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  • 1
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 2015
    In:  BMC Genomics Vol. 16, No. S8 ( 2015-12)
    In: BMC Genomics, Springer Science and Business Media LLC, Vol. 16, No. S8 ( 2015-12)
    Type of Medium: Online Resource
    ISSN: 1471-2164
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2015
    detail.hit.zdb_id: 2041499-7
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 2016
    In:  BMC Genomics Vol. 17, No. S2 ( 2016-6)
    In: BMC Genomics, Springer Science and Business Media LLC, Vol. 17, No. S2 ( 2016-6)
    Type of Medium: Online Resource
    ISSN: 1471-2164
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2016
    detail.hit.zdb_id: 2041499-7
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 2019
    In:  BMC Genomics Vol. 20, No. S8 ( 2019-7)
    In: BMC Genomics, Springer Science and Business Media LLC, Vol. 20, No. S8 ( 2019-7)
    Type of Medium: Online Resource
    ISSN: 1471-2164
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2019
    detail.hit.zdb_id: 2041499-7
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2019
    In:  Nucleic Acids Research Vol. 47, No. W1 ( 2019-07-02), p. W136-W141
    In: Nucleic Acids Research, Oxford University Press (OUP), Vol. 47, No. W1 ( 2019-07-02), p. W136-W141
    Abstract: As the amount of genomic variation data increases, tools that are able to score the functional impact of single nucleotide variants become more and more necessary. While there are several prediction servers available for interpreting the effects of variants in the human genome, only few have been developed for other species, and none were specifically designed for species of veterinary interest such as the dog. Here, we present Fido-SNP the first predictor able to discriminate between Pathogenic and Benign single-nucleotide variants in the dog genome. Fido-SNP is a binary classifier based on the Gradient Boosting algorithm. It is able to classify and score the impact of variants in both coding and non-coding regions based on sequence features within seconds. When validated on a previously unseen set of annotated variants from the OMIA database, Fido-SNP reaches 88% overall accuracy, 0.77 Matthews correlation coefficient and 0.91 Area Under the ROC Curve.
    Type of Medium: Online Resource
    ISSN: 0305-1048 , 1362-4962
    RVK:
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2019
    detail.hit.zdb_id: 1472175-2
    SSG: 12
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  • 5
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2011
    In:  Bioinformatics Vol. 27, No. 13 ( 2011-07-01), p. 1741-1748
    In: Bioinformatics, Oxford University Press (OUP), Vol. 27, No. 13 ( 2011-07-01), p. 1741-1748
    Abstract: Motivation: Widespread availability of low-cost, full genome sequencing will introduce new challenges for bioinformatics. Results: This review outlines recent developments in sequencing technologies and genome analysis methods for application in personalized medicine. New methods are needed in four areas to realize the potential of personalized medicine: (i) processing large-scale robust genomic data; (ii) interpreting the functional effect and the impact of genomic variation; (iii) integrating systems data to relate complex genetic interactions with phenotypes; and (iv) translating these discoveries into medical practice. Contact:  russ.altman@stanford.edu Supplementary information:  Supplementary data are available at Bioinformatics online.
    Type of Medium: Online Resource
    ISSN: 1367-4811 , 1367-4803
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2011
    detail.hit.zdb_id: 1468345-3
    SSG: 12
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  • 6
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2021
    In:  Bioinformatics Vol. 36, No. 24 ( 2021-04-05), p. 5709-5711
    In: Bioinformatics, Oxford University Press (OUP), Vol. 36, No. 24 ( 2021-04-05), p. 5709-5711
    Abstract: Identifying pathogenic variants and annotating them is a major challenge in human genetics, especially for the non-coding ones. Several tools have been developed and used to predict the functional effect of genetic variants. However, the calibration assessment of the predictions has received little attention. Calibration refers to the idea that if a model predicts a group of variants to be pathogenic with a probability P, it is expected that the same fraction P of true positive is found in the observed set. For instance, a well-calibrated classifier should label the variants such that among the ones to which it gave a probability value close to 0.7, approximately 70% actually belong to the pathogenic class. Poorly calibrated algorithms can be misleading and potentially harmful for clinical decision making. Avaliability and implementation The dataset used for testing the methods is available through the DOI:10.5281/zenodo.4448197. Supplementary information Supplementary data are available at Bioinformatics online.
