Zobrazeno 1 - 10
of 35
pro vyhledávání: '"MESH : Neuraminidase"'
Autor:
Andrew G. Watts, A. Carlos Frasch, Ricardo Resende, Jean M. H. van den Elsen, Susan J. Crennell, Patricia Marcé, Pedro M. Alzari, Zexin Chen
Publikováno v:
European Journal of Medicinal Chemistry
European Journal of Medicinal Chemistry, Elsevier, 2018, 158, pp.25-33. ⟨10.1016/j.ejmech.2018.08.089⟩
Chen, Z, Marce Villa, P, Resende, R, Alzari, P M, Frasch, A C, Van Den Elsen, J, Crennell, S & Watts, A 2018, ' The synthesis and kinetic evaluation of aryl α-aminophosphonates as novel inhibitors of T. cruzi trans-sialidase ', European Journal of Medicinal Chemistry, vol. 158, pp. 25-33 . https://doi.org/10.1016/j.ejmech.2018.08.089
European Journal of Medicinal Chemistry, 2018, 158, pp.25-33. ⟨10.1016/j.ejmech.2018.08.089⟩
European Journal of Medicinal Chemistry, Elsevier, 2018, 158, pp.25-33. ⟨10.1016/j.ejmech.2018.08.089⟩
Chen, Z, Marce Villa, P, Resende, R, Alzari, P M, Frasch, A C, Van Den Elsen, J, Crennell, S & Watts, A 2018, ' The synthesis and kinetic evaluation of aryl α-aminophosphonates as novel inhibitors of T. cruzi trans-sialidase ', European Journal of Medicinal Chemistry, vol. 158, pp. 25-33 . https://doi.org/10.1016/j.ejmech.2018.08.089
European Journal of Medicinal Chemistry, 2018, 158, pp.25-33. ⟨10.1016/j.ejmech.2018.08.089⟩
The trans-sialidase protein expressed by Trypanosoma cruzi is an important enzyme in the life cycle of this human pathogenic parasite and is considered a promising target for the development of new drug treatments against Chagas' disease. Here we des
Publikováno v:
Analyst
Analyst, Royal Society of Chemistry, 2017, 143 (1), pp.150-156. ⟨10.1039/c7an01537b⟩
Analyst, Royal Society of Chemistry, 2017, 143 (1), pp.150-156. ⟨10.1039/c7an01537b⟩
WOS: 000418371100013 PubMed ID: 29134205 An effective electrochemical influenza A biosensor based on a graphene-gold (Au) hybrid nanocomposite modified Au-screen printed electrode has been developed. The working principle of the developed biosensor r
Publikováno v:
Analytical Chemistry
Analytical Chemistry, American Chemical Society, 2016, 88 (12), pp.6151-6153. ⟨10.1021/acs.analchem.6b01720⟩
Analytical Chemistry, American Chemical Society, 2016, 88 (12), pp.6151-6153. 〈10.1021/acs.analchem.6b01720〉
Analytical Chemistry, American Chemical Society, 2016, 88 (12), pp.6151-6153. ⟨10.1021/acs.analchem.6b01720⟩
Analytical Chemistry, American Chemical Society, 2016, 88 (12), pp.6151-6153. 〈10.1021/acs.analchem.6b01720〉
WOS: 000378470200011 PubMed ID: 27281347 Neuroaminidase (NA) enzyme is a kind of glycoprotein that is found on the influenza A virus. During infection, NA is important for the release of influenza virions from the host cell surface together with vira
Autor:
Philippe Buchy, Davun Holl, Sareth Rith, Veasna Duong, Sowath Ly, Paul F. Horwood, Philippe Dussart, Juliette Gambaretti, San Sorn, Lotfi Allal, Arnaud Tarantola, Srey Viseth Horm, Phalla Y, Wantanee Kalpravidh
Publikováno v:
Emerging microbes & infections
Emerging microbes & infections, Earliest : Springer-Nature ; Latest : Taylor & Francis, 2016, 5 (7), pp.e70. ⟨10.1038/emi.2016.69⟩
Emerging Microbes & Infections
Emerging microbes & infections, Earliest : Springer-Nature ; Latest : Taylor & Francis, 2016, 5 (7), pp.e70. ⟨10.1038/emi.2016.69⟩
Emerging Microbes & Infections
International audience; Surveillance for avian influenza viruses (AIVs) in poultry and environmental samples was conducted in four live-bird markets in Cambodia from January through November 2013. Through real-time RT-PCR testing, AIVs were detected
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5e9e8a47dbba3123d07f155ed1ff599
https://hal-pasteur.archives-ouvertes.fr/pasteur-01739361/document
https://hal-pasteur.archives-ouvertes.fr/pasteur-01739361/document
Publikováno v:
Avian Pathology
Avian Pathology, Taylor & Francis, 2016, 45 (2), pp.212-20. 〈10.1080/03079457.2016.1143086〉
Avian Pathology, Taylor & Francis, 2016, 45 (2), pp.212-20. 〈10.1080/03079457.2016.1143086〉
International audience; Studies carried out on cell permissivity are of great interest to understand virus replication and pathogenicity. We described the results of a comparative analysis of replication efficiency of two naturally occurring influenz
