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Literature summary for 1.14.14.3 extracted from
- Effect of alkylresorcinols on thermal denaturation and refolding of bacterial luciferase and synthesis of heat shock proteins revealed in the luminescent molecular and cellular test systems (2014), Mikrobiologiia, 83, 640-652 .
General Stability
| General Stability | Organism |
|---|---|
| longchain alkylresorcinol homologues exhibit a protective effect at micromolar concentrations only, while their millimolar concentrations increase the sensitivity of the model proteins to thermal treatment | Aliivibrio fischeri |
| longchain alkylresorcinol homologues exhibit a protective effect at micromolar concentrations only, while their millimolar concentrations increase the sensitivity of the model proteins to thermal treatment | Photobacterium leiognathi |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aliivibrio fischeri | - |
- |
- |
| Photobacterium leiognathi | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| the functional activity of heat-inactivated enzyme is restored by micromolar concentrations of shortchain alkylresorcinols, while longchain homologues inhibit refolding over a wide concentration range. The preincubation of bacterial cells with longchain alkylresorcinols leads to the dose-dependent stimulation of heat shock protein synthesis | Aliivibrio fischeri |
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