Zsuzsanna Dosztányi

Molecular Biology · 2005–2021

A researcher in the Science corpus: 24 papers; trusts 84 researchers and is trusted by 61 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 415 citations into it; #327 of 17,773 by trust here, #1,130 by citations
• Materials Chemistry — 173 citations into it; #499 of 11,513 by trust here, #2,532 by citations
• Spectroscopy — 57 citations into it; #59 of 1,674 by trust here, #99 by citations
• Cell Biology — 52 citations into it
• Computational Biology & Bioinformatics — 38 citations into it; #559 of 660 by trust here, #400 by citations
• Computational Theory and Mathematics — 16 citations into it
• Genetics — 16 citations into it
• Physiology — 11 citations into it

Whom Zsuzsanna Dosztányi trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

1. Vladimir N Uversky
2. Paul D. Thomas
3. Bálint Mészáros
4. Peter Tompa
5. István Simon
6. Peter E. Wright
7. H. J. Dyson
8. A. Keith Dunker
9. Veronika Csizmok
10. Holger Dinkel

Who trusts Zsuzsanna Dosztányi overall

1. Vladimir N Uversky
2. Zhenling Peng
3. Fanchi Meng
4. Gábor Erdös
5. Lukasz Kurgan
6. Bálint Mészáros
7. Nawar Malhis
8. Avner Schlessinger
9. Peter Tompa
10. Bin Xue

Papers from Zsuzsanna Dosztányi's perspective

Ordered by how strongly the researchers Zsuzsanna Dosztányi trusts endorse each paper. Same corpus, a different order for every researcher.

1. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life.
2. The importance of intrinsic disorder for protein phosphorylation. (Nucleic Acids Research)
3. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm.
4. Intrinsically disordered protein.
5. Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical features
6. Intrinsically Disordered Proteins in Cellular Signaling and Regulation
7. Protein data bank
8. Intrinsically unstructured proteins. (TIBS -Trends in Biochemical Sciences. Regular ed)
9. ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins (Nucleic Acids Res.)
10. DisProt: the Database of Disordered Proteins (Nucleic Acids Res.)

Their papers

• IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content (2005) — 2,006 citations
• The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. (2005) — 1,016 citations
• Bioinformatical approaches to characterize intrinsically disordered/unstructured proteins (2010) — 131 citations
• Prediction of Protein Binding Regions in Disordered Proteins (2009) — 587 citations
• InterPro in 2017—beyond protein family and domain annotations (2016) — 1,390 citations
• MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins (2017) — 194 citations
• IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018) — 1,323 citations
• D2P2: database of disordered protein predictions (2012) — 668 citations
• Molecular principles of the interactions of disordered proteins. (2007) — 294 citations
• ANCHOR: web server for predicting protein binding regions in disordered proteins (2009) — 602 citations
• Simultaneous quantification of protein order and disorder. (2017) — 113 citations
• DisProt 7.0: a major update of the database of disordered proteins (2016) — 138 citations
• MobiDB‐lite: fast and highly specific consensus prediction of intrinsic disorder in proteins (2017) — 178 citations
• DIBS: a repository of disordered binding sites mediating interactions with ordered proteins (2017) — 83 citations
• A comprehensive assessment of long intrinsic protein disorder from the DisProt database (2018) — 60 citations
• TMDET: web server for detecting transmembrane regions of proteins by using their 3D coordinates (2005) — 152 citations
• What’s in a name? Why these proteins are intrinsically disordered (2013) — 264 citations
• DisProt 7.0: a major update of the database of disordered proteins (2016) — 203 citations
• Critical assessment of protein intrinsic disorder prediction (2020) — 286 citations
• IUPred3: prediction of protein disorder enhanced with unambiguous experimental annotation and visualization of evolutionary conservation (2021) — 508 citations