Cited by 1,136Cancer-related Molecular PathwaysCell death mechanisms and regulationHeat shock proteins research

The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.

Apoptosis - the p53 network

Haupt, Susan, Berger, Michael, Goldberg, Zehavit, Haupt, Ygal·2003·Journal of Cell Science

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Abstract

Exposure to cellular stress can trigger the p53 tumor suppressor, a sequence-specific transcription factor, to induce cell growth arrest or apoptosis. The choice between these cellular responses is influenced by many factors, including the type of cell and stress, and the action of p53 co-activators. p53 stimulates a wide network of signals that act through two major apoptotic pathways. The extrinsic, death receptor pathway triggers the activation of a caspase cascade, and the intrinsic, mitochondrial pathway shifts the balance in the Bcl-2 family towards the pro-apoptotic members, promoting the formation of the apoptosome, and consequently caspase-mediated apoptosis. The impact of these two apoptotic pathways may be enhanced when they converge through Bid, which is a p53 target. The majority of these apoptotic effects are mediated through the induction of specific apoptotic target genes. However, p53 can also promote apoptosis by a transcription-independent mechanism under certain conditions. Thus, a multitude of mechanisms are employed by p53 to ensure efficient induction of apoptosis in a stage-, tissue- and stress-signal-specific manner. Manipulation of the apoptotic functions of p53 constitutes an attractive target for cancer therapy.

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RETRACTED: Regulation of p53: intricate loops and delicate balances
Oren, M., Damalas, A., Gottlieb, T. M., Michael, D., Taplick, J., Martínez-Leal, J. F., Maya, R. B.-Y., Moas, M., Seger, R., Taya, Y., et al. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01149-8 · Cited by 150
Retracted
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“Indeed, approximately 50% of human cancers bear p53 gene mutations; in the majority of the remaining cancer cases, p53 activity is compromised by alternative mechanisms (Vogelstein et al., 2000).”
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Authors: Haupt, S., Berger, M., Goldberg, Z., & Haupt, Y.
Affiliations: Hebrew University of Jerusalem (IL)
Corresponding author: Haupt, Ygal
ORCID: Berger, Michael
Goldberg, Zehavit
Haupt, Ygal
Venue: Journal of Cell Science
Publisher: The Company of Biologists
Published: 2003-10-15
Volume: 116
Issue: 20
Pages: 4077-4085
ISSN: 0021-9533 (ISSN-L)
1477-9137
DOI: 10.1242/jcs.00739
OpenAlex: W2103616303
Cited by: 1,136
References: 93
Citations by year: 2026: 11 · 2025: 24 · 2024: 34 · 2023: 31 · 2022: 37 · 2021: 53 · 2020: 57 · 2019: 57 · 2018: 57 · 2017: 53 · 2016: 75 · 2015: 66 · 2014: 59 · 2013: 76 · 2012: 76
FWCI: 3.47
Type: journal article
Language: en
Open access: closed
Locations: Journal of Cell Science (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: p53, apoptosis, p53 tumor suppressor, cellular stress response, growth arrest, death receptor signaling, mitochondrial apoptosis, Bcl-2 family proteins, apoptosome, caspase cascade, Bid, p53 target genes, cancer therapy
MeSH terms: Animals, Carrier Proteins, Cell Division, Enzyme Activation, Humans, Mitochondria, Proto-Oncogene Proteins, Signal Transduction, Tumor Suppressor Protein p53, Apoptosis, Protein Serine-Threonine Kinases, Proto-Oncogene Proteins c-bcl-2, Caspases, Protein Interaction Mapping, BH3 Interacting Domain Death Agonist Protein, Proto-Oncogene Proteins c-akt

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