About: Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor

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article by MARKUS LOEFFLER et al published March 2001 in FASEB Journal

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в березні 2001 (uk) im März 2001 veröffentlichter wissenschaftlicher Artikel (de) article scientifique publié en mars 2001 (fr) article by MARKUS LOEFFLER et al published March 2001 in FASEB Journal (en)
publication date	wds:Q57185203-CFE1F0FF-E3B5-4AAF-B191-83B8F1B6C20E
publication date	2001-03-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57185203-41D38564-9C29-4D7E-9F1B-0A4D8AAAE6E3
language of work or name	English
author name string	wds:Q57185203-12428C3C-02A7-44D6-84FB-8F4740F4F1EC wds:Q57185203-44E01B36-D4FC-42DF-9392-392476E4715B wds:Q57185203-9DC6F748-A4D4-4AFE-8ABF-C19686FAC908 wds:Q57185203-D32F11BE-3EAA-4F6A-B983-06AD3099A09C wds:Q57185203-DE08978A-3780-4453-BE11-A51AD6FCDFE0 wds:Q57185203-E0F66345-A3EE-4B22-8F3B-49E10E7367C1
author name string	JOSEF M. PENNINGER ANNA-LIISA NIEMINEN DIDIER MÉTIVIER GREG BROTHERS MARKUS LOEFFLER NAOUFAL ZAMZAMI
rdfs:label	Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor (en) Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor (nl)
skos:prefLabel	Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor (en) Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor (nl)
name	Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor (en) Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor (nl)
author	wds:Q57185203-8E7BE65D-D551-4EB5-8269-5A7A42F187B4 wds:Q57185203-A7D72E90-E847-4733-A6A6-014314122C85 wds:Q57185203-C1A80FFC-E7AD-42CC-9019-BBFBF0C2D41B
author	Guido Kroemer Santos A. Susin Eric Daugas
title	wds:Q57185203-AE4C9332-00A6-4748-94B6-D835CD98C76F
title	Dominant cell death induction by extramitochondrially targeted apoptosis-inducing factor (en)
page(s)	wds:Q57185203-D93D9EA1-6FE0-4926-937D-54C08C34B36C
page(s)	758-767
instance of	wds:Q57185203-B96541B3-CD90-40C2-B05E-4279480D68C6
instance of	scholarly article
main subject	wds:Q57185203-55AABCC9-5972-4318-A64E-1CAAEDD9CABA
main subject	apoptotic process
PubMed ID	wds:Q57185203-9BB620C7-76A6-46AA-A98C-5433FBC4BAAC
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11259394
PubMed ID	11259394
published in	wds:Q57185203-4D212C74-CF3A-4FAA-A219-1D70112F51B9
published in	FASEB Journal
issue	wds:Q57185203-AEB3542D-C2E1-45F9-9DB9-1088983C5816
volume	wds:Q57185203-7E760064-D1F5-464D-8F78-9915E5B28F04
issue	3
volume	15
DOI	wds:Q57185203-60B657E7-E610-42A1-AE9D-9F8D19154F0E
DOI	http://dx.doi.org/10.1096/FJ.00-0388COM
DOI	10.1096/FJ.00-0388COM
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57185203
is cites work of	AIF promotes chromatinolysis and caspase-independent programmed necrosis by interacting with histone H2AX Apoptosis-inducing factor: structure, function, and redox regulation Hypothesis for a common basis for neuroprotection in glaucoma and Alzheimer's disease: anti-apoptosis by alpha-2-adrenergic receptor activation Induction of apoptosis of tumor cells by some potentiated homeopathic drugs: implications on mechanism of action Life and death of lymphocytes: a role in immunesenescence Differential Regulation of Apoptosis in the Corpus Luteum of Pregnancy and Newly Formed Corpus Luteum after Parturition in Rats1 Mitochondria, the killer organelles and their weapons Mitochondria, AIF and caspases--rivaling for cell death execution. Different mitochondrial intermembrane space proteins are released during apoptosis in a manner that is coordinately initiated but can vary in duration AIF deficiency compromises oxidative phosphorylation Mild hypothermia attenuates cytochrome c release but does not alter Bcl-2 expression or caspase activation after experimental stroke Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space AIF and cyclophilin A cooperate in apoptosis-associated chromatinolysis Molecular cloning and characterization of a human AIF-like gene with ability to induce apoptosis Redox-dependent changes in molecular properties of mitochondrial apoptosis-inducing factor C. elegans mitochondrial factor WAH-1 promotes phosphatidylserine externalization in apoptotic cells through phospholipid scramblase SCRM-1. AMID, an apoptosis-inducing factor-homologous mitochondrion-associated protein, induces caspase-independent apoptosis The human apoptosis-inducing protein AMID is an oxidoreductase with a modified flavin cofactor and DNA binding activity AMID is a p53-inducible gene downregulated in tumors Regulation of AIF expression by p53. Targeting tumor-associated fibroblasts improves cancer chemotherapy by increasing intratumoral drug uptake Glutamate-induced apoptosis in neuronal cells is mediated via caspase-dependent and independent mechanisms involving calpain and caspase-3 proteases as well as apoptosis inducing factor (AIF) and this process is inhibited by equine estrogens Parthanatos, a messenger of death Quantitation of mitochondrial alterations associated with apoptosis Apoptosis-inducing factor is involved in the regulation of caspase-independent neuronal cell death Adenine nucleotide translocator mediates the mitochondrial membrane permeabilization induced by lonidamine, arsenite and CD437. The thioredoxin system in retroviral infection and apoptosis AIF suppresses chemical stress-induced apoptosis and maintains the transformed state of tumor cells Muscle-specific loss of apoptosis-inducing factor leads to mitochondrial dysfunction, skeletal muscle atrophy, and dilated cardiomyopathy Loss of apoptosis-inducing factor results in cell-type-specific neurogenesis defects Sequential involvement of Cdk1, mTOR and p53 in apoptosis induced by the HIV-1 envelope Tetraspanin CD37 directly mediates transduction of survival and apoptotic signals Human immunodeficiency virus 1 envelope glycoprotein complex-induced apoptosis involves mammalian target of rapamycin/FKBP12-rapamycin-associated protein-mediated p53 phosphorylation Apoptosis-inducing factor (AIF): a novel caspase-independent death effector released from mitochondria Artesunate overcomes drug resistance in multiple myeloma by inducing mitochondrial stress and non-caspase apoptosis Steroid receptor coactivator-interacting protein (SIP) inhibits caspase-independent apoptosis by preventing apoptosis-inducing factor (AIF) from being released from mitochondria Poly(ADP-ribose) signals to mitochondrial AIF: a key event in parthanatos T-cell ubiquitin ligand affects cell death through a functional interaction with apoptosis-inducing factor, a key factor of caspase-independent apoptosis Gossypol, a BH3 mimetic, induces apoptosis in chronic lymphocytic leukemia cells Heat-shock protein 70 antagonizes apoptosis-inducing factor Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor. Mitochondria as therapeutic targets for cancer chemotherapy Cell death modalities: classification and pathophysiological implications Cytotoxic phospholipid oxidation products. Cell death from mitochondrial damage and the intrinsic caspase cascade Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis

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