Zobrazeno 1 - 10
of 10
pro vyhledávání: '"David L. Niquille"'
Publikováno v:
mAbs, Vol 16, Iss 1 (2024)
ABSTRACTBiparatopic antibodies (bpAbs) bind distinct, non-overlapping epitopes on an antigen. This unique binding mode enables new mechanisms of action beyond monospecific and bispecific antibodies (bsAbs) that can make bpAbs effective therapeutics f
Externí odkaz:
https://doaj.org/article/cded80158e66447d85469dfb9b9c7945
Autor:
Andrew M. King, Daniel A. Anderson, Emerson Glassey, Thomas H. Segall-Shapiro, Zhengan Zhang, David L. Niquille, Amanda C. Embree, Katelin Pratt, Thomas L. Williams, D. Benjamin Gordon, Christopher A. Voigt
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Peptide secondary metabolites have a diverse range of functions. Here the authors present a method to design and screen a large library of modified peptides in E. coli against a target of interest.
Externí odkaz:
https://doaj.org/article/a0b742cce7f140439048d5716ca317c3
Autor:
Aleksa Stanišić, Annika Hüsken, Philipp Stephan, David L. Niquille, Jochen Reinstein, Hajo Kries
Publikováno v:
ACS Catalysis. 11:8692-8700
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ad94a3801a10c6cc9fe3bed56725508e
https://doi.org/10.1021/acscatal.1c01270
https://doi.org/10.1021/acscatal.1c01270
Publikováno v:
Journal of the American Chemical Society. 143:2736-2740
Nonribosomal peptides (NRPs) are a therapeutically important class of secondary metabolites that are produced by modular synthetases in assembly-line fashion. We previously showed that a single Trp-to-Ser mutation in the initial Phe-loading adenylati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::394f175fa0e0c2813078cb5d5d186b50
https://doi.org/10.1021/jacs.1c00925
https://doi.org/10.1021/jacs.1c00925
Autor:
Daniel A. Anderson, Amanda C. Embree, Thomas Williams, Andrew M. King, David L. Niquille, Christopher A. Voigt, Thomas H. Segall-Shapiro, Zhengan Zhang, Katelin Pratt, Emerson Glassey, D. Benjamin Gordon
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Peptide secondary metabolites are common in nature and have diverse pharmacologically-relevant functions, from antibiotics to cross-kingdom signaling. Here, we present a method to design large libraries of modified peptides in Escherichia coli and sc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5af1bb33f5e0c1fc38e67c2cb5664b8
http://europepmc.org/articles/PMC8566587
http://europepmc.org/articles/PMC8566587
Publikováno v:
Synlett. 30:2123-2130
Nonribosomal peptide synthetases produce highly modified bioactive peptides, many of which are used therapeutically. As such, they have been the target of intense protein engineering to enable biosynthetic access to peptide variants with improved dru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::80c077c0bb37eb42849f2aa77999318a
https://doi.org/10.1055/s-0039-1690711
https://doi.org/10.1055/s-0039-1690711
Autor:
Philipp Stephan, Aleksa Stanišić, David L. Niquille, Hajo Kries, Jochen Reinstein, Annika Hüsken
Engineering of nonribosomal peptide synthetases (NRPS) has faced numerous obstacles despite being an attractive path towards novel bioactive molecules. Specificity filters in the nonribosomal peptide assembly line determine engineering success, but t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0abc8db2219e35f62c61772bfc3bf22
https://doi.org/10.26434/chemrxiv.14199695
https://doi.org/10.26434/chemrxiv.14199695
Autor:
David L. Niquille, Takahiro Mori, David Fercher, Douglas A. Hansen, Hajo Kries, Donald Hilvert
Publikováno v:
Nature chemistry. 10(3)
Biosynthetic modification of nonribosomal peptide backbones represents a potentially powerful strategy to modulate the structure and properties of an important class of therapeutics. Using a high-throughput assay for catalytic activity, we show here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d4151a388e3ba5db0659ce2b5300e39
https://pubmed.ncbi.nlm.nih.gov/29461529
https://pubmed.ncbi.nlm.nih.gov/29461529
Publikováno v:
Angewandte Chemie (International ed. in English)
Nonribosomal peptide synthetases (NRPSs) are multifunctional enzymes that produce a wide array of bioactive peptides. Here we show that a single tryptophan-to-serine mutation in phenylalanine-specific NRPS adenylation domains enables the efficient ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::240bca54031d878a20cd9bc626c8c01d
https://doi.org/10.1002/anie.201405281
https://doi.org/10.1002/anie.201405281
Publikováno v:
Chemistry & Biology. (5):640-648
SummaryNonribosomal peptide synthetases (NRPSs) protect microorganisms from environmental threats by producing diverse siderophores, antibiotics, and other peptide natural products. Their modular molecular structure is also attractive from the standp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::920d99d08aa8b6c09f8cc743806dd26f