32 research outputs found
Recombinant human FGF-2 for the treatment of early-stage osteonecrosis of the femoral head: TRION, a single-arm, multicenter, Phase II trial
Aim: This study aimed to evaluate the 2-year outcomes from a clinical trial of recombinant human FGF-2 (rhFGF-2) for osteonecrosis of the femoral head (ONFH). Patients & methods: Sixty-four patients with nontraumatic, precollapse and large ONFHs were percutaneously administered with 800 μg rhFGF-2 contained in gelatin hydrogel. Setting the end point of radiological collapse, we analyzed the joint preservation period of the historical control. Changes in two validated clinical scores, bone regeneration and safety were evaluated. Results: Radiological joint preservation time was significantly higher in the rhFGF-2 group than in the control group. The ONFHs tended to improve to smaller ONFHs. The postoperative clinical scores significantly improved. Thirteen serious adverse events showed recovery. Conclusion: rhFGF-2 treatment increases joint preservation time with clinical efficacy, radiological bone regeneration and safety
Nature of Infrared Sources in 11 micron Selected Sample from Early Data of the AKARI North Ecliptic Pole Deep Survey
We present the properties of 11 m selected sources detected in the early
data of the North Ecliptic Pole Deep (NEP-Deep) Survey of AKARI. The data set
covers 6 wavelength bands from 2.5 to 11 m, with the exposure time of 10 ~
20 minutes. This field lies within the CFHT survey with four filter bands (\mu\mu\mu\mu\muL_{IR} ~ 10^{10}10^{12}
L_{\odot}$ based on the detailed modelling of SEDs. We also find four AGNs
lying at various redshifts in the main sample. In addition, we discuss a few
sources which have non-typical SEDs of the main sample, including a brown dwarf
candidate, a steep power-law source, flat spectrum object, and an early-type
galaxy at moderate redshift.Comment: 22 pages, 10 figure
A Protein Complex Containing Mei5 and Sae3 Promotes the Assembly of the Meiosis-Specific RecA Homolog Dmc1
AbstractMeiotic recombination requires the meiosis-specific RecA homolog Dmc1 as well as the mitotic RecA homolog Rad51. Here, we show that the two meiosis-specific proteins Mei5 and Sae3 are necessary for the assembly of Dmc1, but not for Rad51, on chromosomes including the association of Dmc1 with a recombination hot spot. Mei5, Sae3, and Dmc1 form a ternary and evolutionary conserved complex that requires Rad51 for recruitment to chromosomes. Mei5, Sae3, and Dmc1 are mutually dependent for their chromosome association, and their absence prevents the disassembly of Rad51 filaments. Our results suggest that Mei5 and Sae3 are loading factors for the Dmc1 recombinase and that the Dmc1-Mei5-Sae3 complex is integrated onto Rad51 ensembles and, together with Rad51, plays both catalytic and structural roles in interhomolog recombination during meiosis