RAT:BAX

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Bax
Protein Name(s)	Apoptosis regulator BAX
External Links
UniProt	Q63690
EMBL	U49729 U59184 U32098 S76511
PIR	I53295
UniGene	Rn.10668 Rn.232358
ProteinModelPortal	Q63690
SMR	Q63690
BioGrid	246997
IntAct	Q63690
MINT	MINT-1541764
PaxDb	Q63690
PRIDE	Q63690
UCSC	RGD:2192
RGD	2192
eggNOG	NOG46695
HOGENOM	HOG000095178
HOVERGEN	HBG003606
InParanoid	Q63690
PhylomeDB	Q63690
NextBio	13955757
PRO	PR:Q63690
Proteomes	UP000002494
Genevestigator	Q63690
GO	GO:0097144 GO:0097136 GO:0005737 GO:0005829 GO:0005789 GO:0031966 GO:0005741 GO:0005757 GO:0005739 GO:0005634 GO:0046930 GO:0051400 GO:0051434 GO:0015267 GO:0051087 GO:0031072 GO:0008289 GO:0032403 GO:0046982 GO:0042803 GO:0006919 GO:0008635 GO:0008637 GO:0006915 GO:0097190 GO:0001783 GO:0007420 GO:0045333 GO:0010248 GO:0097192 GO:0034349 GO:0007007 GO:0097193 GO:0008630 GO:0070059 GO:0043653 GO:0008053 GO:0032091 GO:0007008 GO:0001541 GO:0043065 GO:1900103 GO:2001244 GO:0043525 GO:0032461 GO:0090200 GO:0051881 GO:0043496 GO:0001836 GO:0032976 GO:0042220 GO:0046688 GO:0051412 GO:0042493 GO:0009636 GO:1990009 GO:0006927
InterPro	IPR026304 IPR002475 IPR020717 IPR020726 IPR020728 IPR026298
PANTHER	PTHR11256 PTHR11256:SF8
Pfam	PF00452
PRINTS	PR01862
PROSITE	PS50062 PS01080 PS01258 PS01259

