Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Seino A. K. Jongkees"'
Publikováno v:
Molecules, Vol 25, Iss 21, p 4951 (2020)
Targeting of proteins in the histone modification machinery has emerged as a promising new direction to fight disease. The search for compounds that inhibit proteins that readout histone modification has led to several new epigenetic drugs, mostly fo
Externí odkaz:
https://doaj.org/article/55042f92cfac46e0b5b78eeaab29e99c
Autor:
Minglong Liu, Ryoji Yoshisada, Avand Amedi, Antonius J. P. Hopstaken, Mirte N. Pascha, Cornelis A. M. de Haan, Daan P. Geerke, David A. Poole, Seino A. K. Jongkees
Publikováno v:
Liu, M, Yoshisada, R, Amedi, A, Hopstaken, A J P, Pascha, M N, de Haan, C A M, Geerke, D P, Poole, D A & Jongkees, S A K 2023, ' An Efficient, Site-Selective and Spontaneous Peptide Macrocyclisation During in vitro Translation ', Chemistry-A European Journal, vol. 29, no. 14, e202203923, pp. 1-9 . https://doi.org/10.1002/chem.202203923
Chemistry-A European Journal, 29(14):e202203923, 1-9. Wiley-VCH Verlag
Chemistry-A European Journal, 29(14):e202203923, 1-9. Wiley-VCH Verlag
Macrocyclisation provides a means of stabilising the conformation of peptides, often resulting in improved stability, selectivity, affinity, and cell permeability. In this work we report a new approach to peptide macrocyclisation using a cyanobenzoth
Autor:
Vito Thijssen, Daniel L. Hurdiss, Oliver J. Debski-Antoniak, Matthew A. Spence, Charlotte Franck, Alexander Norman, Anupriya Aggarwal, Nadia J. Mokiem, David A. A. van Dongen, Stein W. Vermeir, Minglong Liu, Wentao Li, Marianthi Chatziandreou, Tim Donselaar, Wenjuan Du, Ieva Drulyte, Berend-Jan Bosch, Joost Snijder, Stuart Turville, Richard J. Payne, Colin J. Jackson, Frank J. M. van Kuppeveld, Seino A. K. Jongkees
The ongoing COVID-19 pandemic has had great societal and health consequences. Despite the availability of vaccines, infection rates remain high due to immune evasive Omicron sublineages. Broad-spectrum antivirals are needed to safeguard against emerg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bef323aac59161513088436e62791ac
https://dspace.library.uu.nl/handle/1874/429162
https://dspace.library.uu.nl/handle/1874/429162
Autor:
Mirte N. Pascha, Vito Thijssen, Julia E. Egido, Mirte W. Linthorst, Jipke H. van Lanen, David A. A. van Dongen, Antonius J. P. Hopstaken, Frank J. M. van Kuppeveld, Joost Snijder, Cornelis A. M. de Haan, Seino A. K. Jongkees
Publikováno v:
ACS chemical biology, 17(9), 2425-2436. American Chemical Society
Pascha, M N, Thijssen, V, Egido, J E, Linthorst, M W, Van Lanen, J H, Van Dongen, D A A, Hopstaken, A J P, Van Kuppeveld, F J M, Snijder, J, De Haan, C A M & Jongkees, S A K 2022, ' Inhibition of H1 and H5 Influenza A Virus Entry by Diverse Macrocyclic Peptides Targeting the Hemagglutinin Stem Region ', ACS chemical biology, vol. 17, no. 9, pp. 2425-2436 . https://doi.org/10.1021/acschembio.2c00040
Pascha, M N, Thijssen, V, Egido, J E, Linthorst, M W, Van Lanen, J H, Van Dongen, D A A, Hopstaken, A J P, Van Kuppeveld, F J M, Snijder, J, De Haan, C A M & Jongkees, S A K 2022, ' Inhibition of H1 and H5 Influenza A Virus Entry by Diverse Macrocyclic Peptides Targeting the Hemagglutinin Stem Region ', ACS chemical biology, vol. 17, no. 9, pp. 2425-2436 . https://doi.org/10.1021/acschembio.2c00040
