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AIFM1 (apoptosis-inducing factor, mitochondrion-associated, 1)

Identity

Other namesAIF
PDCD8
MGC111425
HGNC (Hugo) AIFM1
LocusID (NCBI) 9131
Location Xq26.1
Location_base_pair Starts at 129263338 and ends at 129272015 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order Centromere (59,500 Kbp)- ARHGEF9 - (...) - RAB33A- AIFM1 - ELF4 - (...) - IL9R -telomere (154,914 Kbp).

DNA/RNA

Note AIF (Apoptosis-Inducing Factor). Total gene size 36.471 Kb with a transcribed region of 2.215 Kb which codes for 613 amino acids. To date, five isoforms from AIF gene have been described (AIF, AIFexB, AIFsh, AIFsh2, and AIFsh3).
 
  AIF gene structure and known isoforms. Genomic organization of AIF and resulting AIF, AIF-exB, AIFsh, AIFsh2, and AIFsh3 mRNA transcripts (schemas in the left). Translation start (ATG, in green) and stop (TGA/TAA, in red) codons are indicated, and the predicted protein product is shown at the right. Numbers in AIF designate exons (in mRNA transcripts) and amino acids (in the predicted proteins). Mitochondria localization signal (MLS), Pyridoxin-redox (Pyr-Redox), nuclear localization sequence (NLS), and C-terminal domains are indicated. I9 (in green) indicates intron 9. The inclusion of the 203-bp exon 9b (lettering in red) produces AIFsh2 and AIFsh3, which encodes 324- and 237-amino acid proteins, respectively. AIFsh2 contains the MLS and the Pyr-Redox domain, but lacks the C-terminal portion of AIF. AIFsh3 has a similar structure as AIFsh2 with the splicing of exon 2, leading to the loss of MLS. Blue lines indicate the splicing of the different isoforms.
Description 16 exons spanning 36.471 Kb.
Transcription 2,215 bp mRNA.
Pseudogene Not known.

Protein

Note 613 amino acids long protein whose structure may be divided into three domains: a FAD-binding domain (residues 128-262 and 401-480), a NADH-binding domain (residues 263-400), and a C-terminal domain (residues 481-608).
 
  Schematic model representing the three different AIF forms: precursor, mature, and truncated. AIF is a flavoprotein (with an oxidoreductase enzymatic activity) containing a FAD-bipartite domain (yellow, amino-acids 128-262 and 401-480), a NADH-binding motif (violet, amino-acids 263-400), and a C-terminal domain (red, amino-acids 481-608) where the proapoptotic activity of the protein resides. In addition, it has a Mitochondria Localization Sequence (MLS, in green, amino-acids 1-41) placed in its N-terminal region. Between the first-N-terminal FAD motif and the MLS, AIF possesses a potential Transmembrane Domain (TM, in green, amino-acids 67-83). This TM is flanked by two peptidase-processing positions: a Mitochondrial Processing Peptidase (MPP)-cleavage site (in blue, amino-acid 54) and a calpains- and/or cathepsins-cleavage site (in red, amino-acid 103). Hsp70 (Heat Shock Protein-70) and CypA (Cyclophilin A) bind AIF in amino-acids 150-228 and 367-369, respectively. AIF also possesses two DNA-binding sites, which are located in amino-acids 255-265 and 510-518, respectively. AIF precursor protein has 613 amino-acids. The MPP-mediated cleavage generates the mitochondrial mature AIF (amino-acids 55-613). After an apoptotic insult, calpains or cathepsins cleave AIF to produce truncated-AIF (tAIF), which is released from mitochondria to cytosol (amino-acids 104-613).
Description AIF was initially identified as a protein released from the mitochondrial intermembrane space during the apoptotic process. First studies showed that upon an apoptotic stimulus AIF translocates from mitochondria to cytosol and further to the nucleus where it triggers caspase-independent programmed cell death. AIF, expressed as a precursor of 67 kDa, is addressed to mitochondria by the two MLS placed within the N-terminal prodomain of the protein. Once in mitochondria, this precursor is processed to a mature form of 62 kDa by a first proteolytic cleavage. In this configuration, AIF is an inner-membrane-anchored protein in which the N-terminus is exposed to the mitochondrial matrix and the C-terminal portion to the mitochondrial intermembrane space. AIF is here required for maintenance or maturation of the mitochondrial respiratory chain complex I. After a cell death insult, the 62 kDa AIF-mitochondrial form is cleaved by activated calpains and/or cathepsins to yield a soluble proapoptotic protein with an apparent molecular weight of 57 kDa tAIF (truncated AIF). tAIF is released from mitochondria to cytosol and nucleus to generate two typical hallmarks of caspase-independent programmed cell death: chromatin condensation and large-scale approximatively 50 kb DNA fragmentation.
 
