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Expression and purification of intracrine human FGF 11 and study of its FGFR-dependent biological activity
Kyeong Won Lee , Young Jun An , Janet Lee , Ye-Eun Jung , In Young Ko , Jonghwa Jin , Ji Hoon Park , Won Kyu Lee , Kiweon Cha , Sun-Shin Cha , Jung-Hyun Lee , Hyung-Soon Yim
J. Microbiol. 2022;60(11):1086-1094.   Published online November 1, 2022
DOI: https://doi.org/10.1007/s12275-022-2406-3
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AbstractAbstract
Fibroblast growth factor 11 (FGF11) is one of intracrine FGFs (iFGFs), which function within cells. Unlike canonical FGFs, FGF11 remains intracellularly and plays biological roles in FGF receptor (FGFR)-independent manner. Here, we established an expression system of recombinant FGF11 proteins in E. coli and investigated whether the extracellular administration of FGF11 can activate cellular signaling. Human FGF11 has two isoforms, FGF11a and FGF11b, depending on the presence of nuclear localization sequences (NLSs) in the N-terminus. Because these two isoforms are unstable, we prepared an FGF11a-Mut by substituting three cysteine residues in the NLS with serine and FGF11b-ΔC with C-terminal truncation. The introduction of mutation in the NLS improved the solubility of FGF11 prepared from E. coli. Exogenous addition of FGF11b and FGF11b-ΔC to BALB3T3 increased cell proliferation, while FGF11a-Mut exerted no effect. FGF11b-ΔC showed higher cell proliferation activity and FGFR signaling than FGF11b. The cell-proliferating activities of FGF11b and FGF11b-ΔC were blocked by an FGFR1 inhibitor or a recombinant FGFR1, confirming the FGFR1- dependent extracellular activity of FGF11b. The analysis of circular dichroism suggested that the C-terminus of FGF11 has an α-helical structure, which may affect its interaction with FGFR1. These results suggest that the N-and C-terminus of recombinant FGF11 are involved in the activation of FGFR1. The above results provide novel insights into the function and mechanism of FGF11 that may aid the development of useful ligands for FGFR regulation.

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  • Glycosylation of FGF/FGFR: An underrated sweet code regulating cellular signaling programs
    Aleksandra Gędaj, Paulina Gregorczyk, Dominika Żukowska, Aleksandra Chorążewska, Krzysztof Ciura, Marta Kalka, Natalia Porębska, Łukasz Opaliński
    Cytokine & Growth Factor Reviews.2024; 77: 39.     CrossRef
  • FGF homologous factors are secreted from cells to induce FGFR‐mediated anti‐apoptotic response
    Martyna Biadun, Martyna Sochacka, Radoslaw Karelus, Karolina Baran, Aleksandra Czyrek, Jacek Otlewski, Daniel Krowarsch, Lukasz Opalinski, Malgorzata Zakrzewska
    The FASEB Journal.2023;[Epub]     CrossRef
  • FGF/FGFR1 system in paired breast tumor-adjacent and tumor tissues, associations with mammographic breast density and tumor characteristics
    Öykü Boraka, Marie Klintman, Johan Vallon-Christersson, Sophia Zackrisson, Per Hall, Signe Borgquist, Ann H. Rosendahl
    Frontiers in Oncology.2023;[Epub]     CrossRef
Genomic and physiological analysis of C50 carotenoid-producing novel Halorubrum ruber sp. nov.