Influenza A viruses pose a serious pandemic risk, while generation of efficient vaccines against seasonal variants remains challenging. There is thus a pressing need for new treatment options. We report here a set of macrocyclic peptides that inhibit
Autor:
Agnieszka Kij, Davide Sartini, Roberto Campagna, Nathaniel I. Martin, Monica Emanuelli, Seino A. K. Jongkees, Ned Buijs, Matthijs J. van Haren, Yurui Zhang, Filip A. Fedak, Stefan Chlopicki, Yongzhi Gao, Lukasz Mateuszuk, Vito Thijssen
Publikováno v:
RSC Chemical Biology, 2(5), 1546-1555
RSC Chemical Biology, 2(5), 1546-1555. Royal Society of Chemistry
Van Haren, M J, Zhang, Y, Thijssen, V, Buijs, N, Gao, Y, Mateuszuk, L, Fedak, F A, Kij, A, Campagna, R, Sartini, D, Emanuelli, M, Chlopicki, S, Jongkees, S A K & Martin, N I 2021, ' Macrocyclic peptides as allosteric inhibitors of nicotinamide : N-methyltransferase (NNMT) ', RSC Chemical Biology, vol. 2, no. 5, pp. 1546-1555 . https://doi.org/10.1039/d1cb00134e
RSC Chemical Biology, 2(5), 1546-1555. Royal Society of Chemistry
Van Haren, M J, Zhang, Y, Thijssen, V, Buijs, N, Gao, Y, Mateuszuk, L, Fedak, F A, Kij, A, Campagna, R, Sartini, D, Emanuelli, M, Chlopicki, S, Jongkees, S A K & Martin, N I 2021, ' Macrocyclic peptides as allosteric inhibitors of nicotinamide : N-methyltransferase (NNMT) ', RSC Chemical Biology, vol. 2, no. 5, pp. 1546-1555 . https://doi.org/10.1039/d1cb00134e
Nicotinamide N-methyltransferase (NNMT) methylates nicotinamide to form 1-methylnicotinamide (MNA) using S-Adenosyl-l-methionine (SAM) as the methyl donor. The complexity of the role of NNMT in healthy and disease states is slowly being elucidated an
Autor:
Daniel J Ford, Martin J. Stone, Minglong Liu, Ram Prasad Bhusal, Seino A. K. Jongkees, Richard J. Payne, Jason Johansen-Leete, Simon R. Foster, Hiroaki Suga, Toby Passioura
Publikováno v:
Journal of the American Chemical Society. 142:9141-9146
Targeting chemokine signaling is an attractive avenue for the treatment of inflammatory disorders. Tyrosine sulfation is an important post-translational modification (PTM) that enhances chemokine-receptor binding and is also utilized by a number of p
Autor:
Matthijs J, van Haren, Yurui, Zhang, Vito, Thijssen, Ned, Buijs, Yongzhi, Gao, Lukasz, Mateuszuk, Filip A, Fedak, Agnieszka, Kij, Roberto, Campagna, Davide, Sartini, Monica, Emanuelli, Stefan, Chlopicki, Seino A K, Jongkees, Nathaniel I, Martin
Publikováno v:
RSC Chemical Biology
Nicotinamide N-methyltransferase (NNMT) methylates nicotinamide to form 1-methylnicotinamide (MNA) using S-adenosyl-l-methionine (SAM) as the methyl donor. The complexity of the role of NNMT in healthy and disease states is slowly being elucidated an
Autor:
Natalie C. J. Strynadka, Gesa Volkers, Seino A. K. Jongkees, Liam J. Worrall, Angel C. Y. Yu, Stephen G. Withers
Publikováno v:
Glycobiology
Propionibacterium acnes, though generally considered part of the normal flora of human skin, is an opportunistic pathogen associated with acne vulgaris as well as other diseases, including endocarditis, endophthalmitis and prosthetic joint infections
Autor:
Štefan Janeček, Rohan J. Williams, Geoff Pincher, Darrell Cockburn, Gurvan Michel, Wataru Saburi, David R. Rose, Brian P. Rempel, Glyn R. Hemsworth, Wim Van den Ende, Jerry Ståhlberg, Leila LoLeggio, Tom Wennekes, Kiyohiko Igarashi, Cedric Montanier, Etienne Rebuffet, Naotake Konno, Harry J. Gilbert, Markus Linder, Ed Bayer, Tirso Pons, Jan-Hendrik Hehemann, Tomomi Sumida, Thierry Fontaine, Takane Katayama, Elizabeth Ficko-Blean, Florence Vincent, Zui Fujimoto, Masafumi Hidaka, Kyle Robinson, Ana R. Luís, Yuichi Sakamoto, Bernard Henrissat, Gustav Vaaje-Kolstad, Jens M. Eklöf, Ian R. Greig, Harry Brumer, Ryuichiro Suzuki, Mats Sandgren, Takashi Tonozuka, Ryszard Brzezinski, Brian L. Mark, Bareket Dassa, Haruhide Mori, Junho Lee, Vivian L. Y. Yip, Birte Svensson, Wade Abbott, Alfons K. G. Felice, Juha Rouvinen, Takayuki Ohnuma, Satoshi Kaneko, Franz J. St John, Ramon Hurtado-Guerrero, Pedro M. Coutinho, Sine Larsen, Gideon J. Davies, Yuval Shoham, Kiyotaka Fujita, Warren W. Wakarchuk, Fathima Aidha Shaikh, Alisdair B. Boraston, Breeanna R. Urbanowicz, Vincent G. H. Eijsink, Daniel Kracher, Beatrice Cobucci-Ponzano, Ethan D. Goddard-Borger, Anthony J. Clarke, David J. Vocadlo, Katsuro Yaoi, Seino A. K. Jongkees, Anna A. Kulminskaya, Roland Ludwig, Mirko M. Maksimainen, Magali Remaud-Simeon, Edward J. Taylor, Motomitsu Kitaoka, Spencer J. Williams, Shinya Fushinobu, Marco Moracci, David Wilson, Richard McLean, Toki Taira, Jean-Guy Berrin, Ran Zhang, Hiroyuki Nakai, Tracey M. Gloster, Peter J. Reilly, Wim Nerinckx, Takuya Ishida, Alicia Lammerts van Bueren, Orly Alber, Mirjam Czjzek, Kathleen Piens, Annabelle Varrot, Stephen G. Withers, Nathalie Juge, Maxime Versluys, Gerlind Sulzenbacher, Richard W. Pickersgill, Michael D. L. Suits
Publikováno v:
Glycobiology
Glycobiology, Oxford University Press (OUP), 2018, 28 (1), pp.3-8. ⟨10.1093/glycob/cwx089⟩
Glycobiology, 2018, 28 (1), pp.3-8. ⟨10.1093/glycob/cwx089⟩
Glycobiology (Oxf.) 28 (2018): 3–8. doi:10.1093/glycob/cwx089
info:cnr-pdr/source/autori:Abbott, Wade; Alber, Orly; Bayer, Ed; Berrin, Jean-Guy; Boraston, Alisdair; Brumer, Harry; Brzezinski, Ryszard; Clarke, Anthony; Cobucci-Ponzano, Beatrice; Cockburn, Darrell; Coutinho, Pedro; Czjzek, Mirjam; Dassa, Bareket; Davies, Gideon John; Eijsink, Vincent; Eklof, Jens; Felice, Alfons; Ficko-Blean, Elizabeth; Pincher, Geoff; Fontaine, Thierry; Fujimoto, Zui; Fujita, Kiyotaka; Fushinobu, Shinya; Gilbert, Harry; Gloster, Tracey; Goddard-Borger, Ethan; Greig, Ian; Hehemann, Jan-Hendrik; Hemsworth, Glyn; Henrissat, Bernard; Hidaka, Masafumi; Hurtado-Guerrero, Ramon; Igarashi, Kiyohiko; Ishida, Takuya; Janecek, Stefan; Jongkees, Seino; Juge, Nathalie; Kaneko, Satoshi; Katayama, Takane; Kitaoka, Motomitsu; Konno, Naotake; Kracher, Daniel; Kulminskaya, Anna; van Bueren, Alicia Lammerts; Larsen, Sine; Lee, Junho; Linder, Markus; LoLeggio, Leila; Ludwig, Roland; Luis, Ana; Maksimainen, Mirko; Mark, Brian; McLean, Richard; Michel, Gurvan; Michel, Gurvan; Montanier, Cedric; Moracci, Marco; Mori, Haruhide; Nakai, Hiroyuki; Nerinckx, Wim; Ohnuma, Takayuki; Pickersgill, Richard; Piens, Kathleen; Pons, Tirso; Rebuffet, Etienne; Reilly, Peter; Remaud-Simeon, Magali; Rempel, Brian; Robinson, Kyle; Rose, David; Rouvinen, Juha; Saburi, Wataru; Sakamoto, Yuichi; Sandgren, Mats; Shaikh, Fathima; Shoham, Yuval; St