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0009408	response to heat	PMID:11090436^[1]	ECO:0000314			P	Fig. 3) A redistribution of Bax from the cytoplasm to the nuclear periphery was observed in rats that had been exposed once to short-term local testicular heating.	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:9804769^[2]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043525	positive regulation of neuron apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07813	P	Seeded From UniProt	complete
involved_in	GO:2001244	positive regulation of intrinsic apoptotic signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:1900103	positive regulation of endoplasmic reticulum unfolded protein response	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0097193	intrinsic apoptotic signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0097190	apoptotic signaling pathway	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
part_of	GO:0097144	BAX complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	C	Seeded From UniProt	complete
part_of	GO:0097136	Bcl-2 family protein complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	C	Seeded From UniProt	complete
involved_in	GO:0090200	positive regulation of release of cytochrome c from mitochondria	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0070059	intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0051881	regulation of mitochondrial membrane potential	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
enables	GO:0051434	BH3 domain binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	F	Seeded From UniProt	complete
part_of	GO:0046930	pore complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	C	Seeded From UniProt	complete
involved_in	GO:0043653	mitochondrial fragmentation involved in apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0043525	positive regulation of neuron apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0043496	regulation of protein homodimerization activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0032976	release of matrix enzymes from mitochondria	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0032461	positive regulation of protein oligomerization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0032091	negative regulation of protein binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
enables	GO:0015267	channel activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	F	Seeded From UniProt	complete
involved_in	GO:0010248	establishment or maintenance of transmembrane electrochemical gradient	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0009636	response to toxic substance	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0008637	apoptotic mitochondrial changes	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0008635	activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
enables	GO:0008289	lipid binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	F	Seeded From UniProt	complete
involved_in	GO:0008053	mitochondrial fusion	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
part_of	GO:0005789	endoplasmic reticulum membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	C	Seeded From UniProt	complete
part_of	GO:0005757	mitochondrial permeability transition pore complex	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	C	Seeded From UniProt	complete
involved_in	GO:0001783	B cell apoptotic process	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0051412	response to corticosterone	PMID:17562391^[3]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051400	BH domain binding	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:620717	F	Seeded From UniProt	complete
enables	GO:0051400	BH domain binding	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:620621	F	Seeded From UniProt	complete
enables	GO:0051400	BH domain binding	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:620525	F	Seeded From UniProt	complete
enables	GO:0051400	BH domain binding	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2200	F	Seeded From UniProt	complete
enables	GO:0051400	BH domain binding	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2199	F	Seeded From UniProt	complete
enables	GO:0051087	chaperone binding	PMID:12070120^[5]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:621314	F	Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:11299004^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:620717	F	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:620621	F	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:620525	F	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2200	F	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:9356461^[4]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2199	F	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:16579988^[7]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:621314	F	Seeded From UniProt	complete
involved_in	GO:0046688	response to copper ion	PMID:18289470^[8]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045333	cellular respiration	PMID:12460673^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:21561597^[10]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:1307794 RGD:628878	F	Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:20385067^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	PMID:17784886^[12]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0042220	response to cocaine	PMID:17084983^[13]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0034349	glial cell apoptotic process	PMID:18931364^[14]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0031966	mitochondrial membrane	PMID:16084019^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:16579988^[7]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:621314	F	Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:12070120^[5]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:621314	F	Seeded From UniProt	complete
involved_in	GO:0021987	cerebral cortex development	PMID:9813151^[16]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007568	aging	PMID:9813151^[16]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007420	brain development	PMID:18058945^[17]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007008	outer mitochondrial membrane organization	PMID:12460673^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007007	inner mitochondrial membrane organization	PMID:12460673^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:18817839^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:16084019^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:18959742^[19]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:11751624^[20]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16579988^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16084019^[15]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15902200^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	PMID:15044178^[22]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16579988^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:16321138^[23]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:15902200^[21]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:15341589^[24]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16321138^[23]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15341589^[24]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0001541	ovarian follicle development	PMID:17570453^[25]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0097192	extrinsic apoptotic signaling pathway in absence of ligand	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:101769 MGI:MGI:108052 MGI:MGI:1097161 MGI:MGI:88138 MGI:MGI:88139 MGI:MGI:99702 PANTHER:PTN000135648 UniProtKB:Q07820	P	Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88138 MGI:MGI:88139 MGI:MGI:99702 PANTHER:PTN000135648 RGD:2192 RGD:2199 RGD:2200 RGD:620525 RGD:620621 RGD:620717 RGD:621635 RGD:70984 UniProtKB:P10415 UniProtKB:Q07812 UniProtKB:Q07820 UniProtKB:Q16611 UniProtKB:Q92843 ZFIN:ZDB-GENE-000511-7 ZFIN:ZDB-GENE-030825-1 ZFIN:ZDB-GENE-051012-1	F	Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99702 PANTHER:PTN000883418 RGD:2192 UniProtKB:Q07812 ZFIN:ZDB-GENE-000511-6	P	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1330841 MGI:MGI:1858494 MGI:MGI:99702 PANTHER:PTN000135648 RGD:621635 UniProtKB:P10415 UniProtKB:Q07812 UniProtKB:Q16611	F	Seeded From UniProt	complete
