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Phytochrome-interacting factor from Arabidopsis to liverwort
Lee, N.,Choi, G. Current Biology, Ltd ; Elsevier Science Ltd 2017 Current opinion in plant biology Vol.35 No.-
<P>Phytochromes are red and far-red light photoreceptors that regulate the responses of plants to light throughout their life cycles. Phytochromes do this in part by inhibiting the function of a group of basic helix-loop-helix transcription factors called phytochrome-interacting factors (PIFs). Arabidopsis has eight PIFs that function sometimes redundantly and sometimes distinctively depending on their expression patterns and protein stability, as well as on variations in the promoters they target in vivo. PIF-like proteins exist in other seed plants and non-vascular plants where they also regulate light responses. The mechanism by which phytochrome regulates light responses by promoting the degradation of the PIFs is conserved in liverwort, suggesting it must have evolved some time before the last common ancestor shared by seed plants and non-vascular plants.</P>
Lee, N.,Kim, J.-E.,Yoo, H. J.,Gu, J. Y.,Kim, H.,Chung, J.,Koh, Y.,Kim, H. K. INSTITUTE FOR CLINICAL SCIENCE 2016 Annals of clinical and laboratory science Vol.46 No.6
<P>We present a case of acquired dysfibrinogenemia caused by an autoantibody that inhibited fibrin polymerization in a patient previously diagnosed with MELAS (mitochondrial myopathy, encephalopathy, lactic acidosis, stroke-like episodes). The patient showed prolonged PT, aPTT, and thrombin time. There was no factor deficiency but fibrinogen antigen and activity were decreased. ELISA for detection of fibrinogen antibodies were performed and IgG purified from the patient's plasma bound to fibrinogen more strongly than did control IgG, indicating the presence of a fibrinogen-specific antibody. Thrombinmediated fibrin polymerization was severely impaired in the patient, although thrombin-induced fibrinopeptide A release was normal. Scanning electron microscopy was used to investigate the structure of fibrin clots and revealed many pores on the surface of patient's fibrin clots. Since MELAS is often associated with autoimmune disorders, a work-up for the presence of anti-fibrinogen antibody is necessary when bleeding tendency occurs in MELAS patients along with prolonged thrombin time.</P>
Lee, N.,Choi, H.,Kim, S.H. North-Holland Pub. Co ; Elsevier Science Ltd 2016 Computational statistics & data analysis Vol.101 No.-
<P>We propose Bayesian shrinkage methods for coefficient estimation for high-dimensional vector autoregressive (VAR) models using scale mixtures of multivariate normal distributions for independently sampled additive noises. We also suggest an efficient selection procedure for the shrinkage parameter as a computationally feasible alternative to the traditional MCMC sampling methods for high-dimensional data. A shrinkage parameter is selected at the minimum point of a newly proposed score function which is asymptotically equivalent to the mean squared error of the model coefficients. The selected shrinkage parameter is presented in a closed form as a function of sample size, level of noise, and non-normality in data, and it can be efficiently estimated by using a suggested variation of cross validation. Consistency of both of the cross validation estimator and proposed shrinkage estimator is proved. The competitiveness of the proposed methods is demonstrated based on comprehensive experimental results using simulated data and high-dimensional plant gene expression data in the context of coefficient estimation and structural inference for VAR models. The proposed methods are applicable to high dimensional stationary time series with or without near unit roots. (C) 2016 Elsevier B.V. All rights reserved.</P>
Lee, N.,Kwon, D. Y. Springer Science + Business Media 2016 Indian journal of microbiology Vol.56 No.4
<P>2,3-Dihydroxybiphenyl 1,2-dioxygenase (2,3-DBDO) is an extradiol-type dioxygenase that involved in third step of biphenyl degradation pathway. The nucleotide sequence of the bphC gene from Comamonas sp. SMN4, which encodes 2,3-DBDO with His-tag, was cloned into a plasmid pQE30 in E. coli. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of the purified active 2,3-DBDO showed a single band around 33 kDa, corresponding the molecular mass of 2,3-DBDO subunit. Two fractions around 170 and 100 kDa were separated in gel filtration chromatography, but only former one (the fraction of 170 kDa) has 2,3-DBDO activity. The 2,3-DBDO was reported as the polymeric protein consisted of eight subunits. However, the fraction corresponding octameric protein of 2,3-DBDO was not found in the gel filtration chromatography. The 2,3-DBDO was exhibited the maximum activity at pH 9.0 and was stable at pH 8.0, relatively. The circular dichroism (CD) data showed that 2,3-DBDO had an alpha-helical folding structures at neutral pHs ranged from pH 4.5 to pH 9.0. However, this high stable folding structure was converted to unfolded structure in acidic region (pH 2.5) or in high pH (pH 12.0). The enzyme was thermally stable and active up to 40 A degrees C. The conformational data by CD spectra were consistent with the stability of 2,3-DBDO by checking the activity. The binding affinity (K (m) ) for 2,3-dihydroxybiphenyl, 3-metylcatechol, 4-methylcatechol and catechol was 11.7, 24 mu M, 50 mM and 625 mu M, respectively.</P>
Lee, N.,Chung, Y. M. Springer Science + Business Media 2016 Research on chemical intermediates Vol.42 No.1
<P>A two-dimensional layered niobium oxide and its exfoliated nanosheet were examined as potential solid acid supports for direct synthesis of hydrogen peroxide from hydrogen and oxygen under intrinsically safe and noncorrosive reaction conditions. The catalytic performance strongly depended on the acid strength of the support material. The Pd-supported protonated niobium oxide nanosheet catalyst (Pd/HNb3O8-NS) with remarkably enhanced acidity was superior to layered Pd/KNb3O8 or Pd/HNb3O8 to promote the reaction. Hydrogen peroxide decomposition testing revealed that, although HNb3O8 was comparable to its exfoliated counterpart, HNb3O8-NS, in suppressing hydrogen peroxide decomposition without hydrogen, HNb3O8 was virtually ineffective in preventing hydrogen peroxide hydrogenation in the presence of hydrogen. However, compared with HNb3O8, HNb3O8-NS was found to be still effective at suppressing hydrogen peroxide hydrogenation. The different efficiency observed between HNb3O8 and HNb3O8-NS in the prevention of hydrogen peroxide hydrogenation implies that use of a highly acidic support is advantageous to effectively suppress faster and therefore more unfavorable hydrogen peroxide hydrogenation compared with decomposition. This result clearly demonstrates that the highly acidic HNb3O8 nanosheet can serve as an efficient solid acid support for direct synthesis of hydrogen peroxide from hydrogen and oxygen.</P>