  Ribbon structure of mouse AIF in its mature form (pdb id: 1GV4). As depicted here, three domains are present in the protein. The FAD-binding domain and the NAD-binding domain (yellow) are both similar to oxidoreductase domains from members of the glutathione reductase family. In contrast, the C-terminal domain (blue) displays a particular folding with a specific insertion, which includes residues 580 to 610. This picture also includes the AIF cofactor Flavin Adenine Dinucleotide (FAD; magenta).
Expression Ubiquitously expressed.
Localisation Mitochondrion.
Function AIF has a double life/death function.
In its vital role, AIF is required to maintain and/or organize the mitochondrial respiratory complex I, and displays NADH oxidoreductase and peroxide scavenging activities. In addition to this vital function, AIF has been shown to be implicated in programmed cell death (PCD) induction in several experimental models (see bibliography section). In the two most studied AIF-dependent PCD models, AIF death activity is associated with the increase of intracellular Ca2+ (e.g., ischemia/reperfusion injury), or relates with extensive DNA-damage (e.g., treatment with alkylating agents). In the first model, increased intracellular Ca2+ levels trigger depolarization of mitochondrial membrane, subsequent loss of membrane potential, generation of reactive oxygen species (ROS), and AIF mitochondrial release. In the second model, extensive DNA damage, provoked by high doses of alkylating agents such as MNNG or MNU, triggers poly(ADP-ribose) polymerase-1 (PARP-1) over-activation and AIF release from the mitochondrial intermembrane space. This cell death pathway sequentially involves PARP-1, calpains, Bax, and AIF.
Homology AIF is a highly conserved protein ubiquitously present in all primary kingdoms, Bacteria, Archaea and Eucaryota. The aif gene is inherited from the last universal common ancestor and follows the tree topology with the primary radiation of the archaeo-eukaryotic and bacterial clades. AIF also has a highly significant homology with different families of oxidoreductases, including NADH oxydases, Ascorbate reductases, Glutathione reductases and many NADH-dependent ferredoxin reductases from Archaea and Bacteria to invertebrates and vertebrates.
Mouse, Rat homology
 
  Phylogenetic tree representing the relationship between AIF and other oxidoreductases from different species. Note the proximity of the AIF family (red branch) to the NADH-oxidase family from Archaea. The PIR accession codes are enumerated following the abbreviation of each specie: AA: Aquifex aeolicus; AC: Acinetobacter calcoaceticus; AF: Archaeoglobus fulgidus; AT: Arabidopsis thaliana; BC: Burkholderia cepacia; BS: Bacillus subtilis; CE: Caenorhabditis elegans; DD: Dictyostelium discoideum; DM: Drosophila melanogaster; EC: Escherichia coli; HS: Homo sapiens; LS: Lycopersicon esculentum; MJ: Methanocaldococcus jannaschii; MM: Mus musculus; MTH: Methanobacterium thermoautotrophicum; N A: Novosphingobium aromaticivorans; PF: Pseudomonas fluorescens; PH: Pyrococcus horikoshii; PO: Pseudomonas oleovorans; PP: Pseudomonas putida; PS: Pseudomonas sp.; PSA: Pisum sativum; SP: Schizosaccharomyces pombe; SS: Sphingomonas sp.; RE: Rhodococcus erythropolis; RG: Rhodococcus globerulus; XL: Xenopus laevis.

