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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

BCL2-antagonist/killer 1

The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form oligomers or heterodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein localizes to mitochondria, and functions to induce apoptosis. It interacts with and accelerates the opening of the mitochondrial voltage-dependent anion channel, which leads to a loss in membrane potential and the release of cytochrome c. This protein also interacts with the tumor suppressor P53 after exposure to cell stress. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Bax, bcl-2, PrP, Bcl-xL, CAN
Papers using Bak antibodies
Combined Adjuvant Cisplating and Ifosfamide Chemotherapy and Radiotherapy for Malignant Mixed Mullerian Tumors of the Uterus
Diudea Dana et al., In World Journal of Surgical Oncology, 2005
... Bakpolyclonal1/20Dako ...
IKKβ programs to turn on the GADD45α–MKK4–JNK apoptotic cascade specifically via p50 NF-κB in arsenite response
Huang Chuanshu et al., In The Journal of Cell Biology, 2003
... IKKβ, phospho-JNK, JNK, phospho-MKK4, MKK4, phospho-MKK7, MKK7, phospho-c-Jun, c-Jun, caspase3, PARP, Bcl-2, Bcl-XL, Bax, and Bak were purchased from Cell Signaling Technology ...
Cytopathic effects of the cytomegalovirus-encoded apoptosis inhibitory protein vMIA
Kroemer Guido et al., In The Journal of Cell Biology, 1995
... To knock down Bax, Bak, or PiC expression, two siRNAs were used (hBax-384 for Bax1, hBax-208 for Bax2, hBak01-258 for Bak1, [Perfettini et al., 2004] Qiagen hp_Bak_1_5 for Bak2; and ...
Hydrodynamics-based transfection in animals by systemic administration of plasmid DNA
Wang HongYang et al., In Molecular Cancer, 1995
... The primary antibodies specific for Mcl-1 (S-19 and K-20), Bax (N-20) and Bak (N-20) were purchased from Santa Cruz Biotechnology.
Papers on Bak
Ethylene glycol ethers induce apoptosis and disturb glucose metabolism in the rat brain.
Budziszewska et al., Kraków, Poland. In Pharmacol Rep, Feb 2016
BE and PHE increased the level of pro-apoptotic proteins (Bax, Bak) and/or reduced the concentration of anti-apoptotic proteins (Bcl-2, Bcl-xL); whereas, the effect of BE was observed mainly in the cortex and that of PHE in the hippocampus.
Biological evaluation of 2-arylidene-4, 7-dimethyl indan-1-one (FXY-1): a novel Akt inhibitor with potent activity in lung cancer.
Chandramoorthy et al., Abhā, Saudi Arabia. In Cancer Chemother Pharmacol, Feb 2016
Western blot analysis revealed dephosphorylation of Akt (Ser 473) with activation of p53, Bax, Bak, Bid and reduction in Bcl-2 and Bcl-xL levels.
E6 Proteins from Low Risk Human Papillomavirus Types 6 and 11 are able to Protect Keratinocytes from Apoptosis via Bak Degradation.
Tyring et al., Houston, United States. In J Gen Virol, Feb 2016
Recent studies have shown the ability of the HPV E6 protein to degrade the proapoptotic family member, Bak, in high risk and genus beta HPV types, which confers a cytoprotective advantage on E6 expressing cells.
Lovastatin induces platelet apoptosis.
Dai et al., Suzhou, China. In Environ Toxicol Pharmacol, Feb 2016
In the current study, we show that lovastatin dose-dependently induces depolarization of mitochondrial inner transmembrane potential, leading to up-regulation of Bak, down-regulation of Bcl-XL, and activation of caspase-3/8/9.
The Deadly Landscape Of Pro-Apoptotic BCL-2 Proteins In the Outer Mitochondrial Membrane.
Chipuk et al., New York City, United States. In Febs J, Jan 2016
In this mini-review, we will provide a current overview of the BCL-2 family members and discuss the latest structural insights of BAK/BAX activation and oligomerization in the context of the OMM and mitochondrial biology.
Bcl-2 family proteins as regulators of cancer cell invasion and metastasis: a review focusing on mitochondrial respiration and reactive oxygen species.
Um, Seoul, South Korea. In Oncotarget, Dec 2015
Interestingly, cell invasion was recently found to be suppressed by multidomain pro-apoptotic members of the Bcl-2 family, such as Bax and Bak.
An interconnected hierarchical model of cell death regulation by the BCL-2 family.
Cheng et al., Kettering, United States. In Nat Cell Biol, Oct 2015
Multidomain pro-apoptotic BAX and BAK, once activated, permeabilize mitochondria to trigger apoptosis, whereas anti-apoptotic BCL-2 members preserve mitochondrial integrity.
