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9,883 results on '"Kim, In Sik"'

10. Effectiveness of endovascular treatment for in-hospital stroke vs. community-onset stroke: a propensity score-matched analysis

Author

Jung, Jae Wook, Kim, Kwang Hyun, Yun, Jaeseob, Nam, Hyo Suk, Heo, Ji Hoe, Baik, Minyoul, Yoo, Joonsang, Kim, Jinkwon, Park, Hyungjong, Sohn, Sung-Il, Hong, Jeong-Ho, Kim, Byung Moon, Kim, Dong Joon, Heo, JoonNyung, Bang, Oh Young, Seo, Woo-Keun, Chung, Jong-Won, Lee, Kyung-Yul, Jung, Yo Han, Lee, Hye Sun, Ahn, Seong Hwan, Shin, Dong Hoon, Choi, Hye-Yeon, Cho, Han-Jin, Baek, Jang-Hyun, Kim, Gyu Sik, Seo, Kwon-Duk, Kim, Seo Hyun, Song, Tae-Jin, Han, Sang Won, Park, Joong Hyun, Choi, Jin Kyo, and Kim, Young Dae

Published
2024
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13. Asian Pacific Association for the Study of the Liver clinical practice guidelines on liver transplantation

Author

Kim, Dong-Sik, Yoon, Young-In, Kim, Beom Kyung, Choudhury, Ashok, Kulkarni, Anand, Park, Jun Yong, Kim, Jongman, Sinn, Dong Hyun, Joo, Dong Jin, Choi, YoungRok, Lee, Jeong-Hoon, Choi, Ho Joong, Yoon, Ki Tae, Yim, Sun Young, Park, Cheon-Soo, Kim, Deok-Gie, Lee, Hae Won, Choi, Won-Mook, Chon, Young Eun, Kang, Woo-Hyoung, Rhu, Jinsoo, Lee, Jae Geun, Cho, Yuri, Sung, Pil Soo, Lee, Han Ah, Kim, Ji Hoon, Bae, Si Hyun, Yang, Jin Mo, Suh, Kyung-Suk, Al Mahtab, Mamun, Tan, Soek Siam, Abbas, Zaigham, Shresta, Ananta, Alam, Shahinul, Arora, Anil, Kumar, Ashish, Rathi, Pravin, Bhavani, Ruveena, Panackel, Charles, Lee, Kuei Chuan, Li, Jun, Yu, Ming-Lung, George, Jacob, Tanwandee, Tawesak, Hsieh, Sen-Yung, Yong, Chee Chien, Rela, Mohamed, Lin, H. C., Omata, Masao, and Sarin, Shiv Kumar

Published
2024
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17. In Situ Structural Observation of a Substrate- and Peroxide-Bound High-Spin Ferric-Hydroperoxo Intermediate in the P450 Enzyme CYP121

Author

Nguyen, Romie C, Davis, Ian, Dasgupta, Medhanjali, Wang, Yifan, Simon, Philipp S, Butryn, Agata, Makita, Hiroki, Bogacz, Isabel, Dornevil, Kednerlin, Aller, Pierre, Bhowmick, Asmit, Chatterjee, Ruchira, Kim, In-Sik, Zhou, Tiankun, Mendez, Derek, Paley, Daniel W, Fuller, Franklin, Mori, Roberto Alonso, Batyuk, Alexander, Sauter, Nicholas K, Brewster, Aaron S, Orville, Allen M, Yachandra, Vittal K, Yano, Junko, Kern, Jan F, and Liu, Aimin

Subjects
Inorganic Chemistry, Chemical Sciences, Bioengineering, Good Health and Well Being, Peroxides, Peracetic Acid, Ligands, Cytochrome P-450 Enzyme System, Iron, Heme, Tyrosine, Carbon, General Chemistry, Chemical sciences, Engineering
Abstract