Mutations

Note Several polymorphisms have been identified but none of them has shown any association with a disease.

Implicated in

Entity Various cancers
Note Upregulated in cancers (colorectal carcinoma, gastric carcinoma, breast carcinoma and hepatocellular carcinoma, glioblastoma).
AIF expression may play a role in tumor formation and could maintain a transformed state of colon cancer cells involving mitochondrial complex I function.
  
Entity Cell death
Disease AIF has been directly designed as main mediator of cell death in ischemic injuries after overproduction of reactive oxygen species. Indeed, blocking the mitochondrial release of AIF to cytosol and its further nuclear translocation provides protection against neuronal and cardiomyocites cell death. AIF-deficient harlequin mutant mouse presents a significant reduction of neuronal cell death in brain trauma and cerebral ischemia. A similar protective effect was observed in AIF siRNA-treated neurons.
  
Entity Degenerative disorders
Disease AIF is involved in several degenerative disorders. The elevated production of ROS generated in Amyotrophic Lateral Sclerosis, Alzheimer's, or Parkinson diseases concludes in the translocation of AIF. Likewise, AIF release triggered by calpains and cathepsins was observed on in vitro models of Epilepsy and Huntington's disease. AIF-mediated cell death is involved in the pathogenesis of different retinal affections such as retinal detachment, retinitis pigmentosa, or in models of retinal hypoxia. Moreover, an increase of AIF expression has been reported in patients affected with diabetic retinopathy.
  

