@article {68965,
	title = {Multiscale head anatomy of Megaphragma (Hymenoptera: Trichogrammatidae).},
	journal = {Arthropod Structure and Development},
	volume = {76},
	year = {2023},
	month = {2023 Sep 01},
	pages = {101299},
	abstract = {<p>Methods of three-dimensional electron microscopy have been actively developed recently and open up great opportunities for morphological work. This approach is especially useful for studying microinsects, since it is possible to obtain complete series of high-resolution sections of a whole insect. Studies on the genus Megaphragma are especially important, since the unique phenomenon of lysis of most of the neuron nuclei was discovered in species of this genus. In this study we reveal the anatomical structure of the head of Megaphragma viggianii at all levels from organs to subcellular structures. Despite the miniature size of the body, most of the organ systems of M.\&nbsp;viggianii retain the structural plan and complexity of organization at all levels. The set of muscles and the well-developed stomatogastric nervous system of this species correspond to those of larger insects, and there is also a well-developed tracheal system in the head of this species. Reconstructions of the head of M.\&nbsp;viggianii at the cellular and subcellular levels were obtained, and of volumetric data were analyzed. A total of 689 nucleated cells of the head were reconstructed. The ultrastructure of M.\&nbsp;viggianii is surprisingly complex, and the evolutionary benefits of such complexity are probably among the factors limiting the further miniaturization of parasitoid wasps.</p>
},
	issn = {1873-5495},
	doi = {10.1016/j.asd.2023.101299},
	author = {Desyatirkina, Inna A and Makarova, Anastasia A and Pang, Song and Xu, C Shan and Hess, Harald and Polilov, Alexey A}
}
@article {46531,
	title = {A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics.},
	journal = {PLoS Genetics},
	volume = {11},
	year = {2015},
	month = {2015 Apr 07},
	pages = {e1005128},
	abstract = {<p>The prokaryotic tubulin homolog, FtsZ, forms a ring-like structure (FtsZ-ring) at midcell. The FtsZ-ring establishes the division plane and enables the assembly of the macromolecular division machinery (divisome). Although many molecular components of the divisome have been identified and their interactions extensively characterized, the spatial organization of these proteins within the divisome is unclear. Consequently, the physical mechanisms that drive divisome assembly, maintenance, and constriction remain elusive. Here we applied single-molecule based superresolution imaging, combined with genetic and biophysical investigations, to reveal the spatial organization of cellular structures formed by four important divisome proteins in E. coli: FtsZ, ZapA, ZapB and MatP. We show that these interacting proteins are arranged into a multi-layered protein network extending from the cell membrane to the chromosome, each with unique structural and dynamic properties. Further, we find that this protein network stabilizes the FtsZ-ring, and unexpectedly, slows down cell constriction, suggesting a new, unrecognized role for this network in bacterial cell division. Our results provide new insight into the structure and function of the divisome, and highlight the importance of coordinated cell constriction and chromosome segregation.</p>
},
	issn = {1553-7404},
	doi = {10.1371/journal.pgen.1005128},
	author = {Buss, Jackson and Coltharp, Carla and Shtengel, Gleb and Yang, Xinxing and Hess, Harald and Xiao, Jie}
}
