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C1q and tumor necrosis factor superfamily: modularity and versatility.
The Crystal Structure of the Globular Head of Complement Protein C1q Provides a Basis for Its Versatile Recognition Properties*
- C. Gaboriaud, J. Juanhuix, G. Arlaud
- Chemistry, BiologyJournal of Biological Chemistry
- 21 November 2003
The crystal structure of the C1q globular domain responsible for its recognition properties has now been solved and refined to 1.9 Å of resolution, revealing a compact, almost spherical heterotrimeric assembly held together mainly by non-polar interactions.
Expression patterns of GASA genes in Arabidopsis thaliana: the GASA4 gene is up-regulated by gibberellins in meristematic regions
- D. Aubert, M. Chevillard, A. Dorne, G. Arlaud, M. Herzog
- Environmental SciencePlant Molecular Biology
- 1 April 1998
Interestingly, GA strongly inhibit GUS activity in expanding cotyledons and leaves in ga1–3 mutants supplied with exogenous GAs, as well as in the wild type.
Substrate Specificities of Recombinant Mannan-binding Lectin-associated Serine Proteases-1 and -2*
- V. Rossi, S. Cseh, I. Bally, N. Thielens, J. Jensenius, G. Arlaud
- BiologyThe Journal of Biological Chemistry
- 2 November 2001
Data strongly support the hypothesis that MASP-2 is the protease that, in association with MBL, triggers complement activation via the MBL pathway, through combined self-activation and proteolytic properties devoted to C1r and C1s in the C1 complex.
C1q Binds Phosphatidylserine and Likely Acts as a Multiligand-Bridging Molecule in Apoptotic Cell Recognition1
Data suggest that C1q has the unique ability to sense different markers which collectively would provide strong eat me signals, thereby allowing efficient apoptotic cell removal.
Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins
Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains, which define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces.
Structure and activation of the C1 complex of complement: unraveling the puzzle.
Interaction of 125I‐labelled complement subcomponents C r and C s with protease inhibitors in plasma
Interactions of the Extracellular Matrix Proteoglycans Decorin and Biglycan with C1q and Collectins1
Decorin and biglycan act as inhibitors of activation of the complement cascade, cellular interactions, and proinflammatory cytokine production mediated by C1q, and are likely to down-regulate proinflammatory effects mediated by the collectins at the tissue level.
Residue Lys57 in the Collagen-Like Region of Human L-Ficolin and Its Counterpart Lys47 in H-Ficolin Play a Key Role in the Interaction with the Mannan-Binding Lectin-Associated Serine Proteases and…
- M. Lacroix, C. Dumestre-Perard, N. Thielens
- Biology, ChemistryThe Journal of Immunology
- 1 January 2009
R residues Lys57 of L- ficolin and Lys47 of H-ficolin are key components of the interaction with the MASPs and CRT, providing strong indication that MBL and the ficolins share homologous binding sites for both types of proteins.