John, Franz; Stahlberg, Jerry; Suits, Michael; Sulzenbacher, Gerlind; Sumida, Tomomi; Suzuki, Ryuichiro; Svensson, Birte; Taira, Toki; Taylor, Ed; Tonozuka, Takashi; Urbanowicz, Breeanna; Vaaje-Kolstad, Gustav; Van den Ende, Wim; Varrot, Annabelle; Versluys, Maxime; Vincent, Florence; Vocadlo, David; Wakarchuk, Warren; Wennekes, Tom; Williams, Rohan; Williams, Spencer; Wilson, David; Withers, Stephen; Yaoi, Katsuro; Yip, Vivian; Zhang, Ran/titolo:Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes/doi:10.1093%2Fglycob%2Fcwx089/rivista:Glycobiology (Oxf.)/anno:2018/pagina_da:3/pagina_a:8/intervallo_pagine:3–8/volume:28
Abbott, W, Alber, O, bayer, E, Berrin, J-G, Boraston, A, Brumer, H, Brzezinski, R, Clarke, A, Cobucci-Ponzano, B, Cockburn, D, Coutinho, P, Czjzek, M, Dassa, B, Davies, G J, Eijsink, V, Eklöf, J, Felice, A, Ficko-Blean, E, Fincher, G, Fontaine, T, Fujimoto, Z, Fujita, K, Fushinobu, S, Gilbert, H, Gloster, T, Goddard-Borger, E, Greig, I, Hehemann, J-H, Hemsworth, G, Henrissat, B, Hidaka, M, Hurtado-Guerrero, R, Igarashi, K, Ishida, T, Janeček, Š, Jongkees, S, Juge, N, Kaneko, S, Katayama, T, Kitaoka, M, Konno, N, Kracher, D, Kulminskaya, A, Lammerts van Bueren, A, Larsen, S, Lee, J, Linder, M, Lo Leggio, L, Ludwig, R, Luis, A, Maksimainen, M, Mark, B, McLean, R, Michel, G, Montanier, C, Moracci, M, Mori, H, Nakai, H, Nerinckx, W, Ohnuma, T, Pickersgill, R, Piens, K, Pons, T, Rebuffet, E, Reilly, P, Remaud-Simeon, M, Rempel, B, Robinson, K, Rose, D, Rouvinen, J, Saburi, W, Sakamoto, Y, Sandgren, M, Shaikh, F, Shoham, Y, St. John, F, Stahlberg, J, Suits, M, Sulzenbacher, G, Sumida, T, Suzuki, R, Svensson, B, Taira, T, Taylor, E, Tonozuka, T, Urbanowicz, B, Vaaje-Kolstad, G, Van den Ende, W, Varrot, A, Verluys, M, Vincent, F, Vocadlo, D, Wakarchuk, W, Wennekes, T, Williams, R, Williams, S, Wilkens, C, Wilson, D, Withers, S, Yaoi, K, Yip, V & Zhang, R 2018, ' Ten years of CAZypedia : a living encyclopedia of carbohydrate-active enzymes ', Glycobiology, vol. 28, no. 1, pp. 3-8 . https://doi.org/10.1093/glycob/cwx089
GLYCOBIOLOGY
Glycobiology, 28(1), 3. Oxford University Press
Glycobiology, Oxford University Press (OUP), 2018, 28 (1), pp.3-8. ⟨10.1093/glycob/cwx089⟩
Glycobiology, 2018, 28 (1), pp.3-8. ⟨10.1093/glycob/cwx089⟩
Glycobiology (Oxf.) 28 (2018): 3–8. doi:10.1093/glycob/cwx089
info:cnr-pdr/source/autori:Abbott, Wade; Alber, Orly; Bayer, Ed; Berrin, Jean-Guy; Boraston, Alisdair; Brumer, Harry; Brzezinski, Ryszard; Clarke, Anthony; Cobucci-Ponzano, Beatrice; Cockburn, Darrell; Coutinho, Pedro; Czjzek, Mirjam; Dassa, Bareket; Davies, Gideon John; Eijsink, Vincent; Eklof, Jens; Felice, Alfons; Ficko-Blean, Elizabeth; Pincher, Geoff; Fontaine, Thierry; Fujimoto, Zui; Fujita, Kiyotaka; Fushinobu, Shinya; Gilbert, Harry; Gloster, Tracey; Goddard-Borger, Ethan; Greig, Ian; Hehemann, Jan-Hendrik; Hemsworth, Glyn; Henrissat, Bernard; Hidaka, Masafumi; Hurtado-Guerrero, Ramon; Igarashi, Kiyohiko; Ishida, Takuya; Janecek, Stefan; Jongkees, Seino; Juge, Nathalie; Kaneko, Satoshi; Katayama, Takane; Kitaoka, Motomitsu; Konno, Naotake; Kracher, Daniel; Kulminskaya, Anna; van Bueren, Alicia