List all resources, or create a new resource.

GET /api/t/?format=api&function=%22Sequence+analysis%22
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            "name": "clinod",
            "description": "The command line NoD predictor (clinod) can be run from the command line to predict Nucleolar localization sequences (NoLSs) that are short targeting sequences responsible for the localization of proteins to the nucleolus.\nThe predictor accepts a list of FASTA formatted sequences as an input and outputs the NOLS predictions as a result.\nPlease note that currently, JPred secondary structure predictions are not supported by clinod. However, we are working on it.",
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            "name": "BBTools",
            "description": "BBTools is a suite of fast, multithreaded bioinformatics tools designed for analysis of DNA and RNA sequence data. BBTools can handle common sequencing file formats such as fastq, fasta, sam, scarf, fasta+qual, compressed or raw, with autodetection of quality encoding and interleaving. It is written in Java and works on any platform supporting Java, including Linux, MacOS, and Microsoft Windows and Linux; there are no dependencies other than Java (version 7 or higher). Program descriptions and options are shown when running the shell scripts with no parameters.\n\nBBTools is open source and free for unlimited use, and is used regularly by DOE JGI and other institutions around the world.",
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                    "note": "Prediction of the impact of non-synonymous polymorphisms on protein stability from structure.",
                    "cmd": null
                }
            ],
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                    "uri": "http://edamontology.org/topic_0130",
                    "term": "Protein folding, stability and design"
                },
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                    "uri": "http://edamontology.org/topic_0199",
                    "term": "Genetic variation"
                },
                {
                    "uri": "http://edamontology.org/topic_3325",
                    "term": "Rare diseases"
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                "Mac"
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                "Bologna Biocomputing Group"
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                    "url": "https://inpsmd.biocomp.unibo.it/inpsSuite",
                    "type": [
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                    "doi": "10.1093/bioinformatics/btv291",
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                    "version": null,
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                    "metadata": {
                        "title": "INPS: Predicting the impact of non-synonymous variations on protein stability from sequence",
                        "abstract": "Motivation: A tool for reliably predicting the impact of variations on protein stability is extremely important for both protein engineering and for understanding the effects of Mendelian and somatic mutations in the genome. Next Generation Sequencing studies are constantly increasing the number of protein sequences. Given the huge disproportion between protein sequences and structures, there is a need for tools suited to annotate the effect of mutations starting from protein sequence without relying on the structure. Here, we describe INPS, a novel approach for annotating the effect of non-synonymous mutations on the protein stability from its sequence. INPS is based on SVM regression and it is trained to predict the thermodynamic free energy change upon single-point variations in protein sequences. Results: We show that INPS performs similarly to the state-of-the-art methods based on protein structure when tested in cross-validation on a non-redundant dataset. INPS performs very well also on a newly generated dataset consisting of a number of variations occurring in the tumor suppressor protein p53. Our results suggest that INPS is a tool suited for computing the effect of non-synonymous polymorphisms on protein stability when the protein structure is not available. We also show that INPS predictions are complementary to those of the state-of-the-art, structure-based method mCSM. When the two methods are combined, the overall prediction on the p53 set scores significantly higher than those of the single methods.",
                        "date": "2015-02-06T00:00:00Z",
                        "citationCount": 94,
                        "authors": [
                            {
                                "name": "Fariselli P."
                            },
                            {
                                "name": "Martelli P.L."
                            },
                            {
                                "name": "Savojardo C."
                            },
                            {
                                "name": "Casadio R."
                            }
                        ],
                        "journal": "Bioinformatics"
                    }
                },
                {
                    "doi": "10.1093/bioinformatics/btw192",
                    "pmid": "27153629",
                    "pmcid": null,
                    "type": [
                        "Primary"
                    ],
                    "version": null,
                    "note": null,
                    "metadata": {
                        "title": "INPS-MD: A web server to predict stability of protein variants from sequence and structure",
                        "abstract": "Motivation: Protein function depends on its structural stability. The effects of single point variations on protein stability can elucidate the molecular mechanisms of human diseases and help in developing new drugs. Recently, we introduced INPS, a method suited to predict the effect of variations on protein stability from protein sequence and whose performance is competitive with the available state-of-the-art tools. Results: In this article, we describe INPS-MD (Impact of Non synonymous variations on Protein Stability-Multi-Dimension), a web server for the prediction of protein stability changes upon single point variation from protein sequence and/or structure. Here, we complement INPS with a new predictor (INPS3D) that exploits features derived from protein 3D structure. INPS3D scores with Pearson's correlation to experimental ΔΔG values of 0.58 in cross validation and of 0.72 on a blind test set. The sequence-based INPS scores slightly lower than the structure-based INPS3D and both on the same blind test sets well compare with the state-of-the-art methods.",
                        "date": "2016-08-15T00:00:00Z",
                        "citationCount": 147,
                        "authors": [
                            {
                                "name": "Savojardo C."
                            },
                            {
                                "name": "Fariselli P."
                            },
                            {
                                "name": "Martelli P.L."
                            },
                            {
                                "name": "Casadio R."
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                        "journal": "Bioinformatics"
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                    "name": "Piero Fariselli",
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                    "term": "Machine learning"
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                    "uri": "http://edamontology.org/topic_0154",
                    "term": "Small molecules"
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                    "term": "Model organisms"
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                    "term": "Proteomics"
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                        "abstract": "An alarming number of fatalities caused by the COVID-19 pandemic has forced the scientific community to accelerate the process of therapeutic drug discovery. In this regard, the collaboration between biomedical scientists and experts in artificial intelligence (AI) has led to a number of in silico tools being developed for the initial screening of therapeutic molecules. All living organisms produce antiviral peptides (AVPs) as a part of their first line of defense against invading viruses. The Deep-AVPiden model proposed in this paper and its corresponding web app, deployed at https://deep-avpiden.anvil.app , is an effort toward discovering novel AVPs in proteomes of living organisms. Apart from Deep-AVPiden, a computationally efficient model called Deep-AVPiden (DS) has also been developed using the same underlying network but with point-wise separable convolutions. The Deep-AVPiden and Deep-AVPiden (DS) models show an accuracy of 90% and 88%, respectively, and both have a precision of 90%. Also, the proposed models were statistically compared using the Student’s t-test. On comparing the proposed models with the state-of-the-art classifiers, it was found that they are much better than them. To test the proposed model, we identified some AVPs in the natural defense proteins of plants, mammals, and fishes and found them to have appreciable sequence similarity with some experimentally validated antimicrobial peptides. These AVPs can be chemically synthesized and tested for their antiviral activity.",
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