Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Alexander J. Lander"'
Publikováno v:
ACS Bio & Med Chem Au, Vol 4, Iss 1, Pp 68-76 (2023)
Externí odkaz:
https://doaj.org/article/e5e53445b0674d59aeffdd1c31d5f6f9
Autor:
Alexander J. Lander, Laura Domínguez Mercado, Xuefei Li, Irshad Maajid Taily, Brandon L. Findlay, Yi Jin, Louis Y. P. Luk
Publikováno v:
Communications Chemistry, Vol 6, Iss 1, Pp 1-7 (2023)
Abstract Tryptophan is frequently found on the surface of membrane-associated proteins that interact with the lipid membrane. However, because of their multifaceted interactions, it is difficult to pinpoint the structure-activity relationship of each
Externí odkaz:
https://doaj.org/article/6d0f8cfe77604de78e87727469801653
Autor:
Davide Cardella, Jorge Sánchez Escudero, Xuefei Li, T. M. Simon Tang, Yu-Hsuan Tsai, Alexander J. Lander, Louis Y. P. Luk
Asparaginyl endopeptidases (AEPs) are ideal for peptide and protein labeling. However, because of the reaction reversibility, a large excess of labels or backbone modified substrates are needed. In turn, simple and cheap reagents can be used to label
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be60ffda92d7f5347dbea257fe63011b
https://orca.cardiff.ac.uk/id/eprint/132485/1/D0SC02023K.pdf
https://orca.cardiff.ac.uk/id/eprint/132485/1/D0SC02023K.pdf
Aureocin A53 (AucA) and lacticin Q (LnqQ) are class IId bacteriocins that display broad-spectrum activity against Gram-positive bacteria in the nanomolar range, of which their modes of action is unclear and their synthesis has not been reported. Here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d26babf4e5d9800859d1d8358e9d46ac
https://doi.org/10.26434/chemrxiv.12444554
https://doi.org/10.26434/chemrxiv.12444554
Aureocin A53 (AucA) and lacticin Q (LnqQ) are class IId bacteriocins that display broad-spectrum activity against Gram-positive bacteria in the nanomolar range, of which their modes of action is unclear and their synthesis has not been reported. Here
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d8e76fce83746116ea9fd8b23564385a
https://doi.org/10.26434/chemrxiv.12444554.v1
https://doi.org/10.26434/chemrxiv.12444554.v1
Transpeptidases are ideal biocatalysts for site-specific peptide and protein labeling, whereas reactions that target N-terminus cysteine with commercially available reagents have become common practice. However, a versatile approach that allows bioco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e1df7953ec6f7a041bb8d0bf709f78f
https://doi.org/10.26434/chemrxiv.9633032
https://doi.org/10.26434/chemrxiv.9633032
Asparaginyl endopeptides (AEP) are recognized for their catalytic efficiency, presenting as ideal tools for protein bioconjugation. However, the peptide ligation catalyzed by AEP is reversible. In an attempt to obtain high reaction yields, thiodepsip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::328f23436ffc12d4c14657d26fb21054
https://doi.org/10.26434/chemrxiv.9633032.v1
https://doi.org/10.26434/chemrxiv.9633032.v1