The P450 enzyme CYP121 from Mycobacterium tuberculosis catalyzes a carbon-carbon (C-C) bond coupling cyclization of the dityrosine substrate containing a diketopiperazine ring, cyclo(l-tyrosine-l-tyrosine) (cYY). An unusual high-spin (S = 5/2) ferric intermediate maximizes its population in less than 5 ms in the rapid freeze-quenching study of CYP121 during the shunt reaction with peracetic acid or hydrogen peroxide in acetic acid solution. We show that this intermediate can also be observed in the crystalline state by EPR spectroscopy. By developing an on-demand-rapid-mixing method for time-resolved serial femtosecond crystallography with X-ray free-electron laser (tr-SFX-XFEL) technology covering the millisecond time domain and without freezing, we structurally monitored the reaction in situ at room temperature. After a 200 ms peracetic acid reaction with the cocrystallized enzyme-substrate microcrystal slurry, a ferric-hydroperoxo intermediate is observed, and its structure is determined at 1.85 Å resolution. The structure shows a hydroperoxyl ligand between the heme and the native substrate, cYY. The oxygen atoms of the hydroperoxo are 2.5 and 3.2 Å from the iron ion. The end-on binding ligand adopts a near-side-on geometry and is weakly associated with the iron ion, causing the unusual high-spin state. This compound 0 intermediate, spectroscopically and structurally observed during the catalytic shunt pathway, reveals a unique binding mode that deviates from the end-on compound 0 intermediates in other heme enzymes. The hydroperoxyl ligand is only 2.9 Å from the bound cYY, suggesting an active oxidant role of the intermediate for direct substrate oxidation in the nonhydroxylation C-C bond coupling chemistry.

Published
2023

18. Structure of a ribonucleotide reductase R2 protein radical.

Author

Lebrette, Hugo, Srinivas, Vivek, John, Juliane, Aurelius, Oskar, Kumar, Rohit, Lundin, Daniel, Butryn, Agata, Aller, Pierre, Orville, Allen, Fuller, Franklin, Alonso-Mori, Roberto, Batyuk, Alexander, Bhowmick, Asmit, Sirohiwal, Abhishek, Kim, In-Sik, Gul, Sheraz, Pham, Cindy, Sutherlin, Kyle, Kaila, Ville, Sjöberg, Britt-Marie, Roos, Katarina, Högbom, Martin, Yano, Junko, Sauter, Nicholas, Yachandra, Vittal, Brewster, Aaron, Kern, Jan, and Simon, Philipp

Subjects
Electron Transport, Protons, Ribonucleotide Reductases, Crystallography, X-Ray, Entomoplasmataceae, Catalytic Domain, Bacterial Proteins
Abstract

Aerobic ribonucleotide reductases (RNRs) initiate synthesis of DNA building blocks by generating a free radical within the R2 subunit; the radical is subsequently shuttled to the catalytic R1 subunit through proton-coupled electron transfer (PCET). We present a high-resolution room temperature structure of the class Ie R2 protein radical captured by x-ray free electron laser serial femtosecond crystallography. The structure reveals conformational reorganization to shield the radical and connect it to the translocation path, with structural changes propagating to the surface where the protein interacts with the catalytic R1 subunit. Restructuring of the hydrogen bond network, including a notably short O-O interaction of 2.41 angstroms, likely tunes and gates the radical during PCET. These structural results help explain radical handling and mobilization in RNR and have general implications for radical transfer in proteins.

Published
2023

32. Mucosal TLR5 activation controls healthspan and longevity

Author

Lim, Jae Sung, Jeon, Eun Jae, Go, Hye Sun, Kim, Hyung-Jin, Kim, Kye Young, Nguyen, Thi Quynh Trang, Lee, Da Young, Kim, Kyu Suk, Pietrocola, Federico, Hong, Seol Hee, Lee, Shee Eun, Kim, Kyoung-Shim, Park, Tae-Shin, Choi, Dong-Hee, Jeong, Yu-Jin, Park, Jong-Hwan, Kim, Hyeon Sik, Min, Jung-Joon, Kim, Yong Sook, Park, Joon Tae, Cho, Jae-Ho, Lee, Gil-Woo, Lee, Ji Hyeon, Choy, Hyon E., Park, Sang Chul, Lee, Chul-Ho, Rhee, Joon Haeng, Serrano, Manuel, and Cho, Kyung A

Published
2024
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40. Structural evidence for intermediates during O2 formation in photosystem II

