The third component of the complement system, C3, is a common denominator in the activation of the classical, alternative, and lectin pathways. The ability of C3 molecule to interact with at least 20 different proteins makes it the most versatile component of this system. Since these interactions are important for phagocytic, immunoregulatory, and immune evasion mechanisms, the analysis of its structure and functions has been a subject of intense research. Here we review our current work on the C3-ligand interactions, C3-related viral molecular mimicry, evolution of the complement system, and identification of C3-based complement inhibitors.
%0 Journal Article
%1 Sahu:1998ix
%A Sahu, A
%A Sunyer, J O
%A Moore, W T
%A Sarrias, M R
%A Soulika, A M
%A Lambris, J D
%D 1998
%J Immunologic research
%K imported
%N 1-2
%P 109--121
%R 10.1007/BF02786436
%T Structure, functions, and evolution of the third complement component and viral molecular mimicry.
%U http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=9479573&retmode=ref&cmd=prlinks
%V 17
%X The third component of the complement system, C3, is a common denominator in the activation of the classical, alternative, and lectin pathways. The ability of C3 molecule to interact with at least 20 different proteins makes it the most versatile component of this system. Since these interactions are important for phagocytic, immunoregulatory, and immune evasion mechanisms, the analysis of its structure and functions has been a subject of intense research. Here we review our current work on the C3-ligand interactions, C3-related viral molecular mimicry, evolution of the complement system, and identification of C3-based complement inhibitors.
@article{Sahu:1998ix,
abstract = {The third component of the complement system, C3, is a common denominator in the activation of the classical, alternative, and lectin pathways. The ability of C3 molecule to interact with at least 20 different proteins makes it the most versatile component of this system. Since these interactions are important for phagocytic, immunoregulatory, and immune evasion mechanisms, the analysis of its structure and functions has been a subject of intense research. Here we review our current work on the C3-ligand interactions, C3-related viral molecular mimicry, evolution of the complement system, and identification of C3-based complement inhibitors.},
added-at = {2017-12-08T05:18:19.000+0100},
affiliation = {Department of Pathology and Laboratory Medicine, University of Pennsylvania, Philadelphia 19104, USA.},
author = {Sahu, A and Sunyer, J O and Moore, W T and Sarrias, M R and Soulika, A M and Lambris, J D},
biburl = {https://www.bibsonomy.org/bibtex/2bf29533028582531257356fdbef97c68/lambris},
date-added = {2012-03-27T20:49:08GMT},
date-modified = {2017-12-08T04:17:04GMT},
doi = {10.1007/BF02786436},
interhash = {d14bd7a73834ce899eef512a66f66fc9},
intrahash = {bf29533028582531257356fdbef97c68},
journal = {Immunologic research},
keywords = {imported},
language = {English},
number = {1-2},
pages = {109--121},
pmid = {9479573},
rating = {0},
timestamp = {2017-12-08T05:18:19.000+0100},
title = {{Structure, functions, and evolution of the third complement component and viral molecular mimicry.}},
uri = {\url{papers3://publication/doi/10.1007/BF02786436}},
url = {http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=9479573&retmode=ref&cmd=prlinks},
volume = 17,
year = 1998
}