Conduct a noncompartmental analysis as closely as possible to the most widely used commercial software.
             Some features are
             1) CDISC SDTM terms
             2) Automatic slope selection with the same criterion of WinNonlin(R)
             3) Supporting both 'linear-up linear-down' and 'linear-up log-down' method
             4) Interval(partial) AUCs with 'linear' or 'log' interpolation method
             * Reference: Gabrielsson J, Weiner D. Pharmacokinetic and Pharmacodynamic Data Analysis - Concepts and Applications. 5th ed. 2016. (ISBN:9198299107).

Fitting and testing probabilistic knowledge structures,
  especially the basic local independence model (BLIM, Doignon & Flamagne,
  1999) and the simple learning model (SLM), using the minimum discrepancy
  maximum likelihood (MDML) method (Heller & Wickelmaier, 2013
  <doi:10.1016/j.endm.2013.05.145>).

A tool for inferring kinase activity changes from 
    phosphoproteomics data. 'pKSEA' uses kinase-substrate 
    prediction scores to weight observed changes in 
    phosphopeptide abundance to calculate a phosphopeptide-level 
    contribution score, then sums up these contribution scores by 
    kinase to obtain a phosphoproteome-level kinase activity 
    change score (KAC score). 'pKSEA' then assesses the 
    significance of changes in predicted substrate abundances for 
    each kinase using permutation testing. This results in a 
    permutation score (pKSEA significance score) reflecting the 
    likelihood of a similarly high or low KAC from random chance, 
    which can then be interpreted in an analogous manner to an 
    empirically calculated p-value. 'pKSEA' contains default 
    databases of kinase-substrate predictions from 'NetworKIN' 
    (NetworKINPred_db) <http://networkin.info> 
    Horn, et. al (2014) <doi:10.1038/nmeth.2968>
    and of known kinase-substrate links from 'PhosphoSitePlus' 
    (KSEAdb) <https://www.phosphosite.org/>
    Hornbeck PV, et. al (2015) <doi:10.1093/nar/gku1267>.