(Q36594877)

15 August 2017

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title

Apoptosome: a platform for the activation of initiator caspases (English)

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15 August 2017

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Bao Q

1

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PubMed ID

16977332

15 August 2017

Shi Y

series ordinal

2

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15 August 2017

15 September 2006

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Cell Death & Differentiation

15 August 2017

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15 August 2017

14

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15 August 2017

56-65

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15 August 2017

1

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https://scigraph.springernature.com/pub.10.1038/sj.cdd.4402028

15 August 2017

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cites work

Cell death: critical control points

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The CD95(APO-1/Fas) DISC and beyond

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Molecular mechanisms of caspase regulation during apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Mechanisms of caspase activation and inhibition during apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Caspase activation: the induced-proximity model

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The protein structures that shape caspase activity, specificity, activation and inhibition

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Caspase-9 can be activated without proteolytic processing

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Caspase activation: revisiting the induced proximity model

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Caspase-9 and APAF-1 form an active holoenzyme

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Caspase activation involves the formation of the aposome, a large (approximately 700 kDa) caspase-activating complex

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Dark is a Drosophila homologue of Apaf-1/CED-4 and functions in an evolutionarily conserved death pathway

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

HAC-1, a Drosophila homolog of APAF-1 and CED-4 functions in developmental and radiation-induced apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Control of the cell death pathway by Dapaf-1, a Drosophila Apaf-1/CED-4-related caspase activator

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Developmental apoptosis in C. elegans: a complex CEDnario

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The biochemical mechanism of caspase-2 activation

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

A novel Apaf-1-independent putative caspase-2 activation complex

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Solution structure of the RAIDD CARD and model for CARD/CARD interaction in caspase-2 and caspase-9 recruitment

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Crystal structure of RAIDD death domain implicates potential mechanism of PIDDosome assembly

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

FADD/MORT1 is a common mediator of CD95 (Fas/APO-1) and tumor necrosis factor receptor-induced apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Mechanisms of apoptosis through structural biology

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The three-dimensional solution structure and dynamic properties of the human FADD death domain

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

NMR structure and mutagenesis of the FADD (Mort1) death-effector domain

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

A mechanism for death receptor discrimination by death adaptors

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Identification of an expanded binding surface on the FADD death domain responsible for interaction with CD95/Fas

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The structure of FADD and its mode of interaction with procaspase-8

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Crystal structure of a viral FLIP: insights into FLIP-mediated inhibition of death receptor signaling

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Crystal structure of MC159 reveals molecular mechanism of DISC assembly and FLIP inhibition

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

FADD self-association is required for stable interaction with an activated death receptor

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Insights into the regulatory mechanism for caspase-8 activation

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

A unified model for apical caspase activation

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

c-FLIP(L) is a dual function regulator for caspase-8 activation and CD95-mediated apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Activation of caspases-8 and -10 by FLIP(L).

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Structure of the apoptotic protease-activating factor 1 bound to ADP

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Mechanism of Dronc activation in Drosophila cells

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Three-dimensional structure of a double apoptosome formed by the Drosophila Apaf-1 related killer

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Modeling AAA+ ring complexes from monomeric structures.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Structure and activation mechanism of the Drosophila initiator caspase Dronc.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Worms, life, and death (Nobel lecture).

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Essential role of CED-4 oligomerization in CED-3 activation and apoptosis

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

CED-4 forms a 2 : 2 heterotetrameric complex with CED-9 until specifically displaced by EGL-1 or CED-13

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

2:1 Stoichiometry of the CED-4-CED-9 complex and the tetrameric CED-4: insights into the regulation of CED-3 activation

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Structural basis for the activation of human procaspase-7

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

An induced proximity model for caspase-8 activation.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Autoproteolytic activation of pro-caspases by oligomerization.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Synthetic activation of caspases: artificial death switches

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Mechanisms of caspase activation

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

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

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Mechanism of XIAP-mediated inhibition of caspase-9

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

The apoptosome activates caspase-9 by dimerization

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Oligomerization and activation of caspase-9, induced by Apaf-1 CARD.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Apoptosome: the cellular engine for the activation of caspase-9.

1 reference

https://api.crossref.org/works/10.1038%2FSJ.CDD.4402028

7 January 2021

Identifiers

DOI

10.1038/SJ.CDD.4402028

1 reference

15 August 2017

1 reference

PubMed ID

16977332