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Anne-Juliane Geitner

Showing results (1-10 of 8) with videos related to

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Journal of Molecular Biology|May 1, 2012
Combination of the human prolyl isomerase FKBP12 with unrelated chaperone domains leads to chimeric folding enzymes with high activityAnne-Juliane Geitner, Franz Xaver Schmid
Journal of the American Chemical Society|March 1, 2013
The prolyl isomerase SlyD is a highly efficient enzyme but decelerates the conformational folding of a client proteinGabriel Zoldák, Anne-Juliane Geitner, Franz X Schmid
Journal of Molecular Biology|July 23, 2013
Generation of a highly active folding enzyme by combining a parvulin-type prolyl isomerase from SurA with an unrelated chaperone domainAnne-Juliane Geitner, Edina Varga, Marc Wehmer, et al.
Biochemistry|November 21, 2017
Structure-Based Insights into the Dynamics and Function of Two-Domain SlpA from Escherichia coliAnne-Juliane Geitner, Ulrich Weininger, Hauke Paulsen, et al.
Biochemistry|April 23, 2011
Prolyl isomerases show low sequence specificity toward the residue following the prolinePhilipp A M Schmidpeter, Günther Jahreis, Anne-Juliane Geitner, et al.
Molecular Microbiology|May 18, 2012
Structural and energetic basis of infection by the filamentous bacteriophage IKeRoman P Jakob, Anne-Juliane Geitner, Ulrich Weininger, et al.
Biochemistry|December 13, 2016
Dynamics of Aromatic Side Chains in the Active Site of FKBP12Ulrich Weininger, Kristofer Modig, Anne-Juliane Geitner, et al.
Molecules (Basel, Switzerland)|April 13, 2024
Bacterial Chaperone Domain Insertions Convert Human FKBP12 into an Excellent Protein-Folding Catalyst-A Structural and Functional AnalysisGabriel Žoldák, Thomas A Knappe, Anne-Juliane Geitner, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
Journal of Molecular Biology|May 1, 2012
Combination of the human prolyl isomerase FKBP12 with unrelated chaperone domains leads to chimeric folding enzymes with high activityAnne-Juliane Geitner, Franz Xaver Schmid
Journal of the American Chemical Society|March 1, 2013
The prolyl isomerase SlyD is a highly efficient enzyme but decelerates the conformational folding of a client proteinGabriel Zoldák, Anne-Juliane Geitner, Franz X Schmid
Journal of Molecular Biology|July 23, 2013
Generation of a highly active folding enzyme by combining a parvulin-type prolyl isomerase from SurA with an unrelated chaperone domainAnne-Juliane Geitner, Edina Varga, Marc Wehmer, et al.
Biochemistry|November 21, 2017
Structure-Based Insights into the Dynamics and Function of Two-Domain SlpA from Escherichia coliAnne-Juliane Geitner, Ulrich Weininger, Hauke Paulsen, et al.
Biochemistry|April 23, 2011
Prolyl isomerases show low sequence specificity toward the residue following the prolinePhilipp A M Schmidpeter, Günther Jahreis, Anne-Juliane Geitner, et al.
Molecular Microbiology|May 18, 2012
Structural and energetic basis of infection by the filamentous bacteriophage IKeRoman P Jakob, Anne-Juliane Geitner, Ulrich Weininger, et al.
Biochemistry|December 13, 2016
Dynamics of Aromatic Side Chains in the Active Site of FKBP12Ulrich Weininger, Kristofer Modig, Anne-Juliane Geitner, et al.
Molecules (Basel, Switzerland)|April 13, 2024
Bacterial Chaperone Domain Insertions Convert Human FKBP12 into an Excellent Protein-Folding Catalyst-A Structural and Functional AnalysisGabriel Žoldák, Thomas A Knappe, Anne-Juliane Geitner, et al.
Pageof 1