External links

Nomenclature
HGNC (Hugo)AIFM1   8768
Cards
AtlasAIFM1ID44053chXq25
Entrez_Gene (NCBI)AIFM1  9131  apoptosis-inducing factor, mitochondrion-associated, 1
GeneCards (Weizmann)AIFM1
Ensembl (Hinxton)ENSG00000156709 [Gene_View]  chrX:129263338-129272015 [Contig_View]  AIFM1 [Vega]
ICGC DataPortalENSG00000156709
cBioPortalAIFM1
AceView (NCBI)AIFM1
Genatlas (Paris)AIFM1
WikiGenes9131
SOURCE (Princeton)NM_001130846 NM_001130847 NM_004208 NM_145812 NM_145813
Genomic and cartography
GoldenPath (UCSC)AIFM1  -  Xq26.1   chrX:129263338-129272015 -  Xq26.1   [Description]    (hg19-Feb_2009)
EnsemblAIFM1 - Xq26.1 [CytoView]
Mapping of homologs : NCBIAIFM1 [Mapview]
OMIM300169   310490   
Gene and transcription
Genbank (Entrez)AF100928 AF131759 AK000775 AK314446 AL049703
RefSeq transcript (Entrez)NM_001130846 NM_001130847 NM_004208 NM_145812 NM_145813
RefSeq genomic (Entrez)AC_000155 NC_000023 NC_018934 NG_013217 NT_011786 NW_001842398 NW_004929446
Consensus coding sequences : CCDS (NCBI)AIFM1
Cluster EST : UnigeneHs.424932 [ NCBI ]
CGAP (NCI)Hs.424932
Alternative Splicing : Fast-db (Paris)GSHG0032326
Alternative Splicing GalleryENSG00000156709
Gene ExpressionAIFM1 [ NCBI-GEO ]     AIFM1 [ SEEK ]   AIFM1 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtO95831 (Uniprot)
NextProtO95831  [Medical]
With graphics : InterProO95831
Splice isoforms : SwissVarO95831 (Swissvar)
Catalytic activity : Enzyme1.1.1.- [ Enzyme-Expasy ]   1.1.1.-1.1.1.- [ IntEnz-EBI ]   1.1.1.- [ BRENDA ]   1.1.1.- [ KEGG ]   
Domains : Interpro (EBI)AIF_C [organisation]   FAD/NAD-linked_Rdtase_dimer [organisation]   FAD_pyr_nucl-diS_OxRdtase [organisation]   Pyr_nucl-diS_OxRdtase_dimer [organisation]   Pyr_nucl-diS_OxRdtase_FAD/NAD [organisation]   Pyr_OxRdtase_NAD-bd_dom [organisation]  
Related proteins : CluSTrO95831
Domain families : Pfam (Sanger)AIF_C (PF14721)    Pyr_redox (PF00070)    Pyr_redox_2 (PF07992)   
Domain families : Pfam (NCBI)pfam14721    pfam00070    pfam07992   
DMDM Disease mutations9131
Blocks (Seattle)O95831
PDB (SRS)1M6I    4FDC    4LII   
PDB (PDBSum)1M6I    4FDC    4LII   
PDB (IMB)1M6I    4FDC    4LII   
PDB (RSDB)1M6I    4FDC    4LII   
Human Protein AtlasENSG00000156709 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasO95831
HPRD02161
IPIIPI00000690   IPI00300018   IPI00157908   IPI00910786   IPI01015707   IPI00976931   IPI00975625   IPI00977593   
Protein Interaction databases
DIP (DOE-UCLA)O95831
IntAct (EBI)O95831
FunCoupENSG00000156709
BioGRIDAIFM1
InParanoidO95831
Interologous Interaction database O95831
IntegromeDBAIFM1
STRING (EMBL)AIFM1
Ontologies - Pathways
Ontology : AmiGODNA binding  protein binding  nucleus  nucleus  mitochondrion  mitochondrial inner membrane  mitochondrial intermembrane space  mitochondrial intermembrane space  cytosol  DNA catabolic process  apoptotic DNA fragmentation  apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  electron carrier activity  NAD(P)H oxidase activity  oxidoreductase activity, acting on NAD(P)H  neuron differentiation  chromosome condensation  mitochondrial respiratory chain complex I assembly  positive regulation of apoptotic process  cell redox homeostasis  protein dimerization activity  perinuclear region of cytoplasm  flavin adenine dinucleotide binding  neuron apoptotic process  oxidation-reduction process  intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress  
Ontology : EGO-EBIDNA binding  protein binding  nucleus  nucleus  mitochondrion  mitochondrial inner membrane  mitochondrial intermembrane space  mitochondrial intermembrane space  cytosol  DNA catabolic process  apoptotic DNA fragmentation  apoptotic process  activation of cysteine-type endopeptidase activity involved in apoptotic process  electron carrier activity  NAD(P)H oxidase activity  oxidoreductase activity, acting on NAD(P)H  neuron differentiation  chromosome condensation  mitochondrial respiratory chain complex I assembly  positive regulation of apoptotic process  cell redox homeostasis  protein dimerization activity  perinuclear region of cytoplasm  flavin adenine dinucleotide binding  neuron apoptotic process  oxidation-reduction process  intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress  
Pathways : BIOCARTAOpposing roles of AIF in Apoptosis and Cell Survival [Genes]    Role of Mitochondria in Apoptotic Signaling [Genes]    Ceramide Signaling Pathway [Genes]   
Pathways : KEGGApoptosis   
Protein Interaction DatabaseAIFM1
Wikipedia pathwaysAIFM1
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)AIFM1
snp3D : Map Gene to Disease9131
SNP (GeneSNP Utah)AIFM1
SNP : HGBaseAIFM1
Genetic variants : HAPMAPAIFM1
Exome VariantAIFM1
1000_GenomesAIFM1 
ICGC programENSG00000156709 
Somatic Mutations in Cancer : COSMICAIFM1 
CONAN: Copy Number AnalysisAIFM1 
Mutations and Diseases : HGMDAIFM1
Mutations and Diseases : intOGenAIFM1
Genomic VariantsAIFM1  AIFM1 [DGVbeta]
dbVarAIFM1
ClinVarAIFM1
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM300169    310490   
MedgenAIFM1
GENETestsAIFM1
Disease Genetic AssociationAIFM1
Huge Navigator AIFM1 [HugePedia]  AIFM1 [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneAIFM1
Homology/Alignments : Family Browser (UCSC)AIFM1
Phylogenetic Trees/Animal Genes : TreeFamAIFM1
Chemical/Protein Interactions : CTD9131
Chemical/Pharm GKB GenePA162376129
Clinical trialAIFM1
Cancer Resource (Charite)ENSG00000156709
Other databases
Probes
Litterature
PubMed137 Pubmed reference(s) in Entrez
CoreMineAIFM1
iHOPAIFM1
OncoSearchAIFM1

