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

BCL2-associated athanogene 3

BAG3, CAIR-1
BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: bcl-2, HSP70, CAN, V1a, AGE
Papers using BAG3 antibodies
NBR1 is a new PB1 signalling adapter in Th2 differentiation and allergic airway inflammation in vivo
Supplier
Into Takeshi et al., In Cellular and Molecular Life Sciences, 2009
... Sources of antibodies used are: anti-TRIF rabbit polyclonal antibody (Alexis; AL227), anti-BAG3 rabbit polyclonal antibody (Abcam; ab86298), anti-BNIP3L (NIX) rabbit ...
Papers on BAG3
BAG3-mediated miRNA let-7g and let-7i inhibit proliferation and enhance apoptosis of human esophageal carcinoma cells by targeting the drug transporter ABCC10.
New
Zhao et al., Zhengzhou, China. In Cancer Lett, Mar 2016
qRT-PCR and western blot analysis demonstrated that Bcl2-associated athanogene 3 (BAG3) and miR-let-7g/i have the opposite expression levels in primary esophageal squamous cell carcinoma tissues and EC cell lines.
Gold-nanorods-siRNA nanoplex for improved photothermal therapy by gene silencing.
New
Li et al., Wuhan, China. In Biomaterials, Feb 2016
After surface modification, the GNRs show the ability to deliver siRNA oligos targeting BAG3 which is an efficient gene to block the heat-shock response.
Mutations in HSPB8 causing a new phenotype of distal myopathy and motor neuropathy.
New
Udd et al., Sydney, Australia. In Neurology, Jan 2016
However, we now demonstrate that patients can develop a myopathy with histologic features of myofibrillar myopathy with aggregates and rimmed vacuoles, similar to the pathology in myopathies due to gene defects in other compounds of the CASA complex such as BAG3 and DNAJB6 after developing the early neurogenic effects.
Autophagy-associated proteins BAG3 and p62 in testicular cancer.
New
Mani et al., Frankfurt am Main, Germany. In Oncol Rep, Jan 2016
Eighty-four patients were assessed for autophagy (BAG3, p62) and apoptosis (cleaved caspase 3) markers using immunohistochemistry (IHC) on tissue micro- arrays.
BAG3 regulates total MAP1LC3B protein levels through a translational but not transcriptional mechanism.
New
Lavandero et al., Mainz, Germany. In Autophagy, Jan 2016
The cochaperone of the HSP70 system BAG3 (BCL2-associated athanogene 3) has been associated to LC3B lipidation through an unknown mechanism.
BAG3 elevation inhibits cell proliferation via direct interaction with G6PD in hepatocellular carcinomas.
New
Wang et al., Shenyang, China. In Oncotarget, Dec 2015
UNASSIGNED: Bcl-2 associated athanogene 3 (BAG3) contains multiple protein-binding motifs to mediate potential interactions with chaperons and/or other proteins, which is possibly ascribed to the multifaceted functions assigned to BAG3.
BAG3 regulates cell proliferation, migration, and invasion in human colorectal cancer.
New
Xu et al., Jinan, China. In Tumour Biol, Dec 2015
UNASSIGNED: Bcl2-associated athanogene 3 (BAG3) has been reported to be elevated in various tumors.
BAG3-related myopathy, polyneuropathy and cardiomyopathy with long QT syndrome.
New
Rędowicz et al., Warsaw, Poland. In J Muscle Res Cell Motil, Dec 2015
UNASSIGNED: BAG3 belongs to BAG family of molecular chaperone regulators interacting with HSP70 and anti-apoptotic protein Bcl-2.
Mitochondrial abnormalities in the myofibrillar myopathies.
Review
New
Reichmann et al., Dresden, Germany. In Eur J Neurol, Nov 2015
Causative mutations have been identified in the genes MYOT, LDB3, DES, CRYAB, FLNC, BAG3, DNAJB6, FHL1, PLEC and TTN, which encode proteins which either reside in the Z-disc or associate with the Z-disc.
