Zobrazeno 1 - 10
of 96
pro vyhledávání: '"Brigita Urbanc"'
Autor:
Rachit Pandey, Brigita Urbanc
Publikováno v:
Biomolecules, Vol 14, Iss 7, p 774 (2024)
Alzheimer’s disease (AD) is a neurological disorder associated with amyloid β-protein (Aβ) assembly into toxic oligomers. In addition to the two predominant alloforms, Aβ1−40 and Aβ1−42, other C-terminally truncated Aβ peptides, including
Externí odkaz:
https://doaj.org/article/b189b886963f4638ab6817ca7cb01556
Publikováno v:
Biomolecules, Vol 10, Iss 8, p 1121 (2020)
Conformational preferences of amino acid residues in water are determined by the backbone and side-chain properties. Alanine is known for its high polyproline II (pPII) propensity. The question of relative contributions of the backbone and side chain
Externí odkaz:
https://doaj.org/article/3eb94765a416488c9e17002ace34b097
Autor:
Bogdan Barz, Brigita Urbanc
Publikováno v:
PLoS ONE, Vol 7, Iss 4, p e34345 (2012)
Amyloid β-protein (Aβ) is central to the pathology of Alzheimer's disease. A 5% difference in the primary structure of the two predominant alloforms, Aβ(1-40) and Aβ(1-42), results in distinct assembly pathways and toxicity properties. Discrete m
Externí odkaz:
https://doaj.org/article/decd49a6eec9424a95e50f3ee96432b1
Publikováno v:
Physical chemistry chemical physics : PCCP.
It is well established that amyloid β-protein (Aβ) self-assembly is involved in triggering of Alzheimer's disease. On the other hand, evidence of physiological function of Aβ interacting with lipids has only begun to emerge. Details of Aβ-lipid i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68d96b2cc5f7c6dbc21fbbb54e3efd3d
https://pubmed.ncbi.nlm.nih.gov/36602150
https://pubmed.ncbi.nlm.nih.gov/36602150
Publikováno v:
The Journal of Physical Chemistry B. 125:6897-6911
Protein self-assembly plays an important role in cellular processes. Whereas molecular dynamics (MD) represents a powerful tool in studying assembly mechanisms, its predictions depend on the accuracy of underlying force fields, which are known to ove
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6e5433e9b7b65f3c1deb581987c2f24
https://doi.org/10.1021/acs.jpcb.1c04589
https://doi.org/10.1021/acs.jpcb.1c04589
Publikováno v:
Physical chemistry chemical physics : PCCP. 24(5)
Molecular dynamics (MD) is a powerful tool for studying intrinsically disordered proteins, however, its reliability depends on the accuracy of the force field. We assess Amber ff19SB, Amber ff14SB, OPLS-AA/M, and CHARMM36m with respect to their capac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f53306d4ceecc7102b9281c5979a10c7
https://pubmed.ncbi.nlm.nih.gov/35048087
https://pubmed.ncbi.nlm.nih.gov/35048087
Publikováno v:
Journal of Chemical Theory and Computation. 16:510-527
We examine the ability of six molecular dynamics (MD) force fields (Amber ff14SB, Amber ff99SBnmr1, Amber ff03ws, OPLS-AA/L, OPLS-AA/M, and CHARMM36) to reproduce conformational ensembles of the central alanine in GAG and AAA in a way that is consist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f59186f3dbc3a6a7507db4c96aaf34c
https://doi.org/10.1021/acs.jctc.9b00588
https://doi.org/10.1021/acs.jctc.9b00588
Publikováno v:
The Journal of Physical Chemistry B. 123:1068-1084
Amyloid β-protein (Aβ) oligomers play a seminal role in Alzheimer's disease (AD). Cross-linking (X-linking), which can be used to determine Aβ oligomer size distributions experimentally, was reported to stabilize Aβ oligomers. Aβ oligomers X-lin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::109c44f6431682b7165b7ddbfd94d250
https://doi.org/10.1021/acs.jpcb.8b12120
https://doi.org/10.1021/acs.jpcb.8b12120
Autor:
Brigita Urbanc
Publikováno v:
The journal of physical chemistry. B. 125(5)
Amyloid β-protein (Aβ) oligomers are broadly viewed as the proximate mediators of toxicity in Alzheimer's disease (AD). Recent studies, however, provide substantial evidence that Aβ is involved in protection and repair of the central nervous syste
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a53327b37648b8d1eaa50d7f6af61cd8
https://pubmed.ncbi.nlm.nih.gov/33440940
https://pubmed.ncbi.nlm.nih.gov/33440940
Publikováno v:
Biophys J
Intrinsically disordered proteins and intrinsically disordered regions are frequently enriched in charged amino acids. Intrinsically disordered regions are regularly involved in important biological processes in which one or more charged residues is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd1b5a64f729b30d77dcf2e243d8d09b
https://europepmc.org/articles/PMC7896027/
https://europepmc.org/articles/PMC7896027/
