Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Thomas A. Knappe"'
Autor:
Gabriel Žoldák, Thomas A. Knappe, Anne-Juliane Geitner, Christian Scholz, Holger Dobbek, Franz X. Schmid, Roman P. Jakob
Publikováno v:
Molecules, Vol 29, Iss 7, p 1440 (2024)
Many folding enzymes use separate domains for the binding of substrate proteins and for the catalysis of slow folding reactions such as prolyl isomerization. FKBP12 is a small prolyl isomerase without a chaperone domain. Its folding activity is low,
Externí odkaz:
https://doaj.org/article/f5b9ea901fb44c5b9bdeacab0da090c8
Autor:
Femke I. Kraas, Mattia Bosello, Thomas A. Knappe, Mohamed A. Marahiel, Xiulan Xie, Tobias W. Giessen, Kamila B. Franke, Uwe Linne
Publikováno v:
Journal of Natural Products. 75:905-914
In this study we report the isolation, structure elucidation, and biosynthesis of mirubactin (1), a siderophore containing an unprecedented chemical functionality in natural products, namely, an O-acyl hydroxamic acid ester. Mirubactin represents the
Autor:
Yanyan Li, Thomas A. Knappe, Sylvie Rebuffat, Séverine Zirah, Mohamed A. Marahiel, Christophe Goulard, Kok-Phen Yan
Publikováno v:
ChemBioChem
ChemBioChem, Wiley-VCH Verlag, 2012, 13 (7), pp.1046-1052. ⟨10.1002/cbic.201200016⟩
ChemBioChem, Wiley-VCH Verlag, 2012, 13 (7), pp.1046-1052. ⟨10.1002/cbic.201200016⟩
Microcin J25 is the archetype of a growing class of bacterial ribosomal peptides possessing a knotted topology (lasso peptides). It consists of an eight-residue macrolactam ring through which the C-terminal tail is threaded. It is biosynthesized as a
Publikováno v:
FEBS Journal. 277:663-676
The class of nonribosomally assembled siderophores encompasses a multitude of structurally diverse natural products. The genome of the erythromycin-producing strain Saccharopolyspora erythraea contains 25 secondary metabolite gene clusters that are m
Autor:
Stefan A. Samel, Thomas A. Knappe, Georg Schoenafinger, Mohamed A. Marahiel, Lars-Oliver Essen
Publikováno v:
Structure. 15(7):781-792
The crystal structure of the bidomain PCP-C from modules 5 and 6 of the nonribosomal tyrocidine synthetase TycC was determined at 1.8 A resolution. The bidomain structure reveals a V-shaped condensation domain, the canyon-like active site groove of w
Publikováno v:
Journal of Molecular Biology. 368:1458-1468
The catalytic activity of human FKBP12 as a prolyl isomerase is high towards short peptides, but very low in proline-limited protein folding reactions. In contrast, the SlyD proteins, which are members of the FKBP family, are highly active as folding
Autor:
Francesco Saverio Di Leva, Marcel Zimmermann, Stefan Zahler, Luciana Marinelli, Xiulan Xie, Ettore Novellino, Thomas A. Knappe, Horst Kessler, Mohamed A. Marahiel, Julian D. Hegemann, Mariarosaria De Simone
Integrins moderate diverse important functions in the human body and are promising targets in cancer therapy. Hence, the selective inhibition of specific integrins is of great medicinal interest. Here, we report the optimization of a grafted lasso pe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5d15483a8a2c2d8f83890c57f2374a0
http://hdl.handle.net/11588/585755
http://hdl.handle.net/11588/585755
Autor:
Mohamed A. Marahiel, Olaf Burghaus, Leif Flühe, Michael J. Gattner, Thomas A. Knappe, Uwe Linne, Antje Schäfer
Publikováno v:
Nature chemical biology. 8(4)
Subtilosin A is a 35-residue, ribosomally synthesized bacteriocin encoded by the sbo-alb operon of Bacillus subtilis. It is composed of a head-to-tail circular peptide backbone that is additionally restrained by three unusual thioether bonds between
Publikováno v:
Biochemistry. 50(27)
Biosynthesis of the hydroxamate-type siderophore erythrochelin requires the generation of δ-N-acetyl-δ-N-hydroxy-L-ornithine (L-haOrn), which is incorporated into the tetrapeptide at positions 1 and 4. Bioinformatic analysis revealed the FAD-depend
Autor:
Uwe Linne, Thomas A. Knappe, Carlos Afonso, Jean-Claude Tabet, Mohamed A. Marahiel, Séverine Zirah, Sylvie Rebuffat
Publikováno v:
Journal of The American Society for Mass Spectrometry
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), 2011, 22, pp.467-479. ⟨10.1007/s13361-010-0028-1⟩
Journal of The American Society for Mass Spectrometry, 2011, 22, pp.467-479. ⟨10.1007/s13361-010-0028-1⟩
Journal of The American Society for Mass Spectrometry, Springer Verlag (Germany), 2011, 22, pp.467-479. ⟨10.1007/s13361-010-0028-1⟩
Journal of The American Society for Mass Spectrometry, 2011, 22, pp.467-479. ⟨10.1007/s13361-010-0028-1⟩
Lasso peptides constitute a class of bioactive peptides sharing a knotted structure where the C-terminal tail of the peptide is threaded through and trapped within an N-terminalmacrolactamring. The structural characterization of lasso structures and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a83bff144feef986b48d54ec669c224f
https://hal.archives-ouvertes.fr/hal-00578442/document
https://hal.archives-ouvertes.fr/hal-00578442/document