About: Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations

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About: Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations Goto Sponge NotDistinct Permalink

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rdf:type	Item
description	1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած (hyw) artículu científicu espublizáu en 1998 (ast) наукова стаття, опублікована у квітні 1998 (uk) 1998 թվականի ապրիլին հրատարակված գիտական հոդված (hy) vědecký článek publikovaný v roce 1998 (cs) vedecký článok (publikovaný 1998/04/24) (sk) научни чланак (објављен 1998/04/24) (sr) مقالة علمية (نشرت في 24-4-1998) (ar) wetenschappelijk artikel (gepubliceerd op 1998/04/24) (nl) article publié dans la revue scientifique Journal of Biological Chemistry (fr) scientific journal article (en) im April 1998 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28506809-7574F428-A491-4E57-91A1-3E013772024A
publication date	1998-04-24 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28506809-11A3D30C-837E-4006-A057-EF9AA6A5F1E2
language of work or name	English
cites work	wds:Q28506809-FD42D332-D432-4D8B-AE0F-92283C683584
cites work	Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
author name string	wds:Q28506809-7F82C84A-5AC9-4F6B-B771-450AEF6A456B wds:Q28506809-F7B36377-1C14-4F35-8A4E-4553169077EC
OpenCitations bibliographic resource ID	wds:Q28506809-F55648B7-FE3D-4182-A414-C00C2E02A5C7
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/3558122
author name string	R. J. Youle Y. T. Hsu
OpenCitations bibliographic resource ID	3558122
rdfs:label	Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (en) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (nl) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (ast)
skos:prefLabel	Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (en) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (nl) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (ast)
name	Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (en) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (nl) Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (ast)
title	wds:Q28506809-3EB31149-6995-4232-B5F3-E23C327DF56D
title	Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations (en)
page(s)	wds:Q28506809-4A5140F6-7CC1-4942-9FEE-FAD72F1AE36B
page(s)	10777–10783
instance of	wds:Q28506809-768551A7-962C-4053-9415-660187C5B3AA
instance of	scholarly article
main subject	wds:Q28506809-433D78AB-765D-4F8A-945D-524B52CB226F
main subject	wd:Q14905404
PubMed ID	wds:Q28506809-AD49C9EC-29F7-4A89-9A4E-D36F3EAE961D
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/9553144
PubMed ID	9553144
published in	wds:Q28506809-85ABB27C-4E4F-4E51-ADD2-5A9FF699AEBD
published in	Journal of Biological Chemistry
issue	wds:Q28506809-63EAE339-BC14-4AE8-8488-52087DEB421F
volume	wds:Q28506809-07D9ECCD-B5ED-4BC5-9B3D-4351541CFDED
issue	17
volume	273
DOI	wds:Q28506809-D53420E5-6E2A-4585-864A-472123266B1F
DOI	http://dx.doi.org/10.1074/JBC.273.17.10777
DOI	10.1074/JBC.273.17.10777
ResearchGate publication ID	wds:Q28506809-A701667D-B77D-4922-8699-F4FDDE41203D
ResearchGate publication ID	51341815
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28506809
is cites work of	Fas-mediated apoptosis is regulated by the extracellular matrix protein CCN1 (CYR61) in vitro and in vivo Prolyl hydroxylase 3 interacts with Bcl-2 to regulate doxorubicin-induced apoptosis in H9c2 cells IBRDC2, an IBR-type E3 ubiquitin ligase, is a regulatory factor for Bax and apoptosis activation Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis Conserved residues of human XPG protein important for nuclease activity and function in nucleotide excision repair An oncogenic tyrosine kinase inhibits DNA repair and DNA-damage-induced Bcl-xL deamidation in T cell transformation Notch-activated signaling cascade interacts with mitochondrial remodeling proteins to regulate cell survival Bid: a Bax-like BH3 protein. Differential regulation of Bax and Bak by anti-apoptotic Bcl-2 family proteins Bcl-B and Mcl-1. NF-kappaB1 and c-Rel cooperate to promote the survival of TLR4-activated B cells by neutralizing Bim via distinct mechanisms Insig2 is associated with colon tumorigenesis and inhibits Bax-mediated apoptosis Treatment with a BH3 mimetic overcomes the resistance of latency III EBV (+) cells to p53-mediated apoptosis Calphostin C-mediated translocation and integration of Bax into mitochondria induces cytochrome c release before mitochondrial dysfunction. Inhibition of Bax protects neuronal cells from oligomeric Aβ neurotoxicity Protein kinase C-epsilon protects MCF-7 cells from TNF-mediated cell death by inhibiting Bax translocation Protein kinase Cepsilon interacts with Bax and promotes survival of human prostate cancer cells Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane Ku70 suppresses the apoptotic translocation of Bax to mitochondria. E1B 19K blocks Bax oligomerization and tumor necrosis factor alpha-mediated apoptosis How vaccinia virus has evolved to subvert the host immune response. MAP-1, a novel proapoptotic protein containing a BH3-like motif that associates with Bax through its Bcl-2 homology domains Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosis Spatial and temporal changes in Bax subcellular localization during anoikis Activation of pro-death Bcl-2 family proteins and mitochondria apoptosis pathway in tumor necrosis factor-alpha-induced liver injury Tissue transglutaminase is a multifunctional BH3-only protein p73 Induces apoptosis via PUMA transactivation and Bax mitochondrial translocation Inhibition of Bid-induced apoptosis by Bcl-2. tBid insertion, Bax translocation, and Bax/Bak oligomerization suppressed Conformational control of Bax localization and apoptotic activity by Pro168. The protein kinase PKB/Akt regulates cell survival and apoptosis by inhibiting Bax conformational change Conformational change and mitochondrial translocation of Bax accompany proteasome inhibitor-induced apoptosis of chronic lymphocytic leukemic cells. BAX unleashed: the biochemical transformation of an inactive cytosolic monomer into a toxic mitochondrial pore Bcl-2 and Bax mammalian regulators of apoptosis are functional in Drosophila. The Bcl2 family: regulators of the cellular life-or-death switch Activation of ERK1/2 protects melanoma cells from TRAIL-induced apoptosis by inhibiting Smac/DIABLO release from mitochondria Bcl-x(L) sequesters its C-terminal membrane anchor in soluble, cytosolic homodimers Quantitation of mitochondrial dynamics by photolabeling of individual organelles shows that mitochondrial fusion is blocked during the Bax activation phase of apoptosis Structure of Bax: coregulation of dimer formation and intracellular localization Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations Embedded together: the life and death consequences of interaction of the Bcl-2 family with membranes Bcl-x(L) retrotranslocates Bax from the mitochondria into the cytosol Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis

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