    Type of Medium: Online Resource
    ISSN: 1367-4803 , 1367-4811
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2021
    detail.hit.zdb_id: 1468345-3
    SSG: 12
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  • 7
    Online Resource
    Online Resource
    Oxford University Press (OUP) ; 2008
    In:  Bioinformatics Vol. 24, No. 16 ( 2008-08-15), p. i112-i118
    In: Bioinformatics, Oxford University Press (OUP), Vol. 24, No. 16 ( 2008-08-15), p. i112-i118
    Abstract: Motivation: The recent discovery of tiny RNA molecules such as µRNAs and small interfering RNA are transforming the view of RNA as a simple information transfer molecule. Similar to proteins, the native three-dimensional structure of RNA determines its biological activity. Therefore, classifying the current structural space is paramount for functionally annotating RNA molecules. The increasing numbers of RNA structures deposited in the PDB requires more accurate, automatic and benchmarked methods for RNA structure comparison. In this article, we introduce a new algorithm for RNA structure alignment based on a unit-vector approach. The algorithm has been implemented in the SARA program, which results in RNA structure pairwise alignments and their statistical significance. Results: The SARA program has been implemented to be of general applicability even when no secondary structure can be calculated from the RNA structures. A benchmark against the ARTS program using a set of 1275 non-redundant pairwise structure alignments results in ¡«6% extra alignments with at least 50% structurally superposed nucleotides and base pairs. A first attempt to perform RNA automatic functional annotation based on structure alignments indicates that SARA can correctly assign the deepest SCOR classification to & gt;60% of the query structures. Availability: The SARA program is freely available through a World Wide Web server http://sgu.bioinfo.cipf.es/services/SARA/ Contact:  mmarti@cipf.es
    Type of Medium: Online Resource
    ISSN: 1367-4811 , 1367-4803
    Language: English
    Publisher: Oxford University Press (OUP)
    Publication Date: 2008
    detail.hit.zdb_id: 1468345-3
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    Wiley ; 2003
    In:  Proteins: Structure, Function, and Bioinformatics Vol. 54, No. 2 ( 2003-11-24), p. 351-360
    In: Proteins: Structure, Function, and Bioinformatics, Wiley, Vol. 54, No. 2 ( 2003-11-24), p. 351-360
    Type of Medium: Online Resource
    ISSN: 0887-3585
    RVK:
    Language: English
    Publisher: Wiley
    Publication Date: 2003
    detail.hit.zdb_id: 1475032-6
    SSG: 12
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  • 9
    In: Genes, MDPI AG, Vol. 12, No. 6 ( 2021-06-12), p. 911-
    Abstract: Several studies have linked disruptions of protein stability and its normal functions to disease. Therefore, during the last few decades, many tools have been developed to predict the free energy changes upon protein residue variations. Most of these methods require both sequence and structure information to obtain reliable predictions. However, the lower number of protein structures available with respect to their sequences, due to experimental issues, drastically limits the application of these tools. In addition, current methodologies ignore the antisymmetric property characterizing the thermodynamics of the protein stability: a variation from wild-type to a mutated form of the protein structure (XW→XM) and its reverse process (XM→XW) must have opposite values of the free energy difference (ΔΔGWM=−ΔΔGMW). Here we propose ACDC-NN-Seq, a deep neural network system that exploits the sequence information and is able to incorporate into its architecture the antisymmetry property. To our knowledge, this is the first convolutional neural network to predict protein stability changes relying solely on the protein sequence. We show that ACDC-NN-Seq compares favorably with the existing sequence-based methods.
    Type of Medium: Online Resource
    ISSN: 2073-4425
    Language: English
    Publisher: MDPI AG
    Publication Date: 2021
    detail.hit.zdb_id: 2527218-4
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  • 10
    Online Resource
    Online Resource
    Frontiers Media SA ; 2021
    In:  Frontiers in Molecular Biosciences Vol. 8 ( 2021-3-25)
    In: Frontiers in Molecular Biosciences, Frontiers Media SA, Vol. 8 ( 2021-3-25)
    Abstract: During the last years, the increasing number of DNA sequencing and protein mutagenesis studies has generated a large amount of variation data published in the biomedical literature. The collection of such data has been essential for the development and assessment of tools predicting the impact of protein variants at functional and structural levels. Nevertheless, the collection of manually curated data from literature is a highly time consuming and costly process that requires domain experts. In particular, the development of methods for predicting the effect of amino acid variants on protein stability relies on the thermodynamic data extracted from literature. In the past, such data were deposited in the ProTherm database, which however is no longer maintained since 2013. For facilitating the collection of protein thermodynamic data from literature, we developed the semi-automatic tool ThermoScan. ThermoScan is a text mining approach for the identification of relevant thermodynamic data on protein stability from full-text articles. The method relies on a regular expression searching for groups of words, including the most common conceptual words appearing in experimental studies on protein stability, several thermodynamic variables, and their units of measure. ThermoScan analyzes full-text articles from the PubMed Central Open Access subset and calculates an empiric score that allows the identification of manuscripts reporting thermodynamic data on protein stability. The method was optimized on a set of publications included in the ProTherm database, and tested on a new curated set of articles, manually selected for presence of thermodynamic data. The results show that ThermoScan returns accurate predictions and outperforms recently developed text-mining algorithms based on the analysis of publication abstracts. Availability: The ThermoScan server is freely accessible online at https://folding.biofold.org/thermoscan . The ThermoScan python code and the Google Chrome extension for submitting visualized PMC web pages to the ThermoScan server are available at https://github.com/biofold/ThermoScan .
    Type of Medium: Online Resource
    ISSN: 2296-889X
    Language: Unknown
    Publisher: Frontiers Media SA
    Publication Date: 2021
    detail.hit.zdb_id: 2814330-9
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