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Biochemistry
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March 17, 1999
Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
S Liemann, R Glockshuber
Biochemistry
|
December 23, 1998
Conversion of a catalytic into a structural disulfide bond by circular permutation
J 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 protein
S 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 pH
S 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 coli
H Fischer, R Glockshuber
Protein Science : a Publication of the Protein Society
|
May 1, 1993
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
M 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 coli
H Fischer, R Glockshuber
Biochemical and Biophysical Research Communications
|
October 1, 1998
Transmissible spongiform encephalopathies
S Liemann, R Glockshuber
Folding & Design
|
June 18, 1998
A single dipeptide sequence modulates the redox properties of a whole enzyme family
M Huber-Wunderlich, R Glockshuber
Page
of 7
Search research articles
Search
Showing results (1-10 of 68) with videos related to
Sort By:
Page
of 7
Biochemistry
|
March 17, 1999
Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
S Liemann, R Glockshuber
Biochemistry
|
December 23, 1998
Conversion of a catalytic into a structural disulfide bond by circular permutation
J 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 protein
S 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 pH
S 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 coli
H Fischer, R Glockshuber
Protein Science : a Publication of the Protein Society
|
May 1, 1993
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli
M 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 coli
H Fischer, R Glockshuber
Biochemical and Biophysical Research Communications
|
October 1, 1998
Transmissible spongiform encephalopathies
S Liemann, R Glockshuber
Folding & Design
|
June 18, 1998
A single dipeptide sequence modulates the redox properties of a whole enzyme family
M Huber-Wunderlich, R Glockshuber
Page
of 7