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R Glockshuber

Showing results (1-10 of 68) with videos related to

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Biochemistry|March 17, 1999
Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion proteinS Liemann, R Glockshuber
Biochemistry|December 23, 1998
Conversion of a catalytic into a structural disulfide bond by circular permutationJ Hennecke, R Glockshuber
The Journal of Biological Chemistry|November 25, 1993
In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA)M Wunderlich, R Glockshuber
Journal of Molecular Biology|September 6, 1996
Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion proteinS Hornemann, R Glockshuber
Proceedings of the National Academy of Sciences of the United States of America|May 30, 1998
A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pHS Hornemann, R Glockshuber
The Journal of Biological Chemistry|October 25, 1993
ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coliH Fischer, R Glockshuber
Protein Science : a Publication of the Protein Society|May 1, 1993
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coliM Wunderlich, R Glockshuber
FEBS Letters|December 12, 1994
A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coliH Fischer, R Glockshuber
Biochemical and Biophysical Research Communications|October 1, 1998
Transmissible spongiform encephalopathiesS Liemann, R Glockshuber
Folding & Design|June 18, 1998
A single dipeptide sequence modulates the redox properties of a whole enzyme familyM Huber-Wunderlich, R Glockshuber
Pageof 7

Showing results (1-10 of 68) with videos related to

Sort By:
Pageof 7
Biochemistry|March 17, 1999
Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion proteinS Liemann, R Glockshuber
Biochemistry|December 23, 1998
Conversion of a catalytic into a structural disulfide bond by circular permutationJ Hennecke, R Glockshuber
The Journal of Biological Chemistry|November 25, 1993
In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA)M Wunderlich, R Glockshuber
Journal of Molecular Biology|September 6, 1996
Autonomous and reversible folding of a soluble amino-terminally truncated segment of the mouse prion proteinS Hornemann, R Glockshuber
Proceedings of the National Academy of Sciences of the United States of America|May 30, 1998
A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pHS Hornemann, R Glockshuber
The Journal of Biological Chemistry|October 25, 1993
ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coliH Fischer, R Glockshuber
Protein Science : a Publication of the Protein Society|May 1, 1993
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coliM Wunderlich, R Glockshuber
FEBS Letters|December 12, 1994
A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coliH Fischer, R Glockshuber
Biochemical and Biophysical Research Communications|October 1, 1998
Transmissible spongiform encephalopathiesS Liemann, R Glockshuber
Folding & Design|June 18, 1998
A single dipeptide sequence modulates the redox properties of a whole enzyme familyM Huber-Wunderlich, R Glockshuber
Pageof 7