Short CommunicationEukaryotic Expression Vectors That Replicate to Low Copy Number in Bacteria: Transient Expression of the Menkes Protein☆
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Cited by (15)
Analysis of golgi complex function using correlative light-electron microscopy
2013, Methods in Cell BiologyCitation Excerpt :Although ATP7A intracellular localization has an important role in the aforementioned processes, it remains poorly understood at the ultrastructural level due to the lack of an antibody that is suitable for immuno-EM. On the other hand, large size (1465 residues) and complex structure (8 transmembrane domains) allow the cloning of the ATP7A gene only in vectors with low expression efficiency (La Fontaine, Firth, Lockhart, Paynter, & Mercer, 1998). Therefore, the GFP-tagged ATP7A can only be seen in very few cells.
ATP7B mediates vesicular sequestration of copper: Insight into biliary copper excretion
2006, GastroenterologyA single PDZ domain protein interacts with the menkes copper ATPase, ATP7A: A new protein implicated in copper homeostasis
2005, Journal of Biological ChemistryCitation Excerpt :Cultures were incubated at 37 °C in a 5% CO2 humidified incubator. Cloning and Mutagenesis—To generate a bait construct encoding the C terminus of ATP7A, a 312-bp fragment encoding 97 amino acids of the ATP7A C terminus, from the end of transmembrane domain 8 to the stop codon (amino acids 1404-1500), was amplified by PCR using oligonucleotides Y2H7 (5′-ccccatatgTCTCTCTTCCTTAAACTTTAC-3′) and Y2H8 (5′-cccgtcgacTTATAATGCAGTGTCATCATC-3′) (NdeI and SalI restriction sites in lowercase, boldface type) and pCMB19 containing the ATP7A cDNA (35) as a template. This fragment was ligated into the NdeI/SalI sites of the vector pAS2-1 (Clontech) in frame with the GAL4 DNA binding domain (DNA-BD) to generate plasmid pSLB29.
Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein
2003, Journal of Biological ChemistryCitation Excerpt :The detection of peroxidase activity was carried out using the chemiluminescent peroxidase substrate (Roche Molecular Biochemicals). All the protocols were performed essentially as described previously (35). Atox1 Peptide Synthesis—For solid phase synthesis of the 69 amino acids containing Atox1, we employed the Fmoc (N-(9-fluorenyl)methoxycarbonyl) strategy (36, 37) in a fully automated synthesizer (Applied Biosystems 433).
The role of GMXCXXC metal binding sites in the copper-induced redistribution of the menkes protein
1999, Journal of Biological ChemistryCorrection of the copper transport defect of Menkes patient fibroblasts by expression of the menkes and Wilson ATPases
1998, Journal of Biological Chemistry
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C. R. ScriverA. L. BeaudetW. M. SlyD. Valle
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