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Showing results for C. roumenina
Your search for C. Roumenin retrieved no results
C1q+ macrophages: passengers or drivers of cancer progression.
Revel M, Sautès-Fridman C, Fridman WH, Roumenina LT. Revel M, et al. Trends Cancer. 2022 Jul;8(7):517-526. doi: 10.1016/j.trecan.2022.02.006. Epub 2022 Mar 12. Trends Cancer. 2022. PMID: 35288093 Review.
C1q is co-expressed in healthy and tumor macrophages with human leukocyte antigen DR (HLA-DR), Apolipoprotein E (APOE), and mannose receptor C-type 1 (MRC1) (CD206), suggesting a resident origin of this population. ...
C1q is co-expressed in healthy and tumor macrophages with human leukocyte antigen DR (HLA-DR), Apolipoprotein E (APOE), and mannose receptor …
The receptor for advanced glycation end products is a sensor for cell-free heme.
May O, Yatime L, Merle NS, Delguste F, Howsam M, Daugan MV, Paul-Constant C, Billamboz M, Ghinet A, Lancel S, Dimitrov JD, Boulanger E, Roumenina LT, Frimat M. May O, et al. FEBS J. 2021 Jun;288(11):3448-3464. doi: 10.1111/febs.15667. Epub 2020 Dec 29. FEBS J. 2021. PMID: 33314778 Free article.
A Single-Domain Antibody Targeting Complement Component C5 Acts as a Selective Inhibitor of the Terminal Pathway of the Complement System and Thus Functionally Mimicks the C-Terminal Domain of the Staphylococcus aureus SSL7 Protein.
Yatime L, Merle NS, Hansen AG, Friis NA, Østergaard JA, Bjerre M, Roumenina LT, Thiel S, Kristensen P, Andersen GR. Yatime L, et al. Front Immunol. 2018 Nov 29;9:2822. doi: 10.3389/fimmu.2018.02822. eCollection 2018. Front Immunol. 2018. PMID: 30555486 Free PMC article.
In particular, pathogen mimicry has been considered as a promising approach for the design of selective anti-complement drugs. The C-terminal domain of staphylococcal superantigen-like protein 7 (SSL7), a protein secreted by Staphylococcus aureus, was recently found to be …
In particular, pathogen mimicry has been considered as a promising approach for the design of selective anti-complement drugs. The C- …
Case Report: Adult Post-COVID-19 Multisystem Inflammatory Syndrome and Thrombotic Microangiopathy.
Boudhabhay I, Rabant M, Roumenina LT, Coupry LM, Poillerat V, Marchal A, Frémeaux-Bacchi V, El Karoui K, Monchi M, Pourcine F. Boudhabhay I, et al. Front Immunol. 2021 Jun 23;12:680567. doi: 10.3389/fimmu.2021.680567. eCollection 2021. Front Immunol. 2021. PMID: 34248962 Free PMC article.
A clinical series of Kawasaki-like multisystem inflammatory syndrome (MIS), occurring after SARS-CoV-2 infection, have been described in children (MIS-C) and adults (MIS-A), but the pathophysiology remains unknown. ...
A clinical series of Kawasaki-like multisystem inflammatory syndrome (MIS), occurring after SARS-CoV-2 infection, have been described in chi …
Interaction of C1q with IgG1, C-reactive protein and pentraxin 3: mutational studies using recombinant globular head modules of human C1q A, B, and C chains.
Roumenina LT, Ruseva MM, Zlatarova A, Ghai R, Kolev M, Olova N, Gadjeva M, Agrawal A, Bottazzi B, Mantovani A, Reid KB, Kishore U, Kojouharova MS. Roumenina LT, et al. Biochemistry. 2006 Apr 4;45(13):4093-104. doi: 10.1021/bi052646f. Biochemistry. 2006. PMID: 16566583 Free PMC article.
The globular domain of C1q (gC1q), which is the ligand-recognition domain, is a heterotrimeric structure composed of the C-terminal regions of A (ghA), B (ghB), and C (ghC) chains. The expression and functional characterization of ghA, ghB, and ghC modules have reve …
The globular domain of C1q (gC1q), which is the ligand-recognition domain, is a heterotrimeric structure composed of the C-terminal r …
Mutational analyses of the recombinant globular regions of human C1q A, B, and C chains suggest an essential role for arginine and histidine residues in the C1q-IgG interaction.
Kojouharova MS, Gadjeva MG, Tsacheva IG, Zlatarova A, Roumenina LT, Tchorbadjieva MI, Atanasov BP, Waters P, Urban BC, Sim RB, Reid KB, Kishore U. Kojouharova MS, et al. J Immunol. 2004 Apr 1;172(7):4351-8. doi: 10.4049/jimmunol.172.7.4351. J Immunol. 2004. PMID: 15034050
The first step in the activation of the classical complement pathway by immune complexes involves the binding of the globular domain (gC1q) of C1q to the Fc regions of aggregated IgG or IgM. Each gC1q domain is a heterotrimer of the C-terminal halves of one A (ghA), one B …
The first step in the activation of the classical complement pathway by immune complexes involves the binding of the globular domain (gC1q) …
Heme interacts with c1q and inhibits the classical complement pathway.
Roumenina LT, Radanova M, Atanasov BP, Popov KT, Kaveri SV, Lacroix-Desmazes S, Frémeaux-Bacchi V, Dimitrov JD. Roumenina LT, et al. J Biol Chem. 2011 May 6;286(18):16459-69. doi: 10.1074/jbc.M110.206136. Epub 2011 Mar 22. J Biol Chem. 2011. PMID: 21454703 Free PMC article.
Exposure of C1q to heme significantly reduced the activation of the classical complement pathway, mediated by C-reactive protein (CRP) and IgG. Interaction analyses revealed that heme reduces the binding of C1q to CRP and IgG. ...
Exposure of C1q to heme significantly reduced the activation of the classical complement pathway, mediated by C-reactive protein (CRP …
Interaction of the globular domain of human C1q with Salmonella typhimurium lipopolysaccharide.
Roumenina LT, Popov KT, Bureeva SV, Kojouharova M, Gadjeva M, Rabheru S, Thakrar R, Kaplun A, Kishore U. Roumenina LT, et al. Biochim Biophys Acta. 2008 Sep;1784(9):1271-6. doi: 10.1016/j.bbapap.2008.04.029. Epub 2008 May 10. Biochim Biophys Acta. 2008. PMID: 18513495
Here we report, using recombinant forms of the globular head regions of C1q A, B and C chains, that LPS derived from Salmonella typhimurium interact specifically with the B-chain of the gC1q domain in a calcium-dependent manner. ...
Here we report, using recombinant forms of the globular head regions of C1q A, B and C chains, that LPS derived from Salmonella typhi …
An engineered construct combining complement regulatory and surface-recognition domains represents a minimal-size functional factor H.
Hebecker M, Alba-Domínguez M, Roumenina LT, Reuter S, Hyvärinen S, Dragon-Durey MA, Jokiranta TS, Sánchez-Corral P, Józsi M. Hebecker M, et al. J Immunol. 2013 Jul 15;191(2):912-21. doi: 10.4049/jimmunol.1300269. Epub 2013 Jun 14. J Immunol. 2013. PMID: 23772024 Free article.
In this article, we report on an engineered FH construct that directly combines the two major functional regions of FH: the N-terminal complement regulatory domains and the C-terminal surface-recognition domains. This minimal-size FH (mini-FH) binds C3b and has complement …
In this article, we report on an engineered FH construct that directly combines the two major functional regions of FH: the N-terminal compl …
17 results