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Chemical Compound Review

Guanidium chloride     guanidine hydrochloride

Synonyms: eONIEaNI, NIEaeO, qKxPSDQBBsP@, ARONIS27077, ACMC-1AZ7T, ...
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Disease relevance of guanidine

 

Psychiatry related information on guanidine

  • When SBP is subjected to thermal unfolding at high GdnHCl concentrations (5.8-6.9 M), cooperative behavior is observed, which allowed the analysis by the two-state model to determine their thermodynamic parameters [6].
  • PrP also dissociated from aggregates of protease-resistant PrP generated in a cell-free conversion reaction, but only if treated with GdnHCl [7].
 

High impact information on guanidine

  • Inclusion bodies containing beta-lactamase could be refolded at high yields of active protein, even without added GdmHCl [8].
  • Here we observed the effects of acidic pH and guanidine hydrochloride (GdnHCl) on the physicochemical and structural properties of PrP(C) derived from normal human brain and determined the ability of the acid/GdnHCl-treated PrP to form a proteinase K (PK)-resistant species in the absence and presence of PrP(Sc) template [9].
  • The intermediate state induced maximally in 0.96 m GdnHCl is found to be obligatory in the folding/unfolding pathway of hFGF-1 [10].
  • The overall free-energy change for complete unfolding of alpha(3)-1, determined from GdnHCl unfolding data, is +4.6 kcal/mol [11].
  • GdnHCl at millimolar concentrations inhibited ATP hydrolysis [1].
 

Chemical compound and disease context of guanidine

 

Biological context of guanidine

  • (2) The unfolding kinetics showed two phases in the range of final GuHCl concentration above 1.8 M [13].
  • The stability of the folded monomeric species can be calculated as the difference between the dimerization free energy determined from hydrodynamic measurements and the folding free energy extrapolated from GdnHCl denaturation [14].
  • The relationship between D and the protein conformations under equilibrium condition were investigated at various GdnHCl concentrations using a photolabeling reagent [15].
  • SSA1-21 [PSI(+)] strains are hypersensitive to curing of [PSI(+)] by guanidine-hydrochloride and partially cured of [PSI(+)] by rapid induction of the heat-shock response but not by growth at 37 degrees [16].
  • We provide further evidence that propagon generation is blocked by growth in GdnHCl and that it is largely confined to the S phase of the cell cycle [17].
 

Anatomical context of guanidine

 

Associations of guanidine with other chemical compounds

 

Gene context of guanidine

  • Clearly, anti-suppression caused by growth in the presence of GuHCl is not sufficient to distinguish missense mutations in SUP35 or SUP45, from [PSI(+)] [28].
  • Recent reports indicate that GuHCl blocks the inheritance of [PSI(+)] by directly inhibiting the activity of the protein remodelling factor Hsp104, which is required for the transmission of [PSI(+)] from mother to daughter cells [28].
  • The receptor-binding domain of human B7-2 was overexpressed in Escherichia coli as inclusion bodies, solubilized in 6 M guanidine-hydrochloride, and then refolded in vitro by rapid dilution into a renaturing buffer [29].
  • Acid/GdnHCl-treated brain PrP may constitute a "recruitable intermediate" in PrP(Sc) formation [9].
  • GuHCl-induced denaturation was found to be cpn10 concentration dependent, in accord with a native heptamer to denatured monomer transition [30].
 

Analytical, diagnostic and therapeutic context of guanidine

References

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  8. High pressure fosters protein refolding from aggregates at high concentrations. St John, R.J., Carpenter, J.F., Randolph, T.W. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  9. Acidic pH and detergents enhance in vitro conversion of human brain PrPC to a PrPSc-like form. Zou, W.Q., Cashman, N.R. J. Biol. Chem. (2002) [Pubmed]
  10. Characterization of the structure and dynamics of a near-native equilibrium intermediate in the unfolding pathway of an all beta-barrel protein. Srimathi, T., Kumar, T.K., Chi, Y.H., Chiu, I.M., Yu, C. J. Biol. Chem. (2002) [Pubmed]
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  17. Analysis of the generation and segregation of propagons: entities that propagate the [PSI+] prion in yeast. Cox, B., Ness, F., Tuite, M. Genetics (2003) [Pubmed]
  18. Heterogeneity of proteoglycans extracted before and after collagenase treatment of human articular cartilage. II. Variations in composition with age and tissue source. Kuijer, R., van de Stadt, R.J., van Kampen, G.P., de Koning, M.H., van de Voorde-Vissers, E., van der Korst, J.K. Arthritis Rheum. (1986) [Pubmed]
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  28. Guanidine reduces stop codon read-through caused by missense mutations in SUP35 or SUP45. Bradley, M.E., Bagriantsev, S., Vishveshwara, N., Liebman, S.W. Yeast (2003) [Pubmed]
  29. Expression, refolding, purification, molecular characterization, crystallization, and preliminary X-ray analysis of the receptor binding domain of human B7-2. Zhang, X., Schwartz, J.C., Almo, S.C., Nathenson, S.G. Protein Expr. Purif. (2002) [Pubmed]
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  33. Mucus glycoconjugate complexes released from feline trachea by a bacterial toxin. Fung, D.C., Somerville, M., Richardson, P.S., Sheehan, J.K. Am. J. Respir. Cell Mol. Biol. (1995) [Pubmed]
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