The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Unfolding of Ribonuclease A on Silica Nanoparticle Surfaces
Abstract
This paper reports on the unfolding behavior of ribonuclease A (RNase A) on silica nanoparticle surfaces and quantitively demonstrates that nanoscale size and surface curvature play key roles in influencing the stability of adsorbed proteins. Urea denaturation analyses showed that the thermodynamic stability of RNase A decreased upon adsorption onto the nanoparticles, with greater decrease on larger nanoparticles. The stability changes of RNase A correlate well with the changes in the protein-nanoparticle interactions, which increase as the surface contact area and surface charge interaction increases. This study, therefore, provides fundamental information on the effect of nanoscale surfaces on protein structure and function.
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
The protein data bank: A computer-based archival file for macromolecular structures
Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80200-3 · Cited by 8,578
[14]Determination and analysis of urea and guanidine hydrochloride denaturation curves
Pace, C. N. (1986) · Methods in Enzymology · doi:10.1016/0076-6879(86)31045-0 · Cited by 2,258
Silica Nanoparticle Size Influences the Structure and Enzymatic Activity of Adsorbed Lysozyme
Vertegel, A. A., Siegel, R. W., & Dordick, J. S. (2004) · Langmuir · doi:10.1021/la0497200 · Cited by 878
Self-citationThe interaction of proteins with solid surfaces
Gray, J. J. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2003.12.001 · Cited by 797
Roach, P., Farrar, D., & Perry, C. C. (2006) · Journal of the American Chemical Society · doi:10.1021/ja056278e · Cited by 772
Lundqvist, M., Sethson, I., & Jonsson, B.-H. (2004) · Langmuir · doi:10.1021/la0484725 · Cited by 597
Protein adsorption on solid surfaces
Hlady, V., & Buijs, J. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80098-x · Cited by 522
Structure and Function of Enzymes Adsorbed onto Single-Walled Carbon Nanotubes
Karajanagi, S. S., Vertegel, A. A., Kane, R. S., & Dordick, J. S. (2004) · Langmuir · doi:10.1021/la047994h · Cited by 508
Self-citationA SPECTROPHOTOMETRIC METHOD FOR THE MEASUREMENT OF RIBONUCLEASE ACTIVITY
Kunitz, M. (1946) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41259-2 · Cited by 485
Ostuni, E., Yan, L., & Whitesides, G. M. (1999) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/s0927-7765(99)00004-1 · Cited by 453
Cited by
Nanoparticle-induced unfolding of fibrinogen promotes Mac-1 receptor activation and inflammation
Deng, Z. J., Liang, M., Monteiro, M., Toth, I., & Minchin, R. F. (2011) · Nature Nanotechnology · doi:10.1038/nnano.2010.250 · Cited by 893
Preformed albumin corona, a protective coating for nanoparticles based drug delivery system
Peng, Q., Zhang, S., Yang, Q., Zhang, T., Wei, X.-Q., Jiang, L., Zhang, C.-L., Chen, Q.-M., Zhang, Z.-R., & Lin, Y.-F. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.07.102 · Cited by 366
Personalized protein corona on nanoparticles and its clinical implications
Corbo, C., Molinaro, R., Tabatabaei, M., Farokhzad, O. C., & Mahmoudi, M. (2017) · Biomaterials Science · doi:10.1039/c6bm00921b · Cited by 308
Biosafety and Bioapplication of Nanomaterials by Designing Protein–Nanoparticle Interactions
Yang, S., Liu, Y., Wang, Y., & Cao, A. (2013) · Small · doi:10.1002/smll.201201492 · Cited by 296
Multiple aspects of the interaction of biomacromolecules with inorganic surfaces
Fenoglio, I., Fubini, B., Ghibaudi, E. M., & Turci, F. (2011) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2011.08.001 · Cited by 176
Metadata
- Authors
- Shang, W., Nuffer, J. H., Dordick, J. S., & Siegel, R. W.
- Venue
- Nano Letters
- Publisher
- American Chemical Society (ACS)
- Published
- 2007-06-09
- Volume
- 7
- Issue
- 7
- Pages
- 1991-1995
- ISSN
- 1530-6984 (ISSN-L)
- 1530-6992
- OpenAlex
- W2087955709
- Cited by
- 263
- References
- 15
- FWCI
- 4.19
- 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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Unfolding of Ribonuclease A on Silica Nanoparticle Surfaces. https://app.cochat.ai/papers/10.1021/nl070777r
- The paper
- Shang, W., Nuffer, J. H., Dordick, J. S., & Siegel, R. W. (2007). Unfolding of Ribonuclease A on Silica Nanoparticle Surfaces. Nano Letters. https://doi.org/10.1021/nl070777r
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.
