Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Alessandra Zarantonello"'
Autor:
Nadia Sukusu Nielsen, Alessandra Zarantonello, Seandean Lykke Harwood, Kathrine Tejlgård Jensen, Katarzyna Kjøge, Ida B. Thøgersen, Leif Schauser, Jesper Lykkegaard Karlsen, Gregers R. Andersen, Jan J. Enghild
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-15 (2022)
A2ML1 is a human protease inhibitor belonging to the A2M protein family. In this study, the authors determine structures of A2ML1 before and after protease inhibition and investigate its mechanism of action.
Externí odkaz:
https://doaj.org/article/1cf0aa0675724f8aba533fcc6fbc1b1f
Autor:
Alexandra Gerogianni, Jordan D. Dimitrov, Alessandra Zarantonello, Victoria Poillerat, Satheesh Chonat, Kerstin Sandholm, Karin E. McAdam, Kristina N. Ekdahl, Tom E. Mollnes, Camilla Mohlin, Lubka T. Roumenina, Per H. Nilsson
Publikováno v:
Frontiers in Immunology, Vol 13 (2022)
Hemolysis, as a result of disease or exposure to biomaterials, is characterized by excess amounts of cell-free heme intravascularly and consumption of the protective heme-scavenger proteins in plasma. The liberation of heme has been linked to the act
Externí odkaz:
https://doaj.org/article/0a05f1bf9b5b4cc29cb6730c4a4c8d47
Autor:
Nick S. Laursen, Dennis V. Pedersen, Heidi Gytz, Alessandra Zarantonello, Jens Magnus Bernth Jensen, Annette G. Hansen, Steffen Thiel, Gregers R. Andersen
Publikováno v:
Frontiers in Immunology, Vol 11 (2020)
The classical pathway of complement is important for protection against pathogens and in maintaining tissue homeostasis, but excessive or aberrant activation is directly linked to numerous pathologies. We describe the development and in vitro charact
Externí odkaz:
https://doaj.org/article/f5719bd1f44141fd8a64312c7a8685db
Publikováno v:
Biomolecules, Vol 11, Iss 2, p 298 (2021)
The complement system is part of the innate immune response, where it provides immediate protection from infectious agents and plays a fundamental role in homeostasis. Complement dysregulation occurs in several diseases, where the tightly regulated p
Externí odkaz:
https://doaj.org/article/506ee8ba181d45bab96db5027cab3e54
Autor:
Cyril Planchais, Alejandra Reyes‐Ruiz, Robin Lacombe, Alessandra Zarantonello, Maxime Lecerf, Margot Revel, Lubka T. Roumenina, Boris P. Atanasov, Hugo Mouquet, Jordan D. Dimitrov
Publikováno v:
Protein Science
Protein Science, 2022, 31 (11), pp.e4447. ⟨10.1002/pro.4447⟩
Protein Science, 2022, 31 (11), pp.e4447. ⟨10.1002/pro.4447⟩
SARS-CoV-2 infects cells by attachment to its receptor – the angiotensin converting enzyme 2 (ACE2). Regardless of the wealth of structural data, little is known about the physicochemical mechanism of interactions of the viral spike (S) protein wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50051d30e52c9cf9bd36a0d5a2677062
https://hal.sorbonne-universite.fr/hal-03835297
https://hal.sorbonne-universite.fr/hal-03835297
Autor:
Jessy Presumey, Matthew B. Johnson, Steffen Thiel, Beth Stevens, Heidi Gytz Olesen, Esra Yalcin, Annette G. Hansen, Alessandra Zarantonello, Lea Simoni, Gregers R. Andersen, Nick S. Laursen, Michael C. Carroll, Rachel Fox
Publikováno v:
Zarantonello, A, Presumey, J, Simoni, L, Yalcin, E, Fox, R, Hansen, A, Olesen, H G, Thiel, S, Johnson, M B, Stevens, B, Laursen, N S, Carroll, M C & Andersen, G R 2020, ' An Ultrahigh-Affinity Complement C4b-Specific Nanobody Inhibits In Vivo Assembly of the Classical Pathway Proconvertase ', Journal of Immunology, vol. 205, no. 6, pp. 1678-1694 . https://doi.org/10.4049/jimmunol.2000528
