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The Neonatal Fc Receptor (FcRn): A Misnomer?
Pyzik M, Sand KMK, Hubbard JJ, Andersen JT, Sandlie I, Blumberg RS. Pyzik M, et al. Front Immunol. 2019 Jul 10;10:1540. doi: 10.3389/fimmu.2019.01540. eCollection 2019. Front Immunol. 2019. PMID: 31354709 Free PMC article. Review.
Although IgG alone can directly protect the body from infection through the activities of its antigen binding region, the majority of IgG immune functions are mediated via proteins and receptors expressed by specialized cell subsets that bind to …
Although IgG alone can directly protect the body from infection through the activities of its antigen binding region, t …
Synthesis and receptor binding of IgG1 peptides derived from the IgG Fc region.
Uray K, Medgyesi D, Hilbert A, Sármay G, Gergely J, Hudecz F. Uray K, et al. J Mol Recognit. 2004 Mar-Apr;17(2):95-105. doi: 10.1002/jmr.652. J Mol Recognit. 2004. PMID: 15027030
The IgG binding Fcgamma receptors (FcgammaRs) play a key role in defence against pathogens by linking humoral and cell-mediated immune responses. ...Here we report that peptide representing the Arg(255)-Ser(267) sequence of IgG1 is implicated in …
The IgG binding Fcgamma receptors (FcgammaRs) play a key role in defence against pathogens by linking humoral and cell- …
Conformational Plasticity of the Immunoglobulin Fc Domain in Solution.
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M. Remesh SG, et al. Structure. 2018 Jul 3;26(7):1007-1014.e2. doi: 10.1016/j.str.2018.03.017. Epub 2018 May 3. Structure. 2018. PMID: 29731233 Free PMC article.
Fragment crystallizable (Fc) region of immunoglobulin G (IgG) antibody binds to specific Fc receptors (FcgammaRs) to control antibody effector functions. ...However, computational evidence suggests that the conformational va …
Fragment crystallizable (Fc) region of immunoglobulin G (IgG) antibody binds to specific Fc
Analysis of the linear epitope for Fc-binding on the mouse IgG Fc receptor (moFcgammaRI) by synthetic peptide.
Wang FY, Guo JQ, Zhang GP. Wang FY, et al. Genet Mol Res. 2014 Jun 18;13(2):4647-53. doi: 10.4238/2014.June.18.7. Genet Mol Res. 2014. PMID: 25036514 Free article.
To identify the linear epitope for Fc-binding to the mouse immunoglobulin G (IgG) Fc receptor (moFcgammaRI), peptides derived from the membrane-distal extracellular domain (EC2) of moFcgammaRI, corresponding to the ho …
To identify the linear epitope for Fc-binding to the mouse immunoglobulin G (IgG) Fc receptor
TIRF imaging of Fc gamma receptor microclusters dynamics and signaling on macrophages during frustrated phagocytosis.
Lin J, Kurilova S, Scott BL, Bosworth E, Iverson BE, Bailey EM, Hoppe AD. Lin J, et al. BMC Immunol. 2016 Mar 12;17:5. doi: 10.1186/s12865-016-0143-2. BMC Immunol. 2016. PMID: 26970734 Free PMC article.
In macrophages and neutrophils, particles opsonized with immunoglobulin G (IgG) antibodies activate the phagocytic Fcgamma-receptor (FcgammaR) leading to rearrangements of the actin cytoskeleton. ...RESULTS: Upon antibody binding, macrophages fo …
In macrophages and neutrophils, particles opsonized with immunoglobulin G (IgG) antibodies activate the phagocytic Fcga …
Identification of a linear epitope for Fc-binding in the mouse FcgammaRIII.