Chi Young Hwang , Eui-Sang Cho , Won Jong Rhee , Eunjung Kim , Myung-Ji Seo
J. Microbiol. 2022;60(10):1007-1020.   Published online August 26, 2022
DOI: https://doi.org/10.1007/s12275-022-2173-1
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AbstractAbstract
A novel haloarchaeal species designated as MBLA0099T was isolated from seawater near Yeongheung Island. Cells were Gram-negative, non-motile, red-pigmented, and rod-shaped. They grew at 10–45°C, within pH 5.5–9.0, and between 7.5% and 30% NaCl concentrations. Cells were able to grow without Mg2+ and were lysed in distilled water. The size of the whole-genome and G + C content of DNA was 3.02 Mb and 68.9 mol%, respectively. Phylogenetic analysis shows that the strain MBLA0099T belongs to the genus Halorubrum. The average nucleotide and amino acid identity, and in silico DNA-DNA hybridization values were below the species delineation threshold. Pan-genomic analysis revealed that 3.2% of all genes present in strain MBLA0099T were unique to the strain. The red carotenoid produced by strain MBLA0099T was subjected to spectrometric and chromatographic analyses and confirmed to be bacterioruberin as C50 carotenoid. Mevalonic acid, terpenoid backbone, and carotenoid biosynthesis pathway were annotated for strain MBLA0099T. The C50 carotenoid production by strain MBLA0099T was also enhanced under various stress conditions including relatively netural pH, high oxidative and salinity conditions. Additionally, the strain MBLA0099T-derived bacterioruberin showed the antioxidant activity with EC50 value of 12.29 μg/ml, based on the evaluation of DPPH free radical scavenging activity. The present study would be the first report on the identification of C50 carotenoid from the strain MBLA0099T representing a novel species of the genus Halorubrum, for which the name Halorubrum ruber sp. nov. is proposed. The typestrain used was MBLA0099T (= KCTC 4296T = JCM 34701T).

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  • Optimization of bacterioruberin production from Halorubrum ruber and assessment of its antioxidant potential
    Chi Young Hwang, Eui-Sang Cho, Sungjun Kim, Kyobum Kim, Myung-Ji Seo
    Microbial Cell Factories.2024;[Epub]     CrossRef
  • Microbial Bacterioruberin: A Comprehensive Review
    Mouliraj Palanisamy, Sathishkumar Ramalingam
    Indian Journal of Microbiology.2024; 64(4): 1477.     CrossRef
  • Congregibacter variabilis sp. nov. and Congregibacter brevis sp. nov. Within the OM60/NOR5 Clade, Isolated from Seawater, and Emended Description of the Genus Congregibacter
    Hyeonsu Tak, Miri S. Park, Hyerim Cho, Yeonjung Lim, Jang-Cheon Cho
    Journal of Microbiology.2024; 62(9): 739.     CrossRef
  • Genomic insights on carotenoid synthesis by extremely halophilic archaea Haloarcula rubripromontorii BS2, Haloferax lucentense BBK2 and Halogeometricum borinquense E3 isolated from the solar salterns of India
    Devika. N. Nagar, Kabilan Mani, Judith M. Braganca
    Scientific Reports.2024;[Epub]     CrossRef
  • Microbial bacterioruberin: The new C50 carotenoid player in food industries
    Cassamo U. Mussagy, Angie V. Caicedo-Paz, Fabiane O. Farias, Leonardo M. de Souza Mesquita, Daniele Giuffrida, Laurent Dufossé
    Food Microbiology.2024; 124: 104623.     CrossRef
  • Evaluation of Various Escherichia coli Strains for Enhanced Lycopene Production
    Jun Ren, Junhao Shen, Thi Duc Thai, Min-gyun Kim, Seung Ho Lee, Wonseop Lim, Dokyun Na
    Journal of Microbiology and Biotechnology.2023; 33(7): 973.     CrossRef
  • Bioactive molecules from haloarchaea: Scope and prospects for industrial and therapeutic applications
    Jamseel Moopantakath, Madangchanok Imchen, V. T. Anju, Siddhardha Busi, Madhu Dyavaiah, Rosa María Martínez-Espinosa, Ranjith Kumavath
    Frontiers in Microbiology.2023;[Epub]     CrossRef
Description of Corynebacterium poyangense sp. nov., isolated from the feces of the greater white-fronted geese (Anser albifrons)
Qian Liu , Guoying Fan , Kui Wu , Xiangning Bai , Xi Yang , Wentao Song , Shengen Chen , Yanwen Xiong , Haiying Chen
J. Microbiol. 2022;60(7):668-677.   Published online May 25, 2022
DOI: https://doi.org/10.1007/s12275-022-2089-9
