$\require{mediawiki-texvc}$

연합인증

연합인증 가입 기관의 연구자들은 소속기관의 인증정보(ID와 암호)를 이용해 다른 대학, 연구기관, 서비스 공급자의 다양한 온라인 자원과 연구 데이터를 이용할 수 있습니다.

이는 여행자가 자국에서 발행 받은 여권으로 세계 각국을 자유롭게 여행할 수 있는 것과 같습니다.

연합인증으로 이용이 가능한 서비스는 NTIS, DataON, Edison, Kafe, Webinar 등이 있습니다.

한번의 인증절차만으로 연합인증 가입 서비스에 추가 로그인 없이 이용이 가능합니다.

다만, 연합인증을 위해서는 최초 1회만 인증 절차가 필요합니다. (회원이 아닐 경우 회원 가입이 필요합니다.)

연합인증 절차는 다음과 같습니다.

최초이용시에는
ScienceON에 로그인 → 연합인증 서비스 접속 → 로그인 (본인 확인 또는 회원가입) → 서비스 이용

그 이후에는
ScienceON 로그인 → 연합인증 서비스 접속 → 서비스 이용

연합인증을 활용하시면 KISTI가 제공하는 다양한 서비스를 편리하게 이용하실 수 있습니다.

[해외논문] Probing the Neuraminidase Activity of Influenza Virus Using a Cytolysin A Protein Nanopore

Analytical chemistry, v.92 no.21, 2020년, pp.14303 - 14308  

Kwak, Dong-Kyu (Disease Target Structure Research Center, Division of Biomedical Research , KRIBB , Daejeon 34141 , Republic of Korea) ,  Kim, Jin-Sik (Disease Target Structure Research Center, Division of Biomedical Research , KRIBB , Daejeon 34141 , Republic of Korea) ,  Lee, Mi-Kyung (Disease Target Structure Research Center, Division of Biomedical Research , KRIBB , Daejeon 34141 , Republic of Korea) ,  Ryu, Kyoung-Seok (Protein Structure Research Group , Korea Basic Science Institute , 162 Yeongudanji-ro , Ochang-eup, Cheongju-si , Chungcheongbuk-do 28119 , Republic of Korea) ,  Chi, Seung-Wook

Abstract AI-Helper 아이콘AI-Helper

Neuraminidase (NA), one of the major surface glycoproteins of influenza A virus (IAV), is an important diagnostic biomarker and antiviral therapeutic target. Cytolysin A (ClyA) is a nanopore sensor with an internal constriction of 3.3 nm, enabling the detection of protein conformations at the single...

참고문헌 (45)

  1. Iuliano, A Danielle, Roguski, Katherine M, Chang, Howard H, Muscatello, David J, Palekar, Rakhee, Tempia, Stefano, Cohen, Cheryl, Gran, Jon Michael, Schanzer, Dena, Cowling, Benjamin J, Wu, Peng, Kyncl, Jan, Ang, Li Wei, Park, Minah, Redlberger-Fritz, Monika, Yu, Hongjie, Espenhain, Laura, Krishnan, Anand, Emukule, Gideon, van Asten, Liselotte, Pereira da Silva, Susana, Aungkulanon, Suchunya, Buchholz, Udo, Widdowson, Marc-Alain, Bresee, Joseph S, Azziz-Baumgartner, Eduardo, Cheng, Po-Yung, Dawood, Fatimah, Foppa, Ivo, Olsen, Sonja, Haber, Michael, Jeffers, Caprichia, MacIntyre, C Raina, Newall, Anthony T, Wood, James G, Kundi, Michael, Popow-Kraupp, Therese, Ahmed, Makhdum, Rahman, Mahmudur, Marinho, Fatima, Sotomayor Proschle, C Viviana, Vergara Mallegas, Natalia, Luzhao, Feng, Sa, Li, Barbosa-Ramírez, Juliana, Sanchez, Diana Malo, Gomez, Leandra Abarca, Vargas, Xiomara Badilla, Acosta Herrera, aBetsy, Llanés, Marí. Estimates of global seasonal influenza-associated respiratory mortality: a modelling study. The Lancet, vol.391, no.10127, 1285-1300.

