The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
Site-Directed Conjugation of “Clicked” Glycopolymers To Form Glycoprotein Mimics: Binding to Mammalian Lectin and Induction of Immunological Function
Open accessAbstract
Synthesis of well-defined neoglycopolymer-protein biohybrid materials and a preliminary study focused on their ability of binding mammalian lectins and inducing immunological function is reported. Crucial intermediates for their preparation are well-defined maleimide-terminated neoglycopolymers (M(n) = 8-30 kDa; M(w)/M(n) = 1.20-1.28) presenting multiple copies of mannose epitope units, obtained by combination of transition-metal-mediated living radical polymerization (TMM LRP) and Huisgen [2+3] cycloaddition. Bovine serum albumin (BSA) was employed as single thiol-containing model protein, and the resulting bioconjugates were purified following two independent protocols and characterized by circular dichroism (CD) spectroscopy, SDS PAGE, and SEC HPLC. The versatility of the synthetic strategy presented in this work was demonstrated by preparing a small library of conjugating glycopolymers that only differ from each other for their relative epitope density were prepared by coclicking of appropriate mixtures of mannopyranoside and galactopyranoside azides to the same polyalkyne scaffold intermediate. Surface plasmon resonance binding studies carried out using recombinant rat mannose-binding lectin (MBL) showed clear and dose-dependent MBL binding to glycopolymer-conjugated BSA. In addition, enzyme-linked immunosorbent assay (ELISA) revealed that the neoglycopolymer-protein materials described in this work possess significantly enhanced capacity to activate complement via the lectin pathway when compared with native unmodified BSA.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,311
Tornøe, C. W., Christensen, C., & Meldal, M. (2002) · The Journal of Organic Chemistry · doi:10.1021/jo011148j · Cited by 8,696
Atom Transfer Radical Polymerization
Matyjaszewski, K., & Xia, J. (2001) · Chemical Reviews · doi:10.1021/cr940534g · Cited by 7,654
Biological roles of oligosaccharides: all of the theories are correct
Varki, A. (1993) · Glycobiology · doi:10.1093/glycob/3.2.97 · Cited by 5,195
Chiefari, J., Chong, Y. K. (., Ercole, F., Krstina, J., Jeffery, J., Le, T. P. T., Mayadunne, R. T. A., Meijs, G. F., Moad, C. L., Moad, G., et al. (1998) · Macromolecules · doi:10.1021/ma9804951 · Cited by 5,147
Mammen, M., Choi, S.-K., & Whitesides, G. M. (1998) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19981102)37:20<2754::aid-anie2754>3.0.co;2-3 · Cited by 4,110
Metal-Catalyzed Living Radical Polymerization
Kamigaito, M., Ando, T., & Sawamoto, M. (2001) · Chemical Reviews · doi:10.1021/cr9901182 · Cited by 3,275
Kato, M., Kamigaito, M., Sawamoto, M., & Higashimura, T. (1995) · Macromolecules · doi:10.1021/ma00109a056 · Cited by 3,046
Walport, M. J. (2001) · New England Journal of Medicine · doi:10.1056/nejm200104053441406 · Cited by 2,927
Living Radical Polymerization by the RAFT Process
Moad, G., Rizzardo, E., & Thang, S. H. (2005) · Australian Journal of Chemistry · doi:10.1071/ch05072 · Cited by 2,288
Cited by
Atom Transfer Radical Polymerization (ATRP): Current Status and Future Perspectives
Matyjaszewski, K. (2012) · Macromolecules · doi:10.1021/ma3001719 · Cited by 2,606
Nanostructured functional materials prepared by atom transfer radical polymerization
Matyjaszewski, K., & Tsarevsky, N. V. (2009) · Nature Chemistry · doi:10.1038/nchem.257 · Cited by 1,258
Ouchi, M., Terashima, T., & Sawamoto, M. (2009) · Chemical Reviews · doi:10.1021/cr900234b · Cited by 1,257
Gao, H., & Matyjaszewski, K. (2009) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2009.01.001 · Cited by 799
Therapeutic Protein–Polymer Conjugates: Advancing Beyond PEGylation
Pelegri-O’Day, E. M., Lin, E.-W., & Maynard, H. D. (2014) · Journal of the American Chemical Society · doi:10.1021/ja504390x · Cited by 622
Development of Thermal and Photochemical Strategies for Thiol−Ene Click Polymer Functionalization
Campos, L. M., Killops, K. L., Sakai, R., Paulusse, J. M. J., Damiron, D., Drockenmuller, E., Messmore, B. W., & Hawker, C. J. (2008) · Macromolecules · doi:10.1021/ma801630n · Cited by 461
Cu(I)-Catalyzed Click Chemistry in Glycoscience and Their Diverse Applications
Agrahari, A. K., Bose, P., Jaiswal, M. K., Rajkhowa, S., Singh, A. S., Hotha, S., Mishra, N., & Tiwari, V. K. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00920 · Cited by 445
Glycosylation of Therapeutic Proteins: An Effective Strategy to Optimize Efficacy
Solá, R. J., & Griebenow, K. (2010) · BioDrugs · doi:10.2165/11530550-000000000-00000 · Cited by 440
Telechelic polymers by living and controlled/living polymerization methods
Tasdelen, M. A., Kahveci, M. U., & Yagci, Y. (2011) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2010.10.002 · Cited by 393
Kempe, K., Krieg, A., Becer, C. R., & Schubert, U. S. (2012) · Chem. Soc. Rev. · doi:10.1039/c1cs15107j · Cited by 353
Glycopolymer probes of signal transduction
Kiessling, L. L., & Grim, J. C. (2013) · Chemical Society Reviews · doi:10.1039/c3cs60097a · Cited by 335
Johnson, J. A., Finn, M. G., Koberstein, J. T., & Turro, N. J. (2008) · Macromolecular Rapid Communications · doi:10.1002/marc.200800208 · Cited by 320
van Dijk, M., Rijkers, D. T. S., Liskamp, R. M. J., van Nostrum, C. F., & Hennink, W. E. (2009) · Bioconjugate Chemistry · doi:10.1021/bc900087a · Cited by 300
Protein–polymer conjugation — moving beyond PEGylation
Qi, Y., & Chilkoti, A. (2015) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2015.08.009 · Cited by 176
Stability of responsive polymer–protein bioconjugates
Shakya, A. K., Sami, H., Srivastava, A., & Kumar, A. (2010) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2010.01.003 · Cited by 110
Metadata
- Authors
- Geng, J., Mantovani, G., Tao, L., Nicolas, J., Chen, G., Wallis, R., Mitchell, D. A., Johnson, B. R. G., Evans, S. D., & Haddleton, D. M.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-11-17
- Volume
- 129
- Issue
- 49
- Pages
- 15156-15163
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2084561356
- Cited by
- 306
- References
- 51
- FWCI
- 14.30
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
