Human marginal zone B cell development from early T2 progenitors.

B cells emerge from the bone marrow as transitional (TS) B cells that differentiate through T1, T2, and T3 stages to become naive B cells. We have identified a bifurcation of human B cell maturation from the T1 stage forming IgMhi and IgMlo developmental trajectories. IgMhi T2 cells have higher expression of α4β7 integrin and lower expression of IL-4 receptor (IL4R) compared with the IgMlo branch and are selectively recruited into gut-associated lymphoid tissue. IgMhi T2 cells also share transcriptomic features with marginal zone B cells (MZBs). Lineage progression from T1 cells to MZBs via an IgMhi trajectory is identified by pseudotime analysis of scRNA-sequencing data. Reduced frequency of IgMhi gut-homing T2 cells is observed in severe SLE and is associated with reduction of MZBs and their putative IgMhi precursors. The collapse of the gut-associated MZB maturational axis in severe SLE affirms its existence in health

Optical and photovoltaic properties of indium selenide thin films prepared by van der Waals epitaxy

Indium selenide thin films have been grown on p-type gallium selenide single crystal substrates by van der Waals epitaxy. The use of two crucibles in the growth process has resulted in indium selenide films with physical properties closer to these of bulk indium selenide than those prepared by other techniques. The optical properties of the films have been studied by electroabsorption measurements. The band gap and its temperature dependence are very close to those of indium selenide single crystals. The width of the fundamental transition, even if larger than that of the pure single crystal material, decreases monotonously with temperature. Exciton peaks are not observed even at low temperature, which reveals that these layers still contain a large defect concentration. The current–voltage characteristic of indium selenide thin film devices was measured under simulated AM2 conditions. The solar conversion efficiency of these devices is lower than 0.6%. The high concentration of defects reduces the diffusion length of minority carriers down to values round to 0.2 μ[email protected] ; [email protected]

Microtubule structure by cryo-EM: snapshots of dynamic instability

The development of cryo-electron microscopy (cryo-EM) allowed microtubules to be captured in their solution-like state, enabling decades of insight into their dynamic mechanisms and interactions with binding partners. Cryo-EM micrographs provide 2D visualization of microtubules, and these 2D images can also be used to reconstruct the 3D structure of the polymer and any associated binding partners. In this way, the binding sites for numerous components of the microtubule cytoskeleton - including motor domains from many kinesin motors, and the microtubule-binding domains of dynein motors and an expanding collection of microtubule associated proteins - have been determined. The effects of various microtubule-binding drugs have also been studied. High resolution cryo-EM structures have also been used to probe the molecular basis of microtubule dynamic instability, driven by the GTPase activity of β-tubulin. These studies have shown the conformational changes in lattice-confined tubulin dimers in response to steps in the tubulin GTPase cycle, most notably lattice compaction at the longitudinal inter-dimer interface. Although work is ongoing to define a complete structural model of dynamic instability, attention has focused on the role of gradual destabilization of lateral contacts between tubulin protofilaments, particularly at the microtubule seam. Furthermore, lower resolution cryo-electron tomography 3D structures are shedding light on the heterogeneity of microtubule ends and how their 3D organization contributes to dynamic instability. The snapshots of these polymers captured using cryo-EM will continue to provide critical insights into their dynamics, interactions with cellular components, and the way microtubules contribute to cellular functions in diverse physiological contexts

Expression, immunochemical characterization and localization of the Mycobacterium tuberculosis protein p27

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