Bibliography

Molecular characterization of mitochondrial apoptosis-inducing factor.
Susin SA, Lorenzo HK, Zamzami N, Marzo I, Snow BE, Brothers GM, Mangion J, Jacotot E, Costantini P, Loeffler M, Larochette N, Goodlett DR, Aebersold R, Siderovski DP, Penninger JM, Kroemer G
Nature. 1999 ; 397 (6718) : 441-446.
PMID 9989411
 
Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death.
Joza N, Susin SA, Daugas E, Stanford WL, Cho SK, Li CY, Sasaki T, Elia AJ, Cheng HY, Ravagnan L, Ferri KF, Zamzami N, Wakeham A, Hakem R, Yoshida H, Kong YY, Mak TW, Ziga-Pflcker JC, Kroemer G, Penninger JM
Nature. 2001 ; 410 (6828) : 549-554.
PMID 11279485
 
NADH oxidase activity of mitochondrial apoptosis-inducing factor.
Miramar MD, Costantini P, Ravagnan L, Saraiva LM, Haouzi D, Brothers G, Penninger JM, Peleato ML, Kroemer G, Susin SA
The Journal of biological chemistry. 2001 ; 276 (19) : 16391-16398.
PMID 11278689
 
Heat-shock protein 70 antagonizes apoptosis-inducing factor.
Ravagnan L, Gurbuxani S, Susin SA, Maisse C, Daugas E, Zamzami N, Mak T, Jttel M, Penninger JM, Garrido C, Kroemer G
Nature cell biology. 2001 ; 3 (9) : 839-843.
PMID 11533664
 
The harlequin mouse mutation downregulates apoptosis-inducing factor.
Klein JA, Longo-Guess CM, Rossmann MP, Seburn KL, Hurd RE, Frankel WN, Bronson RT, Ackerman SL
Nature. 2002 ; 419 (6905) : 367-374.
PMID 12353028
 
The crystal structure of the mouse apoptosis-inducing factor AIF.
Mat MJ, Ortiz-Lombarda M, Boitel B, Haouz A, Tello D, Susin SA, Penninger J, Kroemer G, Alzari PM
Nature structural biology. 2002 ; 9 (6) : 442-446.
PMID 11967568
 
DNA binding is required for the apoptogenic action of apoptosis inducing factor.
Ye H, Cande C, Stephanou NC, Jiang S, Gurbuxani S, Larochette N, Daugas E, Garrido C, Kroemer G, Wu H
Nature structural biology. 2002 ; 9 (9) : 680-684.
PMID 12198487
 
Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor.
Yu SW, Wang H, Poitras MF, Coombs C, Bowers WJ, Federoff HJ, Poirier GG, Dawson TM, Dawson VL
Science (New York, N.Y.). 2002 ; 297 (5579) : 259-263.
PMID 12114629
 
Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis.
Bidre N, Lorenzo HK, Carmona S, Laforge M, Harper F, Dumont C, Senik A
The Journal of biological chemistry. 2003 ; 278 (33) : 31401-31411.
PMID 12782632
 
Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor.
Gurbuxani S, Schmitt E, Cande C, Parcellier A, Hammann A, Daugas E, Kouranti I, Spahr C, Pance A, Kroemer G, Garrido C
Oncogene. 2003 ; 22 (43) : 6669-6678.
PMID 14555980
 
Poly(ADP-ribose) polymerase-1 and apoptosis inducing factor in neurotoxicity.
Yu SW, Wang H, Dawson TM, Dawson VL
Neurobiology of disease. 2003 ; 14 (3) : 303-317.
PMID 14678748
 
AIF and cyclophilin A cooperate in apoptosis-associated chromatinolysis.
Cand C, Vahsen N, Kouranti I, Schmitt E, Daugas E, Spahr C, Luban J, Kroemer RT, Giordanetto F, Garrido C, Penninger JM, Kroemer G
Oncogene. 2004 ; 23 (8) : 1514-1521.
PMID 14716299
 
Apoptosis-inducing factor determines the chemoresistance of non-small-cell lung carcinomas.
Gallego MA, Joseph B, Hemstrm TH, Tamiji S, Mortier L, Kroemer G, Formstecher P, Zhivotovsky B, Marchetti P
Oncogene. 2004 ; 23 (37) : 6282-6291.
PMID 15286713
 
AIF deficiency compromises oxidative phosphorylation.
Vahsen N, Cand C, Brire JJ, Bnit P, Joza N, Larochette N, Mastroberardino PG, Pequignot MO, Casares N, Lazar V, Feraud O, Debili N, Wissing S, Engelhardt S, Madeo F, Piacentini M, Penninger JM, Schgger H, Rustin P, Kroemer G
The EMBO journal. 2004 ; 23 (23) : 4679-4689.
PMID 15526035
 
Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space.
Otera H, Ohsakaya S, Nagaura Z, Ishihara N, Mihara K
The EMBO journal. 2005 ; 24 (7) : 1375-1386.
PMID 15775970
 
Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria.
Polster BM, Basaez G, Etxebarria A, Hardwick JM, Nicholls DG
The Journal of biological chemistry. 2005 ; 280 (8) : 6447-6454.
PMID 15590628
 
AIF suppresses chemical stress-induced apoptosis and maintains the transformed state of tumor cells.
Urbano A, Lakshmanan U, Choo PH, Kwan JC, Ng PY, Guo K, Dhakshinamoorthy S, Porter A
The EMBO journal. 2005 ; 24 (15) : 2815-2826.
PMID 16001080
 
Cysteine protease inhibition prevents mitochondrial apoptosis-inducing factor (AIF) release.
Yuste VJ, Moubarak RS, Delettre C, Bras M, Sancho P, Robert N, d'Alayer J, Susin SA
Cell death and differentiation. 2005 ; 12 (11) : 1445-1448.
PMID 15933737
 
CD44 ligation induces caspase-independent cell death via a novel calpain/AIF pathway in human erythroleukemia cells.
Artus C, Maquarre E, Moubarak RS, Delettre C, Jasmin C, Susin SA, Robert-Lzns J
Oncogene. 2006 ; 25 (42) : 5741-5751.
PMID 16636662
 
Dissociating the dual roles of apoptosis-inducing factor in maintaining mitochondrial structure and apoptosis.
Cheung EC, Joza N, Steenaart NA, McClellan KA, Neuspiel M, McNamara S, MacLaurin JG, Rippstein P, Park DS, Shore GC, McBride HM, Penninger JM, Slack RS
The EMBO journal. 2006 ; 25 (17) : 4061-4073.
PMID 16917506
 
AIFsh, a novel apoptosis-inducing factor (AIF) pro-apoptotic isoform with potential pathological relevance in human cancer.
Delettre C, Yuste VJ, Moubarak RS, Bras M, Lesbordes-Brion JC, Petres S, Bellalou J, Susin SA
The Journal of biological chemistry. 2006 ; 281 (10) : 6413-6427.
PMID 16365034
 