The classical and lectin pathways of the complement system are important for the elimination of pathogens and apoptotic cells and stimulation of the adaptive immune system. Upon activation of these pathways, complement component C4 is proteolytically
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67c6fbf3123aaa6ad82aced639ed7595
https://doi.org/10.4049/jimmunol.2000528
https://doi.org/10.4049/jimmunol.2000528
Publikováno v:
Immunological Reviews
Immunological Reviews, In press, ⟨10.1111/imr.13147⟩
Immunological Reviews, In press, ⟨10.1111/imr.13147⟩
International audience; C3 is the central effector molecule of the complement system, mediating its multiple functions through different binding sites and their corresponding receptors. We will introduce the C3 forms (native C3, C3 [H2 O], and intrac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::485e7439e2d7307ee5538162a5fe0f65
https://hal.sorbonne-universite.fr/hal-03829321
https://hal.sorbonne-universite.fr/hal-03829321
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2227
Activated complement component C4 (C4b) is the nonenzymatic component of the classical pathway (CP) convertases of the complement system. Preparation of C4 and C4b samples suitable for structural biology studies is challenging due to low yields and c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::939bcfec39317ac1fde0f62525be7862
https://pubmed.ncbi.nlm.nih.gov/33847947
https://pubmed.ncbi.nlm.nih.gov/33847947
Publikováno v:
Biomolecules
Zarantonello, A, Pedersen, H, Laursen, N S & Andersen, G R 2021, ' Nanobodies provide insight into the molecular mechanisms of the complement cascade and offer new therapeutic strategies ', Biomolecules, vol. 11, no. 2, 298 . https://doi.org/10.3390/biom11020298
Biomolecules, Vol 11, Iss 298, p 298 (2021)
Zarantonello, A, Pedersen, H, Laursen, N S & Andersen, G R 2021, ' Nanobodies provide insight into the molecular mechanisms of the complement cascade and offer new therapeutic strategies ', Biomolecules, vol. 11, no. 2, 298 . https://doi.org/10.3390/biom11020298
Biomolecules, Vol 11, Iss 298, p 298 (2021)
The complement system is part of the innate immune response, where it provides immediate protection from infectious agents and plays a fundamental role in homeostasis. Complement dysregulation occurs in several diseases, where the tightly regulated p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be91f65f61fa05090bd8fe2254c7d773
http://europepmc.org/articles/PMC7922070
http://europepmc.org/articles/PMC7922070
Autor:
Jan Skov Pedersen, Alessandra Zarantonello, Jeppe Lyngsø, Peter Kresten Nielsen, Seandean Lykke Harwood, Gregers R. Andersen, Katarzyna Kjøge, Jan J. Enghild
Publikováno v:
Molecular & Cellular Proteomics : MCP
Harwood, S L, Lyngsø, J, Zarantonello, A, Kjøge, K, Nielsen, P K, Andersen, G R, Pedersen, J S & Enghild, J J 2021, ' Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism ', Molecular and Cellular Proteomics, vol. 20, 100090 . https://doi.org/10.1016/J.MCPRO.2021.100090
Harwood, S L, Lyngsø, J, Zarantonello, A, Kjøge, K, Nielsen, P K, Andersen, G R, Pedersen, J S & Enghild, J J 2021, ' Structural Investigations of Human A2M Identify a Hollow Native Conformation That Underlies Its Distinctive Protease-Trapping Mechanism ', Molecular and Cellular Proteomics, vol. 20, 100090 . https://doi.org/10.1016/J.MCPRO.2021.100090
Human α2-macroglobulin (A2M) is the most characterized protease inhibitor in the alpha-macroglobulin (αM) superfamily, but the structure of its native conformation has not been determined. Here, we combined negative stain electron microscopy (EM),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba93a57e998917d521f72c9589576dbf
https://pubmed.ncbi.nlm.nih.gov/33964423
https://pubmed.ncbi.nlm.nih.gov/33964423