(Q40602863)

21 September 2017

title

Uncoupling of the signaling and caspase-inhibitory properties of X-linked inhibitor of apoptosis (English)

1 reference

21 September 2017

5

Anita B Roberts

1 reference

21 September 2017

Stephanie Birkey Reffey

3

object named as

Stephanie Birkey Reffey

1 reference

21 September 2017

Jennifer Lewis

1

1 reference

21 September 2017

Ezra Burstein

2

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21 September 2017

Shawn B Bratton

4

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21 September 2017

Colin S Duckett

6

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21 September 2017

language of work or name

English

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publication date

29 December 2003

1 reference

Journal of Biological Chemistry

21 September 2017

number of pages

7

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based on heuristic

inferred from page(s)

published in

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21 September 2017

volume

279

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21 September 2017

issue

10

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21 September 2017

page(s)

9023-9029

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IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases

21 September 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

X-linked IAP is a direct inhibitor of cell-death proteases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Structural basis of caspase-7 inhibition by XIAP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Structural basis for the inhibition of caspase-3 by XIAP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

The TNFR2-TRAF signaling complex contains two novel proteins related to baculoviral inhibitor of apoptosis proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

TNF-RII and c-IAP1 mediate ubiquitination and degradation of TRAF2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

XIAP, a cellular member of the inhibitor of apoptosis protein family, links the receptors to TAB1-TAK1 in the BMP signaling pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

X-linked inhibitor of apoptosis protein functions as a cofactor in transforming growth factor-beta signaling

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Cell division regulation by BIR1, a member of the inhibitor of apoptosis family in yeast.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-1 plays a conserved role in cytokinesis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Survivin and the inner centromere protein INCENP show similar cell-cycle localization and gene knockout phenotype

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Solution structure of a baculoviral inhibitor of apoptosis (IAP) repeat

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

A single BIR domain of XIAP sufficient for inhibiting caspases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

XIAP inhibition of caspase-3 preserves its association with the Apaf-1 apoptosome and prevents CD95- and Bax-induced apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Structural basis of IAP recognition by Smac/DIABLO

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Role of transforming growth factor-beta signaling in cancer

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Regulation of immune responses by TGF-beta

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

IAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1 signaling cascade and caspase inhibition

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Selective activation of JNK1 is necessary for the anti-apoptotic activity of hILP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Activation of NF-kappa B by XIAP, the X chromosome-linked inhibitor of apoptosis, in endothelial cells involves TAK1

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Caspases signal not only apoptosis but also antigen-induced activation in cells of the immune system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Phosphorylation of IkappaB-alpha inhibits its cleavage by caspase CPP32 in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Apoptosis promotes a caspase-induced amino-terminal truncation of IkappaBalpha that functions as a stable inhibitor of NF-kappaB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Caspase-mediated processing of the Drosophila NF-kappaB factor Relish

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Three mutations in v-Rel render it resistant to cleavage by cell-death protease caspase-3.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Induction of nuclear factor kappaB by the CD30 receptor is mediated by TRAF1 and TRAF2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Human IAP-like protein regulates programmed cell death downstream of Bcl-xL and cytochrome c

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Molecular cloning of ILP-2, a novel member of the inhibitor of apoptosis protein family

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

Caspase-9 and APAF-1 form an active holoenzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

21 January 2018

XIAP, the guardian angel

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

xIAP induces cell-cycle arrest and activates nuclear factor-kappaB : new survival pathways disabled by caspase-mediated cleavage during apoptosis of human endothelial cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M312891200

21 January 2018

Identifiers

DOI

10.1074/JBC.M312891200

1 reference

21 September 2017

1 reference