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AbstractAbstract
Two novel Gram-positive, non-spore-forming, facultatively anaerobic, non-motile, and short rods to coccoid strains were isolated from the feces of the greater white-fronted geese (Anser albifrons) at Poyang Lake. The 16S rRNA gene sequences of strains 4H37-19T and 3HC-13 shared highest identity to that of Corynebacterium uropygiale Iso10T (97.8%). Phylogenetic and phylogenomic analyses indicated that strains 4H37-19T and 3HC-13 formed an independent clade within genus Corynebacterium and clustered with Corynebacterium uropygiale Iso10T. The average nucleotide identity and digital DNA-DNA hybridization value between strains 4H37-19T and 3HC-13 and members within genus Corynebacterium were all below 95% and 70%, respectively. The genomic G + C content of strains 4H37-19T and 3HC-13 was 52.5%. Diphosphatidylglycerol (DPG), phosphatidylglycerol (PG), phosphatidylinositol (PI), phosphatidylcholine, and phosphatidyl inositol mannosides (PIM) were the major polar lipids, with C18:1ω9c, C16:0, and C18:0 as the major fatty acids, and MK-8 (H4), MK-8(H2), and MK-9(H2) as the predominant respiratory quinones. The major whole cell sugar was arabinose, and the cell wall included mycolic acids. The cell wall peptidoglycan contained meso-diaminopimelic acid (meso-DAP). The polyphasic taxonomic data shows that these two strains represent a novel species of the genus Corynebacterium, for which the name Corynebacterium poyangense sp. nov. is proposed. The type strain of Corynebacterium poyangense is 4H37-19T (=GDMCC 1.1738T = KACC 21671T).

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  • Valid and accepted novel bacterial taxa isolated from non-domestic animals and taxonomic revisions published in 2023
    Erik Munson, Claire R. Burbick, Sara D. Lawhon, Trinity Krueger, Elena Ruiz-Reyes, Romney M. Humphries
    Journal of Clinical Microbiology.2024;[Epub]     CrossRef
  • Validation List no. 212. Valid publication of new names and new combinations effectively published outside the IJSEM
    Aharon Oren, Markus Göker
    International Journal of Systematic and Evolutionary Microbiology .2023;[Epub]     CrossRef
  • Keratokonjunktivitisli bir tavuktan Corynebacterium spp. ve Arcanobacterium spp. izolasyonu
    Hüban GÖÇMEN, Banur BOYNUKARA
    Veteriner Hekimler Derneği Dergisi.2023; 94(2): 161.     CrossRef
The periplasmic chaperone protein Psg_2795 contributes to the virulence of Pseudomonas savastanoi pv. glycinea: the causal agent of bacterial blight of soybean
Xiuhua Wang , Xiaoyan Zhang , Bao-Hui Lu , Jie Gao
J. Microbiol. 2022;60(5):478-487.   Published online March 4, 2022
DOI: https://doi.org/10.1007/s12275-022-1469-5
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AbstractAbstract
Pseudomonas savastanoi pv. glycinea (Psg, also named P. syringae pv. glycinea and P. amygdali pv. glycinea) is the causative agent of bacterial blight in soybean. The identification of virulence factors is essential for understanding the pathogenesis of Psg. In this study, a mini-Tn5 transposon mutant library of Psg strain PsgNC12 was screened on soybean, and one low-virulent mini-Tn5 mutant, designated as 4573, was identified. Sequence analysis of the 4573-mutant revealed that the mini-Tn5 transposon was inserted in the Psg_2795 gene. Psg_2795 encodes a FimC-domain protein that is highly conserved in Pseudomonas. Further analysis revealed that the mutation and knockout of Psg_2795 results in a reduced virulence phenotype on soybean, decreased motility, weakened bacterial attachment to a glass surface and delayed the population growth within soybean leaves. The phenotype of the 4573-mutant could be complemented nearly to wild-type levels using an intact Psg_2795 gene. Collectively, our results demonstrate that Psg_2795 plays an important role in the virulence, motility, attachment and the population growth of PsgNC12 in soybean. This finding provides a new insight into the function of periplasmic chaperone proteins in a type I pilus and provides reference information for identifying Psg_2795 homologues in P. savastanoi and other bacteria.

