The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Chemical Compound Review

Guanidium chloride     guanidine hydrochloride

Synonyms: eONIEaNI, NIEaeO, qKxPSDQBBsP@, ARONIS27077, ACMC-1AZ7T, ...
This record was replaced with 3520.
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

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


  1. Characterization of the nucleoside triphosphatase activity of poliovirus protein 2C reveals a mechanism by which guanidine inhibits poliovirus replication. Pfister, T., Wimmer, E. J. Biol. Chem. (1999) [Pubmed]
  2. Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model. Higurashi, T., Nosaka, K., Mizobata, T., Nagai, J., Kawata, Y. J. Mol. Biol. (1999) [Pubmed]
  3. Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes. Newcomb, W.W., Trus, B.L., Booy, F.P., Steven, A.C., Wall, J.S., Brown, J.C. J. Mol. Biol. (1993) [Pubmed]
  4. Chromatographic separation of the polyoma virus proteins and renaturation of the isolated VP1 major capsid protein. Brady, J.N., Consigli, R.A. J. Virol. (1978) [Pubmed]
  5. Salt-resistant association of simian virus 40 T antigen with simian virus 40 DNA in nucleoprotein complexes. Rudolph, K., Mann, K. J. Virol. (1983) [Pubmed]
  6. Thermal unfolding of soybean peroxidase. Appropriate high denaturant concentrations induce cooperativity allowing the correct measurement of thermodynamic parameters. Kamal, J.K., Nazeerunnisa, M., Behere, D.V., Kizhakkedathu, A.K. J. Biol. Chem. (2002) [Pubmed]
  7. Reversibility of scrapie-associated prion protein aggregation. Callahan, M.A., Xiong , L., Caughey, B. J. Biol. Chem. (2001) [Pubmed]
  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]
  11. Folding intermediates of a model three-helix bundle protein. Pressure and cold denaturation studies. Chapeaurouge, A., Johansson, J.S., Ferreira, S.T. J. Biol. Chem. (2001) [Pubmed]
  12. Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study. Yamasaki, K., Ogasahara, K., Yutani, K., Oobatake, M., Kanaya, S. Biochemistry (1995) [Pubmed]
  13. Unfolding-refolding kinetics of the tryptophan synthase alpha subunit by CD and fluorescence measurements. Ogasahara, K., Yutani, K. J. Mol. Biol. (1994) [Pubmed]
  14. A folded monomeric intermediate in the formation of lambda Cro dimer-DNA complexes. Jana, R., Hazbun, T.R., Mollah, A.K., Mossing, M.C. J. Mol. Biol. (1997) [Pubmed]
  15. Kinetics of intermolecular interaction during protein folding of reduced cytochrome c. Nishida, S., Nada, T., Terazima, M. Biophys. J. (2004) [Pubmed]
  16. A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress. Jung, G., Jones, G., Wegrzyn, R.D., Masison, D.C. Genetics (2000) [Pubmed]
  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]
  19. Glycoprotein-like large glucagon immunoreactive species in extracts of the fetal bovine pancreas. Tung, A.K., Cockburn, E., Siu, K.P. Diabetes (1982) [Pubmed]
  20. Bacteriophage proteins associated with the bacterial membrane after bacteriophage T7 infection. Ennis, H.L., Kievitt, K.D. J. Virol. (1977) [Pubmed]
  21. Growth factors, mitogens, cytokines, and bone morphogenetic protein in induced chondrogenesis in tissue culture. Kawamura, M., Urist, M.R. Dev. Biol. (1988) [Pubmed]
  22. Effects of corneal extracts on rabbit corneal stromal cells in culture. Yue, B.Y., Hsieh, P., Baum, J.L. Invest. Ophthalmol. Vis. Sci. (1986) [Pubmed]
  23. Probing conformational changes in the estrogen receptor: evidence for a partially unfolded intermediate facilitating ligand binding and release. Gee, A.C., Katzenellenbogen, J.A. Mol. Endocrinol. (2001) [Pubmed]
  24. Bacteriophage phi29 terminal protein: its association with the 5' termini of the phi29 genome. Ito, J. J. Virol. (1978) [Pubmed]
  25. Refolding of triosephosphate isomerase in low-water media investigated by fluorescence resonance energy transfer. Sepúlveda-Becerra, M.A., Ferreira, S.T., Strasser, R.J., Garzón-Rodríguez, W., Beltrán, C., Gómez-Puyou, A., Darszon, A. Biochemistry (1996) [Pubmed]
  26. Mass spectrometric characterization of the human androgen receptor ligand-binding domain expressed in Escherichia coli. Zhu, Z., Becklin, R.R., Desiderio, D.M., Dalton, J.T. Biochemistry (2001) [Pubmed]
  27. Stabilization of barstar by chemical modification of the buried cysteines. Ramachandran, S., Udgaonkar, J.B. Biochemistry (1996) [Pubmed]
  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]
  30. Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant. Guidry, J.J., Moczygemba, C.K., Steede, N.K., Landry, S.J., Wittung-Stafshede, P. Protein Sci. (2000) [Pubmed]
  31. Conformational change and intermediates in the unfolding of alpha 1-antichymotrypsin. Pearce, M.C., Rubin, H., Bottomley, S.P. J. Biol. Chem. (2000) [Pubmed]
  32. Identification and characterization of an equilibrium intermediate in the unfolding pathway of an all beta-barrel protein. Samuel, D., Kumar, T.K., Srimathi, T., Hsieh, H., Yu, C. J. Biol. Chem. (2000) [Pubmed]
  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]
  34. A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Santoro, M.M., Bolen, D.W. Biochemistry (1992) [Pubmed]
WikiGenes - Universities