The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.
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Cites
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617
Jones, T. A., Zou, J. Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,648
Automated refinement of protein models
Lamzin, V. S., & Wilson, K. S. (1993) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444992008886 · Cited by 883
Musil, D., Zucic, D., Turk, D., Engh, R. A., Mayr, I., Huber, R., Popovic, T., Turk, V., Towatari, T., & Katunuma, N. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07771.x · Cited by 601
DRENTH, J., JANSONIUS, J. N., KOEKOEK, R., SWEN, H. M., & WOLTHERS, B. G. (1968) · Nature · doi:10.1038/218929a0 · Cited by 482
Alignment/Phylogeny of the Papain Superfamily of Cysteine Proteases
Berti, P. J., & Storer, A. C. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.0083 · Cited by 396
Two distinct gene subfamilies within the family of cysteine protease genes.
Karrer, K. M., Peiffer, S. L., & DiTomas, M. E. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.3063 · Cited by 357
Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts.
Tezuka, K., Tezuka, Y., Maejima, A., Sato, T., Nemoto, K., Kamioka, H., Hakeda, Y., & Kumegawa, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42227-7 · Cited by 341
Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution
James, M. N. G., & Sielecki, A. R. (1986) · Nature · doi:10.1038/319033a0 · Cited by 296
Becker, J. W., Marcy, A. I., Rokosz, L. L., Axel, M. G., Burbaum, J. J., Fitzgerald, P. M. D., Cameron, P. M., Esser, C. K., Hagmann, W. K., Hermes, J. D., et al. (1995) · Protein Science · doi:10.1002/pro.5560041002 · Cited by 293
Cited by
Cysteine cathepsins: From structure, function and regulation to new frontiers
Turk, V., Stoka, V., Vasiljeva, O., Renko, M., Sun, T., Turk, B., & Turk, D. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.10.002 · Cited by 1,377
Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family
Eckelman, B. P., Salvesen, G. S., & Scott, F. L. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400795 · Cited by 813
Specialized roles for cysteine cathepsins in health and disease
Reiser, J., Adair, B., & Reinheckel, T. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42918 · Cited by 580
Hosfield, C. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.24.6880 · Cited by 354
Lysosomal cathepsins and their regulation in aging and neurodegeneration
Stoka, V., Turk, V., & Turk, B. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.010 · Cited by 334
Metadata
- Authors
- Coulombe, R., Grochulski, P., Sivaraman, J., Ménard, R., Mort, J. S., & Cygler, M.
- Venue
- The EMBO Journal
- Published
- 1996-10
- Volume
- 15
- Issue
- 20
- Pages
- 5492-5503
- ISSN
- 0261-4189 (ISSN-L)
- OpenAlex
- W1920417980
- Cited by
- 388
- References
- 32
- FWCI
- 10.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- www.springer.com/tdm (tdm)
- www.springer.com/tdm (vor)
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- CoChat. (2026). Citation check: Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. https://app.cochat.ai/papers/10.1002/j.1460-2075.1996.tb00934.x
- The paper
- Coulombe, R., Grochulski, P., Sivaraman, J., Ménard, R., Mort, J. S., & Cygler, M. (1996). Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. The EMBO Journal. https://doi.org/10.1002/j.1460-2075.1996.tb00934.x
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.
