Zobrazeno 1 - 10 of 13 pro vyhledávání: '"Wei-Chao Lee"'
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Akademický článek
Structural insight into host recognition by aggregative adherence fimbriae of enteroaggregative Escherichia coli.
Autor: Andrea A Berry, Yi Yang, Natalia Pakharukova, James A Garnett, Wei-chao Lee, Ernesto Cota, Jan Marchant, Saumendra Roy, Minna Tuittila, Bing Liu, Keith G Inman, Fernando Ruiz-Perez, Inacio Mandomando, James P Nataro, Anton V Zavialov, Steve Matthews
Publikováno v: PLoS Pathogens, Vol 10, Iss 9, p e1004404 (2014)
Enteroaggregative Escherichia coli (EAEC) is a leading cause of acute and persistent diarrhea worldwide. A recently emerged Shiga-toxin-producing strain of EAEC resulted in significant mortality and morbidity due to progressive development of hemolyt
Externí odkaz: https://doaj.org/article/2fd6baa77f094eb08a903919a04007e9
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2
Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity
Autor: Tsutomu Matsui, Hao Hu, Meng-Chiao Ho, Wen-Hsuan W. Lin, Eric S.-W. Chen, Wei-Chao Lee, Yujun George Zheng, Ming-Daw Tsai, Tong-You Wade Wei, Wen-Ling Lin
Publikováno v: Biochemistry
Type I protein arginine methyltransferases (PRMTs) catalyze asymmetric dimethylation of various proteins, and their dysregulations often correlate with tumorigenesis or developmental deficiency. Recent studies have focused on the in vivo substrate id
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6935b91b6809e7a73378321de4e2e7cb
https://doi.org/10.1021/acs.biochem.5b00995
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3
Diamidine Compounds for Selective Inhibition of Protein Arginine Methyltransferase 1
Autor: Leilei Yan, Kun Qian, Xinyang Zhao, Ivaylo Ivanov, Meng-Chiao Ho, Hairui Su, Stephanie A. Kofsky-Wofford, Chunli Yan, Wei-Chao Lee, Yujun George Zheng
Publikováno v: Journal of Medicinal Chemistry
Protein arginine methylation is a posttranslational modification critical for a variety of biological processes. Misregulation of protein arginine methyltransferases (PRMTs) has been linked to many pathological conditions. Most current PRMT inhibitor
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7f91a82a3fa1e85bc592bc7bdb18353
https://doi.org/10.1021/jm401884z
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4
Crystal structure and analysis of HdaB: The enteroaggregative Escherichia coli AAF/IV pilus tip protein
Autor: Wei-Chao, Lee, Steve, Matthews, James A, Garnett
Publikováno v: Protein Science : A Publication of the Protein Society
Enteroaggregative Escherichia coli is the primary cause of pediatric diarrhea in developing countries. They utilize aggregative adherence fimbriae (AAFs) to promote initial adherence to the host intestinal mucosa, promote the formation of biofilms, a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d1a4fac5642af76a8eb46fb2c182bbb4
https://pubmed.ncbi.nlm.nih.gov/27400770
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5
Promoting crystallisation of the Salmonella enteritidis fimbriae 14 pilin SefD using deuterium oxide
Autor: Paula S. Salgado, James A. Garnett, Jonathan D. Taylor, Ernesto Cota, Bing Liu, Yingqi Xu, Sebastian Lambert, Steve Matthews, Jing Lin, Wei-chao Lee
Publikováno v: Biochemical and Biophysical Research Communications. 421:208-213
The use of heavy water (D(2)O) as a solvent is commonplace in many spectroscopic techniques for the study of biological macromolecules. A significant deuterium isotope effect exists where hydrogen-bonding is important, such as in protein stability, d
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef4bc0fb615f70426f9fe889abc04640
https://doi.org/10.1016/j.bbrc.2012.03.136
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6
Complete 1H, 13C and 15N NMR assignments for donor-strand complemented AafA, the major pilin of aggregative adherence fimbriae (AAF/II) from enteroaggregative E. coli
Autor: Jan Marchant, Sarah A. Fogel, Yi Yang, Steven J. Matthews, Wei-chao Lee, James A. Garnett, Andrea A. Berry, Peter Simpson, James P. Nataro, Keith G. Inman, Kristen M. Varney, Jonathan A. Levine
Publikováno v: Biomolecular NMR Assignments. 5:1-5
Aggregative adherence fimbriae (AAF) are the primary adhesive factors of enteroaggregative Escherichia coli (EAEC) and are required for intestinal colonization. They mediate binding to extracellular matrix proteins of the enteric mucosa and display p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff55b53981a923fcda600a9c41c5892b
https://doi.org/10.1007/s12104-010-9252-7
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8
Crystallization and initial crystallographic analysis of theStreptococcus parasanguinisFW213 Fap1-NRαadhesive domain at pH 5.0
Autor: Wei Chao Lee, Stephen Matthews, Stéphanie Ramboarina, Camille Tagliaferri, Wilfred Wu, James A. Garnett
Publikováno v: Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67:274-276
The adhesin fimbriae-associated protein 1 (Fap1) is a surface protein of Streptococcus parasanguinis FW213 and plays a major role in the formation of dental plaque in humans. Increased adherence is highly correlated to a reduction in pH and acid acti
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::234864713fbb9404f5a1e04557d2ead3
https://doi.org/10.1107/s1744309110052772
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9
Atomic resolution insights into curli fiber biogenesis
Autor: Tillmann Pape, Ardan Patwardhan, Grzegorz J. Grabe, Matthew George Chapman, Sean C. Constable, Ernesto Cota, Paula S. Salgado, Peter Simpson, Wei Chao Lee, Yizhou Zhou, Jonathan D. Taylor, Matt McGuffie, Elisabeth M. Ashman, Steve Matthews
Publikováno v: Structure(London, England:1993)
Summary Bacteria produce functional amyloid fibers called curli in a controlled, noncytotoxic manner. These extracellular fimbriae enable biofilm formation and promote pathogenicity. Understanding curli biogenesis is important for appreciating microb
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::915a2706509aadc5a34ec3a9e97c778c
https://pubmed.ncbi.nlm.nih.gov/21893282
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10
Structural insights into serine-rich fimbriae from Gram-positive bacteria
Autor: Stephen Matthews, Camille Tagliaferri, Jonathan D. Taylor, Meixian Zhou, Michael Nilges, Andrew Bodey, James A. Garnett, Benjamin Bardiaux, Peter Simpson, Ernesto Cota, Teresa Ruiz, James W. Murray, Rivka L. Isaacson, Wei Chao Lee, Yilmaz Alguel, Elizabeth B. Sawyer, Zhixiang Peng, Yuebin Li, Hui Wu, Julien R. C. Bergeron, Stéphanie Ramboarina
Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2010, 285 (42), pp.32446-57. ⟨10.1074/jbc.M110.128165⟩
Journal of Biological Chemistry, 2010, 285 (42), pp.32446-57. ⟨10.1074/jbc.M110.128165⟩
The journal of biological chemistry, 285: 32446-32457
The Journal of Biological Chemistry
International audience; The serine-rich repeat family of fimbriae play important roles in the pathogenesis of streptococci and staphylococci. Despite recent attention, their finer structural details and precise adhesion mechanisms have yet to be dete
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::974c9b388de3abfbcd69b5d19dd714ff
https://hal-pasteur.archives-ouvertes.fr/pasteur-01500608/document
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