Interference No. 104,761 PaperII08
Univ. of New Mexico v. Fordham Univ. Page 3
Welch et al., "Rapid Purification of Mammalian 70,000-Dalton Stress
Proteins: Affinity of the Proteins for Nucleotides", 5 Mol. & Cell. Biol. 1229
(1985) [2033]
Lewis et al., " Involvement of ATP in the nuclear and nucleolar functions
of the 70 kd heat shock protein", 4 EMBO J. 3137 (1985) [2035]
Bochner et al., "Escherichia coli DnaK protein possesses a
5'-nucleotidase activity that is inhibited by AppppA", 168 J. Bacteriol. 931
(1986) [2036]
Kassenbrock et al., "Interaction of heavy chain binding protein
(BiP/GRP78) with adenine nucleotides" 8 EMBO J. 1461 (1989) [2037]
Skowyra et al., "The E. coli dnaK gene product, the hsp70 homolog, can
reactivate heat-inactivated RNA polymerase in an ATP hydrolysis
dependent manner", 62 Cell 939 (1990) [2038]
Sadis et al., "Biochemical and biophysical comparison of bacterial DnaK
and mammalian hsc73, two members of an ancient stress protein family',
Curr. Res. in Prot. Chem. 339 (1990) [2039]
Flaherty et al., "Three-dimensional structure of the ATPase fragment of a
70K heat-shock cognate protein ", 346 Nature 623 (1990) [2040]
Sherman et al., "Formation in vtro of complexes between an abnormal
fusion protein and heat shock proteins from Escherichia coli and yeast
mitochondria", 173 J. Bacteriol. 7249 (1991) [2041]
Sadis et al., "Unfolded proteins stimulate molecular chaperone hsc70
ATPase by accelerating ADP/ATP exchange" 31 Biochem. 9406 (1992)
[2042]
Richarme et al., "Specificity of the Escherichia coli chaperon DnaK (70
kDa heat shock protein) for hydrophobic amino acids", 268 J. Biol. Chem.
24074 (1993) [2043]
Blond-EIguindi et al., "Peptide-dependent stimulation of the ATPase
activity of the molecular chaperone BiP is the result of conversion of
oligomers to active monomers", 268 J. Biol. Chem. 12730 (1993) [2044]
[3] UNM also relied on the Welch declaration [2028], which cited the same papers.
[4] The decision on motions concluded:
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