Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Meytal Landau"'
Autor:
Elad Arad, Kasper B. Pedersen, Orit Malka, Sisira Mambram Kunnath, Nimrod Golan, Polina Aibinder, Birgit Schiøtt, Hanna Rapaport, Meytal Landau, Raz Jelinek
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Abstract Antibiotic resistance of bacteria is considered one of the most alarming developments in modern medicine. While varied pathways for bacteria acquiring antibiotic resistance have been identified, there still are open questions concerning the
Externí odkaz:
https://doaj.org/article/2e6f4b67c7264031b3ec5edb8e5ec825
Publikováno v:
Frontiers in Molecular Biosciences, Vol 10 (2023)
Phenol-soluble modulins (PSMs) are virulent peptides secreted by staphylococci that undergo self-assembly into amyloid fibrils. This study focuses on Staphylococcus aureus PSMα1 and PSMα3, which share homologous sequences but exhibit distinct amylo
Externí odkaz:
https://doaj.org/article/13d181f429fb4b468b3d2b4a7e26eb7c
Autor:
Robert Bücker, Carolin Seuring, Cornelia Cazey, Katharina Veith, Maria García-Alai, Kay Grünewald, Meytal Landau
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
In this work the authors provide high-resolution structural support for the amyloid-antimicrobial link via functional amyloids displaying propeller-like and kinked cross-β fibrils.
Externí odkaz:
https://doaj.org/article/09b5dc12870a480fbe761c3014c1047e
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Candida Als family adhesins mediate adhesion to biological and abiotic substrates, as well as fungal cell aggregation, fungal-bacterial co-aggregation and biofilm formation. The activity of at least two family members, Als5 and Als1, is dependent on
Externí odkaz:
https://doaj.org/article/24853ede8f134fe4b96affab53b18bcc
Autor:
Meytal Landau
Publikováno v:
Microorganisms, Vol 11, Iss 5, p 1201 (2023)
Various organisms, including bacteria, protists, fungi, plants, and animals, secrete proteins and peptides that self-assemble into ordered amyloid fibrils that perform different physiological functions [...]
Externí odkaz:
https://doaj.org/article/c0b33883766248ee9523c3eb53512e1b
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:
Nature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
The phenol-soluble modulin PSMα3 secreted by Staphylococcus aureus forms cross-α amyloid-like fibrils. Here the authors reveal the amyloid polymorphism of PSMs by presenting the cross-β amyloid fibril structures of the biofilm-associated PSMα1 an
Externí odkaz:
https://doaj.org/article/263dbdbb26f444669b339f1d02fc76c4
Autor:
Michal Mayer, Yulia Matiuhin, Mickal Nawatha, Orly Tabachnikov, Inbar Fish, Nili Schutz, Hay Dvir, Meytal Landau
Publikováno v:
Biomolecules, Vol 11, Iss 8, p 1196 (2021)
BceF is a bacterial tyrosine kinase (BY-kinase) from Burkholderia cepacia, a Gram-negative bacterium accountable for respiratory infections in immunocompromised and cystic fibrosis patients. BceF is involved in the production of exopolysaccharides se
Externí odkaz:
https://doaj.org/article/6fde84d8554d4f96bed7d8f7cd2ac8e5
Autor:
Einav Ratzon, Itai Bloch, Meshel Nicola, Elad Cohen, Nili Ruimi, Nesly Dotan, Meytal Landau, Maayan Gal
Publikováno v:
ACS Omega, Vol 2, Iss 8, Pp 4398-4410 (2017)
Externí odkaz:
https://doaj.org/article/132bc106bb2a43b098f036c785cdff6e
Autor:
Sergei Perov, Ofir Lidor, Nir Salinas, Nimrod Golan, Einav Tayeb-Fligelman, Maya Deshmukh, Dieter Willbold, Meytal Landau
Publikováno v:
PLoS Pathogens, Vol 15, Iss 8, p e1007978 (2019)
Curli amyloid fibrils secreted by Enterobacteriaceae mediate host cell adhesion and contribute to biofilm formation, thereby promoting bacterial resistance to environmental stressors. Here, we present crystal structures of amyloid-forming segments fr
Externí odkaz:
https://doaj.org/article/83c99c52c5774ca1866971d3d107d047