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  • Vt35 antitoxin plays a central regulatory role in virulence of Pseudomonas savastanoi pv. glycinea on soybean
    Viet Tru Nguyen, Nanami Sakata, Takako Ishiga, Giyu Usuki, Yoshiteru Hashimoto, Yasuhiro Ishiga
    Journal of General Plant Pathology.2023; 89(4): 211.     CrossRef
Constantimarinum furrinae gen. nov., sp. nov., a marine bacterium isolated from saline volcanic rock aquifer (lava seawater) at Jeju Island, Republic of Korea
Sung-Hyun Yang , Hyun-Myung Oh , Mi-Jeong Park , Dongil Jang , Kae Kyoung Kwon
J. Microbiol. 2022;60(1):11-17.   Published online December 29, 2021
DOI: https://doi.org/10.1007/s12275-022-1468-6
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AbstractAbstract
A Gram-stain-negative, aerobic, rod-shaped (0.3–0.5 × 1.0– 1.9 μm), non-motile marine bacterium designated as ALE3EIT was isolated from a saline volcanic rock aquifer (lava seawater) on Jeju Island, Republic of Korea. The 16S rRNA gene sequence analysis revealed that strain ALE3EIT showed high similarity to ‘Altibacter lentus’ JLT2010T (97.2%), followed by Marixanthomonas ophiurae KMM 3046T (94.5%). Growth was observed at 10–41°C (optimum, 30°C), at pH 6.0–8.5 (optimum, pH 7.5) and at 0.5–8% (optimum, 4.0%) NaCl. The predominant cellular fatty acids were iso-C15:0 (23.5%), iso-C16:0 (10.2%), iso-C16:0 3OH (10.5%), and iso-C17:0 3OH (16.8%). The DNA G + C contents was 40.4 mol%. The major respiratory quinone was MK-6. The major polar lipids were determined to be phosphatidylethanolamine, two unidentified glycolipids, and two unidentified aminolipids. Several phenotypic characteristics such as production of acetoin, activities of arginine dihydrolase and acid phosphatase, and utilization pattern of carbon sources differentiate strain ALE3EIT from ‘A. lentus’ JLT2010T. Activities of the lipase, trypsin, α- chymotrypsin and gelatinase and utilization pattern of carbon sources differentiate strain ALE3EIT from M. ophiurae KMM 3046T. The genome of strain ALE3EIT is 3.0 Mbp long and its ANI and AAI values against ‘A. lentus’ JLT2010T were 76.58 and 72.76, respectively, however, AAI values against members in other genera were lower than 72%. The phylogenomic tree inferred by PhyloPhlAn clearly differentiated the strain ALE3EIT together with strain JLT2010T from other genera in the Falvobacteriaceae. This polyphasic taxonomic data indicates that strain ALE3EIT should be identified as a novel species in the genus ‘Altibacter’, however, the name has not been validated. Therefore, the strain is classified as a novel genus and is proposed as Constantimarinum furrinae gen. nov., sp. nov. The type strain is ALE3EIT (= KCCM 43303T = JCM 33022T).

