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Luiz G. Horita

dblp:92/1209 · DBLP profile ↗
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2ranked-venue papers
0as first author
0since 2021 · last 2004
—ORCID · none

Domains — the database's venue-derived domains; a paper can count in several

Applied, interdisciplinary, general and emerging computing · 2

Expertise — from the expertise taxonomy: the topics of the expert's papers under the CCF categories. A weight counts papers with recency: 1 for a paper about the topic, 0.3 when the topic is its context, halved every five years.

Interdisciplinary, comprehensive, and emerging computing
2 papers
Bioinformatics and computational biology · 100%

Topics — the 4 heaviest of 4, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology › structural bioinformatics
protein structure
0.122004
Defining 3D residue environment in protein structures using SCORPION and FORMIGA · Bioinform. 2004
ConSSeq: a web-based application for analysis of amino acid conservation based on HSSP database and within context of structure · Bioinform. 2004
Bioinformatics and computational biology › protein sequence analysis
residue conservation
0.012004
ConSSeq: a web-based application for analysis of amino acid conservation based on HSSP database and within context of structure · Bioinform. 2004
Bioinformatics and computational biology
sequence alignment
0.012004
ConSSeq: a web-based application for analysis of amino acid conservation based on HSSP database and within context of structure · Bioinform. 2004
Bioinformatics and computational biology › protein structure prediction
protein folding
0.012004
Defining 3D residue environment in protein structures using SCORPION and FORMIGA · Bioinform. 2004

Methods — techniques the papers use, named apart from their topics

relative entropy · 0.0knowledge-based force fields · 0.0
YearPublicationVenuePosition
2004 ConSSeq: a web-based application for analysis of amino acid conservation based on HSSP database and within context of structure
abstract
SUMMARY: A web-based application to analyze protein amino acids conservation-Consensus Sequence (ConSSeq) is presented. ConSSeq graphically represents information about amino acid conservation based on sequence alignments reported in homology-derived structures of proteins. Beyond the relative entropy for each position in the alignment, ConSSeq also presents the consensus sequence and information about the amino acids, which are predominant at each position of the alignment. ConSSeq is part of the STING Millennium Suite and is implemented as a Java Applet. AVAILABILITY: http://sms.cbi.cnptia.embrapa.br/SMS/STINGm/consseq/, http://trantor.bioc.columbia.edu/SMS/STINGm/consseq/, http://mirrors.rcsb.org//SMS/STINGm/consseq/, http://www.es.embnet.org/SMS/STINGm/consseq/ and http://www.ar.embnet.org/SMS/STINGm/consseq/
Roberto H. Higa, Arnaldo J. Montagner, Roberto C. Togawa, Paula R. Kuser, Michel Eduardo Beleza Yamagishi, Adauto L. Mancini, Georgios Joannis Pappas Jr., Ronald T. Miura, Luiz G. Horita, Goran Neshich
Bioinform.9
2004 Defining 3D residue environment in protein structures using SCORPION and FORMIGA
abstract
SUMMARY: Two web-based applications to analyze amino acids three-dimensional (3D) local environment within protein structures-SCORPION and FORMIGA-are presented. SCORPION and FORMIGA produce a graphical presentation for simple statistical data showing the frequency of residue occurrence within a given sphere (defined here as the 3D contacts). The center of that sphere is placed at the Calpha and at the last heavy atom in the side chain of the selected amino acid. Further depth of detail is given in terms of a secondary structure to which the profiled amino acid belongs. Results obtained with those two applications are relevant for estimating the importance of the amino acid 3D local environment for protein folding and stability. Effectively, SCORPION and FORMIGA construct knowledge-based force fields. The difference between SCORPION and FORMIGA is in that the latter operates on protein interfaces, while the former only functions for a single protein chain. Both applications are implemented as stand-alone components of STING Millennium Suite. AVAILABILITY: http://sms.cbi.cnptia.embrapa.br/SMS, http://trantor.bioc.columbia.edu/SMS, http://mirrors.rcsb.org/SMS, http://www.es.embnet.org/SMS and http://www.ar.embnet.org/SMS. [options: Scorpion, Formiga]
Roberto H. Higa, Adilton G. Oliveira, Luiz G. Horita, Ronald T. Miura, Marcus K. Inoue, Paula R. Kuser, Adauto L. Mancini, Michel Eduardo Beleza Yamagishi, Roberto C. Togawa, Goran Neshich
Bioinform.3