Mechanisms of caspase activation and inhibition during apoptosis (Q27919623)

PubMed

PubMed publication ID

11931755

26 November 2016

title

Mechanisms of caspase activation and inhibition during apoptosis (English)

1 reference

publication type of scholarly work

PubMed

PubMed publication ID

26 November 2016

0 references

1

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publication date

March 2002

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language of work or name

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1 reference

9

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issue

3

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page(s)

459-70

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review article

1 reference

Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation

Europe PubMed Central

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Livin, a novel inhibitor of apoptosis protein family member

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Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade

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DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis

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The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis

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Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain

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The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif

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An exegesis of IAPs: salvation and surprises from BIR motifs

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Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone

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Nod2, a Nod1/Apaf-1 family member that is restricted to monocytes and activates NF-kappaB

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Identification of Ipaf, a human caspase-1-activating protein related to Apaf-1

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Dimer formation drives the activation of the cell death protease caspase 9

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Structural basis for the activation of human procaspase-7

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A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis

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sickle, a novel Drosophila death gene in the reaper/hid/grim region, encodes an IAP-inhibitory protein

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7 January 2021

Caspase-9 can be activated without proteolytic processing

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NMR structure and mutagenesis of the inhibitor-of-apoptosis protein XIAP

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NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP

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A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death

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Caspases: Enemies Within

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A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis

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7 January 2021

The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity

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Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins

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HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins

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The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID.

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Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex

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Autoproteolytic Activation of Pro-Caspases by Oligomerization

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Essential Role of CED-4 Oligomerization in CED-3 Activation and Apoptosis

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Apoptosis in the nervous system

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7 January 2021

An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9

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7 January 2021