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  • Comparison of the anti-inflammatory effects of carotenoids-rich product from microalgal mass-cultured between natural seawater and magma seawater
    Jayeon Cheon, Eun-A Kim, Nalae Kang, Taeho Kim, Lei Wang, Soo-Jin Heo, Seon-Heui Cha
    Biocatalysis and Agricultural Biotechnology.2024; 62: 103420.     CrossRef
  • Validation List no. 212. Valid publication of new names and new combinations effectively published outside the IJSEM
    Aharon Oren, Markus Göker
    International Journal of Systematic and Evolutionary Microbiology .2023;[Epub]     CrossRef
Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase
Jisub Hwang , Chang-Sook Jeong , Chang Woo Lee , Seung Chul Shin , Han-Woo Kim , Sung Gu Lee , Ui Joung Youn , Chang Sup Lee , Tae-Jin Oh , Hak Jun Kim , Hyun Park , Hyun Ho Park , Jun Hyuck Lee
J. Microbiol. 2020;58(7):606-613.   Published online April 22, 2020
DOI: https://doi.org/10.1007/s12275-020-0089-1
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AbstractAbstract
Crystal structures of enoyl-coenzyme A (CoA) isomerase from Bosea sp. PAMC 26642 (BoECI) and enoyl-CoA hydratase from Hymenobacter sp. PAMC 26628 (HyECH) were determined at 2.35 and 2.70 Å resolution, respectively. BoECI and HyECH are members of the crotonase superfamily and are enzymes known to be involved in fatty acid degradation. Structurally, these enzymes are highly similar except for the orientation of their C-terminal helix domain. Analytical ultracentrifugation was performed to determine the oligomerization states of BoECI and HyECH revealing they exist as trimers in solution. However, their putative ligand-binding sites and active site residue compositions are dissimilar. Comparative sequence and structural analysis revealed that the active site of BoECI had one glutamate residue (Glu135), this site is occupied by an aspartate in some ECIs, and the active sites of HyECH had two highly conserved glutamate residues (Glu118 and Glu138). Moreover, HyECH possesses a salt bridge interaction between Glu98 and Arg152 near the active site. This interaction may allow the catalytic Glu118 residue to have a specific conformation for the ECH enzyme reaction. This salt bridge interaction is highly conserved in known bacterial ECH structures and ECI enzymes do not have this type of interaction. Collectively, our comparative sequential and structural studies have provided useful information to distinguish and classify two similar bacterial crotonase superfamily enzymes.

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  • ECHDC2 inhibits the proliferation of gastric cancer cells by binding with NEDD4 to degrade MCCC2 and reduce aerobic glycolysis
    Jiancheng He, Jianfeng Yi, Li Ji, Lingchen Dai, Yu Chen, Wanjiang Xue
    Molecular Medicine.2024;[Epub]     CrossRef
  • Metagenomic characterization of biomethane transformation by lipid-catalyzed anaerobic fermentation of lignite
    Zhenhong Chen, Bo Song, Hongyu Guo, Dapin Xia, Yidong Cai, Yongjun Wang, Weizhong Zhao
    Environmental Research.2023; 227: 115777.     CrossRef
  • Crystal structure of multi-functional enzyme FadB from Cupriavidus necator: Non-formation of FadAB complex
    Hyeoncheol Francis Son, Jae-Woo Ahn, Jiyeon Hong, Jihye Seok, Kyeong Sik Jin, Kyung-Jin Kim
    Archives of Biochemistry and Biophysics.2022; 730: 109391.     CrossRef
  • Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8
    Sivaraman Padavattan, Sneha Jos, Hemanga Gogoi, Bagautdin Bagautdinov
    Acta Crystallographica Section F Structural Biology Communications.2021; 77(5): 148.     CrossRef
Crystal structure of Streptomyces coelicolor RraAS2, an unusual member of the RNase E inhibitor RraA protein family
Nohra Park , Jihune Heo , Saemee Song , Inseong Jo , Kangseok Lee , Nam-Chul Ha
J. Microbiol. 2017;55(5):388-395.   Published online April 29, 2017
DOI: https://doi.org/10.1007/s12275-017-7053-8
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AbstractAbstract
Bacterial ribonuclease E (RNase E) plays a crucial role in the processing and decay of RNAs. A small protein named RraA negatively regulates the activity of RNase E via protein-protein interaction in various bacteria. Recently, RraAS1 and RraAS2, which are functional homologs of RraA from Escherichia coli, were identified in the Gram-positive species Streptomyces coelicolor. RraAS1 and RraAS2 inhibit RNase ES ribonuclease activity in S. coelicolor. RraAS1 and RraAS2 have a C-termi-nal extension region unlike typical bacterial RraA proteins. In this study, we present the crystal structure of RraAS2, ex-hibiting a hexamer arranged in a dimer of trimers, consistent with size exclusion chromatographic results. Importantly, the C-terminal extension region formed a long α-helix at the junction of the neighboring subunit, which is similar to the trimeric RraA orthologs from Saccharomyces cerevisiae. Trun-cation of the C-terminal extension region resulted in loss of RNase ES inhibition, demonstrating its crucial role. Our find-ings present the first bacterial RraA that has a hexameric assembly with a C-terminal extension α-helical region, which plays an essential role in the regulation of RNase ES activity in S. coelicolor.

