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

RING1 and YY1 binding protein

Top mentioned proteins: Polycomb, ACID, YY1, RING finger protein, CAN
Papers on RYBP
Forced Activation of Notch in Macrophages Represses Tumor Growth by Upregulating miR-125a and Disabling Tumor-Associated Macrophages.
Qin et al., Key West, United States. In Cancer Res, Feb 2016
We also identified a positive feedback loop for miR-125a expression mediated by RYBP and YY1.
Role of Polycomb RYBP in Maintaining the B-1 to B-2 B-Cell Lineage Switch in Adult Hematopoiesis.
Vidal et al., Madrid, Spain. In Mol Cell Biol, Jan 2016
We have studied the hematopoietic activity of RYBP, a direct interactor and proposed modulator of RING1A/RING1B-dependent histone H2A monoubiquitylation (H2AUb).
RYBP predicts survival of patients with non-small cell lung cancer and regulates tumor cell growth and the response to chemotherapy.
Wang et al., Amarillo, United States. In Cancer Lett, Jan 2016
Ring1 and YY1 binding protein (RYBP) is a member of the Polycomb group (PcG) proteins and regulates cell growth through both PcG-dependent and -independent mechanisms.
Absence of Rybp Compromises Neural Differentiation of Embryonic Stem Cells.
Pirity et al., Szeged, Hungary. In Stem Cells Int, Dec 2015
Rybp (Ring1 and Yy1 Binding Protein) is a transcriptional regulator and member of the noncanonical polycomb repressive complex 1 with essential role in early embryonic development.
[Effect of RYBP Gene Silencing on Sensitivity of HL-60 Cells to Chemotherapeutic Drugs].
Lin et al., Guangzhou, China. In Zhongguo Shi Yan Xue Ye Xue Za Zhi, Dec 2015
OBJECTIVE: To investigate the effect of RYBP gene on sensitivity of HL-60 cells to chemotherapy drugs by using RNA interference.
Lack of Rybp in Mouse Embryonic Stem Cells Impairs Cardiac Differentiation.
Pirity et al., Gödöllő, Hungary. In Stem Cells Dev, Oct 2015
Ring1 and Yy1 binding protein (Rybp) has been implicated in transcriptional regulation, apoptotic signaling and as a member of the polycomb repressive complex 1, it has an important function in regulating pluripotency and differentiation of embryonic stem cells (ESCs).
Candidate early detection protein biomarkers for ER+/PR+ invasive ductal breast carcinoma identified using pre-clinical plasma from the WHI observational study.
Li et al., Seattle, United States. In Breast Cancer Res Treat, Sep 2015
Statistically significant differences (P < 0.05) in matched case versus control signals were observed for 39 candidates in both training and testing sets, and four markers (CSF2, RYBP, TFRC, ITGB4) remained significant after Bonferroni correction (P < 2.03 × 10(-5)).
The Role of Amino Acid Permeases and Tryptophan Biosynthesis in Cryptococcus neoformans Survival.
Pascon et al., Diadema, Brazil. In Plos One, 2014
We used bioinformatics to search for amino acid permeases in the C. neoformans and found eight potential global permeases (AAP1 to AAP8).
Profiling of ileal carcinoids.
Nilsson, Göteborg, Sweden. In Neuroendocrinology, 2012
Candidate genes for targeted therapy included ERBB2/HER2, DAD1, PRKCA, RYBP, CASP1, CASP4, CASP5, VMAT1, RET, APLP1, OR51E1, GPR112, SPOCK1, RUNX1, and MIR133A.
A novel target of microRNA-29, Ring1 and YY1-binding protein (Rybp), negatively regulates skeletal myogenesis.
Wang et al., Hong Kong, Hong Kong. In J Biol Chem, 2012
identify Rybp as a novel regulator of myogenesis that co-acts with YY1 to silence miR-29 and other myogenic loci.
RYBP represses endogenous retroviruses and preimplantation- and germ line-specific genes in mouse embryonic stem cells.
Vidal et al., Yokohama, Japan. In Mol Cell Biol, 2012
Rybp efficiently represses endogenous retroviruses (murine endogenous retrovirus [MuERV] class) and preimplantation (including zygotic genome activation stage)- and germ line-specific genes.
RYBP-PRC1 complexes mediate H2A ubiquitylation at polycomb target sites independently of PRC2 and H3K27me3.
Brockdorff et al., Oxford, United Kingdom. In Cell, 2012
RYBP-PRC1 is recruited to target loci in mESCs and is also involved in Xist RNA-mediated silencing, the latter suggesting a wider role in Polycomb silencing.
Integrative genomic profiling of human prostate cancer.
Gerald et al., New York City, United States. In Cancer Cell, 2010
Additionally, the androgen-driven TMPRSS2-ERG fusion was associated with a previously unrecognized, prostate-specific deletion at chromosome 3p14 that implicates FOXP1, RYBP, and SHQ1 as potential cooperative tumor suppressors.
A region of the human HOXD cluster that confers polycomb-group responsiveness.
Kingston et al., Boston, United States. In Cell, 2010
Furthermore, repression was dependent on the PcG proteins BMI1 and EED and a YY1-interacting partner, RYBP.
F1-dependent translation of mitochondrially encoded Atp6p and Atp8p subunits of yeast ATP synthase.
Tzagoloff et al., New York City, United States. In Proc Natl Acad Sci U S A, 2009
These results establish a mechanism by which expression of ATP6 and ATP8 is translationally regulated by F(1) to achieve a balanced output of two compartmentally separated sets of ATP synthase genes.
AAP1 regulates import of amino acids into developing Arabidopsis embryos.
Tegeder et al., Pullman, United States. In Plant J, 2009
AAP1 is important for amino acid import into the embryo for storage protein accumulation and seed yield.
Apoptin: therapeutic potential of an early sensor of carcinogenic transformation.
Noteborn et al., Leiden, Netherlands. In Annu Rev Pharmacol Toxicol, 2007
Apoptin targets include DEDAF, Nur77, Nmi, Hippi, and the potential drug target APC1.
Apoptin acts as a tumor-specific killer: potentials for an anti-tumor therapy.
Noteborn, Leiden, Netherlands. In Cell Mol Biol (noisy-le-grand), 2004
Apoptin interacts with various partners of the human proteome such as DEDAF, which when overexpressed induces apoptosis in various human tumor cell lines but not in primary human cells, similar to Apoptin.
The viral death effector Apoptin reveals tumor-specific processes.
Noteborn et al., Leiden, Netherlands. In Apoptosis, 2004
Finally, Apoptin interacts with various partners of the human proteome including DEDAF, Nmi and Hippi, which may help to regulate either Apoptin's activation or execution processes.
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