enables	GO:0015267	channel activity	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000883418 UniProtKB:Q07812	F	Seeded From UniProt	complete
involved_in	GO:0008630	intrinsic apoptotic signaling pathway in response to DNA damage	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0029131 MGI:MGI:101769 MGI:MGI:1097161 MGI:MGI:88138 MGI:MGI:88139 MGI:MGI:99702 PANTHER:PTN000135648	P	Seeded From UniProt	complete
involved_in	GO:0008053	mitochondrial fusion	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99702 PANTHER:PTN000883418 UniProtKB:Q07812	P	Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:88139 MGI:MGI:99702 PANTHER:PTN000135648 RGD:2192 RGD:2200 UniProtKB:P10415 UniProtKB:Q07817 WB:WBGene00000423	C	Seeded From UniProt	complete
involved_in	GO:0001836	release of cytochrome c from mitochondria	PMID:21873635^[26]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:99702 PANTHER:PTN000883418 UniProtKB:Q07812	P	Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020717 InterPro:IPR020726 InterPro:IPR020728 InterPro:IPR026298 InterPro:IPR036834	P	Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR026304	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C	Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C	Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1000 UniProtKB-SubCell:SL-0172	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Yamamoto, CM et al. (2000) Redistribution of Bax is an early step in an apoptotic pathway leading to germ cell death in rats, triggered by mild testicular hyperthermia. Biol. Reprod. 63 1683-90 PubMed GONUTS page
↑ Hsu, SY & Hsueh, AJ (1998) A splicing variant of the Bcl-2 member Bok with a truncated BH3 domain induces apoptosis but does not dimerize with antiapoptotic Bcl-2 proteins in vitro. J. Biol. Chem. 273 30139-46 PubMed GONUTS page
↑ Yoshimura, A et al. (2007) Influence of age or circadian time on Bcl-2 and Bax mRNA expression in the rat hippocampus after corticosterone exposure. Brain Res. Bull. 73 254-8 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 ^4.9 Hsu, SY et al. (1997) Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members. Proc. Natl. Acad. Sci. U.S.A. 94 12401-6 PubMed GONUTS page
↑ ^5.0 ^5.1 Kirchhoff, SR et al. (2002) Cytosolic heat shock protein 60, apoptosis, and myocardial injury. Circulation 105 2899-904 PubMed GONUTS page
↑ Vis, JC et al. (2001) The mitochondrial toxin 3-nitropropionic acid induces differential expression patterns of apoptosis-related markers in rat striatum. Neuropathol. Appl. Neurobiol. 27 68-76 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Kim, HS et al. (2006) Heat shock protein 60 modified with O-linked N-acetylglucosamine is involved in pancreatic beta-cell death under hyperglycemic conditions. FEBS Lett. 580 2311-6 PubMed GONUTS page
↑ Li, YW et al. (2008) [Excessive copper induces hepatocyte apoptosis and affects Bax and Bcl-2 expression in rat liver]. Zhongguo Dang Dai Er Ke Za Zhi 10 42-6 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Appaix, F et al. (2002) Bax and heart mitochondria: uncoupling and inhibition of respiration without permeability transition. Biochim. Biophys. Acta 1556 155-67 PubMed GONUTS page
↑ Festa, M et al. (2011) BAG3 protein is overexpressed in human glioblastoma and is a potential target for therapy. Am. J. Pathol. 178 2504-12 PubMed GONUTS page
↑ Zhang, QL et al. () Bax gene silencing: a potential intervention in aluminum-induced neural cell death. J. Biol. Regul. Homeost. Agents 24 7-17 PubMed GONUTS page
↑ Yu, W et al. (2007) Angiotension II receptor 1 blocker modifies the expression of apoptosis-related proteins and transforming growth factor-beta1 in prostate tissue of spontaneously hypertensive rats. BJU Int. 100 1161-5 PubMed GONUTS page
↑ Dey, S et al. (2007) Cocaine exposure in vitro induces apoptosis in fetal locus coeruleus neurons by altering the Bax/Bcl-2 ratio and through caspase-3 apoptotic signaling. Neuroscience 144 509-21 PubMed GONUTS page
↑ Bhattacharjee, M et al. (2008) Bax and Bid act in synergy to bring about T11TS-mediated glioma apoptosis via the release of mitochondrial cytochrome c and subsequent caspase activation. Int. Immunol. 20 1489-505 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Lin, CH et al. (2005) Bax-regulated mitochondria-mediated apoptosis is responsible for the in vitro ischemia induced neuronal cell death of Sprague Dawley rat. Neurosci. Lett. 387 22-7 PubMed GONUTS page
↑ ^16.0 ^16.1 Shimohama, S et al. (1998) Differential expression of rat brain bcl-2 family proteins in development and aging. Biochem. Biophys. Res. Commun. 252 92-6 PubMed GONUTS page
↑ Soane, L et al. (2008) Postnatal developmental regulation of Bcl-2 family proteins in brain mitochondria. J. Neurosci. Res. 86 1267-76 PubMed GONUTS page
↑ Song, Y et al. (2008) p,p'-DDE induces mitochondria-mediated apoptosis of cultured rat Sertoli cells. Toxicology 253 53-61 PubMed GONUTS page
↑ Onoue, S et al. (2008) Pituitary adenylate cyclase-activating polypeptide attenuates streptozotocin-induced apoptotic death of RIN-m5F cells through regulation of Bcl-2 family protein mRNA expression. FEBS J. 275 5542-51 PubMed GONUTS page
↑ Van de Casteele, M et al. (2002) Specific expression of Bax-omega in pancreatic beta-cells is down-regulated by cytokines before the onset of apoptosis. Endocrinology 143 320-6 PubMed GONUTS page
↑ ^21.0 ^21.1 Birse-Archbold, JL et al. (2005) Differential profile of Nix upregulation and translocation during hypoxia/ischaemia in vivo versus in vitro. J. Cereb. Blood Flow Metab. 25 1356-65 PubMed GONUTS page
↑ Adachi, M et al. (2004) Bax interacts with the voltage-dependent anion channel and mediates ethanol-induced apoptosis in rat hepatocytes. Am. J. Physiol. Gastrointest. Liver Physiol. 287 G695-705 PubMed GONUTS page
↑ ^23.0 ^23.1 Capano, M & Crompton, M (2006) Bax translocates to mitochondria of heart cells during simulated ischaemia: involvement of AMP-activated and p38 mitogen-activated protein kinases. Biochem. J. 395 57-64 PubMed GONUTS page
↑ ^24.0 ^24.1 Hu, XL et al. (2004) Dynamic changes of the anti- and pro-apoptotic proteins Bcl-w, Bcl-2, and Bax with Smac/Diablo mitochondrial release after photothrombotic ring stroke in rats. Eur. J. Neurosci. 20 1177-88 PubMed GONUTS page
↑ Gürsoy, E et al. (2008) Expression and localisation of Bcl-2 and Bax proteins in developing rat ovary. Res. Vet. Sci. 84 56-61 PubMed GONUTS page
↑ ^26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 ^26.7 ^26.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:11090436-1] Yamamoto, CM et al. (2000) Redistribution of Bax is an early step in an apoptotic pathway leading to germ cell death in rats, triggered by mild testicular hyperthermia. Biol. Reprod. 63 1683-90 PubMed GONUTS page