Citations

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  • Relaxed Cleavage Specificity of Hyperactive Variants of Escherichia coli RNase E on RNA I
    Dayeong Bae, Hana Hyeon, Eunkyoung Shin, Ji-Hyun Yeom, Kangseok Lee
    Journal of Microbiology.2023; 61(2): 211.     CrossRef
  • An oxidative metabolic pathway of 4-deoxy-L-erythro-5-hexoseulose uronic acid (DEHU) from alginate in an alginate-assimilating bacterium
    Ryuji Nishiyama, Takao Ojima, Yuki Ohnishi, Yasuhiro Kumaki, Tomoyasu Aizawa, Akira Inoue
    Communications Biology.2021;[Epub]     CrossRef
  • The coordinated action of RNase III and RNase G controls enolase expression in response to oxygen availability in Escherichia coli
    Minho Lee, Minju Joo, Minji Sim, Se-Hoon Sim, Hyun-Lee Kim, Jaejin Lee, Minkyung Ryu, Ji-Hyun Yeom, Yoonsoo Hahn, Nam-Chul Ha, Jang-Cheon Cho, Kangseok Lee
    Scientific Reports.2019;[Epub]     CrossRef
  • RNase G controls tpiA mRNA abundance in response to oxygen availability in Escherichia coli
    Jaejin Lee, Dong-Ho Lee, Che Ok Jeon, Kangseok Lee
    Journal of Microbiology.2019; 57(10): 910.     CrossRef
  • Functional implications of hexameric assembly of RraA proteins from Vibrio vulnificus
    Saemee Song, Seokho Hong, Jinyang Jang, Ji-Hyun Yeom, Nohra Park, Jaejin Lee, Yeri Lim, Jun-Yeong Jeon, Hyung-Kyoon Choi, Minho Lee, Nam-Chul Ha, Kangseok Lee, Eric Cascales
    PLOS ONE.2017; 12(12): e0190064.     CrossRef
Research Support, Non-U.S. Gov't
Crystal Structure of XoLAP, a Leucine Aminopeptidase, from Xanthomonas oryzae pv. oryzae
Jin-Kwang Kim , Sampath Natarajan , Hanseul Park , Kim-Hung Huynh , Sang Hee Lee , Jeong-Gu Kim , Yeh-Jin Ahn , Lin-Woo Kang
J. Microbiol. 2013;51(5):627-632.   Published online October 31, 2013
DOI: https://doi.org/10.1007/s12275-013-3234-2
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AbstractAbstract
Aminopeptidases are metalloproteinases that degrade N-terminal residues from protein and play important roles in cell growth and development by controlling cell homeostasis and protein maturation. We determined the crystal structure of XoLAP, a leucyl aminopeptidase, at 2.6 Å resolution from Xanthomonas oryzae pv. oryzae, causing the destructive rice disease of bacterial blight. It is the first crystal structure of aminopeptidase from phytopathogens as a drug target. XoLAP existed as a hexamer and the monomer structure consisted of an N-terminal cap domain and a C-terminal peptidase domain with two divalent zinc ions. XoLAP structure was compared with BlLAP and EcLAP (EcPepA) structures. Based on the structural comparison, the molecular model of XoLAP in complex with the natural aminopeptidase inhibitor of microginin FR1 was proposed. The model structure will be useful to develop a novel antibacterial drug against Xoo.

