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ChloroP, a neural network-based method for predicting chloroplast transit peptides and their cleavage sites.

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TLDR
An analysis of 715 Arabidopsis thaliana sequences from SWISS‐PROT suggests that the ChloroP method should be useful for the identification of putative transit peptides in genome‐wide sequence data.
Abstract
We present a neural network based method (ChloroP) for identifying chloroplast transit peptides and their cleavage sites. Using cross-validation, 88% of the sequences in our homology reduced training set were correctly classified as transit peptides or nontransit peptides. This performance level is well above that of the publicly available chloroplast localization predictor PSORT. Cleavage sites are predicted using a scoring matrix derived by an automatic motif-finding algorithm. Approximately 60% of the known cleavage sites in our sequence collection were predicted to within +/-2 residues from the cleavage sites given in SWISS-PROT. An analysis of 715 Arabidopsis thaliana sequences from SWISS-PROT suggests that the ChloroP method should be useful for the identification of putative transit peptides in genome-wide sequence data. The ChloroP predictor is available as a web-server at http://www.cbs.dtu.dk/services/ChloroP/.

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Journal ArticleDOI

Predicting subcellular localization of proteins based on their N-terminal amino acid sequence.

TL;DR: A neural network-based tool, TargetP, for large-scale subcellular location prediction of newly identified proteins has been developed and it is estimated that 10% of all plant proteins are mitochondrial and 14% chloroplastic, and that the abundance of secretory proteins, in both Arabidopsis and Homo, is around 10%.
Journal ArticleDOI

Locating proteins in the cell using TargetP, SignalP and related tools

TL;DR: The properties of three well-known N-terminal sequence motifs directing proteins to the secretory pathway, mitochondria and chloroplasts are described and a brief history of methods to predict subcellular localization based on these sorting signals and other sequence properties are sketched.
Journal ArticleDOI

Prediction of protein subcellular localization.

TL;DR: An approach based on a two‐level support vector machine (SVM) system, which performs well down to 30% sequence identity, although its performance deteriorates considerably for sequences sharing lower sequence identity and when compared with other approaches, this approach performed significantly better.
Journal ArticleDOI

Predicting subcellular localization of proteins for Gram-negative bacteria by support vector machines based on n-peptide compositions

TL;DR: This method uses the support vector machines trained by multiple feature vectors based on n‐peptide compositions to predict subcellular localization for Gram‐negative bacteria, and achieves the highest prediction rate ever reported.
References
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Journal ArticleDOI

Methods for assessing the statistical significance of molecular sequence features by using general scoring schemes

TL;DR: Using an appropriate random model, this work presents a theory that provides precise numerical formulas for assessing the statistical significance of any region with high aggregate score and examples are given of applications to a variety of protein sequences, highlighting segments with unusual biological features.
Journal ArticleDOI

The SWISS-PROT protein sequence data bank and its supplement TrEMBL

TL;DR: This supplement consists of entries in SWiss-PROT-like format derived from the translation of all coding sequences in the EMBL nucleotide sequence database, except the CDS already included in SWISS- PROT.
Journal ArticleDOI

A knowledge base for predicting protein localization sites in eukaryotic cells

TL;DR: An expert system is reported for predicting localization sites of proteins only from the information on the amino acid sequence and the source origin, which is powerful and flexible enough to be used in genome analyses.
Journal ArticleDOI

Predicting the secondary structure of globular proteins using neural network models.

TL;DR: It is concluded from computational experiments on real and artificial structures that no method based solely on local information in the protein sequence is likely to produce significantly better results for non-homologous proteins.
Journal ArticleDOI

Domain structure of mitochondrial and chloroplast targeting peptides.

TL;DR: Representative samples of mitochondrial and chloroplast targeting peptides have been analyzed in terms of amino acid composition, positional amino acid preferences and amphiphilic character and no highly conserved 'homology blocks' are found in either class of topogenic sequence.
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