[PMID:9804769-2] Hsu, SY & Hsueh, AJ (1998) A splicing variant of the Bcl-2 member Bok with a truncated BH3 domain induces apoptosis but does not dimerize with antiapoptotic Bcl-2 proteins in vitro. J. Biol. Chem. 273 30139-46 PubMed GONUTS page

[PMID:17562391-3] Yoshimura, A et al. (2007) Influence of age or circadian time on Bcl-2 and Bax mRNA expression in the rat hippocampus after corticosterone exposure. Brain Res. Bull. 73 254-8 PubMed GONUTS page

[PMID:9356461-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 ^4.9 Hsu, SY et al. (1997) Bok is a pro-apoptotic Bcl-2 protein with restricted expression in reproductive tissues and heterodimerizes with selective anti-apoptotic Bcl-2 family members. Proc. Natl. Acad. Sci. U.S.A. 94 12401-6 PubMed GONUTS page

[PMID:12070120-5] 5.0 ^5.1 Kirchhoff, SR et al. (2002) Cytosolic heat shock protein 60, apoptosis, and myocardial injury. Circulation 105 2899-904 PubMed GONUTS page

[PMID:11299004-6] Vis, JC et al. (2001) The mitochondrial toxin 3-nitropropionic acid induces differential expression patterns of apoptosis-related markers in rat striatum. Neuropathol. Appl. Neurobiol. 27 68-76 PubMed GONUTS page

[PMID:16579988-7] 7.0 ^7.1 ^7.2 ^7.3 Kim, HS et al. (2006) Heat shock protein 60 modified with O-linked N-acetylglucosamine is involved in pancreatic beta-cell death under hyperglycemic conditions. FEBS Lett. 580 2311-6 PubMed GONUTS page

[PMID:18289470-8] Li, YW et al. (2008) [Excessive copper induces hepatocyte apoptosis and affects Bax and Bcl-2 expression in rat liver]. Zhongguo Dang Dai Er Ke Za Zhi 10 42-6 PubMed GONUTS page

[PMID:12460673-9] 9.0 ^9.1 ^9.2 Appaix, F et al. (2002) Bax and heart mitochondria: uncoupling and inhibition of respiration without permeability transition. Biochim. Biophys. Acta 1556 155-67 PubMed GONUTS page

[PMID:21561597-10] Festa, M et al. (2011) BAG3 protein is overexpressed in human glioblastoma and is a potential target for therapy. Am. J. Pathol. 178 2504-12 PubMed GONUTS page

