Justin Lecher

发表

The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria.

P. Neudecker, M. Schmitz, M. Brimble, 2016, Biochemistry.

Conservation of dark recovery kinetic parameters and structural features in the pseudomonadaceae "short" light, oxygen, voltage (LOV) protein family: implications for the design of LOV-based optogenetic tools.

K. Jaeger, D. Willbold, U. Krauss, 2013, Biochemistry.

Crystallization and preliminary X-ray crystallographic studies of an oligomeric species of a refolded C39 peptidase-like domain of the Escherichia coli ABC transporter haemolysin B.

C. Schwarz, S. Panjikar, S. Smits, 2011, Acta crystallographica. Section F, Structural biology and crystallization communications.

Pyroglutamate-Modified Amyloid-β(3-42) Shows α-Helical Intermediates before Amyloid Formation.

D. Willbold, L. Gremer, M. Schwarten, 2017, Biophysical journal.

An RTX transporter tethers its unfolded substrate during secretion via a unique N-terminal domain.

C. Schwarz, S. Smits, L. Schmitt, 2012, Structure.

The crystal structure of UehA in complex with ectoine-A comparison with other TRAP-T binding proteins.

E. Bremer, S. Smits, L. Schmitt, 2009, Journal of molecular biology.

Conformational Polymorphism in Autophagy-Related Protein GATE-16.

B. Strodel, Peixiang Ma, D. Willbold, 2015, Biochemistry.

Structural analysis of the pyroglutamate‐modified isoform of the Alzheimer's disease‐related amyloid‐β using NMR spectroscopy

H. Demuth, D. Willbold, L. Gremer, 2012, Journal of peptide science : an official publication of the European Peptide Society.

Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel

D. Willbold, M. Stoldt, Justin Lecher, 2011, Proceedings of the National Academy of Sciences.

Resonance assignment of the ligand-free cyclic nucleotide-binding domain from the murine ion channel HCN2

D. Willbold, M. Stoldt, Justin Lecher, 2015, Biomolecular NMR assignments.

Resonance assignment of the ligand-free cyclic nucleotide-binding domain from the murine ion channel HCN2

D. Willbold, M. Stoldt, Justin Lecher, 2014, Biomolecular NMR Assignments.

Resonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain

D. Willbold, M. Stoldt, Justin Lecher, 2010, Biomolecular NMR assignments.

Sequestration of a β-hairpin for control of α-synuclein aggregation.

Ewa A. Mirecka, D. Willbold, W. Hoyer, 2014, Angewandte Chemie.

1H, 15N and 13C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB)

C. Schwarz, S. Smits, L. Schmitt, 2011, Biomolecular NMR assignments.

The Compatible-Solute-Binding Protein OpuAC from Bacillus subtilis: Ligand Binding, Site-Directed Mutagenesis, and Crystallographic Studies

E. Bremer, S. Smits, L. Schmitt, 2008, Journal of bacteriology.

nipy/nibabel: 3.2.1

Krzysztof J. Gorgolewski, Felix C. Morency, Gregory R. Lee, 2020 .

The compatible solute-binding protein OpuAC 2 from Bacillus subtilis : ligand-binding , site 3 directed mutagenesis and crystallographic 4 studies 5 6

E. Bremer, S. Smits, L. Schmitt, 2008 .

Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel

U. Kaupp, D. Willbold, M. Stoldt, 2011, Proceedings of the National Academy of Sciences.

Data describing the solution structure of the WW3* domain from human Nedd4-1

D. Willbold, Vineet Panwalkar, A. Dingley, 2016, Data in brief.

The crystal structure of UehA in complex with ectoine-A comparison with other TRAP-T binding proteins.

E. Bremer, S. Smits, L. Schmitt, 2009, Journal of molecular biology.