Zobrazeno 1 - 10 of 35 pro vyhledávání: '"Jin-Ho Moon"'
2
Structural and biochemical characterization of FabK from Thermotoga maritima
Autor: Gyochang Keum, Sang Chul Shin, Byung Hak Ha, Jin Ho Moon, Eunice Eun Kyeong Kim, Chan Wha Kim
Publikováno v: Biochemical and Biophysical Research Communications. 482:968-974
TM0800 from Thermotoga maritima is one of the hypothetical proteins with unknown function. The crystal structure determined at 2.3 Å resolution reveals a two domain structure: the N-terminal domain forming a barrel and the C-terminal forming a lid.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1887e436b0ea2bd91437d7d62a54eff
https://doi.org/10.1016/j.bbrc.2016.11.141
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3
Crystal structure of PduO-Type ATP:Cob(I)alamin adenosyltransferase from Bacillus cereus in a complex with ATP
Autor: Young Min Chi, Jin Ho Moon, Ae Kyung Park
Publikováno v: Biochemical and Biophysical Research Communications. 408:417-421
ATP:Cobalamin adenosyltransferases catalyze the transfer a 5'-deoxyadenosyl moiety from ATP to cob(I)alamin in the synthesis of the Co-C bond of coenzyme B(12). There are three types of adenosyltransferases, CobA, PduO and EutT. Among these adenosylt
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7da8941998afbb55514eb602226cfd19
https://doi.org/10.1016/j.bbrc.2011.04.036
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4
Structural and Kinetic Analysis of Free Methionine-R-sulfoxide Reductase from Staphylococcus aureus
Autor: Seoung Min Bong, Young Min Chi, Hong Seok Kim, Geun Hee Kwak, Ki Seog Lee, Jin Ho Moon, Hwa Young Kim
Publikováno v: Journal of Biological Chemistry. 285:25044-25052
Free methionine-R-sulfoxide reductase (fRMsr) reduces free methionine R-sulfoxide back to methionine, but its catalytic mechanism is poorly understood. Here, we have determined the crystal structures of the reduced, substrate-bound, and oxidized form
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ba8354cc829b2e204dbadf5ca4a4ba6f
https://doi.org/10.1074/jbc.m110.103119
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6
Direct grafting of ɛ-caprolactone on solid core/mesoporous shell silica spheres by surface-initiated ring-opening polymerization
Autor: Jin-Ho Moon, Kuk Ro Yoon, B. Ramaraj, Soo-Min Lee
Publikováno v: Journal of Applied Polymer Science. 107:2689-2694
Poly(ϵ-caprolactone) (PCL) was formed on Solid core/mesoporous shell (SCMS) silica surface by surface-initiated ring-opening polymerization (SI-ROP). The SI-ROP of ϵ-caprolactone was achieved by heating a mixture of SCMS silica, ϵ-caprolactone and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3372a413e6b8bd23070ea119aade7dc8
https://doi.org/10.1002/app.27369
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7
Crystallization and preliminary X-ray crystallographic studies of a new class of enoyl-(acyl-carrier protein) reductase, FabV, fromVibrio fischeri
Autor: Jeong Hye Lee, Young Min Chi, Jin Ho Moon, Ae Kyung Park
Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 68:78-80
Enoyl-(acyl-carrier protein) reductase (ENR) catalyzes the last step of the fatty-acid elongation cycle of the bacterial fatty-acid biosynthesis (FAS II) pathway. Recently, a new class of ENR has been identified from Vibrio cholerae and was named Fab
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d90febaef7f42742903a4b23a1ed61b
https://doi.org/10.1107/s1744309111049426
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8
Crystallization and preliminary X-ray crystallographic analysis of free methionine-(R)-sulfoxide reductase fromStaphylococcus aureus
Autor: Hwa Young Kim, Augustine Yonghwi Kim, Young Min Chi, Jin Ho Moon, Hong Seok Kim, Seoung Min Bong
Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:1120-1122
Free methionine-(R)-sulfoxide reductase (fRMsr) catalyzes the reduction of the free form of methionine-(R)-sulfoxide back to free methionine. The fRMsr protein from Staphylococcus aureus was overexpressed in Escherichia coli, purified and crystallize
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa165fe8cb45ed07cba585d301cbe596
https://doi.org/10.1107/s1744309109037105
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9
Crystallization and preliminary X-ray crystallographic studies of DesR, a thermosensing response regulator in a two-component signalling system fromStreptococcus pneumoniae
Autor: Young Min Chi, Seung Min Bong, Ae Kyung Park, Jin Ho Moon
Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:727-729
The response regulator DesR, which activates the transcription of the des gene by binding to a regulatory region, is essential for controlling the fluidity of membrane phospholipids. DesR from Streptococcus pneumoniae was overexpressed in Escherichia
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::766313d040e76bc6ba66d5c11b7f01b6
https://doi.org/10.1107/s1744309109023082
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10
Crystallization and preliminary X-ray crystallographic studies of the ρ-class glutathioneS-transferase from the Antarctic clamLaternula elliptica
Autor: Eun Hyuk Jang, In Young Ahn, Jin Ho Moon, Young Min Chi, Ae Kyung Park, Hyun Woo Park
Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 64:1132-1134
Glutathione S-transferases are involved in phase II detoxification processes and catalyze the nucleophilic attack of the tripeptide glutathione on a wide range of endobiotic and xenobiotic electrophilic substrates. The rho-class glutathione S-transfe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4a420f2dc56c422d900a4693114620d
https://doi.org/10.1107/s1744309108034003
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