Biophysical Characterization of the Oligomeric States of Recombinant Immunoglobulins Type-M and Their C1q-Binding Kinetics by Biolayer Interferometry

Autor: Anne Chouquet, Andrea J. Pinto, Julia Hennicke, Wai Li Ling, Isabelle Bally, Linda Schwaigerlehner, Nicole M. Thielens, Renate Kunert, Jean-Baptiste Reiser

Publikováno v: Frontiers in Bioengineering and Biotechnology, Vol 10 (2022)

Immunoglobulins type-M (IgMs) are one of the first antibody classes mobilized during immune responses against pathogens and tumor cells. Binding to specific target antigens enables the interaction with the C1 complex which strongly activates the clas

Externí odkaz: https://doaj.org/article/fd92bd410b3d444aa041d51ce9174efb

Two Different Missense C1S Mutations, Associated to Periodontal Ehlers-Danlos Syndrome, Lead to Identical Molecular Outcomes

Autor: Isabelle Bally, Fabien Dalonneau, Anne Chouquet, Rebekka Gröbner, Albert Amberger, Ines Kapferer-Seebacher, Heribert Stoiber, Johannes Zschocke, Nicole M. Thielens, Véronique Rossi, Christine Gaboriaud

Publikováno v: Frontiers in Immunology, Vol 10 (2019)

Ehlers-Danlos syndromes (EDS) are clinically and genetically heterogeneous disorders characterized by soft connective tissue alteration like joint hypermobility and skin hyper-extensibility. We previously identified heterozygous missense mutations in

Externí odkaz: https://doaj.org/article/a3474fe3975b4cf8a32afe8ea80ca13c

Structures of parasite calreticulins provide insights into their flexibility and dual carbohydrate/peptide-binding properties

Autor: Christophe Moreau, Gianluca Cioci, Marina Iannello, Emmanuelle Laffly, Anne Chouquet, Arturo Ferreira, Nicole M. Thielens, Christine Gaboriaud

Publikováno v: IUCrJ, Vol 3, Iss 6, Pp 408-419 (2016)

Calreticulin (CRT) is a multifaceted protein, initially discovered as an endoplasmic reticulum (ER) chaperone protein, that is essential in calcium metabolism. Various implications in cancer, early development and immunology have been discovered more

Externí odkaz: https://doaj.org/article/5ca85c477eb046baad43355d2eaa3caf

X-ray structure of the human calreticulin globular domain reveals a peptide-binding area and suggests a multi-molecular mechanism.

Autor: Anne Chouquet, Helena Païdassi, Wai Li Ling, Philippe Frachet, Gunnar Houen, Gérard J Arlaud, Christine Gaboriaud

Publikováno v: PLoS ONE, Vol 6, Iss 3, p e17886 (2011)

In the endoplasmic reticulum, calreticulin acts as a chaperone and a Ca(2+)-signalling protein. At the cell surface, it mediates numerous important biological effects. The crystal structure of the human calreticulin globular domain was solved at 1.55

Externí odkaz: https://doaj.org/article/eaade0fab6c445af9f24313a60756608

Complement C1q Interacts With LRP1 Clusters II and IV Through a Site Close but Different From the Binding Site of Its C1r and C1s-Associated Proteases

Autor: Jean-Philippe Kleman, Evelyne Gout, Catherine Wicker-Planquart, Guillaume Fouët, Camilla De Nardis, Nicole M. Thielens, Christine Gaboriaud, Anne Chouquet, Véronique Rossi, Isabelle Bally, Stéphane Dedieu

Publikováno v: Frontiers in Immunology, Vol 11 (2020)
Frontiers in Immunology
Frontiers in Immunology, Frontiers, 2020, 11, pp.583754. ⟨10.3389/fimmu.2020.583754⟩
Frontiers in Immunology, 2020, 11, pp.583754. ⟨10.3389/fimmu.2020.583754⟩

LRP1 is a large endocytic modular receptor that plays a crucial role in the scavenging of apoptotic material through binding to pattern-recognition molecules. It is a membrane anchored receptor of the LDL receptor family with 4 extracellular clusters

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c24edb52e5b8a4cb721d46684512baf
https://www.frontiersin.org/articles/10.3389/fimmu.2020.583754/full