The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.
Polymers containing enzymatically degradable bonds, 8. Degradation of oligopeptide sequences in N‐(2‐hydroxypropyl)methacrylamide copolymers by bovine spleen cathepsin B
Abstract
Three types of copolymers of N‐(2‐hydroxypropyl)methacrylamide(HPMA) were prepared which contain oligopeptide sequences: (a) HPMA copolymers containing oligopeptide side‐chains terminated with p‐nitroaniline; (b) soluble HPMA copolymers containing oligopeptide sequences in crosslinks connecting two poly(HPMA) chains; (c) a hydrophilic gel, i.e. a three dimensional copolymer of HPMA containing an oligopeptide sequence in the crosslinks. These polymeric substrates (suitable as drug carriers) containing potentially degradable oligopeptide sequences were incubated with an intracellular proteolytic enzyme, bovine spleen cathespin B. The degradation process of the substrates made it possible to reveal the relationship between the structure of oligopeptide sequences and their degradability. The results suggest an important role played by cathepsin B in the degradation of polymeric substrates investigated in this study under physiological conditions.
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
Automatic Recording Apparatus for Use in Chromatography of Amino Acids
Spackman, D. H., Stein, W. H., & Moore, S. (1958) · Analytical Chemistry · doi:10.1021/ac60139a006 · Cited by 9,585
[41] Cathepsin B, cathepsin H, and cathepsin L
Barrett, A. J., & Kirschke, H. (1981) · Methods in Enzymology · doi:10.1016/s0076-6879(81)80043-2 · Cited by 1,698
Proteinases in mammalian cells and tissues
Kerr, M. (1978) · Biochemical Education · doi:10.1016/0307-4412(78)90169-3 · Cited by 919
Chang, J. Y., Brauer, D., & Wittmann‐Liebold, B. (1978) · FEBS Letters · doi:10.1016/0014-5793(78)81105-3 · Cited by 825
[12] Dansyl chloride procedure
Gray, W. R. (1967) · Methods in Enzymology · doi:10.1016/s0076-6879(67)11014-8 · Cited by 651
Aminolyses of monomeric and polymeric 4‐nitrophenyl esters of N‐methacryloylamino acids
Rejmanová, P., Labský, J., & Kopeček, J. (1977) · Die Makromolekulare Chemie · doi:10.1002/macp.1977.021780803 · Cited by 204
Self-citationDuncan, R., Cable, H. C., Lloyd, J. B., Rejmanová, P., & Kopeček, J. (1983) · Die Makromolekulare Chemie · doi:10.1002/macp.1983.021841005 · Cited by 193
Self-citationAccelerated Automatic Chromatographic Analysis of Amino Acids on a Spherical Resin.
Benson, J. V., & Patterson, J. A. (1965) · Analytical Chemistry · doi:10.1021/ac60228a008 · Cited by 183
Enzymatic cleavage of side chains of synthetic water‐soluble polymers
Drobnik, J., Kopec̆ek, J., Labský, J., Rejmanová, P., Exner, J., Saudek, V., & Kálal, J. (1976) · Die Makromolekulare Chemie · doi:10.1002/macp.1976.021771003 · Cited by 120
Self-citationDuncan, R., Cable, H. C., Lloyd, J. B., Rejmanová, P., & Kopec̆ek, J. (1982) · Bioscience Reports · doi:10.1007/bf01122173 · Cited by 101
Self-citation
Cited by
Stimulus-responsive hydrogels: theory, modern advances, and applications
Koetting, M. C., Peters, J. T., Steichen, S. D., & Peppas, N. A. (2015) · Materials Science and Engineering: R: Reports · doi:10.1016/j.mser.2015.04.001 · Cited by 1,191
Polymeric anticancer drugs with pH-controlled activation
Ulbrich, K. (2004) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2003.10.040 · Cited by 494
Hydrogels as smart biomaterials
Kopeček, J., & Yang, J. (2007) · Polymer International · doi:10.1002/pi.2253 · Cited by 425
Self-citationCheetham, A. G., Chakroun, R. W., Ma, W., & Cui, H. (2017) · Chem. Soc. Rev. · doi:10.1039/c7cs00521k · Cited by 367
Etrych, T., Jelı́nková, M., Řı́hová, B., & Ulbrich, K. (2001) · Journal of Controlled Release · doi:10.1016/s0168-3659(01)00281-4 · Cited by 340
Metadata
- Authors
- Rejmanová, P., Kopeček, J., Pohl, J., Baudyš, M., & Kostka, V.
- Venue
- Die Makromolekulare Chemie
- Publisher
- Wiley
- Published
- 1983-10
- Volume
- 184
- Issue
- 10
- Pages
- 2009-2020
- ISSN
- 0025-116X (ISSN-L)
- OpenAlex
- W2112824007
- Cited by
- 264
- References
- 19
- FWCI
- 4.27
- 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: Polymers containing enzymatically degradable bonds, 8. Degradation of oligopeptide sequences in N‐(2‐hydroxypropyl)methacrylamide copolymers by bovine spleen cathepsin B. https://app.cochat.ai/papers/10.1002/macp.1983.021841006
- The paper
- Rejmanová, P., Kopeček, J., Pohl, J., Baudyš, M., & Kostka, V. (1983). Polymers containing enzymatically degradable bonds, 8. Degradation of oligopeptide sequences in N‐(2‐hydroxypropyl)methacrylamide copolymers by bovine spleen cathepsin B. Die Makromolekulare Chemie. https://doi.org/10.1002/macp.1983.021841006
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.
