 35:803-808
— In the jellyfish Aequorea, the green-fluorescent protein (GFP) functions as the in vivo bio-luminescence emitter via energy transfer from the photoprotein aequorin. Accumulated evidence has indicated that the Aequorea GFP is a relatively inflexib
Publikováno v:
Photochemistry and Photobiology. 31:611-615
— Spectral properties of guanidine-denaturated and pronase-digested green-fluorescent proteins (GFP) from two species of bioluminescent coelenterates have been investigated. Spectrophotometric titrations of Renilla and Aequorea GFP, following denat