A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity

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A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity is …
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scholarly articleQ13442814

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P6179Dimensions Publication ID1028137195
P356DOI10.1038/SJ.ONC.1203948
P3181OpenCitations bibliographic resource ID2778080
P698PubMed publication ID11126360
P5875ResearchGate publication ID12203258

P2093author name stringY Eguchi
Y Tsujimoto
M Kinoshita
M Takeda
S Tagami
P2860cites workCloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activityQ28306175
Bcl-2 promotes regeneration of severed axons in mammalian CNSQ28504892
Caspases: enemies withinQ29547315
Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controlsQ29547730
Mitochondria and apoptosisQ29547905
The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosisQ29616513
The Bcl-2 protein family: arbiters of cell survivalQ29618158
Bcl-2 family: life-or-death switchQ33825160
Maintenance of calcium homeostasis in the endoplasmic reticulum by Bcl-2Q36254782
Mitochondrial control of nuclear apoptosis.Q36366491
Modulation of endoplasmic reticulum calcium pump by Bcl-2.Q41000205
Overexpression of Bcl-2 in a murine dopaminergic neuronal cell line leads to neurite outgrowthQ41240199
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Role of Bcl-2 family proteins in apoptosis: apoptosomes or mitochondria?Q55068261
Neuronal differentiation of PC12 cells as a result of prevention of cell death by bcl-2Q72393491
Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondriaQ22008484
Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDACQ22009974
Cloning of a novel member of the reticulon gene family (RTN3): gene structure and chromosomal localization to 11q13Q22010054
Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell deathQ22010927
Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-betaQ22011091
Identification of the Nogo inhibitor of axon regeneration as a Reticulon proteinQ22253157
Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome cQ24309066
Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascadeQ24311006
Evidence that BCL-2 represses apoptosis by regulating endoplasmic reticulum-associated Ca2+ fluxesQ24313314
Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blockedQ24318845
p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulumQ24318875
cDNA cloning, genomic organization, and expression of the human RTN2 gene, a member of a gene family encoding reticulonsQ24321375
Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3Q24324482
Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue KineticsQ24564912
Bcl-XL interacts with Apaf-1 and inhibits Apaf-1-dependent caspase-9 activationQ24644892
Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosisQ24669892
Nogo-A is a myelin-associated neurite outgrowth inhibitor and an antigen for monoclonal antibody IN-1Q28144424
Synergistic anti-apoptotic activity between Bcl-2 and SMN implicated in spinal muscular atrophyQ28255870
Caspase-9, Bcl-XL, and Apaf-1 form a ternary complexQ28263687
Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)Q28297419
P433issue50
P407language of work or nameEnglishQ1860
P921main subjectendoplasmic reticulumQ79927
apoptotic processQ14599311
regulation of apoptotic processQ14633911
Reticulon 4Q21106505
Reticulon 4Q21981429
P304page(s)5736-46
P577publication date2000-11-23
P1433published inOncogeneQ1568657
P1476titleA novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity
P478volume19