HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins (Q24291802)

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

1 reference

X-linked inhibitor of apoptosis

1 reference

Diablo, IAP-binding mitochondrial protein

1 reference

HtrA serine peptidase 2

1 reference

Richard Burke

9

0 references

Catherine Day

Catherine L Day

7

0 references

Paul G Ekert

Paul G Ekert

3

0 references

John Silke

John Silke

2

0 references

David L Vaux

David L Vaux

13

0 references

Richard Simpson

Richard J Simpson

12

0 references

Lisa Connolly

6

Lisa M Connolly

0 references

Anne M Verhagen

1

Anne M Verhagen

0 references

Miha Pakusch

4

Miha Pakusch

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author name string

Hitto Kaufmann

5

0 references

Anjali Tikoo

8

0 references

Carolyn Wrobel

10

0 references

Robert L Moritz

Journal of Biological Chemistry

11

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language of work or name

English

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publication date

4 January 2002

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published in

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volume

277

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issue

1

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page(s)

445-54

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Expression, purification, and functional analysis of the human serine protease HtrA2

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

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Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures.

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Primary structure of a putative serine protease specific for IGF-binding proteins

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

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

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A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.

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

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Structural and biochemical basis of apoptotic activation by Smac/DIABLO

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

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Structural basis of IAP recognition by Smac/DIABLO

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

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Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes

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

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The HtrA family of serine proteases

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Human HtrA, an evolutionarily conserved serine protease identified as a differentially expressed gene product in osteoarthritic cartilage

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Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia

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Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway

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The Drosophila caspase DRONC cleaves following glutamate or aspartate and is regulated by DIAP1, HID, and GRIM.

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DIABLO promotes apoptosis by removing MIHA/XIAP from processed caspase 9

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The Drosophila caspase DRONC is regulated by DIAP1

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Direct inhibition of caspase 3 is dispensable for the anti-apoptotic activity of XIAP.

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An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif

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Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by Drosophila proteins HID and GRIM.

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