Literature DB >> 4100733

Conformational changes of lysozyme during photodynamic inactivation.

T R Hopkins, J D Spikes.   

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Year:  1970        PMID： 4100733     DOI： 10.1111/j.1751-1097.1970.tb06049.x

Source DB:  PubMed          Journal:  Photochem Photobiol        ISSN： 0031-8655            Impact factor:   3.421


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  6 in total

1.  Potentiation of thermal inactivation of glyceraldehyde-3-phosphate dehydrogenase by photodynamic treatment. A possible model for the synergistic interaction between photodynamic therapy and hyperthermia.

Authors:  C Prinsze; T M Dubbelman; J Van Steveninck
Journal:  Biochem J       Date:  1991-06-01       Impact factor: 3.857

2.  Influence of the pH on the photodynamic effect in lysozyme A comparative kinetic study with the sensitized photooxidation of isolated amino acids.

Authors:  A T Soltermann; M A Biasutti; A Senz; N A García
Journal:  Amino Acids       Date:  1995-06       Impact factor: 3.520

3.  [Photooxidation of lysozyme at different wavelengths (author's transl)].

Authors:  E Silva; S Risi; K Dose
Journal:  Radiat Environ Biophys       Date:  1974-06-10       Impact factor: 1.925

4.  Rate constants studies of the dye-sensitized photoinactivation of lysozyme.

Authors:  E Silva
Journal:  Radiat Environ Biophys       Date:  1979-02-23       Impact factor: 1.925

5.  Light-induced binding of riboflavin to lysozyme.

Authors:  E Silva; J Gaule
Journal:  Radiat Environ Biophys       Date:  1977-12-12       Impact factor: 1.925

6.  Study of a photo-induced lysozyme-riboflavin bond.

Authors:  I Ferrer; E Silva
Journal:  Radiat Environ Biophys       Date:  1985       Impact factor: 1.925
  6 in total

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