Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Aleksandra Fulara"'
Publikováno v:
PLoS ONE, Vol 9, Iss 8, p e105660 (2014)
Poly-L-glutamic acid (PLGA) often serves as a model in studies on amyloid fibrils and conformational transitions in proteins, and as a precursor for synthetic biomaterials. Aggregation of PLGA chains and formation of amyloid-like fibrils was shown to
Externí odkaz:
https://doaj.org/article/edb0a946b0e842beaab3e3775467a2b6
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-14 (2018)
Scientific Reports
SCIENTIFIC REPORTS
Scientific Reports
SCIENTIFIC REPORTS
The ability of bacteria to infect a host relies in part on the secretion of molecular virulence factors across the cell envelope. Pseudomonas aeruginosa, a ubiquitous environmental bacterium causing opportunistic infections in humans, employs the typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb40482438086d01efb664fbf4fb7c0c
Autor:
Wojciech Dzwolak, Hanna Nieznanska, Timothy A. Keiderling, Aleksandra Fulara, Sławomir Wójcik, Ahmed Lakhani
Publikováno v:
The Journal of Physical Chemistry B. 115:11010-11016
Amyloid fibrils, which are often associated with certain degenerative disorders, reveal a number of intriguing spectral properties. However, the relationship between the structure of fibrils and their optical traits remains poorly understood. Poly(L-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42674fd6f9bc3cac219fdde25729dc8c
https://doi.org/10.1021/jp206271e
https://doi.org/10.1021/jp206271e
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 8, p e105660 (2014)
PLoS ONE, Vol 9, Iss 8, p e105660 (2014)
Poly-L-glutamic acid (PLGA) often serves as a model in studies on amyloid fibrils and conformational transitions in proteins, and as a precursor for synthetic biomaterials. Aggregation of PLGA chains and formation of amyloid-like fibrils was shown to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c101562b1b0ce80c38134d1fc208fea
http://europepmc.org/articles/PMC4140804
http://europepmc.org/articles/PMC4140804
Autor:
Hiroshi Imamura, Timothy A. Keiderling, Aleksandra Fulara, Wojciech Dzwolak, Łukasz Bożycki, Minoru Kato, Sławomir Wójcik, Yudai Yamaoki
Publikováno v:
The journal of physical chemistry. B. 116(17)
Under favorable conditions of pH and temperature, poly(L-glutamic acid) (PLGA) adopts different types of secondary and quaternary structures, which include spiral assemblies of amyloid-like fibrils. Heating of acidified solutions of PLGA (or PDGA) tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::471c7ce5c059c308ee8c50a4b107274a
https://pubmed.ncbi.nlm.nih.gov/22506583
https://pubmed.ncbi.nlm.nih.gov/22506583
Autor:
Aleksandra Fulara, Wojciech Dzwolak
Publikováno v:
The journal of physical chemistry. B. 114(24)
Model fibrillating homopolypeptides have been providing many insightful analogies to the clinically important phenomena of protein misfolding and amyloidogenesis. Here we show that the beta(2) structural variant of poly(l-glutamic) acid forms fibrils
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebc2e5629eebafe7a07ceb95fee921f9
https://pubmed.ncbi.nlm.nih.gov/20509699
https://pubmed.ncbi.nlm.nih.gov/20509699
Publikováno v:
The journal of physical chemistry. B. 112(29)
While thermodynamic penalties associated with protein-water interactions are the key driving force of folding, perturbed hydration of destabilized protein molecules may trigger aggregation, which in vivo often causes cellular and histological damage.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bc03d3671fddc5cd398101649dcfab9
https://pubmed.ncbi.nlm.nih.gov/18582016
https://pubmed.ncbi.nlm.nih.gov/18582016
Publikováno v:
Journal of Physical Chemistry B; Jun2008, Vol. 112 Issue 29, p8744-8747, 4p