Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Yizhaq Engelberg"'
Autor:
Yizhaq Engelberg, Meytal Landau
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
The human antibacterial and immunomodulatory peptide LL-37 is a hCAP-18 protein cleavage product that self-assembles. Here, the authors present the human and gorilla LL-37 (17–29) crystal structures, revealing a self-assembly of amphipathic helices
Externí odkaz:
https://doaj.org/article/32dc3f228962462da03ce14896285cc7
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$_{17–29}$
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fb961d037bb2cb33ac835482f978935
https://doi.org/10.1021/acs.biomac.1c01353
https://doi.org/10.1021/acs.biomac.1c01353
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5082455cc15af27e9c2e896ad93db280
https://pubmed.ncbi.nlm.nih.gov/35947777
https://pubmed.ncbi.nlm.nih.gov/35947777
Publikováno v:
Annual review of biochemistry. 91
The remarkable variety of microbial species of human pathogens and microbiomes generates significant quantities of secreted amyloids, which are structured protein fibrils that serve diverse functions related to virulence and interactions with the hos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea1413220ce749e3cd078c053d5daac3
https://pubmed.ncbi.nlm.nih.gov/35729071
https://pubmed.ncbi.nlm.nih.gov/35729071
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
Publikováno v:
Food Hydrocolloids. 128:107536
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4907aceefb440e4d484ef804a09ba9d2
https://doi.org/10.1016/j.foodhyd.2022.107536
https://doi.org/10.1016/j.foodhyd.2022.107536
Autor:
Meytal Landau, Yizhaq Engelberg
Publikováno v:
Nature Communications 11(1), 3894 (2020). doi:10.1038/s41467-020-17736-x
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
'Nature Communications ', vol: 11, pages: 3894-1-3894-10 (2020)
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
'Nature Communications ', vol: 11, pages: 3894-1-3894-10 (2020)
Nature Communications
Nature Communications 11(1), 3894 (2020). doi:10.1038/s41467-020-17736-x
Here, we demonstrate the self-assembly of the antimicrobial human LL-37 active core (residues 17–29) into a protein fibril of densely packed helices. The surface of the f
Here, we demonstrate the self-assembly of the antimicrobial human LL-37 active core (residues 17–29) into a protein fibril of densely packed helices. The surface of the f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c449c206229e5f22c1b08f0b1c45c924
https://bib-pubdb1.desy.de/record/442743
https://bib-pubdb1.desy.de/record/442743