Zobrazeno 1 - 10
of 385
pro vyhledávání: '"R, Buller"'
Autor:
Rushad Patell, Charles Hsu, Minggao Shi, Michael A. Grosso, Anil Duggal, Harry R. Buller, Gary Raskob, Jeffrey I. Zwicker
Publikováno v:
Haematologica, Vol 109, Iss 6 (2023)
Thrombocytopenia occurs frequently in patients with cancer-associated thrombosis (CAT), however prospective evaluation of clinical outcomes following randomization to anticoagulants is limited. The HOKUSAI VTE Cancer study was a randomized, open-labe
Externí odkaz:
https://doaj.org/article/13859d1fc1a340ee999c569237cc3101
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
Efficient engineering of enzymes for expanded substrate scope is currently challenging. Here, the authors develop simple principles of how to design and interpret Substrate Multiplexed Screening assays to guide protein engineering to enable activity
Externí odkaz:
https://doaj.org/article/4fcb3b4ff801406d940e0e74431531f4
Autor:
Ketan D. Patel, Felipe B. d’Andrea, Nicole M. Gaudelli, Andrew R. Buller, Craig A. Townsend, Andrew M. Gulick
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
NocTE is a nonribosomal peptide synthetase thioesterase that completes the biosynthesis of pro-nocardicin G, the precursor for nocardicin β-lactam antibiotics. Here the authors provide mechanistic insights into NocTE by determining its crystal struc
Externí odkaz:
https://doaj.org/article/0edee8fbfb374cbf8bab9f96d03b7963
Publikováno v:
CHIMIA, Vol 73, Iss 6 (2019)
Externí odkaz:
https://doaj.org/article/a0bdd1d26f78404ebb226d1f95f81388
Akademický článek
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Autor:
Jonathan M, Ellis, Andrew R, Buller
Publikováno v:
Nature chemical biology.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f48361a0971201a8e5c3d48e7012b36a
https://pubmed.ncbi.nlm.nih.gov/36509905
https://pubmed.ncbi.nlm.nih.gov/36509905
Publikováno v:
Angew Chem Int Ed Engl
Biocatalytic cascades are uniquely powerful for the efficient, asymmetric synthesis of bioactive compounds. However, high substrate specificity can hinder the scope of biocatalytic cascades because the constituent enzymes may have non-complementary a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b7b2ff8cb6644c35efd77e028972ab3
https://doi.org/10.1002/anie.202212637
https://doi.org/10.1002/anie.202212637
Biocatalytic cascades are uniquely powerful for the efficient, asymmetric synthesis of bioactive compounds. The high specificity of enzymes can enable one-pot reactions where the substrates, intermediates, and products react only with the intended en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e64515efa630298da6cd30ce9aae513c
https://doi.org/10.26434/chemrxiv-2022-snxxm
https://doi.org/10.26434/chemrxiv-2022-snxxm
Publikováno v:
ChemBioChem. 23
Pyridoxal-5'-phosphate (PLP)-dependent enzymes have garnered interest for their ability to synthesize non-standard amino acids (nsAAs). One such class of enzymes, O-acetylserine sulfhydrylases (OASSs), catalyzes the final step in the biosynthesis of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0a37f115d0aaff5dfa10451250a289c
https://doi.org/10.1002/cbic.202200157
https://doi.org/10.1002/cbic.202200157
Autor:
Prasanth Kumar, Craig A. Bingman, Jonathan M. Ellis, Andrew R. Buller, Grace A Carlson, Anthony Meza
Publikováno v:
ACS Chem Biol
l-Threonine transaldolases (lTTAs) are a poorly characterized class of pyridoxal-5'-phosphate (PLP) dependent enzymes responsible for the biosynthesis of diverse β-hydroxy amino acids. Here, we study the catalytic mechanism of ObiH, an lTTA essentia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4371cb1a1ebf89367e80dfa71abfe977
https://doi.org/10.1021/acschembio.0c00753
https://doi.org/10.1021/acschembio.0c00753