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[PC-0012] Pre-study for early detection of Fusarium fujikuroi via fluorescence imaging method
Jaeyoung Kim(Jaeyoung Kim),Younguk Kim(Younguk Kim),Hyeonso Ji(Hyeonso Ji),Songlim Kim(Songlim Kim),Hyoja Oh(Hyoja Oh),Youngjun Mo(Youngjun Mo),Kyunghwan Kim(Kyunghwan Kim),Jeongho Baek(Jeongho Baek) 한국육종학회 2022 한국육종학회 공동학술발표집 Vol.2022 No.-
Kim, Min-Ji,Bae, Soo Han,Ryu, Jae-Chan,Kwon, Younghee,Oh, Ji-Hwan,Kwon, Jeongho,Moon, Jong-Seok,Kim, Kyubo,Miyawaki, Atsushi,Lee, Min Goo,Shin, Jaekyoon,Kim, Young Sam,Kim, Chang-Hoon,Ryter, Stefan W. Informa UK (TaylorFrancis) 2016 AUTOPHAGY Vol.12 No.8
<P>Proper regulation of mitophagy for mitochondrial homeostasis is important in various inflammatory diseases. However, the precise mechanisms by which mitophagy is activated to regulate inflammatory responses remain largely unknown. The NLRP3 (NLR family, pyrin domain containing 3) inflammasome serves as a platform that triggers the activation of CASP1 (caspase 1) and secretion of proinflammatory cytokines. Here, we demonstrate that SESN2 (sestrin 2), known as stress-inducible protein, suppresses prolonged NLRP3 inflammasome activation by clearance of damaged mitochondria through inducing mitophagy in macrophages. SESN2 plays a dual role in inducing mitophagy in response to inflammasome activation. First, SESN2 induces mitochondrial priming by marking mitochondria for recognition by the autophagic machinery. For mitochondrial preparing, SESN2 facilitates the perinuclear-clustering of mitochondria by mediating aggregation of SQSTM1 (sequestosome 1) and its binding to lysine 63 (Lys63)-linked ubiquitins on the mitochondrial surface. Second, SESN2 activates the specific autophagic machinery for degradation of primed mitochondria via an increase of ULK1 (unc-51 like kinase 1) protein levels. Moreover, increased SESN2 expression by extended LPS (lipopolysaccharide) stimulation is mediated by NOS2 (nitric oxide synthase 2, inducible)-mediated NO (nitric oxide) in macrophages. Thus, Sesn2-deficient mice displayed defective mitophagy, which resulted in hyperactivation of inflammasomes and increased mortality in 2 different sepsis models. Our findings define a unique regulatory mechanism of mitophagy activation for immunological homeostasis that protects the host from sepsis.</P>
Kim, Kyung Hwan,Ki, Hosung,Oang, Key Young,Nozawa, Shunsuke,Sato, Tokushi,Kim, Joonghan,Kim, Tae Kyu,Kim, Jeongho,Adachi, Shin‐,ichi,Ihee, Hyotcherl WILEY‐VCH Verlag 2013 Chemphyschem Vol.14 No.16
<P><B>Abstract</B></P><P>The mechanism of a photochemical reaction involves the formation and dissociation of various short‐lived species on ultrafast timescales and therefore its characterization requires detailed structural information on the transient species. By making use of a structurally sensitive X‐ray probe, time‐resolved X‐ray liquidography (TRXL) can directly elucidate the structures of reacting molecules in the solution phase and thus determine the comprehensive reaction mechanism with high accuracy. In this work, by performing TRXL measurements at two different wavelengths (400 and 267 nm), the reaction mechanism of I<SUB>3</SUB><SUP>−</SUP> photolysis, which changes subtly depending on the excitation wavelength, is elucidated. Upon 400 nm photoexcitation, the I<SUB>3</SUB><SUP>−</SUP> ion dissociates into I<SUB>2</SUB><SUP>−</SUP> and I. By contrast, upon 267 nm photoexcitation, the I<SUB>3</SUB><SUP>−</SUP> ion undergoes both two‐body dissociation (I<SUB>2</SUB><SUP>−</SUP>+I) and three‐body dissociation (I<SUP>−</SUP>+2I) with 7:3 molar ratio. At both excitation wavelengths, all the transient species ultimately disappear in 80 ns by recombining to form the I<SUB>3</SUB><SUP>−</SUP> ion nongeminately. In addition to the reaction dynamics of solute species, the results reveal the transient structure of the solute/solvent cage and the changes in solvent density and temperature as a function of time.</P>
Kim, Tae Wu,Lee, Jae Hyuk,Choi, Jungkweon,Kim, Kyung Hwan,van Wilderen, Luuk J.,Guerin, Laurent,Kim, Youngmin,Jung, Yang Ouk,Yang, Cheolhee,Kim, Jeongho,Wulff, Michael,van Thor, Jasper J.,Ihee, Hyotch American Chemical Society 2012 JOURNAL OF THE AMERICAN CHEMICAL SOCIETY - Vol.134 No.6
<P>Photoreceptor proteins play crucial roles in receiving light stimuli that give rise to the responses required for biological function. However, structural characterization of conformational transition of the photoreceptors has been elusive in their native aqueous environment, even for a prototype photoreceptor, photoactive yellow protein (PYP). We employ pump probe X-ray solution scattering to probe the structural changes that occur during the photocycle of PYP in a wide time range from 3.16 mu s to 300 ms. By the analysis of both kinetics and structures of the intermediates, the structural progression of the protein in the solution phase is vividly visualized. We identify four structurally distinct intermediates and their associated five time constants and reconstructed the molecular shapes of the four intermediates from time-independent, species-associated difference scattering curves. The constructed structures of the intermediates show the large conformational changes such as the protrusion of N-terminus, which is restricted in the crystalline phase due to the crystal contact and thus could not be clearly observed by X-ray crystallography. The protrusion of the N-terminus and the protein volume gradually increase with the progress of the photocycle and becomes maximal in the final intermediate, which is proposed to be the signaling state. The data not only reveal that a common kinetic mechanism is applicable to both the crystalline and the solution phases, but also provide direct evidence for how the sample environment influences structural dynamics and the reaction rates of the PYP photocycle.</P>