Author

Bhowmick, Asmit, Hussein, Rana, Bogacz, Isabel, Simon, Philipp S, Ibrahim, Mohamed, Chatterjee, Ruchira, Doyle, Margaret D, Cheah, Mun Hon, Fransson, Thomas, Chernev, Petko, Kim, In-Sik, Makita, Hiroki, Dasgupta, Medhanjali, Kaminsky, Corey J, Zhang, Miao, Gätcke, Julia, Haupt, Stephanie, Nangca, Isabela I, Keable, Stephen M, Aydin, A Orkun, Tono, Kensuke, Owada, Shigeki, Gee, Leland B, Fuller, Franklin D, Batyuk, Alexander, Alonso-Mori, Roberto, Holton, James M, Paley, Daniel W, Moriarty, Nigel W, Mamedov, Fikret, Adams, Paul D, Brewster, Aaron S, Dobbek, Holger, Sauter, Nicholas K, Bergmann, Uwe, Zouni, Athina, Messinger, Johannes, Kern, Jan, Yano, Junko, and Yachandra, Vittal K

Subjects
Inorganic Chemistry, Chemical Sciences, Physical Sciences, Oxidation-Reduction, Oxygen, Photosynthesis, Photosystem II Protein Complex, Protons, Water, Manganese, Calcium, Peroxides, CSD-06-PS-A, CSD-46-All CSGB, CSD-45-Featured, General Science & Technology
Abstract

In natural photosynthesis, the light-driven splitting of water into electrons, protons and molecular oxygen forms the first step of the solar-to-chemical energy conversion process. The reaction takes place in photosystem II, where the Mn4CaO5 cluster first stores four oxidizing equivalents, the S0 to S4 intermediate states in the Kok cycle, sequentially generated by photochemical charge separations in the reaction center and then catalyzes the O-O bond formation chemistry1-3. Here, we report room temperature snapshots by serial femtosecond X-ray crystallography to provide structural insights into the final reaction step of Kok's photosynthetic water oxidation cycle, the S3→[S4]→S0 transition where O2 is formed and Kok's water oxidation clock is reset. Our data reveal a complex sequence of events, which occur over micro- to milliseconds, comprising changes at the Mn4CaO5 cluster, its ligands and water pathways as well as controlled proton release through the hydrogen-bonding network of the Cl1 channel. Importantly, the extra O atom Ox, which was introduced as a bridging ligand between Ca and Mn1 during the S2→S3 transition4-6, disappears or relocates in parallel with Yz reduction starting at approximately 700 μs after the third flash. The onset of O2 evolution, as indicated by the shortening of the Mn1-Mn4 distance, occurs at around 1,200 μs, signifying the presence of a reduced intermediate, possibly a bound peroxide.

Published
2023

41. Activation of mGluR1 negatively modulates glutamate-induced phase shifts of the circadian pacemaker in the mouse suprachiasmatic nucleus

Author

Kim, Yoon Sik, Lee, C Justin, Kim, Ji-Hyeon, Kim, Young-Beom, Colwell, Christopher S, and Kim, Yang In

Subjects
Pharmacology and Pharmaceutical Sciences, Biomedical and Clinical Sciences, Sleep Research, Basic Behavioral and Social Science, Neurosciences, Behavioral and Social Science, CaV1.3, Glutamate, PKA, PKG, Suprachiasmatic nucleus, mGluR, Biological psychology
Abstract

In mammals, photic information delivered to the suprachiasmatic nucleus (SCN) via the retinohypothalamic tract (RHT) plays a crucial role in synchronizing the master circadian clock located in the SCN to the solar cycle. It is well known that glutamate released from the RHT terminals initiates the synchronizing process by activating ionotropic glutamate receptors (iGluRs) on retinorecipient SCN neurons. The potential role of metabotropic glutamate receptors (mGluRs) in modulating this signaling pathway has received less attention. In this study, using extracellular single-unit recordings in mouse SCN slices, we investigated the possible roles of the Gq/11 protein-coupled mGluRs, mGluR1 and mGluR5, in photic resetting. We found that mGluR1 activation in the early night produced phase advances in neural activity rhythms in the SCN, while activation in the late night produced phase delays. In contrast, mGluR5 activation had no significant effect on the phase of these rhythms. Interestingly, mGluR1 activation antagonized phase shifts induced by glutamate through a mechanism that was dependent upon CaV1.3 L-type voltage-gated Ca2+ channels (VGCCs). While both mGluR1-evoked phase delays and advances were inhibited by knockout (KO) of CaV1.3 L-type VGCCs, different signaling pathways appeared to be involved in mediating these effects, with mGluR1 working via protein kinase G in the early night and via protein kinase A signaling in the late night. We conclude that, in the mouse SCN, mGluR1s function to negatively modulate glutamate-evoked phase shifts.

Published
2023

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