Caspase functions in cell death and disease.
By David Mcilwain, T. Berger, T. Mak. Cold Spring Harbor Perspectives in Biology, 2013
2,388 citations recorded by the source corpus.
Subfields: Epidemiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/b8b039bdde3e5f07ba15cd1614d4bc2fffbb384b
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Epidemiology
- D. Tang
- R. Kang
- Guido Kroemer
- Peter Vandenabeele
- T. Vanden Berghe
- T. Kanneganti
- Beth Levine
- L. Galluzzi
In Molecular Biology
- Guido Kroemer
- D. Tang
- R. Kang
- T. Kanneganti
- Peter Vandenabeele
- R. Malireddi
- S. Kesavardhana
- T. Vanden Berghe
Citations in the corpus
- Apoptotic Caspases Suppress mtDNA-Induced STING-Mediated Type I IFN Production (2014, positive): “Caspases are a family of 12 cysteinyl aspartate-specific proteases traditionally classified as inflammatory or apoptotic (McIlwain et al., 2013).”
- Bactericidal and Cytotoxic Properties of Silver Nanoparticles (2019, background): “Caspase-3 is the main caspase responsible for apoptosis execution [223].”
- Caspases in Cell Death, Inflammation, and Gasdermin-Induced Pyroptosis (2020, background): “Genetic and biochemical inactivation of caspases has revealed caspase-independent forms of cell death and a more complex relationship between apoptosis and inflammation (33, 58, 59).”
- BCL-2 family proteins: changing partners in the dance towards death (2017, background): “homeostasis culminating in the typical biochemical and morphological features of apoptosis.(2) Commitment to the apoptotic dance of death is due in part to”
- The molecular machinery of regulated cell death (2019, background): “Caspases are a family of cysteine-dependent aspartate-specific proteases that play a critical role in the regulation of cell death, connecting to development, inflammation, and immunity.(10,11) RCD is therefore categorized into two groups: caspase-dependent (e.”