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

Neighbor of BRCA1 gene 1

NBR1, neighbor of BRCA1 gene 1, 1A1-3B
The protein encoded by this gene was originally identified as an ovarian tumor antigen monitored in ovarian cancer. The encoded protein contains a B-box/coiled coil motif, which is present in many genes with transformation potential, but the function of this protein is unknown. This gene is located on a region of chromosome 17q21.1 that is in close proximity to tumor suppressor gene BRCA1. Three alternatively spliced variants encoding the same protein have been identified for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, Iris, LC3, CAN, PB1
Papers using NBR1 antibodies
NBR1 is a new PB1 signalling adapter in Th2 differentiation and allergic airway inflammation in vivo
Into Takeshi et al., In Cellular and Molecular Life Sciences, 2009
... 05-1308), anti-Lys48-linked polyUb rabbit monoclonal antibody Apu2 (Millipore; 05-1307), FK2 anti-polyUb antibody (Nippon Biotest; MFK-004), anti-NBR1 rabbit polyclonal antibody (Cell Signaling Technology; 5202), anti-GFP rabbit ...
Papers on NBR1
A selective autophagy pathway takes an unconventional route.
Du et al., Beijing, China. In Autophagy, Nov 2015
In our recent work, we found that fission yeast Nbr1, a homolog of the mammalian macroautophagy receptor NBR1, acts together with an unconventional autophagy-associated cargo sequestration apparatus, the endosomal sorting complexes required for transport (ESCRTs), to deliver 2 hydrolytic enzymes from the cytosol to the vacuole lumen.
Nbr1, a Receptor for ESCRT-Dependent Endosomal Microautophagy in Fission Yeast.
Mizushima, Tokyo, Japan. In Mol Cell, Oct 2015
(2015) report that fission yeast Nbr1, sharing a partial homology to the mammalian macroautophagy receptor NBR1, acts as a receptor for ESCRT-dependent endosomal microautophagy that delivers two hydrolytic enzymes from the cytosol to the vacuole.
ESCRTs Cooperate with a Selective Autophagy Receptor to Mediate Vacuolar Targeting of Soluble Cargos.
Du et al., Beijing, China. In Mol Cell, Oct 2015
Here, we show that fission yeast Nbr1, a homolog of mammalian autophagy receptor NBR1, interacts with and facilitates the transport of two cytosolic hydrolases into vacuoles, in a way reminiscent of the budding yeast cytoplasm-to-vacuole targeting (Cvt) pathway, a prototype of selective autophagy.
The receptor proteins: pivotal roles in selective autophagy.
Cao et al., Changsha, China. In Acta Biochim Biophys Sin (shanghai), Aug 2015
The discovery and characterization of autophagic adapters, such as p62/Sequestosome 1 (SQSTM1) and Neighbor of BRCA1 gene 1 (NBR1), have provided mechanistic insights into selective autophagy.
Identification of a lung cancer cell line deficient in atg7-dependent autophagy.
D'Amore et al., Cambridge, United States. In Autophagy, Jul 2015
In addition, parental H1650 cells that lacked ATG7 were still able to consume autophagy substrates SQSTM1, NBR1 and TAX1BP1 via a bafilomycin A1-sensitive pathway, suggesting that these proteins were not exclusively degraded by autophagy.
Emerging themes in bacterial autophagy.
Girardin et al., Toronto, Canada. In Curr Opin Microbiol, Feb 2015
We review the importance of bacterial targeting by ubiquitination, diacylglycerol (DAG) or proteins such as Nod1, Nod2, NDP52, p62, NBR1, optineurin, LRSAM1 and parkin in the process of xenophagy.
The GST-BHMT assay reveals a distinct mechanism underlying proteasome inhibition-induced macroautophagy in mammalian cells.
Zhang et al., In Autophagy, 2014
However, mechanistically this proteasome inhibition-induced autophagy is different from that induced by starvation as it does not rely on regulation by MTOR (mechanistic target of rapamycin [serine/threonine kinase]) and PRKAA/AMPK (protein kinase, AMP-activated, α catalytic subunit), the upstream central sensors of cellular nutrition and energy status, but requires the presence of the cargo receptors SQSTM1/p62 (sequestosome 1) and NBR1 (neighbor of BRCA1 gene 1) that are normally involved in the selective autophagy pathway.
Induction of Ankrd1 in Dilated Cardiomyopathy Correlates with the Heart Failure Progression.
