Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Annamária F. Ángyán"'
Autor:
Annamária Kiss-Tóth, Laszlo Dobson, Bálint Péterfia, Annamária F. Ángyán, Balázs Ligeti, Gergely Lukács, Zoltán Gáspári
Publikováno v:
Entropy, Vol 21, Iss 8, p 761 (2019)
The human postsynaptic density is an elaborate network comprising thousands of proteins, playing a vital role in the molecular events of learning and the formation of memory. Despite our growing knowledge of specific proteins and their interactions,
Externí odkaz:
https://doaj.org/article/05548e5f20594cf99437d73d6b567ec5
Autor:
Annamária F. Ángyán, Zoltán Gáspári
Publikováno v:
Molecules, Vol 18, Iss 9, Pp 10548-10567 (2013)
NMR spectroscopy is the leading technique to characterize protein internal dynamics at the atomic level and on multiple time scales. However, the structural interpretation of the observables obtained by various measurements is not always straightforw
Externí odkaz:
https://doaj.org/article/e6636241eec24b1aa222e6c49b63b01e
Autor:
Zsolt Dürvanger, Eszter Boros, Zoltán Attila Nagy, Rózsa Hegedüs, Márton Megyeri, József Dobó, Péter Gál, Gitta Schlosser, Annamária F. Ángyán, Zoltán Gáspári, András Perczel, Veronika Harmat, Gábor Mező, Dóra K. Menyhárd, Gábor Pál
Publikováno v:
ACS Chemical Biology. 17:969-986
MASP-1 and MASP-2 are key activator proteases of the complement lectin pathway. The first specific mannose-binding lectin-associated serine protease (MASP) inhibitors had been developed from the 14-amino-acid sunflower trypsin inhibitor (SFTI) peptid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f3b092faa4cf89aef96103b48ea5111
https://doi.org/10.1021/acschembio.2c00114
https://doi.org/10.1021/acschembio.2c00114
Publikováno v:
Bioinformatics. 24:272-275
Summary: PRIDE-NMR is a fast novel method to relate known protein folds to NMR distance restraints. It can be used to obtain a first guess about a structure being determined, as well as to estimate the completeness or verify the correctness of NOE da
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c2946792334d71156f20ce86145b036e
https://doi.org/10.1093/bioinformatics/btm564
https://doi.org/10.1093/bioinformatics/btm564
Publikováno v:
Journal of molecular evolution. 78(5)
Proteins are elaborate biopolymers balancing between contradicting intrinsic propensities to fold, aggregate, or remain disordered. Assessing their primary structural preferences observable without evolutionary optimization has been reinforced by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f5c2eb3035b5e674986b3e825f75b5a
https://pubmed.ncbi.nlm.nih.gov/24826911
https://pubmed.ncbi.nlm.nih.gov/24826911
Publikováno v:
FEBS letters. 586(16)
Present-day proteins are believed to have evolved features to reduce the risk of aggregation. However, proteins can emerge de novo by translation of non-coding DNA segments. In this study we assess the aggregation, disorder and transmembrane propensi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4894ac74c48dd38fcc78e9c4ba63a32c
https://pubmed.ncbi.nlm.nih.gov/22728433
https://pubmed.ncbi.nlm.nih.gov/22728433
Autor:
Zoltán Gáspári, András Perczel, Dino Franklin, Somdutta Dhir, Annamária F. Ángyán, Sándor Pongor, Alessandro Pintar
Publikováno v:
Current proteinpeptide science. 11(7)
The emerging role of internal dynamics in protein fold and function requires new avenues of structure analysis. We analyzed the dynamically restrained conformational ensemble of ubiquitin generated from residual dipolar coupling data, in terms of pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ab58f2f5ad2f0378ac2a2f41bb3f759
https://pubmed.ncbi.nlm.nih.gov/20887264
https://pubmed.ncbi.nlm.nih.gov/20887264
Publikováno v:
BMC Structural Biology
BMC Structural Biology, Vol 10, Iss 1, p 39 (2010)
BMC Structural Biology, Vol 10, Iss 1, p 39 (2010)
Background In conjunction with the recognition of the functional role of internal dynamics of proteins at various timescales, there is an emerging use of dynamic structural ensembles instead of individual conformers. These ensembles are usually subst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cdb478525d5064a929cda0961e99ae3
http://hdl.handle.net/10831/91173
http://hdl.handle.net/10831/91173