Lammerts; Larsen, Sine; Lee, Junho; Linder, Markus; LoLeggio, Leila; Ludwig, Roland; Luis, Ana; Maksimainen, Mirko; Mark, Brian; McLean, Richard; Michel, Gurvan; Michel, Gurvan; Montanier, Cedric; Moracci, Marco; Mori, Haruhide; Nakai, Hiroyuki; Nerinckx, Wim; Ohnuma, Takayuki; Pickersgill, Richard; Piens, Kathleen; Pons, Tirso; Rebuffet, Etienne; Reilly, Peter; Remaud-Simeon, Magali; Rempel, Brian; Robinson, Kyle; Rose, David; Rouvinen, Juha; Saburi, Wataru; Sakamoto, Yuichi; Sandgren, Mats; Shaikh, Fathima; Shoham, Yuval; St John, Franz; Stahlberg, Jerry; Suits, Michael; Sulzenbacher, Gerlind; Sumida, Tomomi; Suzuki, Ryuichiro; Svensson, Birte; Taira, Toki; Taylor, Ed; Tonozuka, Takashi; Urbanowicz, Breeanna; Vaaje-Kolstad, Gustav; Van den Ende, Wim; Varrot, Annabelle; Versluys, Maxime; Vincent, Florence; Vocadlo, David; Wakarchuk, Warren; Wennekes, Tom; Williams, Rohan; Williams, Spencer; Wilson, David; Withers, Stephen; Yaoi, Katsuro; Yip, Vivian; Zhang, Ran/titolo:Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes/doi:10.1093%2Fglycob%2Fcwx089/rivista:Glycobiology (Oxf.)/anno:2018/pagina_da:3/pagina_a:8/intervallo_pagine:3–8/volume:28
Abbott, W, Alber, O, bayer, E, Berrin, J-G, Boraston, A, Brumer, H, Brzezinski, R, Clarke, A, Cobucci-Ponzano, B, Cockburn, D, Coutinho, P, Czjzek, M, Dassa, B, Davies, G J, Eijsink, V, Eklöf, J, Felice, A, Ficko-Blean, E, Fincher, G, Fontaine, T, Fujimoto, Z, Fujita, K, Fushinobu, S, Gilbert, H, Gloster, T, Goddard-Borger, E, Greig, I, Hehemann, J-H, Hemsworth, G, Henrissat, B, Hidaka, M, Hurtado-Guerrero, R, Igarashi, K, Ishida, T, Janeček, Š, Jongkees, S, Juge, N, Kaneko, S, Katayama, T, Kitaoka, M, Konno, N, Kracher, D, Kulminskaya, A, Lammerts van Bueren, A, Larsen, S, Lee, J, Linder, M, Lo Leggio, L, Ludwig, R, Luis, A, Maksimainen, M, Mark, B, McLean, R, Michel, G, Montanier, C, Moracci, M, Mori, H, Nakai, H, Nerinckx, W, Ohnuma, T, Pickersgill, R, Piens, K, Pons, T, Rebuffet, E, Reilly, P, Remaud-Simeon, M, Rempel, B, Robinson, K, Rose, D, Rouvinen, J, Saburi, W, Sakamoto, Y, Sandgren, M, Shaikh, F, Shoham, Y, St. John, F, Stahlberg, J, Suits, M, Sulzenbacher, G, Sumida, T, Suzuki, R, Svensson, B, Taira, T, Taylor, E, Tonozuka, T, Urbanowicz, B, Vaaje-Kolstad, G, Van den Ende, W, Varrot, A, Verluys, M, Vincent, F, Vocadlo, D, Wakarchuk, W, Wennekes, T, Williams, R, Williams, S, Wilkens, C, Wilson, D, Withers, S, Yaoi, K, Yip, V & Zhang, R 2018, ' Ten years of CAZypedia : a living encyclopedia of carbohydrate-active enzymes ', Glycobiology, vol. 28, no. 1, pp. 3-8 . https://doi.org/10.1093/glycob/cwx089
GLYCOBIOLOGY
Glycobiology, 28(1), 3. Oxford University Press
CAZypedia was initiated in 2007 to create a comprehensive, living encyclopedia of the carbohydrate-active enzymes (CAZymes) and associated carbohydrate-binding modules involved in the synthesis, modification, and degradation of complex carbohydrates.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7dd922fbf8f91c4c149f1a6b7dd921fd
https://hal.archives-ouvertes.fr/hal-01886461/document
https://hal.archives-ouvertes.fr/hal-01886461/document
Publikováno v:
New Journal of Chemistry. 39:3197-3207
Foldamers are synthetic molecules that seek to mimic the structure-forming propensity of biomolecules, such as proteins. However, on a short oligomer scale, peptides often do not fold in the same manner as large proteins, despite being composed of th