Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Markus Ritzefeld"'
Autor:
Cyril Dian, Inmaculada Pérez-Dorado, Frédéric Rivière, Thomas Asensio, Pierre Legrand, Markus Ritzefeld, Mengjie Shen, Ernesto Cota, Thierry Meinnel, Edward W. Tate, Carmela Giglione
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
N-terminal glycine myristoyl transferases (NMTs) catalyse the myristoylation of eukaryotic proteins. Here, the authors provide insights into the catalytic mechanism of NMTs by determining the crystal structures of human NMT1 in complex with reactive
Externí odkaz:
https://doaj.org/article/1d7d6b525886413db95bc8b3e99c1d00
Autor:
Milon Mondal, Balazs Pogranyi, Matthew J. Fuchter, Leran Zhang, Christian Siebold, Jake L. Greenfield, Lea Sefer, Sebastian A. Andrei, Thomas Lanyon-Hogg, Markus Ritzefeld, Callum D. Johnston, Joshua Newington, Claire E. Coupland, Anthony I. Magee, Edward W. Tate
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie (International Ed. in English)
Angewandte Chemie (International Ed. in English)
The mammalian membrane‐bound O‐acyltransferase (MBOAT) superfamily is involved in biological processes including growth, development and appetite sensing. MBOATs are attractive drug targets in cancer and obesity; however, information on the bindi
Autor:
Anthony I. Magee, Nattawadee Panyain, Thomas Lanyon-Hogg, Markus Ritzefeld, Nicola O’Reilly, Ganka Bineva-Todd, Jasmine K. Bickel, Edward W. Tate, Cory A Ocasio, Lea Sefer, Christian Siebold, A.F. Rudolf
Publikováno v:
Chemical Science
A highly accurate and versatile fluorescence polarisation assay for any enzyme adding or removing lipid posttranslational modifications, with the potential to accelerate drug discovery against these targets.
Posttranslational attachment of lipid
Posttranslational attachment of lipid
Autor:
Thomas Lanyon-Hogg, Markus Ritzefeld, Leran Zhang, Balazs Pogranyi, Milon Mondal, Lea Sefer, Callum D. Johnston, Claire E. Coupland, Sebastian A. Andrei, Joshua Newington, Anthony I. Magee, Christian Siebold, Edward W. Tate
The mammalian membrane-bound O-acyltransferase (MBOAT) superfamily is involved in biological processes including growth, development and appetite sensing. MBOATs are attractive drug targets in cancer and obesity; however, information on the binding s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9e59cf7fba46be40356dcde9c651c2d
http://hdl.handle.net/10044/1/87627
http://hdl.handle.net/10044/1/87627
Autor:
Z. Yu, Shirley M. Roberts, J.A. Hutton, James A. Brannigan, Andrew Simon Bell, Robin J. Leatherbarrow, Daniel Paape, Anthony J. Wilkinson, Megan H. Wright, Charlotte L. Sutherell, Edward W. Tate, Markus Ritzefeld, Deborah F. Smith
Publikováno v:
Journal of Medicinal Chemistry
The leishmaniases, caused by Leishmania species of protozoan parasites, are neglected tropical diseases with millions of cases worldwide. Current therapeutic approaches are limited by toxicity, resistance, and cost. N-Myristoyltransferase (NMT), an e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b9f2666a304fae6a1cac6032c4a5f81
http://hdl.handle.net/10044/1/80204
http://hdl.handle.net/10044/1/80204
Autor:
Mengjie Shen, Cyril Dian, Ernesto Cota, Carmela Giglione, Pierre Legrand, Frédéric Rivière, Edward W. Tate, Thierry Meinnel, Thomas Asensio, Inmaculada Pérez-Dorado, Markus Ritzefeld
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
Nature Communications
'Nature Communications ', vol: 11, pages: 1132-1-1132-15 (2020)
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.1132. ⟨10.1038/s41467-020-14847-3⟩
Nature Communications, 2020, 11 (1), pp.1132. ⟨10.1038/s41467-020-14847-3⟩
Nature Communications
'Nature Communications ', vol: 11, pages: 1132-1-1132-15 (2020)
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.1132. ⟨10.1038/s41467-020-14847-3⟩
Nature Communications, 2020, 11 (1), pp.1132. ⟨10.1038/s41467-020-14847-3⟩
The promising drug target N-myristoyltransferase (NMT) catalyses an essential protein modification thought to occur exclusively at N-terminal glycines (Gly). Here, we present high-resolution human NMT1 structures co-crystallised with reactive cognate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e1596060677e5c95c6f14ce070e70f8
http://hdl.handle.net/10044/1/77568
http://hdl.handle.net/10044/1/77568
Autor:
Stuart Weston, Boon Han Teo, Markus Ritzefeld, Michela Mazzon, Mark Marsh, Edward W. Tate, Camilla T. O. Benfield, Edward C. Holmes, Paul Kellam, Sarah E. Smith, Farrell MacKenzie
Publikováno v:
Life Science Alliance
Comparative analysis reveals adaptive evolution of bat IFITMs and a naturally polymorphic site within the conserved CD225 domain that affects S-palmitoylation and antiviral function of bat IFITM3.
Host interferon-induced transmembrane proteins (
Host interferon-induced transmembrane proteins (
Publikováno v:
Parasitology. 145:157-174
SUMMARYInfections by protozoan parasites, such asPlasmodium falciparumorLeishmania donovani, have a significant health, social and economic impact and threaten billions of people living in tropical and sub-tropical regions of developing countries wor
Autor:
Stuart Weston, Markus Ritzefeld, Edward W. Tate, Edward C. Holmes, Paul Kellam, Farrell MacKenzie, Michela Mazzon, Boon Han Teo, Camilla T. O. Benfield, Sarah E. Smith, Mark Marsh
Host interferon-induced transmembrane proteins (IFITMs) are broad-spectrum antiviral restriction factors. Of these, IFITM3 potently inhibits viruses that enter cells through acidic endosomes, many of which are zoonotic and emerging viruses with bats
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c50037dd6c85e23deee1e3a9e7fd0ec
Autor:
Boon Han Teo, Farrell MacKenzie, Michela Mazzon, Edward C. Holmes, Paul Kellam, Edward W. Tate, Camilla T. O. Benfield, Stuart Weston, Markus Ritzefeld, Sarah E. Smith, Mark Marsh
Publikováno v:
Life Science Alliance
Host interferon-induced transmembrane proteins (IFITMs) are broad-spectrum antiviral restriction factors. Of these, IFITM3 potently inhibits viruses that enter cells through acidic endosomes, many of which are zoonotic and emerging viruses with bats