The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis.
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Citations
Cites
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
A Simple Chemically Defined Medium for the Production of Phase I Bordetella pertussis
Stainer, D. W., & Scholte, M. J. (1970) · Journal of General Microbiology · doi:10.1099/00221287-63-2-211 · Cited by 636
Katada, T., & Ui, M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34558-7 · Cited by 600
Nucleotide sequence of an Escherichia coli chromosomal hemolysin
Felmlee, T., Pellett, S., & Welch, R. A. (1985) · Journal of Bacteriology · doi:10.1128/jb.163.1.94-105.1985 · Cited by 545
Virulence Factors of Bordetella Pertussis
Weiss, A. A., & Hewlett, E. L. (1986) · Annual Review of Microbiology · doi:10.1146/annurev.mi.40.100186.003305 · Cited by 431
Glaser, P., Ladant, D., Sezer, O., Pichot, F., Ullmann, A., & Danchin, A. (1988) · Molecular Microbiology · doi:10.1111/j.1365-2958.1988.tb00003.x · Cited by 313
Self-citationCalmodulin activates prokaryotic adenylate cyclase.
Wolff, J., Cook, G. H., Goldhammer, A. R., & Berkowitz, S. A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.7.3841 · Cited by 276
New versatile cloning and sequencing vectors based on bacteriophage M13
Kiény, M. P., Lathe, R., & Lecocq, J. (1983) · Gene · doi:10.1016/0378-1119(83)90039-2 · Cited by 260
Transport of hemolysin across the outer membrane of Escherichia coli requires two functions
Wagner, W., Vogel, M., & Goebel, W. (1983) · Journal of Bacteriology · doi:10.1128/jb.154.1.200-210.1983 · Cited by 255
Cited by
ABC Transporters: From Microorganisms to Man
Higgins, C. F. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.000435 · Cited by 3,985
Poole, K., Krebes, K., McNally, C., & Neshat, S. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.22.7363-7372.1993 · Cited by 688
Botsford, J. L., & Harman, J. G. (1992) · Microbiological Reviews · doi:10.1128/mr.56.1.100-122.1992 · Cited by 558
RTX proteins: a highly diverse family secreted by a common mechanism
Linhartová, I., Bumba, L., Mašín, J., Basler, M., Osička, R., Kamanová, J., Procházková, K., Adkins, I., Hejnová-Holubová, J., Sadílková, L., et al. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00231.x · Cited by 530
Translocation of a hybrid YopE‐adenylate cyclase from Yersinia enterocolitica into HeLa cells
Sory, M., & Cornelis, G. R. (1994) · Molecular Microbiology · doi:10.1111/j.1365-2958.1994.tb02191.x · Cited by 532
Metadata
- Authors
- Glaser, P., Sakamoto, H., Bellalou, J., Ullmann, A., & Danchin, A.
- Venue
- The EMBO Journal
- Published
- 1988-12
- Volume
- 7
- Issue
- 12
- Pages
- 3997-4004
- ISSN
- 0261-4189 (ISSN-L)
- OpenAlex
- W1745436806
- Cited by
- 421
- References
- 23
- FWCI
- 25.37
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. https://app.cochat.ai/papers/10.1002/j.1460-2075.1988.tb03288.x
- The paper
- Glaser, P., Sakamoto, H., Bellalou, J., Ullmann, A., & Danchin, A. (1988). Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-haemolysin bifunctional protein of Bordetella pertussis. The EMBO Journal. https://doi.org/10.1002/j.1460-2075.1988.tb03288.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.