The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Mechanism of enzymatic degradation of beta-sheet crystals
Open accessAbstract
The anti-parallel beta pleated sheet is a fundamental secondary structure in proteins and a major component in silk fibers generated by silkworms and spiders, with a key role to stabilize these proteins via physical cross-links. Importantly, these beta-sheets are fully degradable and nontoxic structures in biology, in contrast for example to beta-amyloid structures formed in disease states. Thus, insight into mechanism of enzymatic degradation would be instructive as a route to elucidating differences among these stable yet different structural features in biological systems. We report on the mechanism of enzymatic degradation of anti-parallel beta pleated sheets with Bombyx mori silk structures, leading to fibrils and subsequently to nanofilaments (2 nm thickness and 160 nm length). These nanofilaments play a role as nucleators of the crystalline regions, an important feature of the system that can be exploited to design silk-based biomaterials with predictable biodegradability and mechanical properties. The potential toxicity of degradation products from these proteolytic enzymes was also assessed in vitro and no cell toxicity found in vitro for the protease found in vivo in the human body. The degradation mechanism of beta-sheet silk crystals provides additional insight into the significant differences in biological impact between the anti-parallel beta-sheet silk biomaterials reported in this work vs. amyloid structures in disease states, adding to prior descriptions of chemical and structural differences that are more extensively documented.
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
Mechanism of silk processing in insects and spiders
Jin, H.-J., & Kaplan, D. L. (2003) · Nature · doi:10.1038/nature01809 · Cited by 1,376
Self-citationReview: History of the Amyloid Fibril
Sipe, J. D., & Cohen, A. S. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4221 · Cited by 1,054
A Self-Consistent Method for the Analysis of Protein Secondary Structure from Circular Dichroism
Sreerama, N., & Woody, R. W. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1079 · Cited by 1,045
Surprising strength of silkworm silk
Shao, Z., & Vollrath, F. (2002) · Nature · doi:10.1038/418741a · Cited by 1,003
In vivo degradation of three-dimensional silk fibroin scaffolds
Wang, Y., Rudym, D. D., Walsh, A., Abrahamsen, L., Kim, H.-J., Kim, H. S., Kirker-Head, C., & Kaplan, D. L. (2008) · Biomaterials · doi:10.1016/j.biomaterials.2008.05.002 · Cited by 789
Self-citationIn vitro degradation of silk fibroin
Horan, R. L., Antle, K., Collette, A. L., Wang, Y., Huang, J., Moreau, J. E., Volloch, V., Kaplan, D. L., & Altman, G. H. (2005) · Biomaterials · doi:10.1016/j.biomaterials.2004.09.020 · Cited by 743
Self-citationAn investigation of the structure of silk fibroin
Marsh, R. E., Corey, R. B., & Pauling, L. (1955) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(55)90178-5 · Cited by 721
What is the role of protein aggregation in neurodegeneration?
Ross, C. A., & Poirier, M. A. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1742 · Cited by 604
Chimon, S., Shaibat, M. A., Jones, C. R., Calero, D. C., Aizezi, B., & Ishii, Y. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1345 · Cited by 544
Enzymatic degradation behavior of porous silk fibroin sheets
Li, M., Ogiso, M., & Minoura, N. (2003) · Biomaterials · doi:10.1016/s0142-9612(02)00326-5 · Cited by 460
Cited by
Silk fibroin biomaterials for tissue regenerations
Kundu, B., Rajkhowa, R., Kundu, S. C., & Wang, X. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2012.09.043 · Cited by 1,391
Structures, mechanical properties and applications of silk fibroin materials
Koh, L.-D., Cheng, Y., Teng, C.-P., Khin, Y.-W., Loh, X.-J., Tee, S.-Y., Low, M., Ye, E., Yu, H.-D., Zhang, Y.-W., et al. (2015) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2015.02.001 · Cited by 1,241
Silk biomaterials in wound healing and skin regeneration therapeutics: From bench to bedside
Chouhan, D., & Mandal, B. B. (2020) · Acta Biomaterialia · doi:10.1016/j.actbio.2019.11.050 · Cited by 348
Silk scaffolds in bone tissue engineering: An overview
Bhattacharjee, P., Kundu, B., Naskar, D., Kim, H.-W., Maiti, T. K., Bhattacharya, D., & Kundu, S. C. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.09.027 · Cited by 318
Biodegradable Piezoelectric Polymers: Recent Advancements in Materials and Applications
Ali, M., Bathaei, M. J., Istif, E., Karimi, S. N. H., & Beker, L. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202300318 · Cited by 211
Metadata
- Authors
- Numata, K., Cebe, P., & Kaplan, D. L.
- Venue
- Biomaterials
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 31
- Issue
- 10
- Pages
- 2926-2933
- ISSN
- 0142-9612 (ISSN-L)
- OpenAlex
- W1972086723
- Cited by
- 278
- References
- 31
- FWCI
- 3.97
- Type
- journal article
- Language
- en
- Open access
- green
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: Mechanism of enzymatic degradation of beta-sheet crystals. https://app.cochat.ai/papers/10.1016/j.biomaterials.2009.12.026
- The paper
- Numata, K., Cebe, P., & Kaplan, D. L. (2010). Mechanism of enzymatic degradation of beta-sheet crystals. Biomaterials. https://doi.org/10.1016/j.biomaterials.2009.12.026
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.