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Accelerating the Association of the Most Stable Protein-Ligand Complex by More than Two Orders of Magnitude.
- Published in:
- Angewandte Chemie, 2016, v. 128, n. 32, p. 9496, doi. 10.1002/ange.201603652
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Accelerating the Association of the Most Stable Protein-Ligand Complex by More than Two Orders of Magnitude.
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- Angewandte Chemie International Edition, 2016, v. 55, n. 32, p. 9350, doi. 10.1002/anie.201603652
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- Article
Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation.
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- Angewandte Chemie International Edition, 2015, v. 54, n. 1, p. 331, doi. 10.1002/anie.201408598
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- Article
Cytotoxin ClyA from Escherichia coli assembles to a 13-meric pore independent of its redox-state.
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- EMBO Journal, 2006, v. 25, n. 11, p. 2652, doi. 10.1038/sj.emboj.7601130
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- Article
Structural basis of chaperone–subunit complex recognition by the type 1 pilus assembly platform FimD.
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- EMBO Journal, 2005, v. 24, n. 12, p. 2075, doi. 10.1038/sj.emboj.7600693
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- Article
Structural basis and kinetics of inter- and intramolecular disulfide exchange in the redox catalyst DsbD.
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- EMBO Journal, 2004, v. 23, n. 8, p. 1709, doi. 10.1038/sj.emboj.7600178
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- Article
Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm.
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- EMBO Journal, 1999, v. 18, n. 12, p. 3271, doi. 10.1093/emboj/18.12.3271
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- Article
Mechanism of fibre assembly through the chaperone–usher pathway.
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- EMBO Reports, 2006, v. 7, n. 7, p. 734, doi. 10.1038/sj.embor.7400722
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- Article
The cryo-EM structure of the human uromodulin filament core reveals a unique assembly mechanism.
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- eLife, 2020, p. 1, doi. 10.7554/eLife.60265
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- Article
A metabolite binding protein moonlights as a bile‐responsive chaperone.
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- EMBO Journal, 2020, v. 39, n. 20, p. 1, doi. 10.15252/embj.2019104231
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- Article
Die atomare dreidimensionale Struktur von Amyloid-β-Fibrillen mit der Osaka-Mutation.
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- Angewandte Chemie, 2015, v. 127, n. 1, p. 337, doi. 10.1002/ange.201408598
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- Publication type:
- Article
Mechanism of the Prokaryotic Transmembrane Disulfide Reduction Pathway and Its In Vitro Reconstitution from Purified Components.
- Published in:
- Angewandte Chemie, 2012, v. 124, n. 28, p. 7006, doi. 10.1002/ange.201201337
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- Publication type:
- Article
Innenrücktitelbild: Der stabilste Protein-Liganden-Komplex: Anwendung für die Einschritt-Affinitätsreinigung und Identifizierung von Proteinkomplexen (Angew. Chem. 18/2012).
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- Angewandte Chemie, 2012, v. 124, n. 18, p. 4569, doi. 10.1002/ange.201202060
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- Article
Der stabilste Protein-Liganden-Komplex: Anwendung für die Einschritt-Affinitätsreinigung und Identifizierung von Proteinkomplexen.
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- Angewandte Chemie, 2012, v. 124, n. 18, p. 4551, doi. 10.1002/ange.201108747
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- Article
Stochastic chain termination in bacterial pilus assembly.
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- Nature Communications, 2023, v. 14, n. 1, p. 1, doi. 10.1038/s41467-023-43449-y
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- Article
The pCri System: A Vector Collection for Recombinant Protein Expression and Purification.
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- PLoS ONE, 2014, v. 9, n. 11, p. 1, doi. 10.1371/journal.pone.0112643
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- Article
Fluorescence quenching in the DsbA protein from Escherichia coli: Complete picture of the excited-state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan.
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- Proteins, 1999, v. 37, n. 2, p. 253, doi. 10.1002/(SICI)1097-0134(19991101)37:2<253::AID-PROT10>3.0.CO;2-J
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- Article
Direct Evidence for Self-Propagation of Different Amyloid-β Fibril Conformations.
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- Neurodegenerative Diseases, 2014, v. 14, n. 3, p. 151, doi. 10.1159/000363623
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- Article
Amyloid-β Aggregation.
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- Neurodegenerative Diseases, 2007, v. 4, n. 1, p. 13, doi. 10.1159/000100355
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- Article
Development of the Mitochondrial Intermembrane Space Disulfide Relay Represents a Critical Step in Eukaryotic Evolution.
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- Molecular Biology & Evolution, 2019, v. 36, n. 4, p. 742, doi. 10.1093/molbev/msz011
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- Article
Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline.
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- ChemBioChem, 2015, v. 16, n. 15, p. 2162, doi. 10.1002/cbic.201500342
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Inside Cover: (4 R)- and (4 S)-Fluoroproline in the Conserved cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering (ChemBioChem 9/2013).
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- ChemBioChem, 2013, v. 14, n. 9, p. 1018, doi. 10.1002/cbic.201390030
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- Article
(4 R)- and (4 S)-Fluoroproline in the Conserved cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering.
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- ChemBioChem, 2013, v. 14, n. 9, p. 1053, doi. 10.1002/cbic.201300178
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- Article
The structure of a cytolytic α-helical toxin pore reveals its assembly mechanism.
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- Nature, 2009, v. 459, n. 7247, p. 726, doi. 10.1038/nature08026
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- Article
Rücktitelbild: Elongated Bacterial Pili as a Versatile Alignment Medium for NMR Spectroscopy (Angew. Chem. 37/2023).
