The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32.
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Towbin, H., Staehelin, T., & Gordon, J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4350 · Cited by 53,385
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,221
Yanisch-Perron, C., Vieira, J., & Messing, J. (1985) · Gene · doi:10.1016/0378-1119(85)90120-9 · Cited by 15,041
Escherichia coli and Salmonella typhimurium: Cellular and molecular biology
Lejeune, P. (1988) · Biochimie · doi:10.1016/0300-9084(88)90119-8 · Cited by 4,072
Zinc coordination, function, and structure of zinc enzymes and other proteins
Vallee, B. L., & Auld, D. S. (1990) · Biochemistry · doi:10.1021/bi00476a001 · Cited by 1,777
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Evolutionary families of peptidases
Rawlings, N. D., & Barrett, A. J. (1993) · Biochemical Journal · doi:10.1042/bj2900205 · Cited by 923
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The htpR gene product of E. coli is a sigma factor for heat-shock promoters
Grossman, A. D., Erickson, J. W., & Gross, C. A. (1984) · Cell · doi:10.1016/0092-8674(84)90493-8 · Cited by 586
Cited by
MOLECULAR AND EVOLUTIONARY BASIS OF THE CELLULAR STRESS RESPONSE
Kültz, D. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.67.040403.103635 · Cited by 1,511
Multiple Sigma Subunits and the Partitioning of Bacterial Transcription Space
Gruber, T. M., & Gross, C. A. (2003) · Annual Review of Microbiology · doi:10.1146/annurev.micro.57.030502.090913 · Cited by 934
Gottesman, S., Roche, E., Zhou, Y., & Sauer, R. T. (1998) · Genes & Development · doi:10.1101/gad.12.9.1338 · Cited by 835
Evolutionary history and higher order classification of AAA+ ATPases
Iyer, L. M., Leipe, D. D., Koonin, E. V., & Aravind, L. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.10.010 · Cited by 787
PROTEASES AND THEIR TARGETS IN ESCHERICHIA COLI
Gottesman, S. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.465 · Cited by 717
Metadata
- Authors
- Tomoyasu, T., Gamer, J., Bukau, B., Kanemori, M., Mori, H., Rutman, A. J., Oppenheim, A. B., Yura, T., Yamanaka, K., & Niki, H.
- Venue
- The EMBO Journal
- Published
- 1995-06
- Volume
- 14
- Issue
- 11
- Pages
- 2551-2560
- ISSN
- 0261-4189 (ISSN-L)
- OpenAlex
- W1483637431
- Cited by
- 437
- References
- 63
- FWCI
- 11.49
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
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- This page
- CoChat. (2026). Citation check: Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. https://app.cochat.ai/papers/10.1002/j.1460-2075.1995.tb07253.x
- The paper
- Tomoyasu, T., Gamer, J., Bukau, B., Kanemori, M., Mori, H., Rutman, A. J., Oppenheim, A. B., Yura, T., Yamanaka, K., & Niki, H. (1995). Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32. The EMBO Journal. https://doi.org/10.1002/j.1460-2075.1995.tb07253.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.