Discoveries and controversies in BCL-2 protein-mediated apoptosis.
Moldoveanu et al., Memphis, United States. In Febs J, Oct 2015
Anti-apoptotic proteins, such as BCL-2 and BCL-xL, and the pro-apoptotic effectors of MOMP, including BAK and BAX, interact with pro-apoptotic BCL-2 homology 3 (BH3)-only proteins similarly.
Targeting BCL-2 to enhance vulnerability to therapy in estrogen receptor-positive breast cancer.
Lindeman et al., Australia. In Oncogene, Sep 2015
BCL-2 and other pro-survival family members including Mcl-1 and BCL-XL have been shown to have a key role in keeping pro-apoptotic 'effector' proteins BAK and BAX in check.
Regulated necrotic cell death: the passive aggressive side of Bax and Bak.
Molkentin et al., Cincinnati, United States. In Circ Res, Jun 2015
In apoptosis, the B-cell leukemia/lymphoma 2 (Bcl-2) family members Bcl-2-associated protein x (Bax) and Bcl-2 homologues antagonist/killer (Bak) undergo oligomerization in the outer mitochondrial membrane resulting in the release of apoptosis inducing substrates and the activation of caspases and nucleases.
Apoptotic caspases prevent the induction of type I interferons by mitochondrial DNA.
Flavell et al., New Haven, United States. In Cell, 2015
In the absence of active caspases, mitochondrial outer membrane permeabilization by Bax and Bak results in the expression of type I interferons (IFNs).
Antiapoptotic Mcl-1 is critical for the survival and niche-filling capacity of Foxp3⁺ regulatory T cells.
Liston et al., Leuven, Belgium. In Nat Immunol, 2013
By contrast, excess Treg cells are removed by attrition, dependent on the Bim-initiated Bak- and Bax-dependent intrinsic apoptotic pathway.
Epidermal growth factor regulates hematopoietic regeneration after radiation injury.
Chute et al., Durham, United States. In Nat Med, 2013
We identified epidermal growth factor (EGF) to be highly enriched in the bone marrow serum of mice bearing deletion of Bak and Bax in TIE2-expressing cells in Tie2Cre; Bak1(-/-); Bax(flox/-) mice.
Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis.
Colman et al., Melbourne, Australia. In Cell, 2013
In stressed cells, apoptosis ensues when Bcl-2 family members Bax or Bak oligomerize and permeabilize the mitochondrial outer membrane.
Denervation-induced mitochondrial dysfunction and autophagy in skeletal muscle of apoptosis-deficient animals.
Hood et al., Toronto, Canada. In Am J Physiol Cell Physiol, 2012
This study showed that denervation-induced muscle disuse activates both apoptotic and autophagic signaling pathways in muscle, and autophagic protein expression does not exhibit a compensatory increase in the presence of attenuated apoptosis.
Nigericin-induced impairment of autophagic flux in neuronal cells is inhibited by overexpression of Bak.
Oh et al., Seoul, South Korea. In J Biol Chem, 2012
Results indicate that a protective role for Bak during ionophore-induced cell death may be closely associated with its regulatory effect on maintenance of autophagic flux and vacuole homeostasis.
Autocrine TNF is critical for the survival of human dendritic cells by regulating BAK, BCL-2, and FLIPL.
Holter et al., Erlangen, Germany. In J Immunol, 2012
Dendritic cells (DC) stimulated by known inducers of DC apoptosis are characterized by high levels and activation of the proapoptotic protein BAK.
NMR solution structure of a photoswitchable apoptosis activating Bak peptide bound to Bcl-xL.
Allemann et al., Cardiff, United Kingdom. In J Am Chem Soc, 2012
The study reports the first NMR solution structure of a photoswitchable peptide derived from the proapoptotic protein BAK in complex with the antiapoptotic protein bcl-xL.
Charge profile analysis reveals that activation of pro-apoptotic regulators Bax and Bak relies on charge transfer mediated allosteric regulation.
Koča et al., Brno, Czech Republic. In Plos Comput Biol, 2011
Sequence and structural alignment revealed that a hub was conserved in the Bak amino acid sequence, and in the 3D structure of folded Bak.
Apoptosis and in vivo models to study the molecules related to this phenomenon.
Pantaleão et al., São Paulo, Brazil. In Einstein (sao Paulo), 2010
Antiapoptotic members of the Bcl-2 family (B cell CLL/lymphoma 2), that belong to the intrinsic route of the activation of caspases, such as Bcl-xL (extra-large B-cell lymphoma) and Bcl-w (Bcl-2-like 2), act predominantly to prevent that pro-apoptotic members, such as Bax (Bcl-2-associated X protein) and Bak (Bcl-2 relative bak) lead to cell death.
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