The DOI matches its Crossref record.
Site-Specific Protein Immobilization by Staudinger Ligation
Abstract
The Staudinger ligation between an azido-protein and a phosphinothioester-derivatized surface is demonstrated to be an effective means for the site-specific, covalent immobilization of a protein. Immobilization yields of >50% are obtained in <1 min, and immobilized proteins have >80% of their expected activity. No other method enables more rapid immobilization or a higher yield of active protein. Because azido-peptides and azido-proteins are readily attainable by synthesis, biosynthesis, or semisynthesis, the Staudinger ligation could be of unsurpassed utility in creating microarrays of functional peptides and proteins.
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
Cited by
Prescher, J. A., & Bertozzi, C. R. (2005) · Nature Chemical Biology · doi:10.1038/nchembio0605-13 · Cited by 1,456
Enzyme immobilization: an update
Homaei, A. A., Sariri, R., Vianello, F., & Stevanato, R. (2013) · Journal of Chemical Biology · doi:10.1007/s12154-013-0102-9 · Cited by 875
Protein Immobilization Strategies for Protein Biochips
Rusmini, F., Zhong, Z., & Feijen, J. (2007) · Biomacromolecules · doi:10.1021/bm061197b · Cited by 869
Engineering Silicon Oxide Surfaces Using Self‐Assembled Monolayers
Onclin, S., Ravoo, B. J., & Reinhoudt, D. N. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200500633 · Cited by 721
The Staudinger Ligation—A Gift to Chemical Biology
Köhn, M., & Breinbauer, R. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200401744 · Cited by 585
Selective Covalent Protein Immobilization: Strategies and Applications
Wong, L. S., Khan, F., & Micklefield, J. (2009) · Chemical Reviews · doi:10.1021/cr8004668 · Cited by 489
Mechanistic Investigation of the Staudinger Ligation
Lin, F. L., Hoyt, H. M., van Halbeek, H., Bergman, R. G., & Bertozzi, C. R. (2005) · Journal of the American Chemical Society · doi:10.1021/ja044461m · Cited by 383
Chemical Synthesis of Proteins
Nilsson, B. L., Soellner, M. B., & Raines, R. T. (2005) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.34.040204.144700 · Cited by 329
Self-citation
Metadata
- Authors
- Soellner, M. B., Dickson, K. A., Nilsson, B. L., & Raines, R. T.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-09-04
- Volume
- 125
- Issue
- 39
- Pages
- 11790-11791
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1994696054
- Cited by
- 227
- References
- 0
- FWCI
- 4.50
- Type
- journal article
- Language
- en
- Open access
- closed
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.