Anne M. Verhagen
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Research Interests
Anne M. Verhagen has a total of 16 co-authors. Here are the top co-authors by number of shared publications:
- David Lawrence Vaux
The Walter and Eliza Hall Institute of Medical Research, Melbourne, Australia
5 shared publications - John Silke
The Walter and Eliza Hall Institute of Medical Research, Parkville, Australia
4 shared publications Miha Pakusch
2 shared publications- Paul G. Ekert
Peter MacCallum Cancer Centre, Melbourne, VIC 3000, Australia
2 shared publications Anjali Tikoo
1 shared publicationCarolyn Wrobel
1 shared publication
Latest Publications
- Open Access
- 23 June 2006
- Published by Springer Nature in Cell Death & Differentiation
- Vol. 14 (2) , 348-357
Identification of mammalian mitochondrial proteins that interact with IAPs via N-terminal IAP binding motifs
Direct IAP binding protein with low pI/second mitochondrial activator of caspases, HtrA2/Omi and GstPT/eRF3 are mammalian proteins that bind via N-terminal inhibitor of apoptosis protein (IAP) binding motifs (IBMs) to the baculoviral IAP repeat (BIR) domains of IAPs. These interactions can prevent IAPs from inhibiting caspases, or displace active caspases, thereby promoting cell death. We have identified several additional potential IAP antagonists, including glutamate dehydrogenase (GdH), Nipsnap 3 and 4, CLPX, leucine-rich pentatricopeptide repeat motif-containing protein and 3-hydroxyisobutyrate dehydrogenase. All are mitochondrial proteins from which N-terminal import sequences are removed generating N-terminal IBMs. Whereas most of these proteins have alanine at the N-terminal position, as observed for previously described antagonists, GdH has an N-terminal serine residue that is essential for X-linked IAP (XIAP) interaction. These newly described IAP binding proteins interact with XIAP mainly via BIR2, with binding eliminated or significantly reduced by a single point mutation (D214S) within this domain. Through this interaction, many are able to antagonise XIAP inhibition of caspase 3 in vitro.
- 23 June 2006
- Published by Springer Nature in Cell Death & Differentiation
- Vol. 14 (2) , 348-357
Open AccessIdentification of mammalian mitochondrial proteins that interact with IAPs via N-terminal IAP binding motifs
Direct IAP binding protein with low pI/second mitochondrial activator of caspases, HtrA2/Omi and GstPT/eRF3 are mammalian proteins that bind via N-terminal inhibitor of apoptosis protein (IAP) binding motifs (IBMs) to the baculoviral IAP repeat (BIR) domains of IAPs. These interactions can prevent IAPs from inhibiting caspases, or displace active caspases, thereby promoting cell death. We have identified several additional potential IAP antagonists, including glutamate dehydrogenase (GdH), Nipsnap 3 and 4, CLPX, leucine-rich pentatricopeptide repeat motif-containing protein and 3-hydroxyisobutyrate dehydrogenase. All are mitochondrial proteins from which N-terminal import sequences are removed generating N-terminal IBMs. Whereas most of these proteins have alanine at the N-terminal position, as observed for previously described antagonists, GdH has an N-terminal serine residue that is essential for X-linked IAP (XIAP) interaction. These newly described IAP binding proteins interact with XIAP mainly via BIR2, with binding eliminated or significantly reduced by a single point mutation (D214S) within this domain. Through this interaction, many are able to antagonise XIAP inhibition of caspase 3 in vitro.
- Open Access
- 13 May 2002
- Vol. 3 (6)
Revealing the intricacies of cancer.
A report on the 14th Lorne Cancer Conference, Lorne, Victoria, Australia, 14-17 February 2002.
- 13 May 2002
- Vol. 3 (6)
Open AccessRevealing the intricacies of cancer.
A report on the 14th Lorne Cancer Conference, Lorne, Victoria, Australia, 14-17 February 2002.
- 1 April 2002
- Published by Springer Nature in Apoptosis
- Vol. 7 (2) , 163-166
Cell death regulation by the mammalian IAP antagonist Diablo/Smac
In Drosophila, the genetic locus 75CI1,2 is essential for all developmental cell death. Within this region are the genes for three pro-death proteins, Grim, Reaper and HID. These proteins are...
- 1 April 2002
- Published by Springer Nature in Apoptosis
- Vol. 7 (2) , 163-166
Cell death regulation by the mammalian IAP antagonist Diablo/Smac
In Drosophila, the genetic locus 75CI1,2 is essential for all developmental cell death. Within this region are the genes for three pro-death proteins, Grim, Reaper and HID. These proteins are...
- 28 March 2002
- Published by Springer Nature in Cell Death & Differentiation
- Vol. 9 (4) , 362-363
Jekyll and Hyde; changing places, changing faces
- 28 March 2002
- Published by Springer Nature in Cell Death & Differentiation
- Vol. 9 (4) , 362-363
Jekyll and Hyde; changing places, changing faces
- Open Access
- 1 January 2002
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (1) , 445-454
HtrA2 Promotes Cell Death through Its Serine Protease Activity and Its Ability to Antagonize Inhibitor of Apoptosis Proteins
- 1 January 2002
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (1) , 445-454
Open AccessHtrA2 Promotes Cell Death through Its Serine Protease Activity and Its Ability to Antagonize Inhibitor of Apoptosis Proteins
- Open Access
- 5 July 2001
- Published by Institute of Electrical and Electronics Engineers (IEEE)
- Vol. 2 (7)
Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs
The inhibitor of apoptosis (IAP) proteins prevent cell death by binding to and inhibiting caspases. They share the BIR domain with a second group of proteins that regulate cytokinesis and chromosomal segregation.
- 5 July 2001
- Published by Institute of Electrical and Electronics Engineers (IEEE)
- Vol. 2 (7)
Open AccessInhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs
The inhibitor of apoptosis (IAP) proteins prevent cell death by binding to and inhibiting caspases. They share the BIR domain with a second group of proteins that regulate cytokinesis and chromosomal segregation.