Citations

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  • Expression, Characterisation, Homology Modelling and Molecular Docking of a Novel M17 Family Leucyl-Aminopeptidase from Bacillus cereus CZ
    Jie Liu, Tangbing Cui
    International Journal of Molecular Sciences.2023; 24(21): 15939.     CrossRef
  • Screening and verification for proteins that interact with leucine aminopeptidase of Taenia pisiformis using a yeast two-hybrid system
    Shaohua Zhang
    Parasitology Research.2019; 118(12): 3387.     CrossRef
  • Transcriptional expression of aminoacyl tRNA synthetase genes of Xanthomonas oryzae pv. oryzae (Xoo) on rice-leaf extract treatment and crystal structure of Xoo glutamyl-tRNA synthetase
    Thien-Hoang Ho, Myoung-Ki Hong, Seunghwan Kim, Jeong-Gu Kim, Jongha Lee, Kyoungho Jung, Inho Lee, Munyoung Choi, Hyunjae Park, Sanghee Lee, Yeh-Jin Ahn, Lin-Woo Kang
    Crop and Pasture Science.2017; 68(5): 434.     CrossRef
  • An angiotensin-converting enzyme-inhibitory metabolite with partial structure of microginin in a cyanobacterium Anabaena fertilissima CCC597, producing fibrinolytic protease
    Suvendra Nath Bagchi, Shobha Sondhia, Manish Kumar Agrawal, Sonali Banerjee
    Journal of Applied Phycology.2016; 28(1): 177.     CrossRef
  • Structure and Substrate Recognition of the Bottromycin Maturation Enzyme BotP
    Greg Mann, Liujie Huo, Sebastian Adam, Brunello Nardone, Jeremie Vendome, Nicholas James Westwood, Rolf Müller, Jesko Koehnke
    ChemBioChem.2016; 17(23): 2286.     CrossRef
  • Crystal Structures of Peptide Deformylase from Rice Pathogen Xanthomonas oryzae pv. oryzae in Complex with Substrate Peptides, Actinonin, and Fragment Chemical Compounds
    Ho-Phuong-Thuy Ngo, Thien-Hoang Ho, Inho Lee, Huyen-Thi Tran, Bookyo Sur, Seunghwan Kim, Jeong-Gu Kim, Yeh-Jin Ahn, Sun-Shin Cha, Lin-Woo Kang
    Journal of Agricultural and Food Chemistry.2016; 64(39): 7307.     CrossRef
  • Crystallization and preliminary X-ray crystallographic analysis of the XoGroEL chaperonin fromXanthomonas oryzaepv.oryzae
    Huyen-Thi Tran, Tan-Viet Pham, Ho-Phuong-Thuy Ngo, Myoung-Ki Hong, Jeong-Gu Kim, Sang Hee Lee, Yeh-Jin Ahn, Lin-Woo Kang
    Acta Crystallographica Section F Structural Biology Communications.2014; 70(5): 604.     CrossRef
Retraction of Publication
Retraction Note to: Cryptic prophages in a blaNDM‑1‑bearing plasmid increase bacterial survival against high NaCl concentration, high and low temperatures, and oxidative and immunological stressors
So Yeon Kim , Kwan Soo Ko
J. Microbiol. 2023;61(4):481-481.
DOI: https://doi.org/10.1007/s12275-023-00049-1
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AbstractAbstract
Retraction Note to: Journal of Microbiology (2020) Vol. 58, No. 6, pp. 483–488 https://doi.org/10.1007/s12275-020-9605-6 The Editor-in-Chief has retracted this article at the request of the authors. After publication concerns were raised that prophage sequences do not exist in the genome of the plasmid pNDM-A1 used in this study. The authors have not been able to confirm the existence of prophage sequences in the plasmid. As a result, the Editor-in-Chief no longer has confidence in the results and conclusions presented in this article. Kwan Soo Ko agrees with this retraction. So Yeon Kim has not responded to correspondence from the Editor-in-Chief about this retraction.

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