Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Jorge Ripoll‐Rozada"'
Self-recycling and partially conservative replication of mycobacterial methylmannose polysaccharides
Autor:
Ana Maranha, Mafalda Costa, Jorge Ripoll-Rozada, José A. Manso, Vanessa Miranda, Vera M. Mendes, Bruno Manadas, Sandra Macedo-Ribeiro, M. Rita Ventura, Pedro José Barbosa Pereira, Nuno Empadinhas
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-17 (2023)
The mechanism of methylmannose polysaccharide (MMP) biogenesis in nontuberculous mycobacteria (NTM) is characterized, which involves an MMP-specific hydrolase (MmpH) and a rare mannosyltransferase (ManT). MmpH and ManT structures are presented.
Externí odkaz:
https://doaj.org/article/160414c28e904d199761ec1e0d62082e
Autor:
Emma E. Watson, Xuyu Liu, Robert E. Thompson, Jorge Ripoll-Rozada, Mike Wu, Imala Alwis, Alessandro Gori, Choy-Theng Loh, Benjamin L. Parker, Gottfried Otting, Shaun Jackson, Pedro José Barbosa Pereira, Richard J. Payne
Publikováno v:
ACS Central Science, Vol 4, Iss 4, Pp 468-476 (2018)
Externí odkaz:
https://doaj.org/article/39f6c6008a294a2faf94d657f88622d6
Publikováno v:
Biochemical Society Transactions. 50:387-401
Tyrosine-O-sulfation is a common post-translational modification (PTM) of proteins following the cellular secretory pathway. First described in human fibrinogen, tyrosine-O-sulfation has long been associated with the modulation of protein–protein i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e373b6e06444dcb86976b109c5b0ceaf
https://doi.org/10.1042/bst20210600
https://doi.org/10.1042/bst20210600
Potent Cyclic Peptide Inhibitors of FXIIa Discovered by mRNA Display with Genetic Code Reprogramming
Autor:
Daniel J Ford, Henri M. H. Spronk, Wenyu Liu, Vishnu M. Sasi, Colin J. Jackson, Tilman M. Hackeng, Nisharnthi M Duggan, Pedro Pereira, Hiroaki Suga, Stijn M. Agten, Anneliese S. Ashhurst, Rene van Oerle, Jorge Ripoll-Rozada, Richard J. Payne, Joe A. Kaczmarski, Leo Corcilius, Toby Passioura, Sarah E. Fry
Publikováno v:
Journal of Medicinal Chemistry, 64(11), 7853-7876. American Chemical Society
The contact system comprises a series of serine proteases that mediate procoagulant and proinflammatory activities via the intrinsic pathway of coagulation and the kallikrein-kinin system, respectively. Inhibition of Factor XIIa (FXIIa), an initiator
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a0a2fcd6f50b94b3bfc83aa64363fc4
https://doi.org/10.1021/acs.jmedchem.1c00651
https://doi.org/10.1021/acs.jmedchem.1c00651
Autor:
Mike C. L. Wu, Imala Alwis, Richard J. Payne, Pedro Pereira, Shaun P. Jackson, Emma E. Watson, Jorge Ripoll-Rozada, Stijn M. Agten, Luke J. Dowman
Publikováno v:
Angewandte Chemie-International Edition, 60(10), 5348-5356. Wiley-VCH Verlag
Blood feeding arthropods, such as leeches, ticks, flies and mosquitoes, provide a privileged source of peptidic anticoagulant molecules. These primarily operate through inhibition of the central coagulation protease thrombin by binding to the active
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62b8ae05a719d1ad3bf8caa24794e3ba
https://doi.org/10.1002/anie.202015127
https://doi.org/10.1002/anie.202015127
Autor:
Stijn M. Agten, Emma E. Watson, Jorge Ripoll‐Rozada, Luke J. Dowman, Mike C. L. Wu, Imala Alwis, Shaun P. Jackson, Pedro José Barbosa Pereira, Richard J. Payne
Publikováno v:
Angewandte Chemie. 133:5408-5416
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::22079735b5dec7102353a97fb283be13
https://doi.org/10.1002/ange.202015127
https://doi.org/10.1002/ange.202015127
Synthesis and evaluation of peptidic thrombin inhibitors bearing acid-stable sulfotyrosine analogues
Autor:
Jorge Ripoll-Rozada, Bárbara M. Calisto, Pedro Pereira, Richard J. Payne, Stijn M. Agten, Luke J. Dowman
Publikováno v:
Chemical Communications, 57(83), 10923-10926. Royal Society of Chemistry
Tyrosine sulfation is an important post-translational modification of peptides and proteins which underpins and modulates many protein-protein interactions. In order to overcome the inherent instability of the native modification, we report the synth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2832f1a00825e0326796a93da730a64
https://doi.org/10.1039/d1cc04742f
https://doi.org/10.1039/d1cc04742f
Self-recycling and partially conservative replication of mycobacterial methylmannose polysaccharides
Autor:
Ana Maranha, Mafalda Costa, Jorge Ripoll-Rozada, José A. Manso, Vanessa Miranda, Vera M. Mendes, Bruno Manadas, Sandra Macedo-Ribeiro, M. Rita Ventura, Pedro José Barbosa Pereira, Nuno Empadinhas
Publikováno v:
Communications biology, 2023, 6(1), 108
The steep increase in nontuberculous mycobacteria (NTM) infections makes understanding their unique physiology an urgent health priority. NTM synthesize two polysaccharides proposed to modulate fatty acid metabolism: the ubiquitous 6-O-methylglucose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c01017da7a80725bb99e047c42290260
https://doi.org/10.21203/rs.3.rs-1362692/v1
https://doi.org/10.21203/rs.3.rs-1362692/v1
Autor:
Richard J. Payne, Daniel Clayton, Sameer S. Kulkarni, Jorge Ripoll-Rozada, Jessica Sayers, Pedro Pereira, Luke J. Dowman
Publikováno v:
RSC Chemical Biology. 1:379-384
The haemathrins are tick-derived thrombin-inhibiting proteins predicted to be post-translationally sulfated. This study reports the ligation-based assembly of eight homogeneously sulfated variants of haemathrin-1 and haemathrin-2. Functional assays r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b2e14be1be4adaff04bd10a578492867
https://doi.org/10.1039/d0cb00146e
https://doi.org/10.1039/d0cb00146e
Autor:
Ashley Lee, Tim Pasch, Charlotte Franck, Shaun P. Jackson, Emma E. Watson, Jessica Sayers, Bhavesh Premdjee, Pedro M. Martins, Pedro Pereira, Jorge Ripoll-Rozada, Richard J. Payne, Mike C. L. Wu, Maria Filipa Pinto
Publikováno v:
Proceedings of the National Academy of Sciences. 116:13873-13878
Hematophagous organisms produce a suite of salivary proteins which interact with the host's coagulation machinery to facilitate the acquisition and digestion of a bloodmeal. Many of these biomolecules inhibit the central blood-clotting serine protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e62b200a1628977e0588688668e3c323
https://doi.org/10.1073/pnas.1905177116
https://doi.org/10.1073/pnas.1905177116