Myofibrillar myopathies: State of the art, present and future challenges.
Review
New
Eymard et al., Paris, France. In Rev Neurol (paris), Oct 2015
The boundaries of this concept are still uncertain, and whereas six genes (DES, CRYAB, LDB3/ZASP, MYOT, FLNC and BAG3) are now classically considered as responsible for MFM, other entities such as FHL1 myopathy or Hereditary Myopathy with Early Respiratory Failure linked to mutations of titin can now as well be included in this group.
BAG3: a new player in the heart failure paradigm.
Review
New
Feldman et al., Philadelphia, United States. In Heart Fail Rev, Jul 2015
BAG3 is a cellular protein that is expressed predominantly in skeletal and cardiac muscle but can also be found in the brain and in the peripheral nervous system.
Diagnosis of muscle diseases presenting with early respiratory failure.
Review
New
Chinnery et al., Newcastle upon Tyne, United Kingdom. In J Neurol, May 2015
Disorders which have recently had their genetic aetiologies identified include hereditary myopathy with early respiratory failure (due to TTN mutations), the FHL1-related syndromes, and myofibrillar myopathy due to BAG3 mutation.
Biomechanical characterization of myofibrillar myopathies.
Review
New
Goldmann et al., Erlangen, Germany. In Cell Biol Int, Apr 2015
Most MFMs are caused by mutations in genes encoding desmin, plectin, VCP, filamin C, BAG3, FHL-1, αB-crystallin, DNAJB6, myotilin, and ZASP.
BAG3 mutations: another cause of giant axonal neuropathy.
GeneRIF
Reilly et al., London, United Kingdom. In J Peripher Nerv Syst, 2012
This report confirms the association of giant axonal neuropathy with BAG3-associated myofibrillar myopathy
Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6 cause limb-girdle muscular dystrophy.
Impact
Udd et al., Helsinki, Finland. In Nat Genet, 2012
Further, we show that DNAJB6 interacts with members of the CASA complex, including the myofibrillar myopathy-causing protein BAG3.
NF-κB regulates protein quality control after heat stress through modulation of the BAG3-HspB8 complex.
GeneRIF
Kretz-Remy et al., Lyon, France. In J Cell Sci, 2012
findings show that during heat shock recovery NF-kappaB activates selective removal of misfolded or aggregated proteins by controlling expression of BAG3 and HSPB8 and by modulating the level of the BAG3-HspB8 complex
Involvement of JNK and NF-κB pathways in lipopolysaccharide (LPS)-induced BAG3 expression in human monocytic cells.
GeneRIF
Du et al., Shenyang, China. In Exp Cell Res, 2012
the data support that BAG3 is induced by LPS via JNK and NF-kappaB-dependent signals, and involved in monocytic cell-extracellular matrix interaction, suggesting that BAG3 may have a role in the host response to LPS stimulation
Bag3 promotes resistance to apoptosis through Bcl-2 family members in non-small cell lung cancer.
GeneRIF
Wang et al., Xi'an, China. In Oncol Rep, 2012
non-small cell lung cancer cells were protected from apoptosis through increasing Bag3 expression and consequently promoted the expression of Bcl-XL and Bcl-2.
BAG3 down-modulation reduces anaplastic thyroid tumor growth by enhancing proteasome-mediated degradation of BRAF protein.
GeneRIF
Turco et al., Napoli, Italy. In J Clin Endocrinol Metab, 2012
BAG3 protein sustains anaplastic thyroid tumor growth in vitro and in vivo. The underlying molecular mechanism appears to rely on BAG3 binding to BRAF, thus protecting it from proteasome-dependent degradation.
Systems analysis of protein modification and cellular responses induced by electrophile stress.
Review
Impact
Marnett et al., Nashville, United States. In Acc Chem Res, 2010
Among the genes induced by HSF1, Bcl-2- associated athanogene 3 (BAG3) is notable for its actions in promoting cell survival through stabilization of antiapoptotic Bcl-2 proteins, appearing to have a critical role in mediating cellular protection against electrophile-induced death.
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