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Interdomain interactions

Yano, M., Okuda, S., Oda, T., Tokuhisa, T., Tateishi, H., Mochizuki, M., Noma, T., Doi, M., Kobayashi, S., Yamamoto, T., Ikeda, Y., Ohkusa, T., Ikemoto, N., and Matsuzaki, M. (2005) Correction of defective interdomain interaction within ryanodine receptor by antioxidant is a new therapeutic strategy against heart failure. Circulation 112, 3633-3643. [Pg.1130]

Davio, S.R., K.M. Kienle, and B.E. Collins. 1995. Interdomain interactions in the chimeric protein toxin sCD4(178)-PE40 a differential scanning calorimetry (DSC) study. Pharm Res 12 642-648. [Pg.374]

Ryu, K. S. et al. Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a. J Biol Chem 2003, 278, 36621-7. [Pg.243]

The reactive domains are cleaved from the precursor at a highly conserved repeat domain with the sequence EEKKN. Identification of small quantities of peptides with extended or shortened termini has been taken as an indicator for the involvement of unspecific proteases in the cleavage of the precursor. Structural studies of a Cl-Tl construct derived from the precursor protein using NMR indicate that the domains within the precursor fold independently from each other and that no interdomain interactions are detectable on long-term scale. ... [Pg.274]

The thermodynamic stability of hemopexin has been examined using DSC (Fig. 13), which showed apo-hemopexin to be a stable protein with a single Tm of 54°C (AH 185 kcal/mol), which increases to 66.5°C (AH 290 kcal/mol) upon binding heme (130). The N-domain of hemopexin is less stable (Tm 52°C, AH 95 kcal/mol) but is even more strikingly stabilized by ferri-heme (T 78°C, AH 370 kcal/mol). The presence of C-domain (Tii 49.5°C, AH 140 kcal/mol) slightly destabilizes heme-N-domain (Tm 75°C, AH 320 kcal/mol) (130), showing another effect of interdomain interactions that may act in heme release. [Pg.227]

Dimitrova, M.N. Szczepanowski, R.H. Ruvinov, S.B. Peterkofsky, A. Gins-burg. A. Interdomain Interaction and Substrate Coupling Effects on Di-... [Pg.421]

Weston M. C., Gertler C., Mayer M. L., and Rosenmund C. (2006). Interdomain interactions in AMPA and kainate receptors regulate affinity for glutamate. J. Neurosci. 26 7650-7658. [Pg.50]

S2246L N4104K R4497C FRET in CHO/HL1 cells N/A N/A N/A abnormal interdomain interactions t (w/ caffeine) (George 2006)... [Pg.300]

Future studies will hopefully enlighten our understanding of the extent to which similar alterations in RyR structure and function, such as altered interdomain interactions, phosphorylation, modulator binding, and redox modifications, occur in both RyRl and RyR2 and how such alterations lead to diseases of skeletal and cardiac muscle. [Pg.307]

Ikemoto, N., and Yamamoto, T. (2002). Regulation of Calcium Release by Interdomain Interaction within Ryanodine Receptors. Front Biosci 7 d671—83. [Pg.312]

The relative activity of the fragmentary enzyme to the wild-type enzyme was much higher than that of the clipped to the native DadB enzyme. This was explained by the assumption that the thermostable enzyme has more extensive hydrophobic interdomain interactions than the DadB enzyme with less thermostability.12 The importance of hydrophobic interdomain interactions for catalysis was pointed out by studies on lactate dehydrogenase.23,24 ... [Pg.154]

This result is equivalent to the renormalized perturbation theory of ref. 53, which these authors found to be at least qualitatively valid for ID and 2D lattices. Thus, at the scale of our n-domains, we may forget about interdomain interactions Bn and take a localized hamiltonian ... [Pg.184]

Feng C (2012) Mechanism of nitric oxide synthase regulation electron transfer and interdomain interactions. Coord Chem Rev 256 393-411... [Pg.60]

Studies of the hybrid and chimeric molecules of CAD domains and other complex proteins make it possible to draw a few general principles about the interdomain interactions. [Pg.266]

There are many conserved aminoacyl residues in domains II and III. The function of most of these residues is not yet known. ArginineSOO [54] of domain II apparently plays an important role in stabilization of interdomain interactions and threonine394 was suggested as a phosphorylation site regulating aminoacyl-tRNA binding to EF-Tu GTP [55]. The amino acid residues on the interface between the domains I and II are often conserved and are important targets for binding antibiotics. [Pg.386]

The He increases with the shrink of particle size because of the enhancement of interdomain interaction. [Pg.383]


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See also in sourсe #XX -- [ Pg.97 , Pg.98 , Pg.119 , Pg.455 , Pg.467 , Pg.505 , Pg.514 ]




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