General Purpose Coarse-Grained Force Field 
An interesting study from the Wilson lab shows how Martini 3 can reproduce complex chromonic self-assembly, whereas specifically parameterized CG models obtained with force matching (FM) cannot. To see the details and the underlying reasons for the failure of FM, see: Yu & Wilson, J. Mol. Liq., online.
The challenge for modern day force fields to correctly describe self-assembling supramolecular polymers is nicely illustrated in a paper from Piskorz et al., JCIM, online. Most atomistic force fields, as well as standard Martini, are not capable of maintaining the fibrous structure of the compound 1,3,5-trisamidocyclohexane. Only Charmm-Drude and GAFF perform well, along with ..... polarizable Martini !
Components from all three domains of life are used by the Maglia group to fabricate an integrated multiprotein complex that controls the unfolding and threading of individual proteins across a nanopore.
Multiscale models including Martini contributed to unravel the details of the structure and functioning of this megacomplex.
For details, see: Zhang et al., Nature Chem. 2021.
Watch in molecular detail how vitamins are delivered to your skin !
Nice work from Machado et al., just published in Nanoscale.
The Vanni lab performed a critical assessment on the performance of Martini 3 to model binding of peripheral proteins to membranes. Conclusion in short: Martini is "mostly able to correctly characterize the membrane binding behavior of peripheral proteins, and to identify key residues found to disrupt membrane binding in mutagenesis experiments", and "While preliminary, our investigations suggest that transferable chemical-specific CG force fields have enormous potential in the characterization of the membrane binding process by peripheral proteins, and that the identification of negative results could help drive future force field development efforts". Not bad at all ! For more details, see the full publication.
A brand new tool to detect topological changes in lipid systems, as part of the PhD work of Bart Bruininks and Albert Thie: pubs.acs.org/doi/abs/10.102