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Articles by Bo Xu
Total Records ( 3 ) for Bo Xu
  Shelley A. Haveman , Raymond J. DiDonato Jr. , Laura Villanueva , Evgenya S. Shelobolina , Bradley L. Postier , Bo Xu , Anna Liu and Derek R. Lovley
  Although Pelobacter species are closely related to Geobacter species, recent studies suggested that Pelobacter carbinolicus may reduce Fe(III) via a different mechanism because it lacks the outer-surface c-type cytochromes that are required for Fe(III) reduction by Geobacter sulfurreducens. Investigation into the mechanisms for Fe(III) reduction demonstrated that P. carbinolicus had growth yields on both soluble and insoluble Fe(III) consistent with those of other Fe(III)-reducing bacteria. Comparison of whole-genome transcript levels during growth on Fe(III) versus fermentative growth demonstrated that the greatest apparent change in gene expression was an increase in transcript levels for four contiguous genes. These genes encode two putative periplasmic thioredoxins; a putative outer-membrane transport protein; and a putative NAD(FAD)-dependent dehydrogenase with homology to disulfide oxidoreductases in the N terminus, rhodanese (sulfurtransferase) in the center, and uncharacterized conserved proteins in the C terminus. Unlike G. sulfurreducens, transcript levels for cytochrome genes did not increase in P. carbinolicus during growth on Fe(III). P. carbinolicus could use sulfate as the sole source of sulfur during fermentative growth, but required elemental sulfur or sulfide for growth on Fe(III). The increased expression of genes potentially involved in sulfur reduction, coupled with the requirement for sulfur or sulfide during growth on Fe(III), suggests that P. carbinolicus reduces Fe(III) via an indirect mechanism in which (i) elemental sulfur is reduced to sulfide and (ii) the sulfide reduces Fe(III) with the regeneration of elemental sulfur. This contrasts with the direct reduction of Fe(III) that has been proposed for Geobacter species.
  Xiao-Lin Li , Jian-Jun Li , Yuan-Lin Guo , Cheng-Gang Zhu , Rui-Xia Xu , Sha Li , Ping Qing , Na-Qiong Wu , Li-Xin Jiang , Bo Xu and Run-Lin Gao
 

Background

Lower levels of low-density lipoprotein cholesterol (LDL-C) are associated with less cardiovascular risk in patients with coronary artery disease.

Objectives

To assess whether lower preprocedural LDL-C levels are associated with less risk of periprocedural myocardial injury in patients undergoing elective percutaneous coronary intervention (PCI).

Methods

We enrolled 2529 consecutive patients with normal preprocedural cardiac troponin I (cTnI) who successfully underwent elective PCI. The association between preprocedural LDL-C levels and peak cTnI levels within 24 hours after PCI was evaluated.

Results

Preprocedural LDL-C levels were correlated to postprocedural cTnI levels (r = 0.059, P = .003). In the multivariable model, preprocedural LDL-C levels between 70 and 99 mg/dL were associated with less risk of postprocedural cTnI elevation above 1 x upper limit of normal (ULN) (odds ratio [OR]: 0.804; 95% confidence interval [CI]: 0.663-0.975; P = .027) up to 15 x ULN (OR: 0.709; 95% CI: 0.530-0.949; P = .021) compared with preprocedural LDL-C levels ≥100 mg/dL. Moreover, preprocedural LDL-C levels <70 mg/dL were more strongly associated with less risk of postprocedural cTnI elevation above 1 x ULN (OR: 0.736; 95% CI: 0.584-0.927; P = .009) up to 15 x ULN (OR: 0.655; 95% CI: 0.452-0.950; P = .026).

Conclusions

Lower preprocedural LDL-C levels were associated with less risk of periprocedural myocardial injury in patients undergoing elective PCI.

  Xi Tang , Zhou- guang Hui , Xiao -li Cui , Renu Garg , Michael B. Kastan and Bo Xu
  Protein phosphatase 1 (PP1), a major protein phosphatase important for a variety of cellular responses, is activated in response to ionizing irradiation (IR)-induced DNA damage. Here, we report that IR induces the rapid dissociation of PP1 from its regulatory subunit inhibitor-2 (I-2) and that the process requires ataxia-telangiectasia mutated (ATM), a protein kinase central to DNA damage responses. In response to IR, ATM phosphorylates I-2 on serine 43, leading to the dissociation of the PP1-I-2 complex and the activation of PP1. Furthermore, ATM-mediated I-2 phosphorylation results in the inhibition of the Aurora-B kinase, the down-regulation of histone H3 serine 10 phosphorylation, and the activation of the G2/M checkpoint. Collectively, the results of these studies demonstrate a novel pathway that links ATM, PP1, and I-2 in the cellular response to DNA damage.
 
 
 
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