Published in Biochim Biophys Acta on July 29, 1983
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A transmembrane form of the prion protein contains an uncleaved signal peptide and is retained in the endoplasmic Reticulum. Mol Biol Cell (2001) 1.23
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Nucleotide-binding properties of native and cold-treated mitochondrial ATPase. Biochim Biophys Acta (1975) 1.08
The N-terminal domain of a glycolipid-anchored prion protein is essential for its endocytosis via clathrin-coated pits. J Biol Chem (1995) 1.08
Tightly bound nucleotides of the energy-transducing ATPase of chloroplasts and their role in photophosphorylation. Biochim Biophys Acta (1975) 1.07
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Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform. Proc Natl Acad Sci U S A (1996) 1.01
Specificity of nucleotide binding and coupled reactions utilising the mitochondrial ATPase. Biochim Biophys Acta (1978) 1.01
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Probing interactions of the Escherichia coli F0F1 ATP synthase beta and gamma subunits with disulphide cross-links. Biochem Soc Trans (1995) 1.00
Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site. Proc Natl Acad Sci U S A (1987) 1.00
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Identification of intermediate steps in the conversion of a mutant prion protein to a scrapie-like form in cultured cells. J Biol Chem (1997) 0.98
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Short-time low-temperature pasteurisation of human milk. Early Hum Dev (1982) 0.95
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Control of mitochondrial ATP synthase in heart cells: inactive to active transitions caused by beating or positive inotropic agents. Cardiovasc Res (1990) 0.95
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Clotting factors and hepatitis A. Lancet (1992) 0.93
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