L
Lucía B. Chemes
Researcher at National Scientific and Technical Research Council
Publications - 44
Citations - 1871
Lucía B. Chemes is an academic researcher from National Scientific and Technical Research Council. The author has contributed to research in topics: Short linear motif & Eukaryotic Linear Motif resource. The author has an hindex of 16, co-authored 39 publications receiving 1191 citations. Previous affiliations of Lucía B. Chemes include Facultad de Ciencias Exactas y Naturales & National University of General San Martín.
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Journal ArticleDOI
The eukaryotic linear motif resource ELM: 10 years and counting
Holger Dinkel,Kim Van Roey,Sushama Michael,Norman E. Davey,Robert J. Weatheritt,Diana Born,Tobias Speck,Daniel Krüger,Gleb Grebnev,Marta Kubań,Marta Strumillo,Bora Uyar,Aidan Budd,Brigitte Altenberg,Markus Seiler,Lucía B. Chemes,Lucía B. Chemes,Juliana Glavina,Ignacio E. Sánchez,Francesca Diella,Toby J. Gibson +20 more
TL;DR: The eukaryotic linear motif (ELM) resource is a hub for collecting, classifying and curating information about short linear motifs (SLiMs) and detailed information about motif-mediated interactions has been annotated and made available in standard exchange formats.
Journal ArticleDOI
ELM-the eukaryotic linear motif resource in 2020.
Manjeet Kumar,Marc Gouw,Sushama Michael,Hugo Sámano-Sánchez,Rita Pancsa,Juliana Glavina,Athina Diakogianni,Jesús Alvarado Valverde,Dayana Bukirova,Jelena Čalyševa,Nicolas Palopoli,Norman E. Davey,Lucía B. Chemes,Toby J. Gibson +13 more
TL;DR: The eukaryotic linear motif resource is a repository of manually curated experimentally validated short linear motifs (SLiMs) and the current release of the ELM database contains 289 motif classes and 3523 individual protein motif instances manually curated from 3467 scientific publications.
Journal ArticleDOI
The eukaryotic linear motif resource – 2018 update
Marc Gouw,Sushama Michael,Hugo Sámano-Sánchez,Manjeet Kumar,András Zeke,Benjamin Lang,Benoit Bely,Lucía B. Chemes,Lucía B. Chemes,Lucía B. Chemes,Norman E. Davey,Ziqi Deng,Francesca Diella,Clara-Marie Gürth,Ann-Kathrin Huber,Stefan Kleinsorg,Lara S. Schlegel,Nicolas Palopoli,Kim Van Roey,Brigitte Altenberg,Attila Reményi,Holger Dinkel,Toby J. Gibson +22 more
TL;DR: The latest additions to the eukaryotic linear motif (ELM) database are presented including 32 new motif classes, and new features including Uniprot and Reactome integration.
Journal ArticleDOI
DisProt: intrinsic protein disorder annotation in 2020.
András Hatos,Borbála Hajdu-Soltész,Alexander Miguel Monzon,Nicolas Palopoli,Lucía Álvarez,Burcu Aykac-Fas,Claudio Bassot,Guillermo Ignacio Benitez,Martina Bevilacqua,Anastasia Chasapi,Lucía B. Chemes,Norman E. Davey,Radoslav Davidovic,A. Keith Dunker,Arne Elofsson,Julien Gobeill,Nicolás Sebastián González Foutel,Govindarajan Sudha,Mainak Guharoy,Mainak Guharoy,Tamas L. Horvath,Valentin Iglesias,Andrey V. Kajava,Orsolya P Kovacs,John Lamb,Matteo Lambrughi,Tamas Lazar,Tamas Lazar,Jeremy Y Leclercq,Emanuela Leonardi,Sandra Macedo-Ribeiro,Mauricio Macossay-Castillo,Mauricio Macossay-Castillo,Emiliano Maiani,José A. Manso,Cristina Marino-Buslje,Elizabeth Martínez-Pérez,Bálint Mészáros,Ivan Mičetić,Giovanni Minervini,Nikoletta Murvai,Marco Necci,Christos A. Ouzounis,Mátyás Pajkos,Lisanna Paladin,Rita Pancsa,Elena Papaleo,Gustavo Parisi,Emilie Pasche,Pedro Pereira,Vasilis J. Promponas,Jordi Pujols,Federica Quaglia,Patrick Ruch,Marco Salvatore,Eva Schad,Beáta Szabó,Tamás Szaniszló,Stella Tamana,Agnes Tantos,Nevena Veljkovic,Salvador Ventura,Wim F. Vranken,Wim F. Vranken,Zsuzsanna Dosztányi,Peter Tompa,Peter Tompa,Peter Tompa,Silvio C. E. Tosatto,Damiano Piovesan +69 more
TL;DR: Recent developments with DisProt (version 8), including the doubling of protein entries, a new disorder ontology, improvements of the annotation format and a completely new website are reported.
Book ChapterDOI
Circular dichroism techniques for the analysis of intrinsically disordered proteins and domains.
TL;DR: This chapter presents the basic methodology for performing Far-UV CD measurements on a protein of interest and for identifying and characterizing intrinsically disordered regions, and several protocols for the analysis of residual secondary structure present in the protein under study.