Protection of GroEL by its methionine residues against oxidation by hydrogen peroxide.

Methionine sulphoxide reductases protect iron-sulphur clusters from oxidative inactivation in yeast. Microbiology (2009) 0.81

Identification of crucial amino acids of bacterial Peptide deformylases affecting enzymatic activity in response to oxidative stress. J Bacteriol (2013) 0.75

Human fibronectin and MMP-2 collagen binding domains compete for collagen binding sites and modify cellular activation of MMP-2. Matrix Biol (2002) 0.97

Crosslinking of fibrinogen and fibronectin by free radicals: a possible initial step in adhesion formation in osteoarthritis of the temporomandibular joint. J Oral Maxillofac Surg (2003) 0.93

Amphipols stabilize the Chlamydia major outer membrane protein and enhance its protective ability as a vaccine. Vaccine (2011) 0.91

Advanced glycation of type I collagen and fibronectin modifies periodontal cell behavior. J Periodontol (2008) 0.90

Free radical damage in facsimile synovium: correlation with adhesion formation in osteoarthritic TMJs. J Prosthodont (2006) 0.82

Local blockade of integrins in the temporomandibular joint region reduces Fos-positive neurons in trigeminal subnucleus caudalis of female rats produced by jaw movement. Pain (2006) 0.79

Divalent cations stabilize GroEL under conditions of oxidative stress. Biochem Biophys Res Commun (2008) 0.78

Oxidized GroEL can function as a chaperonin. Front Biosci (2004) 0.77

Inhibition of CD95-mediated apoptosis through beta 1 integrin in the HSG epithelial cell line. Cell Commun Adhes (2006) 0.77

On the chaperonin activity of GroEL at heat-shock temperature. Int J Biochem Cell Biol (2005) 0.76

GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation. Biochem Biophys Res Commun (2002) 0.76

Hydrogen peroxide induces the dissociation of GroEL into monomers that can facilitate the reactivation of oxidatively inactivated rhodanese. Int J Biochem Cell Biol (2004) 0.76

GTP binds to α-crystallin and causes a significant conformational change. Int J Biol Macromol (2012) 0.75

The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure. Biometals (2003) 0.75

Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures. Biosci Rep (2012) 0.75