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Makrozyklische FKBP51‐Liganden enthüllen einen transienten Bindungsmodus mit erhöhter Selektivität.
- Published in:
- Angewandte Chemie, 2021, v. 133, n. 24, p. 13366, doi. 10.1002/ange.202017352
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- Article
Rational Design and Asymmetric Synthesis of Potent and Neurotrophic Ligands for FK506-Binding Proteins (FKBPs).
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- Angewandte Chemie International Edition, 2015, v. 54, n. 1, p. 345, doi. 10.1002/anie.201408776
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- Article
Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.
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- EMBO Journal, 2006, v. 25, n. 11, p. 2519, doi. 10.1038/sj.emboj.7601138
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- Article
Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p.
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- EMBO Journal, 2002, v. 21, n. 22, p. 6114, doi. 10.1093/emboj/cdf608
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- Article
Crystal structure of the Habc domain of neuronal syntaxin from the squid Loligo pealei reveals conformational plasticity at its C-terminus.
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- BMC Structural Biology, 2004, v. 4, p. 1
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- Article
Maintaining photosynthetic CO fixation via protein remodelling: the Rubisco activases.
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- Photosynthesis Research, 2014, v. 119, n. 1/2, p. 191, doi. 10.1007/s11120-013-9819-0
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- Article
L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle.
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- EMBO Reports, 2007, v. 8, n. 11, p. 1086, doi. 10.1038/sj.embor.7401114
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- Article
L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle.
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- EMBO Reports, 2006, v. 7, n. 1, p. 78, doi. 10.1038/sj.embor.7400551
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- Article
Crystal structure of the GABA<sub>A</sub>-receptor-associated protein, GABARAP.
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- EMBO Reports, 2002, v. 3, n. 2, p. 183, doi. 10.1093/embo-reports/kvf026
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- Article
Crystal structure of phosphoribulokinase from Synechococcus sp. strain PCC 6301.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2019, v. 75, n. 4, p. 278, doi. 10.1107/S2053230X19002693
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- Article
Crystal structure of the Thermoplasma acidophilum protein Ta1207.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2017, v. 73, n. 6, p. 328, doi. 10.1107/S2053230X17007087
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- Article
The Hsc70 disaggregation machinery removes monomer units directly from α-synuclein fibril ends.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-25966-w
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- Article
The extracellular chaperone Clusterin enhances Tau aggregate seeding in a cellular model.
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- Nature Communications, 2021, v. 12, n. 1, p. 1, doi. 10.1038/s41467-021-25060-1
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- Article
Firefly luciferase mutants as sensors of proteome stress.
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- Nature Methods, 2011, v. 8, n. 10, p. 879, doi. 10.1038/nmeth.1697
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- Article
Structure and mechanism of the Rubisco-assembly chaperone Raf1.
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- Nature Structural & Molecular Biology, 2015, v. 22, n. 9, p. 720, doi. 10.1038/nsmb.3062
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- Article
Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle.
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- Nature Structural & Molecular Biology, 2013, v. 20, n. 8, p. 929, doi. 10.1038/nsmb.2608
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- Article
Structure of green-type Rubisco activase from tobacco.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 12, p. 1366, doi. 10.1038/nsmb.2171
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- Article
Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco.
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- Nature Structural & Molecular Biology, 2011, v. 18, n. 8, p. 875, doi. 10.1038/nsmb.2090
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- Article
Hsp90 structure: when two ends meet.
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- Nature Structural & Molecular Biology, 2006, v. 13, n. 6, p. 478, doi. 10.1038/nsmb0606-478
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- Article
Rationales Design und asymmetrische Synthese potenter neuritotropher Liganden für FK506-bindende Proteine (FKBPs).
- Published in:
- Angewandte Chemie, 2015, v. 127, n. 1, p. 352, doi. 10.1002/ange.201408776
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- Article
Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii.
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- PLoS ONE, 2015, v. 10, n. 8, p. 1, doi. 10.1371/journal.pone.0135448
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- Article
Post-Exposure Antioxidant Treatment in Rats Decreases Airway Hyperplasia and Hyperreactivity Due to Chlorine Inhalation.
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- American Journal of Respiratory Cell & Molecular Biology, 2012, v. 46, n. 5, p. 599, doi. 10.1165/rcmb.2011-0196OC
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Molecular chaperones in protein folding and proteostasis.
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- Nature, 2011, v. 475, n. 7356, p. 324, doi. 10.1038/nature10317
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- Article
Coupled chaperone action in folding and assembly of hexadecameric Rubisco.
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- Nature, 2010, v. 463, n. 7278, p. 197, doi. 10.1038/nature08651
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- Article
Structure and conformational cycle of a bacteriophage-encoded chaperonin.
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- PLoS ONE, 2020, v. 15, n. 4, p. 1, doi. 10.1371/journal.pone.0230090
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- Article
Macrocyclic FKBP51 Ligands Define a Transient Binding Mode with Enhanced Selectivity.
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- Angewandte Chemie International Edition, 2021, v. 60, n. 24, p. 13257, doi. 10.1002/anie.202017352
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- Article
A c-kit Mutation in Exon 18 in Familial Mastocytosis.
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- Journal of Investigative Dermatology, 2013, v. 133, n. 3, p. 839, doi. 10.1038/jid.2012.394
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- Article
Epidermal Growth Factor Facilitates Melanoma Lymph Node Metastasis by Influencing Tumor Lymphangiogenesis.
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- Journal of Investigative Dermatology, 2013, v. 133, n. 1, p. 230, doi. 10.1038/jid.2012.272
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- Article
Wnt1 Is Anti-Lymphangiogenic in a Melanoma Mouse Model.
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- Journal of Investigative Dermatology, 2012, v. 132, n. 9, p. 2235, doi. 10.1038/jid.2012.138
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- Article
Combination of Dacarbazine and Dimethylfumarate Efficiently Reduces Melanoma Lymph Node Metastasis.
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- Journal of Investigative Dermatology, 2010, v. 130, n. 4, p. 1087, doi. 10.1038/jid.2009.368
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- Article
Selective inhibitors of the FK506-binding protein 51 by induced fit.
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- Nature Chemical Biology, 2015, v. 11, n. 1, p. 33, doi. 10.1038/nchembio.1699
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Structure and function of the AAA<sup>+</sup> protein CbbX, a red-type Rubisco activase.
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- Nature, 2011, v. 479, n. 7372, p. 194, doi. 10.1038/nature10568
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- Article
The chaperone Clusterin in neurodegeneration−friend or foe?
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- BioEssays, 2022, v. 44, n. 7, p. 1, doi. 10.1002/bies.202100287
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- Article
Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum
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- FEBS Letters, 2005, v. 579, n. 29, p. 6595, doi. 10.1016/j.febslet.2005.10.052
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- Article
Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p.
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- Biological Chemistry, 2006, v. 387, n. 12, p. 1593, doi. 10.1515/BC.2006.198
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- Article