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- Angewandte Chemie, 2023, v. 135, n. 37, p. 1, doi. 10.1002/ange.202308984
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- Article
Elongated Bacterial Pili as a Versatile Alignment Medium for NMR Spectroscopy.
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- Angewandte Chemie, 2023, v. 135, n. 37, p. 1, doi. 10.1002/ange.202305120
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- Article
Catch-bond mechanism of the bacterial adhesin FimH.
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- Nature Communications, 2016, v. 7, n. 3, p. 10738, doi. 10.1038/ncomms10738
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- Article
Erratum: The assembly dynamics of the cytolytic pore toxin ClyA.
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- Nature Communications, 2016, v. 7, n. 2, p. 10650, doi. 10.1038/ncomms10650
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- Article
The assembly dynamics of the cytolytic pore toxin ClyA.
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- Nature Communications, 2015, v. 6, n. 2, p. 6198, doi. 10.1038/ncomms7198
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- Article
Back Cover: Elongated Bacterial Pili as a Versatile Alignment Medium for NMR Spectroscopy (Angew. Chem. Int. Ed. 37/2023).
- Published in:
- Angewandte Chemie International Edition, 2023, v. 62, n. 37, p. 1, doi. 10.1002/anie.202308984
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- Publication type:
- Article
Elongated Bacterial Pili as a Versatile Alignment Medium for NMR Spectroscopy.
- Published in:
- Angewandte Chemie International Edition, 2023, v. 62, n. 37, p. 1, doi. 10.1002/anie.202305120
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- Publication type:
- Article
Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.
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- Journal of Inherited Metabolic Disease, 2011, v. 34, n. 4, p. 869, doi. 10.1007/s10545-011-9337-1
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- Article
Pilus chaperones represent a new type of protein-folding catalyst.
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- Nature, 2004, v. 431, n. 7006, p. 329, doi. 10.1038/nature02891
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- Article
Extremely rapid folding of the C-terminal domain of the prion protein without kinetic intermediates.
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- Nature Structural Biology, 1999, v. 6, n. 6, p. 550
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- Article
Pilus chaperone FimC?adhesin FimH interactions mapped by TROSY-NMR.
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- Nature Structural Biology, 1999, v. 6, n. 4, p. 336
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- Article
NMR solution structure of the periplasmic chaperone FimC.
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- Nature Structural Biology, 1998, v. 5, n. 10, p. 885, doi. 10.1038/2325
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- Article
Peptides and proteins in neurodegenerative disease: Helix propensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy.
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- Biopolymers, 1999, v. 51, n. 2, p. 145, doi. 10.1002/(SICI)1097-0282(1999)51:2<145::AID-BIP4>3.0.CO;2-4
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- Article
Acceleration of protein folding by four orders of magnitude through a single amino acid substitution.
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- Scientific Reports, 2015, p. 11840, doi. 10.1038/srep11840
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- Article
Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (Aβ1−40 E22Δ) fibrils.
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- Biomolecular NMR Assignments, 2015, v. 9, n. 1, p. 7, doi. 10.1007/s12104-013-9535-x
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- Article
Biochemical pathway for the biosynthesis of the Cu<sub>A</sub> center in bacterial cytochrome c oxidase.
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- FEBS Letters, 2019, v. 593, n. 21, p. 2977, doi. 10.1002/1873-3468.13587
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- Article
Thioredoxin-like protein TlpA from Bradyrhizobium japonicum is a reductant for the copper metallochaperone ScoI
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- FEBS Letters, 2012, v. 586, n. 23, p. 4094, doi. 10.1016/j.febslet.2012.10.026
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- Article
Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
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- FEBS Letters, 2008, v. 582, n. 23/24, p. 3301, doi. 10.1016/j.febslet.2008.07.063
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- Article
The Escherichia coli glycophage display system.
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- Glycobiology, 2010, v. 20, n. 11, p. 1366, doi. 10.1093/glycob/cwq102
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- Article
Crystal structure of the ternary FimC–FimF<sub>t</sub>–FimD<sub>N</sub> complex indicates conserved pilus chaperone–subunit complex recognition by the usher FimD
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- FEBS Letters, 2008, v. 582, n. 5, p. 651, doi. 10.1016/j.febslet.2008.01.030
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- Article
Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.
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- Protein Science: A Publication of the Protein Society, 1998, v. 7, n. 5, p. 1233, doi. 10.1002/pro.5560070519
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- Article
Structural analysis of three His32 mutants of DsbA: Support for an electrostatic role of His32 in DsbA stability.
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- Protein Science: A Publication of the Protein Society, 1997, v. 6, n. 9, p. 1893, doi. 10.1002/pro.5560060910
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- Article
Quality control of disulfide bond formation in pilus subunits by the chaperone FimC.
- Published in:
- Nature Chemical Biology, 2012, v. 8, n. 8, p. 707, doi. 10.1038/nchembio.1019
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- Article
Where do the electrons go?
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- Nature, 1999, v. 401, n. 6748, p. 30, doi. 10.1038/43344
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- Article
Structure of native glycolipoprotein filaments in honeybee royal jelly.
- Published in:
- Nature Communications, 2020, v. 11, n. 1, p. 1, doi. 10.1038/s41467-020-20135-x
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- Publication type:
- Article
Mechanism of the Prokaryotic Transmembrane Disulfide Reduction Pathway and Its In Vitro Reconstitution from Purified Components.
- Published in:
- Angewandte Chemie International Edition, 2012, v. 51, n. 28, p. 6900, doi. 10.1002/anie.201201337
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- Publication type:
- Article