Gene interactions and pathways from curated databases and text-mining

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ATP5O — HSPE1

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Terlesky et al., Biochemistry 1991 : The E. coli chaperonin 60 ATPase activity was inhibited by chaperonin 10 from both R. sphaeroides and E. coli
Bonshtien et al., Cell Stress Chaperones 2009 : In contrast, ATPase of beta ( 14 ) ch-cpn60 was inhibited only by mitochondrial cpn10 , supporting previous reports showing that beta ( 14 ) is functional only with mitochondrial cpn10 and not with other cpn10 homologs
Rospert et al., Proc Natl Acad Sci U S A 1993 : Although the potassium dependent ATPase activity of E. coli cpn60 can be inhibited by cpn10 from either E. coli or yeast, neither of these cpn10s inhibits the ATPase activity of yeast cpn60
Cejka et al., J Struct Biol 1993 : This antibody, previously shown to affect the ability of chaperonin 10 (cpn10) to inhibit the ATPase activity of cpn60, is attached at the ends of the cpn60 and links the molecules into long chains
Dubaquié et al., Proc Natl Acad Sci U S A 1997 : Hsp10 inhibits the ATPase activity of hsp60 by about 40 % ... However, this decrease in affinity does not correlate with the functional defect, because hsp10 ( P36H ) fully assists the GroEL mediated refolding of malate dehydrogenase at 30 degrees C. Refolding activity, rather, correlates with the ability of hsp10 ( P36H ) to inhibit the ATPase of GroEL but not that of hsp60