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Dataset of shell commands used by participants of hands-on cybersecurity training.

ABSTRACT: We present a dataset of 13446 shell commands from 175 participants who attended cybersecurity training and solved assignments in the Linux terminal. Each acquired data record contains a command with its arguments and metadata, such as a timestamp, working directory, and host identification in the emulated training infrastructure. The commands were captured in Bash, ZSH, and Metasploit shells. The data are stored as JSON records, enabling vast possibilities for their further use in research and development. These include educational data mining, learning analytics, student modeling, and evaluating machine learning models for intrusion detection. The data were collected from 27 cybersecurity training sessions using an open-source logging toolset and two open-source interactive learning environments. Researchers and developers may use the dataset or deploy the learning environments with the logging toolset to generate their own data in the same format. Moreover, we provide a set of common analytical queries to facilitate the exploratory analysis of the dataset.

SUBMITTER: Svabensky V

PROVIDER: S-EPMC8479389 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:BackgroundAmyloids are proteins capable of forming aberrant intramolecular contact sites, characteristic of beta zipper configuration. Amyloids can underlie serious health conditions, e.g. Alzheimer's or Parkinson's diseases. It has been proposed that short segments of amino acids can be responsible for protein amyloidogenicity, but no more than two hundred such hexapeptides have been experimentally found. The authors of the computational tool Pafig published in BMC Bioinformatics a method for extending the amyloid hexapeptide dataset that could be used for training and testing models. They assumed that all hexapeptides belonging to an amyloid protein can be regarded as amylopositive, while those from proteins never reported as amyloid are always amylonegative. Here we show why the above described method of extending datasets is wrong and discuss the reasons why the incorrect data could lead to falsely correct classification.ResultsThe amyloid classification of hexapeptides by Pafig was confronted with the classification results from different state of the art computational methods and the outputs of all methods were studied by clustering analysis. The clustering methods show that Pafig is an outlier with regard to other approaches. Our study of the statistical patterns of its training and testing datasets showed a strong bias towards STVIIE hexapeptide in their positive part. Different statistical patterns of seemingly amylo-positive and -negative hexapeptides allow for a repeatable classification, which is not related to amyloid propensity of the hexapetides.ConclusionsOur study on recognition of amyloid hexapeptides showed that occurrence of incidental patterns in wrongly selected datasets can produce falsely correct results of classification. The assumption that all hexapeptides belonging to amyloid protein can be regarded as amylopositive and those from proteins never reported as amyloid are always amylonegative is not supported by any other computational method. This is in line with experimental observations that amyloid propensity of a full protein can result from only one amyloidogenic fragment in this protein, while the occurrence of amyliodogenic part that is well hidden inside the protein may never lead to fibril formation. This leads to the conclusion that Pafig does not provide correct classification with regard to amyloidogenicity.

Dataset Information

Dataset of shell commands used by participants of hands-on cybersecurity training.

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