  2. Acta Virol. Sovinova O. 52 2 1 1958 

  3. Geraci, St Aubin, DJ, Barker, IK, Webster, RG, Hinshaw, VS, Bean, WJ, Ruhnke, HL, Prescott, JH, Early, G, Baker, AS, Madoff, S, Schooley, RT. Mass mortality of harbor seals: pneumonia associated with influenza A virus. Science, vol.215, no.4536, 1129-1131.

  4. Shope, Richard E.. SWINE INFLUENZA : I. EXPERIMENTAL TRANSMISSION AND PATHOLOGY. The Journal of experimental medicine, vol.54, no.3, 349-359.

  5. McAuley, Julie L., Gilbertson, Brad P., Trifkovic, Sanja, Brown, Lorena E., McKimm-Breschkin, Jennifer L.. Influenza Virus Neuraminidase Structure and Functions. Frontiers in microbiology, vol.10, 39-.

  6. Wu, Xiaoai, Wu, Xiuli, Sun, Qizheng, Zhang, Chunhui, Yang, Shengyong, Li, Lin, Jia, Zhiyun. Progress of small molecular inhibitors in the development of anti-influenza virus agents. Theranostics, vol.7, no.4, 826-845.

  7. Grienke, Ulrike, Schmidtke, Michaela, von Grafenstein, Susanne, Kirchmair, Johannes, Liedl, Klaus R., Rollinger, Judith M.. Influenza neuraminidase: A druggable target for natural products. Natural product reports : a journal of current developments in bio-organic chemistry, vol.29, no.1, 11-36.

  8. Corfield, T. Bacterial sialidases--roles in pathogenicity and nutrition.. Glycobiology, vol.2, no.6, 509-521.

  9. von Itzstein, Mark. The war against influenza: discovery and development of sialidase inhibitors. Nature reviews. Drug discovery, vol.6, no.12, 967-974.

  10. Moscona, Anne. Neuraminidase Inhibitors for Influenza. The New England journal of medicine, vol.353, no.13, 1363-1373.

  11. Palese, P., Tobita, K., Ueda, M., Compans, R.W.. Characterization of temperature sensitive influenza virus mutants defective in neuraminidase. Virology, vol.61, no.2, 397-410.

  12. Dziąbowska, Karolina, Czaczyk, Elżbieta, Nidzworski, Dawid. Detection Methods of Human and Animal Influenza Virus—Current Trends. Biosensors, vol.8, no.4, 94-.

  13. Tobita, K., Sugiura, A., Enomoto, C., Furuyama, M.. Plaque assay and primary isolation of influenza a viruses in an established line of canine kidney cells (MDCK) in the presence of trypsin. Medical microbiology and immunology, vol.162, no.1, 9-14.

  14. Novak-Weekley, S. M., Marlowe, E. M., Poulter, M., Dwyer, D., Speers, D., Rawlinson, W., Baleriola, C., Robinson, C. C.. Evaluation of the Cepheid Xpert Flu Assay for Rapid Identification and Differentiation of Influenza A, Influenza A 2009 H1N1, and Influenza B Viruses. Journal of clinical microbiology, vol.50, no.5, 1704-1710.

  15. Hawaii J. Med. Public Health Trombetta V. K. 226 77 9 2018 

  16. Galenkamp, Nicole Stéphanie, Soskine, Misha, Hermans, Jos, Wloka, Carsten, Maglia, Giovanni. Direct electrical quantification of glucose and asparagine from bodily fluids using nanopores. Nature communications, vol.9, no.1, 4085-.

  17. Bayley, Hagan. Nanopore Sequencing: From Imagination to Reality. Clinical chemistry, vol.61, no.1, 25-31.

  18. Kasianowicz, John J., Brandin, Eric, Branton, Daniel, Deamer, David W.. Characterization of individual polynucleotide molecules using a membrane channel. Proceedings of the National Academy of Sciences of the United States of America, vol.93, no.24, 13770-13773.

  19. Majd, S., Yusko, E.C., Billeh, Y.N., Macrae, M.X., Yang, J., Mayer, M.. Applications of biological pores in nanomedicine, sensing, and nanoelectronics. Current opinion in biotechnology, vol.21, no.4, 439-476.

