Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Peleg Ragonis-Bachar"'
Autor:
Peter N. Lipke, Peleg Ragonis-Bachar
Publikováno v:
Journal of Fungi, Vol 9, Iss 4, p 419 (2023)
Bacterial and fungal adhesins mediate microbial aggregation, biofilm formation, and adhesion to host. We divide these proteins into two major classes: professional adhesins and moonlighting adhesins that have a non-adhesive activity that is evolution
Externí odkaz:
https://doaj.org/article/abd5c417a9e14af9a916a258c631989f
Publikováno v:
Biomacromolecules 23(3), 926 – 936 (2022). doi:10.1021/acs.biomac.1c01353
Biomacromolecules 23(3), 926 – 936 (2022). doi:10.1021/acs.biomac.1c01353
Human LL-37$_{17–29}$ is an antimicrobial peptide forming thermostable supramolecular fibrils that surround bacterial cells. The crystal structure of LL-37$_{17–29}$
Human LL-37$_{17–29}$ is an antimicrobial peptide forming thermostable supramolecular fibrils that surround bacterial cells. The crystal structure of LL-37$_{17–29}$
Autor:
Peleg Ragonis-Bachar, Bader Rayan, Eilon Barnea, Yizhaq Engelberg, Alexander Upcher, Meytal Landau
Publikováno v:
Biomacromolecules. 23(9)
Amyloid protein fibrils and some antimicrobial peptides (AMPs) share biophysical and structural properties. This observation suggests that ordered self-assembly can act as an AMP-regulating mechanism, and, vice versa, that human amyloids play a role
Autor:
Meytal Landau, Peleg Ragonis-Bachar
Publikováno v:
Current Opinion in Structural Biology. 68:184-193
The amyloid state of protein aggregation is associated with neurodegenerative and systemic diseases but can play physiological roles in many organisms, including as stress granules and virulence determinants. The recent resolution revolution in cryog
Short helical antimicrobial peptides forming inter-molecular disulfide bonds are selected against in nature, and were utilized here to design switchable antimicrobials via the formation of functional supramolecular fibrils. Specifically, using the av
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c2b9777b072dc170feff64be83eeafbf
https://doi.org/10.21203/rs.3.rs-578319/v1
https://doi.org/10.21203/rs.3.rs-578319/v1