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Nature Structural & Molecular Biology|June 7, 2005
Prolyl isomerization as a molecular timer in phage infectionBarbara Eckert, Andreas Martin, Jochen Balbach, et al.Proceedings of the National Academy of Sciences of the United States of America|July 21, 2009
A remote prolyl isomerization controls domain assembly via a hydrogen bonding networkUlrich Weininger, Roman P Jakob, Barbara Eckert, et al.Biological Chemistry|April 16, 2013
Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyDMichael Kovermann, Franz X Schmid, Jochen BalbachJournal of Molecular Biology|September 8, 2007
A conformational unfolding reaction activates phage fd for the infection of Escherichia coliBarbara Eckert, Franz X SchmidThe Journal of Biological Chemistry|March 15, 2013
Initiation of phage infection by partial unfolding and prolyl isomerizationStephanie Hoffmann-Thoms, Ulrich Weininger, Barbara Eckert, et al.Journal of Molecular Biology|August 21, 2003
A proline switch controls folding and domain interactions in the gene-3-protein of the filamentous phage fdAndreas Martin, Franz X SchmidJournal of Molecular Biology|May 6, 2003
Evolutionary stabilization of the gene-3-protein of phage fd reveals the principles that govern the thermodynamic stability of two-domain proteinsAndreas Martin, Franz X SchmidJournal of Molecular Biology|May 28, 2003
The folding mechanism of a two-domain protein: folding kinetics and domain docking of the gene-3 protein of phage fdAndreas Martin, Franz X SchmidProtein Science : a Publication of the Protein Society|October 30, 2009
The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activityUlrich Weininger, Roman P Jakob, Michael Kovermann, et al.Journal of Molecular Biology|June 27, 2002
Origins of the high stability of an in vitro-selected cold-shock proteinAndreas Martin, Insa Kather, Franz X SchmidPageof 34