  20. Shi, Wenqing, Friedman, Alicia K., Baker, Lane A.. Nanopore Sensing. Analytical chemistry, vol.89, no.1, 157-188.

  21. Cao, Chan, Long, Yi-Tao. Biological Nanopores: Confined Spaces for Electrochemical Single-Molecule Analysis. Accounts of chemical research, vol.51, no.2, 331-341.

  22. Kwak, Dong‐Kyu, Chae, Hongsik, Lee, Mi‐Kyung, Ha, Ji‐Hyang, Goyal, Gaurav, Kim, Min Jun, Kim, Ki‐Bum, Chi, Seung‐Wook. Probing the Small‐Molecule Inhibition of an Anticancer Therapeutic Protein‐Protein Interaction Using a Solid‐State Nanopore. Angewandte Chemie. international edition, vol.55, no.19, 5713-5717.

  23. Chae, Hongsik, Kwak, Dong-Kyu, Lee, Mi-Kyung, Chi, Seung-Wook, Kim, Ki-Bum. Solid-state nanopore analysis on conformation change of p53TAD-MDM2 fusion protein induced by protein-protein interaction. Nanoscale, vol.10, no.36, 17227-17235.

  24. Oh, Sohee, Lee, Mi-Kyung, Chi, Seung-Wook. Single-Molecule-Based Detection of Conserved Influenza A Virus RNA Promoter Using a Protein Nanopore. ACS sensors, vol.4, no.11, 2849-2853.

  25. Soskine, Misha, Biesemans, Annemie, De Maeyer, Marc, Maglia, Giovanni. Tuning the Size and Properties of ClyA Nanopores Assisted by Directed Evolution. Journal of the American Chemical Society, vol.135, no.36, 13456-13463.

  26. Zernia, Sarah, van der Heide, Nieck Jordy, Galenkamp, Nicole Stéphanie, Gouridis, Giorgos, Maglia, Giovanni. Current Blockades of Proteins inside Nanopores for Real-Time Metabolome Analysis. ACS nano, vol.14, no.2, 2296-2307.

  27. Wloka, Carsten, Van Meervelt, Veerle, van Gelder, Dewi, Danda, Natasha, Jager, Nienke, Williams, Chris P., Maglia, Giovanni. Label-Free and Real-Time Detection of Protein Ubiquitination with a Biological Nanopore. ACS nano, vol.11, no.5, 4387-4394.

  28. Biesemans, Annemie, Soskine, Misha, Maglia, Giovanni. A Protein Rotaxane Controls the Translocation of Proteins Across a ClyA Nanopore. Nano letters : a journal dedicated to nanoscience and nanotechnology, vol.15, no.9, 6076-6081.

  29. Zukin, Ruth S., Strange, Philip G., Heavey, Laurence R., Koshland Jr., D. E.. Properties of the galactose binding protein of Salmonella typhimurium and Escherichia coli. Biochemistry, vol.16, no.3, 381-386.

  30. Borrok, M. Jack, Kiessling, Laura L., Forest, Katrina T.. Conformational changes of glucose/galactose‐binding protein illuminated by open, unliganded, and ultra‐high‐resolution ligand‐bound structures. Protein science : a publication of the Protein Society, vol.16, no.6, 1032-1041.

  31. Unione, Luca, Ortega, Gabriel, Mallagaray, Alvaro, Corzana, Francisco, Pérez-Castells, Javier, Canales, Angeles, Jiménez-Barbero, Jesús, Millet, Oscar. Unraveling the Conformational Landscape of Ligand Binding to Glucose/Galactose-Binding Protein by Paramagnetic NMR and MD Simulations. ACS chemical biology, vol.11, no.8, 2149-2157.

  32. Soskine, Misha, Biesemans, Annemie, Moeyaert, Benjamien, Cheley, Stephen, Bayley, Hagan, Maglia, Giovanni. An Engineered ClyA Nanopore Detects Folded Target Proteins by Selective External Association and Pore Entry. Nano letters : a journal dedicated to nanoscience and nanotechnology, vol.12, no.9, 4895-4900.

  33. Li, Xin, Lee, Kuo Hao, Shorkey, Spencer, Chen, Jianhan, Chen, Min. Different Anomeric Sugar Bound States of Maltose Binding Protein Resolved by a Cytolysin A Nanopore Tweezer. ACS nano, vol.14, no.2, 1727-1737.

