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Biochemical experiments as well as confocal microscopy analyses indicate that the translocation of PLC-γ2 is mediated by the direct association of this protein with the actin cytoskeleton.
X-ray diffraction, selected-area electron diffraction and high-resolution electron microscopy analyses indicate that the field changes the preferred orientation.
High-resolution X-ray diffraction and transmission electron microscopy analyses indicate that good crystalline quality of the AlGaN/GaN MQW layer could be achieved when the AlGaN interlayer is inserted.
Electron microscopy analyses indicate that endosome maturation is impaired at distinct steps by hrs and stam mutations.
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Transmission electron microscopy analyses indicated that the formation of β-SiC on the Si1 − xCx layer occurred when the oxidation temperature exceeded 900 °C.
X-ray diffraction and scanning electron microscopy analyses indicated that the strength of the new materials increases due to the synthesis of amorphous and crystalline compounds.
Fluorescence spectroscopy and electron microscopy analyses indicated that RL and its derivatives killed microbial cells by permeabilizing the cell membrane and damaging membrane integrity.
Scanning electron microscopy analyses indicated that the vanadium oxide nanofibers change the morphology after 10 charge/discharge cycles while hybrid nanofibers retain the defined morphology after electrochemical cycling.
The X-ray diffraction and scanning electron microscopy analyses indicated that the main hydration products formed are nearly amorphous calcium silicate hydrates, calcium sulphoaluminate hydrates (ettrringite and monosulfate hydrates) and portlandite (CH).
Moreover, immunofluorescence microscopy analyses indicated that p62 downregulation was concomitant with reduced immunoreactive for ubiquitin-positive bodies (data not shown), further suggesting that Tzb-refractory cells exhibit a significantly enhanced turnover of autophagic substrates [57], including potentially toxic aggregate-prone ubiquitinated proteins.
Immunofluorescence and confocal microscopy analyses indicated that coexpression of PLZF with HDAC3 or SIRT1 disrupts the punctate nuclear localization pattern of PLZF (Fig. 4b), resulting in a diffuse nuclear PLZF staining consistent with immunoblot results indicating no change in total PLZF protein (Fig. 2a.1, a.2).
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