Publications by authors named "Won K Cho"

3 Publications

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End-stage renal disease is associated with increased post endoscopic retrograde cholangiopancreatography adverse events in hospitalized patients.

World J Gastroenterol 2018 Nov;24(41):4691-4697

Division of Gastroenterology and Hepatology, Mayo Clinic, Rochester, MN 55905, United States.

Aim: To determine if end-stage renal disease (ESRD) is a risk factor for post endoscopic retrograde cholangiopancreatography (ERCP) adverse events (AEs).

Methods: We performed a retrospective cohort study using the Nationwide Inpatient Sample (NIS) 2011-2013. We identified adult patients who underwent ERCP using the International Classification of Diseases 9 Revision (ICD-9-CM). Included patients were divided into three groups: ESRD, chronic kidney disease (CKD), and control. The primary outcome was post-ERCP AEs including pancreatitis, bleeding, and perforation determined based on specific ICD-9-CM codes. Secondary outcomes were length of hospital stay, in-hospital mortality, and admission cost. AEs and mortality were compared using multivariate logistic regression analysis.

Results: There were 492175 discharges that underwent ERCP during the 3 years. The ESRD and CKD groups contained 7347 and 39403 hospitalizations respectively, whereas the control group had 445424 hospitalizations. Post-ERCP pancreatitis (PEP) was significantly higher in the ESRD group (8.3%) compared to the control group (4.6%) with adjusted odd ratio (aOR) = 1.7 (95%CI: 1.4-2.1, < 0.001). ESRD was associated with significantly higher ERCP-related bleeding (5.1%) compared to the control group 1.5% (aOR = 1.86, 95%CI: 1.4-2.4, < 0.001). ESRD had increased hospital mortality 7.1% 1.15% in the control OR = 6.6 (95%CI: 5.3-8.2, < 0.001), longer hospital stay with adjusted mean difference (aMD) = 5.9 d (95%CI: 5.0-6.7 d, < 0.001) and higher hospitalization charges aMD = $+82064 (95%CI: $68221-$95906, < 0.001).

Conclusion: ESRD is a risk factor for post-ERCP AEs and is associated with higher hospital mortality. Careful selection and close monitoring is warranted to improve outcomes.
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http://dx.doi.org/10.3748/wjg.v24.i41.4691DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6224476PMC
November 2018

Genome Sequence of Dengue virus 3 from the Pythium insidiosum Transcriptomes.

Front Microbiol 2016 15;7:926. Epub 2016 Jun 15.

Department of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National UniversitySeoul, Republic of Korea; The Taejin Genome InstituteHoengseong, Republic of Korea.

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http://dx.doi.org/10.3389/fmicb.2016.00926DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4908670PMC
July 2016

Vipp1 is required for basic thylakoid membrane formation but not for the assembly of thylakoid protein complexes.

Plant Physiol Biochem 2007 Feb 20;45(2):119-28. Epub 2007 Jan 20.

Dept. Biologie I, Ludwig-Maximillian-Universität München, Menzinger Strasse 67, D-80638 München, Germany.

Vipp1 (vesicle inducing protein in plastids 1) is found in cyanobacteria and chloroplasts where it is essential for thylakoid formation. Arabidopsis thaliana mutant plants with a reduction of Vipp1 to about 20% of wild type content become albinotic at an early stage. We propose that this drastic phenotype results from an inability of the remaining Vipp1 protein to assemble into a homo-oligomeric complex, indicating that oligomerization is a prerequisite for Vipp1 function. A Vipp1-ProteinA fusion protein, expressed in the Deltavipp1 mutant background, is able to reinstate oligomerization and restore photoautotrophic growth. Plants containing Vipp1-ProteinA in amounts comparable to Vipp1 in the wild type exhibit a wild type phenotype. However, plants with a reduced amount of Vipp1-ProteinA protein are growth-retarded and significantly paler than the wild type. This phenotype is caused by a decrease in thylakoid membrane content and a concomitant reduction in photosynthetic activity. To the extent that thylakoid membranes are made in these plants they are properly assembled with protein-pigment complexes and are photosynthetically active. This strongly supports a function of Vipp1 in basic thylakoid membrane formation and not in the functional assembly of thylakoid protein complexes. Intriguingly, electron microscopic analysis shows that chloroplasts in the mutant plants are not equally affected by the Vipp1 shortage. Indeed, a wide range of different stages of thylakoid development ranging from wild-type-like chloroplasts to plastids nearly devoid of thylakoids can be observed in organelles of one and the same cell.
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http://dx.doi.org/10.1016/j.plaphy.2007.01.005DOI Listing
February 2007
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