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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1950 1
1953 3
1955 1
1956 4
1957 7
1958 17
1959 8
1960 10
1961 13
1962 15
1963 21
1964 21
1965 13
1966 5
1967 1
1968 10
1969 30
1970 212
1971 428
1972 487
1973 558
1974 675
1975 566
1976 540
1977 580
1978 611
1979 803
1980 868
1981 1192
1982 1300
1983 1438
1984 1483
1985 1096
1986 1195
1987 1007
1988 855
1989 764
1990 662
1991 599
1992 431
1993 409
1994 368
1995 364
1996 279
1997 260
1998 296
1999 237
2000 231
2001 225
2002 194
2003 228
2004 216
2005 201
2006 241
2007 228
2008 211
2009 200
2010 175
2011 212
2012 234
2013 218
2014 200
2015 180
2016 206
2017 157
2018 173
2019 59
2020 0
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24,374 results
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Page 1
Promoting Multivalent Antibody-Antigen Interactions by Tethering Antibody Molecules on a PEGylated Dendrimer-Supported Lipid Bilayer.
Yeh PY, et al. Biomacromolecules 2018. PMID 29281787
The combination of a hydrated, stretchable dendrimer and a laterally mobile supported lipid bilayer (SLB) provide attached antibody molecules with 2.5-dimensional chain movement, achieving multivalency between the surface antibody and cell antigen molecules. ...In summary, we have demonstrated a material design to enhance multivalent antibody-antigen interaction, which is useful for rare cell enrichment and cancer detection....
The combination of a hydrated, stretchable dendrimer and a laterally mobile supported lipid bilayer (SLB) provide attached antibody m …
Local and global anatomy of antibody-protein antigen recognition.
Wang M, et al. J Mol Recognit 2018. PMID 29218757 Free PMC article.
We investigated the physicochemical properties of regions on and away from the antibody-antigen interfaces, including net charge, overall antibody charge distributions, and their potential role in antigen interaction. ...Here we describe some features of antibody-antigen interfaces and of Fab domains as compared with nonantibody protein-protein interactions. ...
We investigated the physicochemical properties of regions on and away from the antibody-antigen interfaces, including net char …
The interfacial character of antibody paratopes: analysis of antibody-antigen structures.
Nguyen MN, et al. Bioinformatics 2017. PMID 28633399
SUMMARY: In this study, computational methods are applied to investigate the general properties of antigen engaging residues of a paratope from a non-redundant dataset of 403 antibody-antigen complexes to dissect the contribution of hydrogen bonds, hydrophobic, van der Waals contacts and ionic interactions, as well as role of water molecules in the antigen-antibody interface. ...Furthermore, antibody-antigen interactions can be mediated by interfacial waters. However, there is no reported comprehensive analysis for a large number of structured waters that engage in higher ordered structures at the antibody-antigen interface. ...
SUMMARY: In this study, computational methods are applied to investigate the general properties of antigen engaging residues of a par …
Large-scale sequence and structural comparisons of human naive and antigen-experienced antibody repertoires.
DeKosky BJ, et al. Proc Natl Acad Sci U S A 2016. PMID 27114511 Free PMC article.
Elucidating how antigen exposure and selection shape the human antibody repertoire is fundamental to our understanding of B-cell immunity. ...Analysis of a dataset comprising 55,000 antibody clusters from CD19(+)CD20(+)CD27(-) IgM-naive B cells, >120,000 antibody clusters from CD19(+)CD20(+)CD27(+) antigen-experienced B cells, and >2,000 RosettaAntibody-predicted structural models across three healthy donors led to a number of key findings: (i) VH and VL gene sequences pair in a combinatorial fashion without detectable pairing restrictions at the population level; (ii) certain VH:VL gene pairs were significantly enriched or depleted in the antigen-experienced repertoire relative to the naive repertoire; (iii) antigen selection increased antibody paratope net charge and solvent-accessible surface area; and (iv) public heavy-chain third complementarity-determining region (CDR-H3) antibodies in the antigen-experienced repertoire showed signs of convergent paired light-chain genetic signatures, including shared light-chain third complementarity-determining region (CDR-L3) amino acid sequences and/or Vκ,λ-Jκ,λ genes. ...
Elucidating how antigen exposure and selection shape the human antibody repertoire is fundamental to our understanding of B-ce …
Modeling antigen-antibody nanoparticle bioconjugates and their polymorphs.
Desgranges C and Delhommelle J. J Chem Phys 2018. PMID 29604830
In this work, we develop a coarse-grained model for nanoparticles grafted with antibody molecules and their binding with antigens. In particular, we isolate two possible states for antigen-antibody pairs during the binding process, termed as recognition and anchoring states. ...
In this work, we develop a coarse-grained model for nanoparticles grafted with antibody molecules and their binding with antigens. In …
Human Milk Oligosaccharides Attenuate Antigen-Antibody Complex Induced Chemokine Release from Human Intestinal Epithelial Cell Lines.
Zehra S, et al. J Food Sci 2018. PMID 29377120
Here we demonstrate that the HMO, 6'-sialyllactose (6'SL) inhibited chemokine (IL-8 and CCL20) release from T-84 and HT-29 cells stimulated with antigen-antibody complex, TNFα or PGE(2) ; an effect that was PPARγ dependent and associated with decreased activity of the transcription factors AP-1 and NFκB. In contrast, 2'-fucosyllactose (2'FL) selectively inhibited CCL20 release in response to antigen antibody complex in a PPARγ independent manner. ...
Here we demonstrate that the HMO, 6'-sialyllactose (6'SL) inhibited chemokine (IL-8 and CCL20) release from T-84 and HT-29 cells stimulated …
Structure-based cross-docking analysis of antibody-antigen interactions.
Kilambi KP and Gray JJ. Sci Rep 2017. PMID 28811664 Free PMC article.
Antibody-antigen interactions are critical to our immune response, and understanding the structure-based biophysical determinants for their binding specificity and affinity is of fundamental importance. We present a computational structure-based cross-docking study to test the identification of native antibody-antigen interaction pairs among cognate and non-cognate complexes. ...
Antibody-antigen interactions are critical to our immune response, and understanding the structure-based biophysical determina
Cell-free synthesis of functional antibody fragments to provide a structural basis for antibody-antigen interaction.
Matsuda T, et al. PLoS One 2018. PMID 29462206 Free PMC article.
Here, we developed a rapid, high-yield cell-free system using dialysis mode to synthesize antibody fragments for the structural analysis of antibody-antigen complexes. ...Analyses of purified 059-152-Fv and Fab showed that the cell-free synthesized antibody fragments were disulfide-bridged, with antigen binding activity comparable to that of clinical antibodies. ...
Here, we developed a rapid, high-yield cell-free system using dialysis mode to synthesize antibody fragments for the structural analy …
Beyond binding: antibody effector functions in infectious diseases.
Lu LL, et al. Nat Rev Immunol 2018 - Review. PMID 29063907 Free PMC article.
Specifically, antibodies collaboratively form immune complexes that drive sequestration and uptake of pathogens, clear toxins, eliminate infected cells, increase antigen presentation and regulate inflammation. The diverse effector functions that are deployed by antibodies are dynamically regulated via differential modification of the antibody constant domain, which provides specific instructions to the immune system. ...
Specifically, antibodies collaboratively form immune complexes that drive sequestration and uptake of pathogens, clear toxins, eliminate inf …
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