Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Matthew B. Calvert"'
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 14, Iss 1, Pp 2607-2617 (2018)
The rapid development of antimicrobial resistance is threatening mankind to such an extent that the World Health Organization expects more deaths from infections than from cancer in 2050 if current trends continue. To avoid this scenario, new classes
Externí odkaz:
https://doaj.org/article/174a1e34626146cca24368047e57b498
Publikováno v:
Beilstein Journal of Organic Chemistry, Vol 13, Iss 1, Pp 2631-2636 (2017)
A novel synthesis of 1,6-anhydro-N-acetylmuramic acid is described, which proceeds in only five steps from the cheap starting material N-acetylglucosamine. This efficient synthesis should enable future studies into the importance of 1,6-anhydromurami
Externí odkaz:
https://doaj.org/article/a383a007b3394b7fa7438dc8f3bc4de9
Autor:
Isabel Hottmann, Valentina M. T. Mayer, Markus B. Tomek, Valentin Friedrich, Matthew B. Calvert, Alexander Titz, Christina Schäffer, Christoph Mayer
Publikováno v:
Frontiers in Microbiology, Vol 9 (2018)
Tannerella forsythia is an anaerobic, Gram-negative oral pathogen that thrives in multispecies gingival biofilms associated with periodontitis. The bacterium is auxotrophic for the commonly essential bacterial cell wall sugar N-acetylmuramic acid (Mu
Externí odkaz:
https://doaj.org/article/c1ad03f035874cc2b3fa05440bbe2b1f
Publikováno v:
Natural Product Reports. 39:410-443
Covering: from 1938 up to March 2021The electron-rich indole side chain of tryptophan is a versatile substrate for peptide modification. Upon the action of various cyclases, the tryptophan side chain may be linked to a nearby amino acid residue, open
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fede13102b7b06eb246586bd641af856
https://doi.org/10.1039/d1np00043h
https://doi.org/10.1039/d1np00043h
Publikováno v:
Natural product reports. 39(2)
Covering: from 1938 up to March 2021The electron-rich indole side chain of tryptophan is a versatile substrate for peptide modification. Upon the action of various cyclases, the tryptophan side chain may be linked to a nearby amino acid residue, open
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::253345c5b53422c821172ebbd367f042
https://pubmed.ncbi.nlm.nih.gov/34581375
https://pubmed.ncbi.nlm.nih.gov/34581375
Autor:
Maraike Müller, Robert Maria Kluj, Qingping Xu, Alicia Engelbrecht, Marina Borisova, Christoph Mayer, Khaled A. Selim, Alexander Titz, Tim Teufel, Katja Balbuchta, Matthew B. Calvert, Isabel Hottmann
Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial enzymes that potentially lyse bacterial cells. They catalyze an endo-lytic cleavage of the peptidoglycan, the structural component of the bacterial cell wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f53e0923112be7de28920505f126ab3
https://doi.org/10.1101/2021.01.10.425899
https://doi.org/10.1101/2021.01.10.425899
Autor:
Alexander Titz, Qingping Xu, Marina Borisova, Alicia Engelbrecht, Isabel Hottmann, Christoph Mayer, Maraike Müller, Matthew B. Calvert, Robert Maria Kluj, Khaled A. Selim, Tim Teufel, Katja Balbuchta
Publikováno v:
The Journal of Biological Chemistry
The Journal of biological chemistry
United States
The Journal of biological chemistry
United States
Endo-β-N-acetylmuramidases, commonly known as lysozymes, are well-characterized antimicrobial enzymes that catalyze an endo-lytic cleavage of peptidoglycan; i.e., they hydrolyze the β-1,4-glycosidic bonds connecting N-acetylmuramic acid (MurNAc) an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e70e3e2be80887f413760f79d4b107d3
https://pubmed.ncbi.nlm.nih.gov/33684445
https://pubmed.ncbi.nlm.nih.gov/33684445
Autor:
Christina R. Tysoe, Sami Caner, Matthew B. Calvert, Anna Win-Mason, Gary D. Brayer, Stephen G. Withers
Publikováno v:
Chemical Science
Simplified analogues of montbretin A bind similarly to human alpha amylase and with nanomolar affinity.
Simplified analogues of the potent human amylase inhibitor montbretin A were synthesised and shown to bind tightly, KI = 60 and 70 nM, with i
Simplified analogues of the potent human amylase inhibitor montbretin A were synthesised and shown to bind tightly, KI = 60 and 70 nM, with i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18982f3cc8fb86724cbae779804f55d2
https://pubmed.ncbi.nlm.nih.gov/32206255
https://pubmed.ncbi.nlm.nih.gov/32206255
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 30:127172
Bedaquiline is a diarylquinoline drug that demonstrates potent and selective inhibition of mycobacterial ATP synthase, and is clinically administered for the treatment of multi-drug resistant tuberculosis. Due to its excellent activity and novel mech
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04fd9bf101513a81c21f7bc23d7522be
https://doi.org/10.1016/j.bmcl.2020.127172
https://doi.org/10.1016/j.bmcl.2020.127172
Publikováno v:
Beilstein Journal of Organic Chemistry
Beilstein Journal of Organic Chemistry, Vol 14, Iss 1, Pp 2607-2617 (2018)
Beilstein Journal of Organic Chemistry, Vol 14, Iss 1, Pp 2607-2617 (2018)
The rapid development of antimicrobial resistance is threatening mankind to such an extent that the World Health Organization expects more deaths from infections than from cancer in 2050 if current trends continue. To avoid this scenario, new classes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17a63df059b57ef81d822ecc2f75a9eb
https://hdl.handle.net/10033/621532
https://hdl.handle.net/10033/621532