Gene interactions and pathways from curated databases and text-mining

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CALM1 — HSP90AA1

Pathways - manually collected, often from reviews:

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

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Someren et al., Biochem Biophys Res Commun 1999 : HSP-90 ( 75 or 100 nM ) significantly increased calcineurin V ( max ) in the presence of calmodulin , while maximal stimulation by HSP-70 occurred at 50 nM
Whittier et al., J Biol Chem 2004 : Hsp90 enhances degradation of oxidized calmodulin by the 20 S proteasome ... To elucidate the role of Hsp90 in promoting the degradation of oxidized calmodulin ( CaM ( ox ) ), we have purified red blood cell 20 S proteasomes free of Hsp90 and assessed their ability to degrade CaM ( ox ) in the absence or presence of Hsp90
Okano et al., J Cardiovasc Pharmacol 2006 (Body Weight) : Tyrosine phosphorylation of eNOS and expression of calmodulin increased, but Hsp90 decreased with all treatments and only raloxifene treatment increased caveolin-1 compared with OVX
Edlich et al., J Biol Chem 2007 : The Bcl-2 regulator FKBP38-calmodulin-Ca2+ is inhibited by Hsp90
Peng et al., Biochemistry 2009 : NO production by neuronal nitric oxide synthase (nNOS) requires calmodulin and is enhanced by the chaperone Hsp90 , which cycles dynamically with the enzyme
Nishida et al., J Biol Chem 1986 : Here we show that calmodulin regulates the binding of HSP90 to F-actin in a Ca2+ dependent manner ... Ca2+ dependent interaction of HSP90 with calmodulin as well as calmodulin regulated binding of HSP90 to F-actin revealed here may provide new insight into the function of HSP90 and the regulation of actin structure in cells