Identification and characterization of AIFsh2, a mitochondrial apoptosis-inducing factor (AIF) isoform with NADH oxidase activity.
Delettre C, Yuste VJ, Moubarak RS, Bras M, Robert N, Susin SA
The Journal of biological chemistry. 2006 ; 281 (27) : 18507-18518.
PMID 16644725
 
Immunohistochemical and mutational analysis of apoptosis-inducing factor (AIF) in colorectal carcinomas.
Jeong EG, Lee JW, Soung YH, Nam SW, Kim SH, Lee JY, Yoo NJ, Lee SH
APMIS : acta pathologica, microbiologica, et immunologica Scandinavica. 2006 ; 114 (12) : 867-873.
PMID 17207087
 
Apoptosis-inducing factor: vital and lethal.
Modjtahedi N, Giordanetto F, Madeo F, Kroemer G
Trends in cell biology. 2006 ; 16 (5) : 264-272.
PMID 16621561
 
Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation.
Ruchalski K, Mao H, Li Z, Wang Z, Gillers S, Wang Y, Mosser DD, Gabai V, Schwartz JH, Borkan SC
The Journal of biological chemistry. 2006 ; 281 (12) : 7873-7880.
PMID 16407317
 
Regulation of AIF expression by p53.
Stambolsky P, Weisz L, Shats I, Klein Y, Goldfinger N, Oren M, Rotter V
Cell death and differentiation. 2006 ; 13 (12) : 2140-2149.
PMID 16729031
 
Physical interaction of apoptosis-inducing factor with DNA and RNA.
Vahsen N, Cand C, Dupaigne P, Giordanetto F, Kroemer RT, Herker E, Scholz S, Modjtahedi N, Madeo F, Le Cam E, Kroemer G
Oncogene. 2006 ; 25 (12) : 1763-1774.
PMID 16278674
 
Apoptosis-inducing factor mediates poly(ADP-ribose) (PAR) polymer-induced cell death.
Yu SW, Andrabi SA, Wang H, Kim NS, Poirier GG, Dawson TM, Dawson VL
Proceedings of the National Academy of Sciences of the United States of America. 2006 ; 103 (48) : 18314-18319.
PMID 17116881
 
AIF-mediated programmed necrosis: a highly regulated way to die.
Boujrad H, Gubkina O, Robert N, Krantic S, Susin SA
Cell cycle (Georgetown, Tex.). 2007 ; 6 (21) : 2612-2619.
PMID 17912035
 
Therapeutic potential of AIF-mediated caspase-independent programmed cell death.
Lorenzo HK, Susin SA
Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy. 2007 ; 10 (6) : 235-255.
PMID 18180198
 
Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis.
Moubarak RS, Yuste VJ, Artus C, Bouharrour A, Greer PA, Menissier-de Murcia J, Susin SA
Molecular and cellular biology. 2007 ; 27 (13) : 4844-4862.
PMID 17470554
 
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Contributor(s)

Written10-2007Victor J Yuste, Hans K Lorenzo, Santos A Susin
Cell Death, Senescence and Survival Research Group, Institut de Neurociencies, Universitat Autonoma de Barcelona (UAB), Edifici M, Campus de Bellaterra, 08193 Bellaterra (Cerdanyola del Valles), Spain (VJY); University of Paris XI, School of Medicine, Hospital Paul Brousse, INSERM U542, 14, av. Paul Vaillant Couturier, 94807 Villejuif, France (HKL); Apoptosis and Immune System, Institut Pasteur, URA 1961-CNRS, 25, rue du Dr. Roux, 75724 Paris Cedex 15, France (SAS)

Citation

This paper should be referenced as such :
Yuste, VJ ; Lorenzo, HK ; Susin, SA
AIFM1 (apoptosis-inducing factor, mitochondrion-associated, 1)
Atlas Genet Cytogenet Oncol Haematol. 2008;12(3):190-194.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/AIFM1ID44053chXq25.html

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indexed on : Sat Oct 4 12:53:33 CEST 2014

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