Zobrazeno 1 - 10
of 366
pro vyhledávání: '"Lisandra L. Martin"'
Autor:
Tim J. Bull, Tulika Munshi, Paula M. Lopez-Perez, Andy C. Tran, Catherine Cosgrove, Angela Bartolf, Melissa Menichini, Laura Rindi, Lena Parigger, Nermina Malanovic, Karl Lohner, Carl J. H. Wang, Anam Fatima, Lisandra L. Martin, Semih Esin, Giovanna Batoni, Kai Hilpert
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 24, p 17555 (2023)
The culture confirmation of Mycobacterium tuberculosis (MTB) remains the gold standard for the diagnosis of Tuberculosis (TB) with culture conversion representing proof of cure. However, over 40% of TB samples fail to isolate MTB even though many pat
Externí odkaz:
https://doaj.org/article/fb362e1b73c343efbdaff60a49579bd6
Publikováno v:
Data in Brief, Vol 45, Iss , Pp 108598- (2022)
Nanostructured surfaces are widespread in nature and are being further developed in materials science. This makes them highly relevant for biomolecules, such as peptides. In this data article, we present a curvature model and molecular dynamics (MD)
Externí odkaz:
https://doaj.org/article/728448e701d94f99978f7c8bde6058fd
Autor:
Chenyang Yin, Yuqing Li, Ziyu Liao, Zekun Wang, Chunxue Dai, Weiyun Wang, Endong Yang, Feng Guo, India R. Wright, Lisandra L. Martin, Dongdong Sun
Publikováno v:
Acta Biomaterialia. 155:491-506
Sonosensitizers that can increase the concentration of reactive oxygen species (ROS) within a tumor microenvironment is a high priority for sonodynamic therapy (SDT). In this study, a functionalized, smart nanosonosensitizer based on Au-RuO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::566831b51bc703b10e97ebff90a3feaf
https://doi.org/10.1016/j.actbio.2022.11.037
https://doi.org/10.1016/j.actbio.2022.11.037
Publikováno v:
Physical Chemistry Chemical Physics. 25:12134-12147
The formation of helical intermediates and an increase in local concentration in peptide aggregates appear to be crucial in the amyloid formation of amyloidogenic amphibian peptide uperin-3.5.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::90243bc1062fc3b817faf1a22d92450c
https://doi.org/10.1039/d3cp00104k
https://doi.org/10.1039/d3cp00104k
Lipid oxidation controls peptide self-assembly near membranes through a surface attraction mechanism
Autor:
Torsten John, Stefania Piantavigna, Tiara J. A. Dealey, Bernd Abel, Herre Jelger Risselada, Lisandra L. Martin
Publikováno v:
Chemical Science. 14:3730-3741
Oxidized model membranes have differential effects on peptide fibril formation, driven by surface attraction, peptide charge and secondary structure stabilization.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::88aa5cc77085977684b16fbeaa6283a1
https://doi.org/10.1039/d3sc00159h
https://doi.org/10.1039/d3sc00159h
Publikováno v:
Food & Function.
Mammalian milk proteins are known to encrypt antimicrobial peptides (AMPs) which can be passively released and exert bioactivity in the gastrointestinal and cardiovascular systems pre- or post-absorption, respectively.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fce87fb6d93df8b891702f540d216773
https://doi.org/10.1039/d3fo00748k
https://doi.org/10.1039/d3fo00748k
Publikováno v:
Chemistry – A European Journal. 27:12922-12939
Membrane proteins (MPs) play a pivotal role in cellular function and are therefore predominant pharmaceutical targets. Although detailed understanding of MP structure and mechanistic activity is invaluable for rational drug design, challenges are ass
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef232ff60203418aacf8e4609fbd7e48
https://doi.org/10.1002/chem.202101572
https://doi.org/10.1002/chem.202101572
Autor:
Torsten John, Stefania Piantavigna, Tiara J. A. Dealey, Bernd Abel, Herre Jelger Risselada, Lisandra L. Martin
The self-assembly of peptides into supramolecular fibril structures has been linked to neurodegenerative diseases such as Alzheimer’s disease but has also been observed in functional roles. Peptides are physiologically exposed to crowded environmen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6d5f4db46393c6224688d2aa5f247a94
https://doi.org/10.1101/2022.08.02.502408
https://doi.org/10.1101/2022.08.02.502408
Publikováno v:
The Journal of Physical Chemistry B. 124:11659-11670
Antimicrobial peptides of the uperin 3.x family, obtained from the skin secretions of Uperoleia mjobergii, have an inherent ability to form amyloid with possible functional roles and can serve as model peptides to understand mechanistic aspects of am
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::809ec76cc0e6200e8ad22cae45ba3df2
https://doi.org/10.1021/acs.jpcb.0c10000
https://doi.org/10.1021/acs.jpcb.0c10000
Autor:
Martina E. C. Bluhm, Viktoria A. F. Schneider, Ingo eSchäfer, Stefania ePiantavigna, Tina eGoldbach, Daniel eKnappe, Peter eSeibel, Lisandra L. Martin, Edwin J. A. Veldhuizen, Ralf eHoffmann
Publikováno v:
Frontiers in Cell and Developmental Biology, Vol 4 (2016)
The Gram-negative bacterium Pseudomonas aeruginosa is a life-threatening nosocomial pathogen due to its generally low susceptibility towards antibiotics. Furthermore, many strains have acquired resistance mechanisms requiring new antimicrobials with
Externí odkaz:
https://doaj.org/article/620203145e714419b077135725faf21d