  34. Sakaguchi-Mikami, Akane, Taneoka, Atsushi, Yamoto, Rie, Ferri, Stefano, Sode, Koji. Engineering of ligand specificity of periplasmic binding protein for glucose sensing. Biotechnology letters. : a monthly journal for the rapid communication of results and developments in all aspects of biotechnology, vol.30, no.8, 1453-1460.

  35. Clin. Biochem. Rev. Armbruster D. A. S49 29 1 2008 

  36. Cui, Xikai, Das, Amrita, Dhawane, Abasaheb N., Sweeney, Joyce, Zhang, Xiaohu, Chivukula, Vasanta, Iyer, Suri S.. Highly specific and rapid glycan based amperometric detection of influenza viruses. Chemical science, vol.8, no.5, 3628-3634.

  37. Wahyuni, W.T., Ivandini, T.A., Saepudin, E., Einaga, Y.. Development of neuraminidase detection using gold nanoparticles boron-doped diamond electrodes. Analytical biochemistry, vol.497, 68-75.

  38. Gerentes, L, Kessler, N, Aymard, M. A sensitive and specific ELISA immunocapture assay for rapid quantitation of influenza A/H3N2 neuraminidase protein. Journal of virological methods, vol.73, no.2, 185-195.

  39. Collins, P.J., Haire, L.F., Lin, Y.P., Liu, J., Russell, R.J., Walker, P.A., Martin, S.R., Daniels, R.S., Gregory, V., Skehel, J.J., Gamblin, S.J., Hay, A.J.. Structural basis for oseltamivir resistance of influenza viruses. Vaccine, vol.27, no.45, 6317-6323.

  40. McKimm‐Breschkin, Jennifer L.. Influenza neuraminidase inhibitors: antiviral action and mechanisms of resistance. Influenza and other respiratory viruses, vol.7, no.suppl1, 25-36.

  41. Antivir. Ther. Abed Y. 971 11 8 2006 10.1177/135965350601100804 

  42. Jeong, Hyung Jae, Kim, Young Min, Kim, Jang Hoon, Kim, Ji Young, Park, Ji-Young, Park, Su-Jin, Ryu, Young Bae, Lee, Woo Song. Homoisoflavonoids from Caesalpinia sappan Displaying Viral Neuraminidases Inhibition. Biological & pharmaceutical bulletin, vol.35, no.5, 786-790.

  43. Liu, Ai-Lin, Shu, Shi-Hui, Qin, Hai-Lin, Lee, Simon Ming Yuen, Wang, Yi-Tao, Du, Guan-Hua. In vitro anti-influenza viral activities of constituents from Caesalpinia sappan.. Planta medica, vol.75, no.4, 337-339.

  44. Liu, Ai-Lin, Wang, Hai-Di, Lee, Simon MingYuen, Wang, Yi-Tao, Du, Guan-Hua. Structure–activity relationship of flavonoids as influenza virus neuraminidase inhibitors and their in vitro anti-viral activities. Bioorganic & medicinal chemistry, vol.16, no.15, 7141-7147.

  45. Yang, W., Liu, X., Peng, X., Li, P., Wang, T., Tai, G., James Li, X., Zhou, Y.. Synthesis of novel N-acetylneuraminic acid derivatives as substrates for rapid detection of influenza virus neuraminidase. Carbohydrate research, vol.359, 92-96.

LOADING...

활용도 분석정보

상세보기
다운로드
내보내기

활용도 Top5 논문

해당 논문의 주제분야에서 활용도가 높은 상위 5개 콘텐츠를 보여줍니다.
더보기 버튼을 클릭하시면 더 많은 관련자료를 살펴볼 수 있습니다.

관련 콘텐츠

유발과제정보 저작권 관리 안내
섹션별 컨텐츠 바로가기

AI-Helper ※ AI-Helper는 오픈소스 모델을 사용합니다.

AI-Helper 아이콘
AI-Helper
안녕하세요, AI-Helper입니다. 좌측 "선택된 텍스트"에서 텍스트를 선택하여 요약, 번역, 용어설명을 실행하세요.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.

선택된 텍스트

맨위로