Literature DB >> 25237391

VERMONT: Visualizing mutations and their effects on protein physicochemical and topological property conservation.

Sabrina A Silveira1, Alexandre V Fassio1,2, Valdete M Gonçalves-Almeida1, Raquel C de Melo-Minardi1, Elisa B de Lima1,2, Yussif T Barcelos1, Flávia F Aburjaile2, Laerte M Rodrigues1,2, Wagner Meira1.   

Abstract

In this paper, we propose an interactive visualization called VERMONT which tackles the problem of visualizing mutations and infers their possible effects on the conservation of physicochemical and topological properties in protein families. More specifically, we visualize a set of structure-based sequence alignments and integrate several structural parameters that should aid biologists in gaining insight into possible consequences of mutations. VERMONT allowed us to identify patterns of position-specific properties as well as exceptions that may help predict whether specific mutations could damage protein function.

Entities:  

Keywords:  Bioinformatics; Molecular Structure and Function; Mutation; Network Analysis; Visualization

Year:  2014        PMID: 25237391      PMCID: PMC4155615          DOI: 10.1186/1753-6561-8-S2-S4

Source DB:  PubMed          Journal:  BMC Proc        ISSN: 1753-6561


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2.  Vermont: a multi-perspective visual interactive platform for mutational analysis.

Authors:  Alexandre V Fassio; Pedro M Martins; Samuel da S Guimarães; Sócrates S A Junior; Vagner S Ribeiro; Raquel C de Melo-Minardi; Sabrina de A Silveira
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3.  visGReMLIN: graph mining-based detection and visualization of conserved motifs at 3D protein-ligand interface at the atomic level.

Authors:  Vagner S Ribeiro; Charles A Santana; Alexandre V Fassio; Fabio R Cerqueira; Carlos H da Silveira; João P R Romanelli; Adriana Patarroyo-Vargas; Maria G A Oliveira; Valdete Gonçalves-Almeida; Sandro C Izidoro; Raquel C de Melo-Minardi; Sabrina de A Silveira
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