Xi J, Zhang LN, Hu GP, Wang L, Qiao SL, Guo JQ, Lu QY, Zhang GP, Yang YY. Xi J, et al. Peptides. 2010 Sep;31(9):1684-8. doi: 10.1016/j.peptides.2010.05.022. Epub 2010 Jun 8. Peptides. 2010. PMID: 20566342
Fc receptors are transmembrane proteins, found on the surfaces of immune cells, that aid in the removal of foreign pathogens by binding to antibody-coated targets via the Fc regions of the antibodies. ...Binding of mouse IgG to the
Fc receptors are transmembrane proteins, found on the surfaces of immune cells, that aid in the removal of foreign pathogens b
Identification of the linear epitope for Fc-binding on the bovine IgG2 Fc receptor (boFcgamma2R) using synthetic peptides.
Zhang G, Guo J, Zhou J, Wang X, Li Q, Yang Y, Shen H, Zhao D, Zhang H, Xi J, Wang L, Qiao S, Jin X. Zhang G, et al. FEBS Lett. 2006 Feb 20;580(5):1383-90. doi: 10.1016/j.febslet.2006.01.060. Epub 2006 Jan 26. FEBS Lett. 2006. PMID: 16457820 Free article.
To identify the linear epitope for Fc-binding on the bovine IgG2 Fc receptor (boFcgamma2R), peptides derived from the membrane-distal extracellular domain (EC1) of boFcgamma2R corresponding to the homologous region of human Fcalpha …
To identify the linear epitope for Fc-binding on the bovine IgG2 Fc receptor (boFcgamma2R), peptides d
ABD-Derived Protein Blockers of Human IL-17 Receptor A as Non-IgG Alternatives for Modulation of IL-17-Dependent Pro-Inflammatory Axis.
Hlavničková M, Kuchař M, Osička R, Vaňková L, Petroková H, Malý M, Černý J, Arenberger P, Malý P. Hlavničková M, et al. Int J Mol Sci. 2018 Oct 9;19(10):3089. doi: 10.3390/ijms19103089. Int J Mol Sci. 2018. PMID: 30304852 Free PMC article.
To modulate IL-17-mediated inflammatory cascade, we generated a unique collection of IL-17RA-targeting protein binders that prevent from binding of human IL-17A cytokine to its cell-surface receptor. To this goal, we used a highly complex combinatorial library de
To modulate IL-17-mediated inflammatory cascade, we generated a unique collection of IL-17RA-targeting protein binders that prevent from …
Diabody-Ig: a novel platform for the generation of multivalent and multispecific antibody molecules.
Seifert O, Rau A, Beha N, Richter F, Kontermann RE. Seifert O, et al. MAbs. 2019 Jul;11(5):919-929. doi: 10.1080/19420862.2019.1603024. Epub 2019 May 3. MAbs. 2019. PMID: 30951400 Free PMC article.
The antigen-binding site of Db-Ig is composed of a diabody in the V(H)-V(L) orientation stabilized by fusion to antibody-derived homo- or heterodimerization domains, e.g., C(H)1/C(L) or the heavy chain domain 2 of IgE (EHD2) or IgM (MHD2), further fused to an Fc
The antigen-binding site of Db-Ig is composed of a diabody in the V(H)-V(L) orientation stabilized by fusion to antibody-derived
SCM, the M Protein of Streptococcus canis Binds Immunoglobulin G.
Bergmann S, Eichhorn I, Kohler TP, Hammerschmidt S, Goldmann O, Rohde M, Fulde M. Bergmann S, et al. Front Cell Infect Microbiol. 2017 Mar 28;7:80. doi: 10.3389/fcimb.2017.00080. eCollection 2017. Front Cell Infect Microbiol. 2017. PMID: 28401063 Free PMC article.
Here, we report that SCM has an additional high-affinity immunoglobulin G (IgG) binding activity. The ability of a particular S. canis isolate to bind to IgG significantly correlates with a scm-positive phenotype, suggesting a dominant role of S …
Here, we report that SCM has an additional high-affinity immunoglobulin G (IgG) binding activity. The ability of …
31 results