[PMID:20385067-11] Zhang, QL et al. () Bax gene silencing: a potential intervention in aluminum-induced neural cell death. J. Biol. Regul. Homeost. Agents 24 7-17 PubMed GONUTS page

[PMID:17784886-12] Yu, W et al. (2007) Angiotension II receptor 1 blocker modifies the expression of apoptosis-related proteins and transforming growth factor-beta1 in prostate tissue of spontaneously hypertensive rats. BJU Int. 100 1161-5 PubMed GONUTS page

[PMID:17084983-13] Dey, S et al. (2007) Cocaine exposure in vitro induces apoptosis in fetal locus coeruleus neurons by altering the Bax/Bcl-2 ratio and through caspase-3 apoptotic signaling. Neuroscience 144 509-21 PubMed GONUTS page

[PMID:18931364-14] Bhattacharjee, M et al. (2008) Bax and Bid act in synergy to bring about T11TS-mediated glioma apoptosis via the release of mitochondrial cytochrome c and subsequent caspase activation. Int. Immunol. 20 1489-505 PubMed GONUTS page

[PMID:16084019-15] 15.0 ^15.1 ^15.2 Lin, CH et al. (2005) Bax-regulated mitochondria-mediated apoptosis is responsible for the in vitro ischemia induced neuronal cell death of Sprague Dawley rat. Neurosci. Lett. 387 22-7 PubMed GONUTS page

[PMID:9813151-16] 16.0 ^16.1 Shimohama, S et al. (1998) Differential expression of rat brain bcl-2 family proteins in development and aging. Biochem. Biophys. Res. Commun. 252 92-6 PubMed GONUTS page

[PMID:18058945-17] Soane, L et al. (2008) Postnatal developmental regulation of Bcl-2 family proteins in brain mitochondria. J. Neurosci. Res. 86 1267-76 PubMed GONUTS page

[PMID:18817839-18] Song, Y et al. (2008) p,p'-DDE induces mitochondria-mediated apoptosis of cultured rat Sertoli cells. Toxicology 253 53-61 PubMed GONUTS page

[PMID:18959742-19] Onoue, S et al. (2008) Pituitary adenylate cyclase-activating polypeptide attenuates streptozotocin-induced apoptotic death of RIN-m5F cells through regulation of Bcl-2 family protein mRNA expression. FEBS J. 275 5542-51 PubMed GONUTS page

[PMID:11751624-20] Van de Casteele, M et al. (2002) Specific expression of Bax-omega in pancreatic beta-cells is down-regulated by cytokines before the onset of apoptosis. Endocrinology 143 320-6 PubMed GONUTS page

[PMID:15902200-21] 21.0 ^21.1 Birse-Archbold, JL et al. (2005) Differential profile of Nix upregulation and translocation during hypoxia/ischaemia in vivo versus in vitro. J. Cereb. Blood Flow Metab. 25 1356-65 PubMed GONUTS page

[PMID:15044178-22] Adachi, M et al. (2004) Bax interacts with the voltage-dependent anion channel and mediates ethanol-induced apoptosis in rat hepatocytes. Am. J. Physiol. Gastrointest. Liver Physiol. 287 G695-705 PubMed GONUTS page

[PMID:16321138-23] 23.0 ^23.1 Capano, M & Crompton, M (2006) Bax translocates to mitochondria of heart cells during simulated ischaemia: involvement of AMP-activated and p38 mitogen-activated protein kinases. Biochem. J. 395 57-64 PubMed GONUTS page

[PMID:15341589-24] 24.0 ^24.1 Hu, XL et al. (2004) Dynamic changes of the anti- and pro-apoptotic proteins Bcl-w, Bcl-2, and Bax with Smac/Diablo mitochondrial release after photothrombotic ring stroke in rats. Eur. J. Neurosci. 20 1177-88 PubMed GONUTS page

[PMID:17570453-25] Gürsoy, E et al. (2008) Expression and localisation of Bcl-2 and Bax proteins in developing rat ovary. Res. Vet. Sci. 84 56-61 PubMed GONUTS page

[PMID:21873635-26] 26.0 ^26.1 ^26.2 ^26.3 ^26.4 ^26.5 ^26.6 ^26.7 ^26.8 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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