Z
Zsuzsanna Dosztányi
Researcher at Eötvös Loránd University
Publications - 83
Citations - 11927
Zsuzsanna Dosztányi is an academic researcher from Eötvös Loránd University. The author has contributed to research in topics: Intrinsically disordered proteins & Protein structure. The author has an hindex of 37, co-authored 76 publications receiving 9749 citations. Previous affiliations of Zsuzsanna Dosztányi include Hungarian Academy of Sciences & Australian National University.
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Journal ArticleDOI
IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
TL;DR: The IUPred server presents a novel algorithm for predicting such regions from amino acid sequences by estimating their total pairwise interresidue interaction energy, based on the assumption that IUP sequences do not fold due to their inability to form sufficient stabilizing inter Residue interactions.
Journal ArticleDOI
InterPro in 2017-beyond protein family and domain annotations
Robert D. Finn,Teresa K. Attwood,Patricia C. Babbitt,Alex Bateman,Peer Bork,Alan Bridge,Hsin-Yu Chang,Zsuzsanna Dosztányi,Sara El-Gebali,Matthew Fraser,Julian Gough,David R. Haft,Gemma L. Holliday,Hongzhan Huang,Xiaosong Huang,Ivica Letunic,Rodrigo Lopez,Shennan Lu,Aron Marchler-Bauer,Huaiyu Mi,Jaina Mistry,Darren A. Natale,Marco Necci,Gift Nuka,Christine A. Orengo,Youngmi Park,Sebastien Pesseat,Damiano Piovesan,Simon C. Potter,Neil D. Rawlings,Nicole Redaschi,Lorna Richardson,Catherine Rivoire,Amaia Sangrador-Vegas,Christian J. A. Sigrist,Ian Sillitoe,Ben Smithers,Silvano Squizzato,Granger G. Sutton,Narmada Thanki,Paul Thomas,Silvio C. E. Tosatto,Cathy H. Wu,Ioannis Xenarios,Lai-Su L. Yeh,Siew Yit Young,Alex L. Mitchell +46 more
TL;DR: Recent developments with InterPro are reported, including the addition of two new databases, and the functionality to include residue-level annotation and prediction of intrinsic disorder, which enrich the annotations provided by InterPro, increase the overall number of residues annotated and allow more specific functional inferences.
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IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding
TL;DR: A combined web interface that allows to generate energy estimation based predictions for ordered and disordered residues by IUPred2 and for disordered binding regions by ANCHOR2 is presented and the updated web server retains the robustness of the original programs but offers several new features.
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The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins.
TL;DR: IUPred, a novel method for estimating the total pairwise interaction energy of proteins of known structure, based on a quadratic form in the amino acid composition of the protein, is presented and substantiates the concept of protein disorder.
Journal ArticleDOI
D2P2: database of disordered protein predictions
Matt E. Oates,Pedro Romero,Takashi Ishida,Mohamed Ghalwash,Marcin J. Mizianty,Bin Xue,Zsuzsanna Dosztányi,Vladimir N. Uversky,Zoran Obradovic,Lukasz Kurgan,A. Keith Dunker,Julian Gough +11 more
TL;DR: The Database of Disordered Protein Prediction (D2P2) will increase the understanding of the interplay between disorder and structure, the genomic distribution of disorder, and its evolutionary history.