Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Joseph D. Koos"'
Autor:
Hader E. Elashal, Joseph D. Koos, Wai Ling Cheung-Lee, Brian Choi, Li Cao, Michelle A. Richardson, Heather L. White, A. James Link
Publikováno v:
Nat Chem
Microviridins and other ω-ester-linked peptides, collectively known as graspetides, are characterized by side-chain-side-chain linkages installed by ATP-grasp enzymes. Here we report the discovery of a family of graspetides, the gene clusters of whi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f17cdbbd89b001d19dbd6fb8190d7a9e
https://doi.org/10.1038/s41557-022-01022-y
https://doi.org/10.1038/s41557-022-01022-y
Autor:
Margarita Orlova, Li Cao, Hader E. Elashal, A. J. Link, Joseph D. Koos, H. V. Schroeder, M. Beiser
Publikováno v:
J Am Chem Soc
Lasso peptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) defined by their threaded structure. Besides the class-defining isopeptide bond, other post-translational modifications (PTMs) that further tail
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb6231f2abe57d87262f25e395e90e92
https://doi.org/10.1021/jacs.1c05017
https://doi.org/10.1021/jacs.1c05017
Autor:
Joseph D. Koos, Brian Choi, Michelle A. Richardson, Heather L. White, A. James Link, Hader E. Elashal, Li Cao, Wai Ling Cheung-Lee
Microviridins and other ω−ester linked peptides (OEPs) are characterized by sidechain-sidechain linkages installed by ATP-grasp enzymes. Here we describe the discovery of a new family of OEPs, the gene clusters of which also encode an O-methyltran
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d97ce54816d022746991ac673218a34e
https://doi.org/10.1101/2021.05.19.444834
https://doi.org/10.1101/2021.05.19.444834
Structure of the Lasso Peptide Isopeptidase Identifies a Topology for Processing Threaded Substrates
Autor:
Satish K. Nair, Chuhan Zong, Mikhail O. Maksimov, A. James Link, Jonathan R. Chekan, Joseph D. Koos
Publikováno v:
Journal of the American Chemical Society. 138:16452-16458
Lasso peptides are a class of bioactive ribosomally synthesized and post-translationally modified peptides (RiPPs), with a threaded knot structure that is formed by an isopeptide bond attaching the N-terminus of the peptide to a side chain carboxylat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a3fe6c80b372071b3bd36d17c866b5f
https://doi.org/10.1021/jacs.6b10389
https://doi.org/10.1021/jacs.6b10389
Autor:
Joseph D. Koos, A. James Link
Publikováno v:
Journal of the American Chemical Society. 141(2)
Lasso peptides are a class of ribosomally derived natural products typified by their threaded rotaxane structure. The conversion of a linear precursor peptide into a lasso peptide structure requires two enzymatic activities: cleavage of the precursor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a50f87fadc4413179304b90b52fae9e6
https://pubmed.ncbi.nlm.nih.gov/30532970
https://pubmed.ncbi.nlm.nih.gov/30532970
Autor:
Joseph D. Koos, Derek G. Rudge, Nikola P. Pavletich, Hyo J. Yang, Bhamini Vaidialingam, Haijuan Yang
Publikováno v:
Nature
The mammalian target of rapamycin (mTOR), a phosphoinositide 3-kinase-related protein kinase, controls cell growth in response to nutrients and growth factors and is frequently deregulated in cancer. Here we report co-crystal structures of a complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98d904daf63cd4b3319e176fc4551b20
http://europepmc.org/articles/PMC4512754
http://europepmc.org/articles/PMC4512754
Publikováno v:
The Journal of biological chemistry. 290(52)
Lasso peptide isopeptidase is an enzyme that specifically hydrolyzes the isopeptide bond of lasso peptides, rendering these peptides linear. To carry out a detailed structure-activity analysis of the lasso peptide isopeptidase AtxE2 from Asticcacauli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a22eca04a722690c7b1165b24c405d68
https://pubmed.ncbi.nlm.nih.gov/26534965
https://pubmed.ncbi.nlm.nih.gov/26534965