Labeit et al., Mannheim, Germany. In Biomed Res Int, 2014
Expression patterns of 8 mechanoptotic machinery-associated titin ligands (ANKRD1, ANKRD2, TRIM63, TRIM55, NBR1, MLP, FHL2, and TCAP) were quantitated in endomyocardial biopsies from 25 patients with advanced IDCM.
NBR1 is dispensable for PARK2-mediated mitophagy regardless of the presence or absence of SQSTM1.
Luo et al., Vancouver, Canada. In Cell Death Dis, 2014
Here we investigated whether NBR1, a functional homolog of SQSTM1, has a role in PARK2-mediated mitophagy, either alone or as a compensatory mechanism.
A macrophage NBR1-MEKK3 complex triggers JNK-mediated adipose tissue inflammation in obesity.
Moscat et al., Los Angeles, United States. In Cell Metab, 2014
Here we report that the levels of the PB1 domain-containing adaptor NBR1 correlated with the expression of proinflammatory molecules in adipose tissue from human patients with metabolic syndrome, suggesting that NBR1 plays a key role in adipose-tissue inflammation.
The role of the selective adaptor p62 and ubiquitin-like proteins in autophagy.
Lőw et al., Budapest, Hungary. In Biomed Res Int, 2013
Selective substrates of autophagy include damaged mitochondria, intracellular pathogens, and even a subset of cytosolic proteins with the help of ubiquitin-binding autophagic adaptors, such as p62/SQSTM1, NBR1, NDP52, and Optineurin.
What to eat: evidence for selective autophagy in plants.
Bassham et al., Ames, United States. In J Integr Plant Biol, 2012
The degradation of protein aggregates was the first selective autophagy described in plants, and, more recently, a hybrid protein of the mammalian selective autophagy adaptors p62 and NBR1, which interacts with the autophagy machinery and may function in autophagy of protein aggregates, was described in plants.
Autophagy-related proteins (p62, NBR1 and LC3) in intranuclear inclusions in neurodegenerative diseases.
Wakabayashi et al., Hirosaki, Japan. In Neurosci Lett, 2012
Autophagy-related NBR1 protein is not involved in the formation/degradation of neuronal intranuclear inclusions in neurodegenerative diseases.
Breast and ovarian cancer risk and risk reduction in Jewish BRCA1/2 mutation carriers.
Rebbeck et al., Philadelphia, United States. In J Clin Oncol, 2012
Breast and ovarian cancer risk are high in Jewish women with BRCA1 genetic mutation.
The atypical PKCs in inflammation: NF-κB and beyond.
Moscat et al., Los Angeles, United States. In Immunol Rev, 2012
This observation is of relevance in T cells, where p62, PKCζ, PKCλ/ι, and NBR1 establish a mesh of interactions that culminate in the regulation of T-cell effector responses through the modulation of T-cell polarity.
Midbody accumulation through evasion of autophagy contributes to cellular reprogramming and tumorigenicity.
Doxsey et al., Worcester, United States. In Nat Cell Biol, 2011
MB(d) loss accompanies stem-cell differentiation, and involves autophagic degradation mediated by binding of the autophagic receptor NBR1 to the midbody protein CEP55.
Plant NBR1 is a selective autophagy substrate and a functional hybrid of the mammalian autophagic adapters NBR1 and p62/SQSTM1.
Johansen et al., Tromsø, Norway. In Autophagy, 2011
AtNBR1 is more similar to mammalian NBR1 than to p62 in domain architecture and amino acid sequence.
Characterization of the interaction of GABARAPL-1 with the LIR motif of NBR1.
Dötsch et al., Frankfurt am Main, Germany. In J Mol Biol, 2011
Results indicate that the presence of a tryptophan residue in the LIR motif increases the binding affinity of GABARAPL-1/NBR1-LIR complex.
Developmental regulation of MURF ubiquitin ligases and autophagy proteins nbr1, p62/SQSTM1 and LC3 during cardiac myofibril assembly and turnover.
Gautel et al., London, United Kingdom. In Dev Biol, 2011
MURF2 expression parallels that of the autophagy-associated proteins LC3, p62/SQSTM1 and nbr1
The kinase domain of titin controls muscle gene expression and protein turnover.
Gautel et al., London, United Kingdom. In Science, 2005
We identified a signaling complex where TK interacts with the zinc-finger protein nbr1 through a mechanically inducible conformation.
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