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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,Kim, Jeongho,Oang, Key Young,Lee, Jae Hyuk,Grolimund, Daniel,Milne, Christopher J.,Penfold, Thomas J.,Johnson, Steven L.,Galler, Andreas,Kim, Tae Wu,Kim, Jong Goo,Suh, Deokbeom,Moon, J The Royal Society of Chemistry 2015 Physical chemistry chemical physics Vol.17 No.36
<P>Identifying the intermediate species along a reaction pathway is a first step towards a complete understanding of the reaction mechanism, but often this task is not trivial. There has been a strong on-going debate: which of the three intermediates, the CHI<SUB>2</SUB> radical, the CHI<SUB>2</SUB>–I isomer, and the CHI<SUB>2</SUB><SUP>+</SUP> ion, is the dominant intermediate species formed in the photolysis of iodoform (CHI<SUB>3</SUB>)? Herein, by combining time-resolved X-ray liquidography (TRXL) and time-resolved X-ray absorption spectroscopy (TR-XAS), we present strong evidence that the CHI<SUB>2</SUB> radical is dominantly formed from the photolysis of CHI<SUB>3</SUB> in methanol at 267 nm within the available time resolution of the techniques (∼20 ps for TRXL and ∼100 ps for TR-XAS). The TRXL measurement, conducted using the time-slicing scheme, detected no CHI<SUB>2</SUB>–I isomer within our signal-to-noise ratio, indicating that, if formed, the CHI<SUB>2</SUB>–I isomer must be a minor intermediate. The TR-XAS transient spectra measured at the iodine L<SUB>1</SUB> and L<SUB>3</SUB> edges support the same conclusion. The present work demonstrates that the application of these two complementary time-resolved X-ray methods to the same system can provide a detailed understanding of the reaction mechanism.</P> <P>Graphic Abstract</P><P>We identify a major transient species formed in the photolysis of CHI<SUB>3</SUB> by combining time-resolved X-ray liquidography (TRXL) and time-resolved X-ray absorption spectroscopy (TR-XAS). <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c5cp03686k'> </P>
Kim, Jeongho,Kim, Kyung Hwan,Oang, Key Young,Lee, Jae Hyuk,Hong, Kiryong,Cho, Hana,Huse, Nils,Schoenlein, Robert W.,Kim, Tae Kyu,Ihee, Hyotcherl The Royal Society of Chemistry 2016 Chemical communications Vol.52 No.19
<P>Characterization of transient molecular structures formed during chemical and biological processes is essential for understanding their mechanisms and functions. Over the last decade, time-resolved X-ray liquidography (TRXL) and time-resolved X-ray absorption spectroscopy (TRXAS) have emerged as powerful techniques for molecular and electronic structural analysis of photoinduced reactions in the solution phase. Both techniques make use of a pump-probe scheme that consists of (1) an optical pump pulse to initiate a photoinduced process and (2) an X-ray probe pulse to monitor changes in the molecular structure as a function of time delay between pump and probe pulses. TRXL is sensitive to changes in the global molecular structure and therefore can be used to elucidate structural changes of reacting solute molecules as well as the collective response of solvent molecules. On the other hand, TRXAS can be used to probe changes in both local geometrical and electronic structures of specific X-ray-absorbing atoms due to the element-specific nature of core-level transitions. These techniques are complementary to each other and a combination of the two methods will enhance the capability of accurately obtaining structural changes induced by photoexcitation. Here we review the principles of TRXL and TRXAS and present recent application examples of the two methods for studying chemical and biological processes in solution. Furthermore, we briefly discuss the prospect of using X-ray free electron lasers for the two techniques, which will allow us to keep track of structural dynamics on femtosecond time scales in various solution-phase molecular reactions.</P>
Kim, Tae Wu,Yang, Cheolhee,Kim, Youngmin,Kim, Jong Goo,Kim, Jeongho,Jung, Yang Ouk,Jun, Sunhong,Lee, Sang Jin,Park, Sungjun,Kosheleva, Irina,Henning, Robert,van Thor, Jasper J.,Ihee, Hyotcherl The Royal Society of Chemistry 2016 Physical chemistry chemical physics Vol.18 No.13
<P>Real-time probing of structural transitions of a photoactive protein is challenging owing to the lack of a universal time-resolved technique that can probe the changes in both global conformation and light-absorbing chromophores of the protein. In this work, we combine time-resolved X-ray solution scattering (TRXSS) and transient absorption (TA) spectroscopy to investigate how the global conformational changes involved in the photoinduced signal transduction of photoactive yellow protein (PYP) is temporally and spatially related to the local structural change around the light-absorbing chromophore. In particular, we examine the role of internal proton transfer in developing a signaling state of PYP by employing its E46Q mutant (E46Q-PYP), where the internal proton transfer is inhibited by the replacement of a proton donor. The comparison of TRXSS and TA spectroscopy data directly reveals that the global conformational change of the protein, which is probed by TRXSS, is temporally delayed by tens of microseconds from the local structural change of the chromophore, which is probed by TA spectroscopy. The molecular shape of the signaling state reconstructed from the TRXSS curves directly visualizes the three-dimensional conformations of protein intermediates and reveals that the smaller structural change in E46Q-PYP than in wild-type PYP suggested by previous studies is manifested in terms of much smaller protrusion, confirming that the signaling state of E46Q-PYP is only partially developed compared with that of wildtype PYP. This finding provides direct evidence of how the environmental change in the vicinity of the chromophore alters the conformational change of the entire protein matrix.</P>