Výsledky vyhledávání - "N M, Thielens"

Autor: G J, Arlaud, C, Gaboriaud, N M, Thielens, V, Rossi

Publikováno v: Biochemical Society transactions. 30(Pt 6)

The classical complement pathway is a major element of innate immunity against infection, and is also involved in immune tolerance, graft rejection and various pathologies. This pathway is triggered by C1, a multimolecular protease formed from the as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::db828f07c9c70e9010245176ad0c8018
https://pubmed.ncbi.nlm.nih.gov/12440961

Zobrazit plný text záznamu

Structural biology of C1: dissection of a complex molecular machinery

Autor: G J, Arlaud, C, Gaboriaud, N M, Thielens, V, Rossi, B, Bersch, J F, Hernandez, J C, Fontecilla-Camps

Publikováno v: Immunological reviews. 180

The classical pathway of complement is initiated by the C1 complex, a multimolecular protease comprising a recognition subunit (C1q) and two modular serine proteases (C1r and C1s) associated as a Ca2+-dependent tetramer (C1s-C1r-C1r-C1s). Early studi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::91e084373472629591968f78c1cc68b5
https://pubmed.ncbi.nlm.nih.gov/11414355

Zobrazit plný text záznamu

Baculovirus-mediated expression of truncated modular fragments from the catalytic region of human complement serine protease C1s. Evidence for the involvement of both complement control protein modules in the recognition of the C4 protein substrate

Autor: V, Rossi, I, Bally, N M, Thielens, A F, Esser, G J, Arlaud

Publikováno v: The Journal of biological chemistry. 273(2)

C1s is the modular serine protease responsible for cleavage of C4 and C2, the protein substrates of the first component of complement. Its catalytic region (gamma-B) comprises two complement control protein (CCP) modules, a short activation peptide (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f76652d1715a0d80b45cb6c718a2498a
https://pubmed.ncbi.nlm.nih.gov/9422791

Zobrazit plný text záznamu

Identification of a cryptic protein kinase CK2 phosphorylation site in human complement protease Clr, and its use to probe intramolecular interaction

Autor: S, Pelloux, N M, Thielens, G, Hudry-Clergeon, Y, Pétillot, O, Filhol, G J, Arlaud

Publikováno v: FEBS letters. 386(1)

Treatment of human (activated)C1r by CK2 resulted in the incorporation of [32P]phosphate into the N-terminal alpha region of its non-catalytic A chain. Fragmentation of 32P-labelled (activated)C1r followed by N-terminal sequence and mass spectrometry

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6a2f016dccb40d91e79766221675a12b
https://pubmed.ncbi.nlm.nih.gov/8635594

Zobrazit plný text záznamu

Interaction of C1 with HIV-1

Autor: N M, Thielens, I M, Bally, C F, Ebenbichler, M P, Dierich, G J, Arlaud

Publikováno v: Behring Institute Mitteilungen. (93)

In contrast to animal retroviruses such as murine leukemia virus, HIV-1 is not lysed by human complement. Nevertheless, HIV-1 activates complement via the classical pathway independently of antibody. Evidence is provided for activation of the reconst

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6317afa45257fc79be1eae26246727b7
https://pubmed.ncbi.nlm.nih.gov/8172563

Zobrazit plný text záznamu

Human complement serine proteases C1r and C1s and their proenzymes

Autor: G J, Arlaud, N M, Thielens

Publikováno v: Methods in enzymology. 223

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::622c7db6455b07ed55691e61f749d87b
https://pubmed.ncbi.nlm.nih.gov/8271968

Zobrazit plný text záznamu

Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-dependent interactions of human C1s. Location of the iodination sites

Autor: C, Illy, N M, Thielens, J, Gagnon, G J, Arlaud

Publikováno v: Biochemistry. 30(29)

C-1s, one of the two serine proteases of C-1, the first component of complement, has the ability to mediate heterologous (C-1r-C-1s) as well as homologous (C-1s-C-1s) Ca(2+)-dependent interactions both involving the NH2-terminal alpha region of its A

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f59516f914aa90bcef643c5e9db6866e
https://pubmed.ncbi.nlm.nih.gov/1854725

Zobrazit plný text záznamu

Neutron scattering study of the (gamma-B) catalytic domains of complement proteases activated C1r and C1s

Autor: G, Zaccaï, C A, Aude, N M, Thielens, G J, Arlaud

Publikováno v: FEBS letters. 269(1)

The catalytic domains of activated C1r and C1s, comprising the C-terminal region of the A chain (gamma), disulphide-linked to the B chain, were obtained by limited proteolysis of the native proteases with chymotrypsin and plasmin, respectively, and s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9ecf2097d7617f53aadd5b02f30eaef3
https://pubmed.ncbi.nlm.nih.gov/2143735

Zobrazit plný text záznamu

Comparative study of the fluid-phase proteolytic cleavage of human complement subcomponents C4 and C2 by C1s and C1r2-C1s2

Autor: N M, Thielens, C L, Villiers, M B, Villiers, M G, Colomb

Publikováno v: FEBS letters. 165(1)

The C3 convertase of the classical pathway of complement is composed of fragments C4b and C2a resulting from cleavage of C4 and C2 by activated C1. The limited proteolysis of these two different substrates by the same protease, C1s, has been studied

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::844301774c0299623626af2e35f9228b
https://pubmed.ncbi.nlm.nih.gov/6319179

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání