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Showing 13 to 18 of 18 entries
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Recognition of LD motifs by the focal adhesion targeting domains of focal adhesion kinase and proline-rich tyrosine kinase 2-beta: Insights from molecular dynamics simulations.

Proteins

Michael E, Polydorides S, Promponas VJ, Skourides P, Archontis G.
PMID: 32776636
Proteins. 2020 Aug 10; doi: 10.1002/prot.25992. Epub 2020 Aug 10.

The focal adhesion kinase (FAK) and the proline-rich tyrosine kinase 2-beta (PYK2) are implicated in cancer progression and metastasis and represent promising biomarkers and targets for cancer therapy. FAK and PYK2 are recruited to focal adhesions (FAs) via interactions...

An intrinsically disordered proteins community for ELIXIR.

F1000Research

Davey NE, Babu MM, Blackledge M, Bridge A, Capella-Gutierrez S, Dosztanyi Z, Drysdale R, Edwards RJ, Elofsson A, Felli IC, Gibson TJ, Gutmanas A, Hancock JM, Harrow J, Higgins D, Jeffries CM, Le Mercier P, Mészáros B, Necci M, Notredame C, Orchard S, Ouzounis CA, Pancsa R, Papaleo E, Pierattelli R, Piovesan D, Promponas VJ, Ruch P, Rustici G, Romero P, Sarntivijai S, Saunders G, Schuler B, Sharan M, Shields DC, Sussman JL, Tedds JA, Tompa P, Turewicz M, Vondrasek J, Vranken WF, Wallace BA, Wichapong K, Tosatto SCE.
PMID: 31824649
F1000Res. 2019 Oct 15;8. doi: 10.12688/f1000research.20136.1. eCollection 2019.

Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) are now recognised as major determinants in cellular regulation. This white paper presents a roadmap for future e-infrastructure developments in the field of IDP research within the ELIXIR framework. The...

Annotation inconsistencies beyond sequence similarity-based function prediction - phylogeny and genome structure.

Standards in genomic sciences

Promponas VJ, Iliopoulos I, Ouzounis CA.
PMID: 26594309
Stand Genomic Sci. 2015 Nov 19;10:108. doi: 10.1186/s40793-015-0101-2. eCollection 2015.

The function annotation process in computational biology has increasingly shifted from the traditional characterization of individual biochemical roles of protein molecules to the system-wide detection of entire metabolic pathways and genomic structures. The so-called genome-aware methods broaden misannotation inconsistencies...

DisProt in 2022: improved quality and accessibility of protein intrinsic disorder annotation.

Nucleic acids research

Quaglia F, Mészáros B, Salladini E, Hatos A, Pancsa R, Chemes LB, Pajkos M, Lazar T, Peña-Díaz S, Santos J, Ács V, Farahi N, Fichó E, Aspromonte MC, Bassot C, Chasapi A, Davey NE, Davidović R, Dobson L, Elofsson A, Erdős G, Gaudet P, Giglio M, Glavina J, Iserte J, Iglesias V, Kálmán Z, Lambrughi M, Leonardi E, Longhi S, Macedo-Ribeiro S, Maiani E, Marchetti J, Marino-Buslje C, Mészáros A, Monzon AM, Minervini G, Nadendla S, Nilsson JF, Novotný M, Ouzounis CA, Palopoli N, Papaleo E, Pereira PJB, Pozzati G, Promponas VJ, Pujols J, Rocha ACS, Salas M, Sawicki LR, Schad E, Shenoy A, Szaniszló T, Tsirigos KD, Veljkovic N, Parisi G, Ventura S, Dosztányi Z, Tompa P, Tosatto SCE, Piovesan D.
PMID: 34850135
Nucleic Acids Res. 2022 Jan 07;50:D480-D487. doi: 10.1093/nar/gkab1082.

The Database of Intrinsically Disordered Proteins (DisProt, URL: https://disprot.org) is the major repository of manually curated annotations of intrinsically disordered proteins and regions from the literature. We report here recent updates of DisProt version 9, including a restyled web...

Active Surveillance-Is It Feasible for Intermediate-risk Localised Prostate Cancer?.

European urology open science

Mukherjee S, Promponas I, Petrides N, Hossain D, Abbaraju J, Madaan S.
PMID: 34337491
Eur Urol Open Sci. 2021 Jan 08;24:17-24. doi: 10.1016/j.euros.2020.12.005. eCollection 2021 Feb.

BACKGROUND: Although active surveillance (AS) is a well-recognised treatment option for localised low-risk prostate cancer (LRPC), its role in the management of localised intermediate-risk prostate cancer (IRPC) is not clear yet and the available literature is slightly contradictory.OBJECTIVE: To...

DisProt: intrinsic protein disorder annotation in 2020.

Nucleic acids research

Hatos A, Hajdu-Soltész B, Monzon AM, Palopoli N, Álvarez L, Aykac-Fas B, Bassot C, Benítez GI, Bevilacqua M, Chasapi A, Chemes L, Davey NE, Davidović R, Dunker AK, Elofsson A, Gobeill J, Foutel NSG, Sudha G, Guharoy M, Horvath T, Iglesias V, Kajava AV, Kovacs OP, Lamb J, Lambrughi M, Lazar T, Leclercq JY, Leonardi E, Macedo-Ribeiro S, Macossay-Castillo M, Maiani E, Manso JA, Marino-Buslje C, Martínez-Pérez E, Mészáros B, Mičetić I, Minervini G, Murvai N, Necci M, Ouzounis CA, Pajkos M, Paladin L, Pancsa R, Papaleo E, Parisi G, Pasche E, Barbosa Pereira PJ, Promponas VJ, Pujols J, Quaglia F, Ruch P, Salvatore M, Schad E, Szabo B, Szaniszló T, Tamana S, Tantos A, Veljkovic N, Ventura S, Vranken W, Dosztányi Z, Tompa P, Tosatto SCE, Piovesan D.
PMID: 31713636
Nucleic Acids Res. 2020 Jan 08;48:D269-D276. doi: 10.1093/nar/gkz975.

The Database of Protein Disorder (DisProt, URL: https://disprot.org) provides manually curated annotations of intrinsically disordered proteins from the literature. Here we report recent developments with DisProt (version 8), including the doubling of protein entries, a new disorder ontology, improvements...

Showing 13 to 18 of 18 entries