Autor:
Alberto C.C. Frasch, Michael H. Charlton, Paul N. Mortenson, Richard A. Bryce, Horacio Botti, Mark L. Brewer, Pedro M. Alzari, Alejandro Buschiazzo, João Neres, Kenneth T. Douglas, Laura Ratier, Philip Neil Edwards
Publikováno v:
Bioorganic and Medicinal Chemistry Letters
Bioorganic and Medicinal Chemistry Letters, Elsevier, 2009, 19 (3), pp.589-596. ⟨10.1016/j.bmcl.2008.12.065⟩
Bioorganic and Medicinal Chemistry Letters, 2009, 19 (3), pp.589-596. ⟨10.1016/j.bmcl.2008.12.065⟩
Bioorganic and Medicinal Chemistry Letters, Elsevier, 2009, 19 (3), pp.589-596. ⟨10.1016/j.bmcl.2008.12.065⟩
Bioorganic and Medicinal Chemistry Letters, 2009, 19 (3), pp.589-596. ⟨10.1016/j.bmcl.2008.12.065⟩
International audience; trans-Sialidase from Trypanosoma cruzi (TcTS) has emerged as a potential drug target for treatment of Chagas disease. Here, we report the results of virtual screening for the discovery of novel TcTS inhibitors, which targeted
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2008, 47 (14), pp.2700-2703. ⟨10.1002/anie.200705435⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2008, 47 (14), pp.2700-2703. ⟨10.1002/anie.200705435⟩
International audience
Autor:
Stéphane Carpentier, Stéphanie Durand, Roy A. Gravel, Claudia Zwingmann, Feng Liang, Jacques L. Michaud, Karine Landry, Jibin Zeng, Aurore Caqueret, Thierry Levade, Sergio Marchesini, Alexey V. Pshezhetsky, Maryssa Canuel, Carlos R. Morales, Volkan Seyrantepe
Publikováno v:
Human Molecular Genetics
Human Molecular Genetics, 2008, 17 (11), pp.1556-68. ⟨10.1093/hmg/ddn043⟩
Human Molecular Genetics, Oxford University Press (OUP), 2008, 17 (11), pp.1556-68. ⟨10.1093/hmg/ddn043⟩
Human Molecular Genetics, 2008, 17 (11), pp.1556-68. ⟨10.1093/hmg/ddn043⟩
Human Molecular Genetics, Oxford University Press (OUP), 2008, 17 (11), pp.1556-68. ⟨10.1093/hmg/ddn043⟩
International audience; Mammalian sialidase Neu4, ubiquitously expressed in human tissues, is located in the lysosomal and mitochondrial lumen and has broad substrate specificity against sialylated glycoconjugates. To investigate whether Neu4 is invo
Autor:
Alejandro Buschiazzo, Maria Fernanda Amaya, Andrew G. Watts, T. Nguyen, Alberto C.C. Frasch, Stephen G. Withers, Gastón Paris, Pedro M. Alzari, Annemarie Wehenkel, Iben Damager
Publikováno v:
Structure
Structure, Elsevier (Cell Press), 2004, 12 (5), pp.775-784. ⟨10.1016/j.str.2004.02.036⟩
Structure, 2004, 12 (5), pp.775-784. ⟨10.1016/j.str.2004.02.036⟩
Structure, Elsevier (Cell Press), 2004, 12 (5), pp.775-784. ⟨10.1016/j.str.2004.02.036⟩
Structure, 2004, 12 (5), pp.775-784. ⟨10.1016/j.str.2004.02.036⟩
International audience; Sialidases are a superfamily of sialic-acid-releasing enzymes that are of significant interest due to their implication as virulence factors in the pathogenesis of a number of diseases. However, extensive studies of viral and
Autor:
Jean-Paul Rolland, Christine Moriscot, Emmanuel Giudice, Bruno Lina, Vincent Moules, Olivier Terrier, Guy Schoehn, Emilie Frobert, Thomas Julien, M. Bouscambert-Duchamp, Yi Pu Lin, Béatrice Riteau, Olivier Ferraris, Alan J. Hay, Daniel Thomas, Alexandra Erny, Matthieu Yver, Manuel Rosa-Calatrava
Publikováno v:
Virology
Virology, Elsevier, 2011, 414 (1), pp.51-62. ⟨10.1016/j.virol.2011.03.011⟩
Virology, Elsevier, 2011, 414 (1), pp.51-62. 〈10.1016/j.virol.2011.03.011〉
Virology, 2011, 414 (1), pp.51-62. ⟨10.1016/j.virol.2011.03.011⟩
Virology, Elsevier, 2011, 414 (1), pp.51-62. ⟨10.1016/j.virol.2011.03.011⟩
Virology, Elsevier, 2011, 414 (1), pp.51-62. 〈10.1016/j.virol.2011.03.011〉
Virology, 2011, 414 (1), pp.51-62. ⟨10.1016/j.virol.2011.03.011⟩
International audience; Despite progress in our knowledge of the internal organisation of influenza virus particles, little is known about the determinants of their morphology and, more particularly, of the actual abundance of structural proteins at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff00305492611a501e1e6b184e03f38e
https://hal.archives-ouvertes.fr/hal-00599618
https://hal.archives-ouvertes.fr/hal-00599618