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

Origin recognition complex, subunit 1

Origin Recognition Complex, Orc1, GPX3, extracellular glutathione peroxidase, Orc1p
The origin recognition complex (ORC) is a highly conserved six subunits protein complex essential for the initiation of the DNA replication in eukaryotic cells. Studies in yeast demonstrated that ORC binds specifically to origins of replication and serves as a platform for the assembly of additional initiation factors such as Cdc6 and Mcm proteins. The protein encoded by this gene is the largest subunit of the ORC complex. While other ORC subunits are stable throughout the cell cycle, the levels of this protein vary during the cell cycle, which has been shown to be controlled by ubiquitin-mediated proteolysis after initiation of DNA replication. This protein is found to be selectively phosphorylated during mitosis. It is also reported to interact with MYST histone acetyltransferase 2 (MyST2/HBO1), a protein involved in control of transcription silencing. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2010] (from NCBI)
Top mentioned proteins: gpx1, Ethanolaminephosphotransferase, CAN, Cdc6, ACID
Papers on Origin Recognition Complex
MMSET is dynamically regulated during cell-cycle progression and promotes normal DNA replication.
Lou et al., Rochester, United States. In Cell Cycle, Feb 2016
During mitosis and G1, the Origin Recognition Complex (ORC) binds to future replication origins, coordinating with multiple factors to load the minichromosome maintenance (MCM) complex onto future replication origins as part of the pre-replication complex (pre-RC).
Genetic polymorphisms that affect selenium status and response to selenium supplementation in United Kingdom pregnant women.
Rayman et al., Shenyang, China. In Am J Clin Nutr, Jan 2016
Selenium status was represented by the concentration of whole-blood selenium at 12 and 35 wk of gestation, the concentration of toenail selenium at 16 wk of gestation, and plasma glutathione peroxidase (GPx3) activity at 12 and 35 wk of gestation.
GPX1*Pro198Leu and GPX3 rs2070593 as genetic risk markers for Italian asthmatic patients.
Fuciarelli et al., Roma, Italy. In Clin Exp Pharmacol Physiol, Jan 2016
The GPX1*Pro198Leu (rs1050450) polymorphism and a GPX3 non-coding variant (rs2070593) were screened.
Mitochondrial transporters for ornithine and related amino acids: a review.
Palmieri et al., Bari, Italy. In Amino Acids, Sep 2015
The mitochondrial carriers ORC1, ORC2, and SLC25A29 from Homo sapiens, BAC1 and BAC2 from Arabidopsis thaliana, and Ort1p from Saccharomyces cerevisiae have been biochemically characterized by transport assays in liposomes.
Biomarkers of selenium status.
Combs, Grand Forks, United States. In Nutrients, Apr 2015
Some Se-biomarkers, such as the selenoproteins and particularly GPX3 and SEPP1, provide information about function directly and are of value in identifying nutritional Se deficiency and tracking responses of deficient individuals to Se-treatment.
Meier-Gorlin syndrome.
Bongers et al., Nijmegen, Netherlands. In Orphanet J Rare Dis, 2014
Mutations in one of five genes (ORC1, ORC4, ORC6, CDT1, and CDC6) of the pre-replication complex, involved in DNA-replication, are detected in approximately 67-78% of patients with MGS.
The hyperornithinemia-hyperammonemia-homocitrullinuria syndrome.
Dionisi-Vici et al., In Orphanet J Rare Dis, 2014
HHH syndrome is caused by impaired ornithine transport across the inner mitochondrial membrane due to mutations in SLC25A15 gene, which encodes for the mitochondrial ornithine carrier ORC1.
Significance of Polymorphisms and Expression of Enzyme-Encoding Genes Related to Glutathione in Hematopoietic Cancers and Solid Tumors.
Filip et al., Lublin, Poland. In Biomed Res Int, 2014
The changes in activity of GPX1, GPX2, and GPX3 isoforms may be associated with the development of cancers, for example, prostate cancer or even colon cancer.
Protective Effects of Red Guava on Inflammation and Oxidative Stress in Streptozotocin-Induced Diabetic Mice.
Chao et al., Taiwan. In Molecules, 2014
Furthermore, the expression of inflammatory proteins, such as iNOS and NF-κB, was suppressed via activated PPARγ, and the expression levels of GPx3 and ACO increased.
Diagnostic value of serum glutathione peroxidase 3 levels in patients with lung cancer.
Lee et al., Hwasun, South Korea. In Thorac Cancer, 2014
BACKGROUND: We selected glutathione peroxidase 3 (GPx3) as a specific candidate that is down regulated in patients with lung cancer.
Sterol-dependent nuclear import of ORP1S promotes LXR regulated trans-activation of apoE.
Michaely et al., Dallas, United States. In Exp Cell Res, 2012
ORP1S is a cytoplasmic sterol sensor, which transports sterols to the nucleus and promotes LXR regulated trans-activation of apoE.
Meier-Gorlin syndrome mutations disrupt an Orc1 CDK inhibitory domain and cause centrosome reduplication.
Stillman et al., New York City, United States. In Genes Dev, 2012
Orc1 harbors a PACT centrosome-targeting domain and a separate domain that differentially inhibits the protein kinase activities of Cyclin E-CDK2 and Cyclin A-CDK2
Epstein-Barr nuclear antigen 1 (EBNA1)-dependent recruitment of origin recognition complex (Orc) on oriP of Epstein-Barr virus with purified proteins: stimulation by Cdc6 through its direct interaction with EBNA1.
Masai et al., Tokyo, Japan. In J Biol Chem, 2012
Data show that purified Epstein-Barr nuclear antigen 1 EBNA1 recruits purified Human Orc1 and Cdc6 onto replication origin oriP.
p53-induced gene 3 mediates cell death induced by glutathione peroxidase 3.
Yu et al., Pittsburgh, United States. In J Biol Chem, 2012
a novel signaling pathway of GPx3-PIG3 in the regulation of cell death in prostate cancer.
A role for GPx3 in activity of normal and leukemia stem cells.
Sauvageau et al., Montréal, Canada. In J Exp Med, 2012
In human primary acute myeloid leukemia samples, GPX3 expression level directly correlated with adverse prognostic outcome and positively correlated with the frequency of leukemia stem cells (LSCs).
The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier-Gorlin syndrome.
Gozani et al., Stanford, United States. In Nature, 2012
results identify the BAH domain as a novel methyl-lysine-binding module, thereby establishing the first direct link between histone methylation and the metazoan DNA replication machinery, and defining a pivotal aetiological role for the canonical H4K20me2 mark, via ORC1, in primordial dwarfism
Mutations in the pre-replication complex cause Meier-Gorlin syndrome.
Jackson et al., Edinburgh, United Kingdom. In Nat Genet, 2011
We report here that individuals with this disorder show marked locus heterogeneity, and we identify mutations in five separate genes: ORC1, ORC4, ORC6, CDT1 and CDC6.
Mutations in ORC1, encoding the largest subunit of the origin recognition complex, cause microcephalic primordial dwarfism resembling Meier-Gorlin syndrome.
Jeggo et al., Edinburgh, United Kingdom. In Nat Genet, 2011
Mutations in ORC1, encoding a subunit of the origin recognition complex, cause microcephalic primordial dwarfism resembling Meier-Gorlin syndrome. These mutations disrupt ORC1 functions including pre-replicative complex formation and origin activation.
Mutations in origin recognition complex gene ORC4 cause Meier-Gorlin syndrome.
Samuels et al., Halifax, Canada. In Nat Genet, 2011
Using marker-assisted mapping in multiple families from a founder population and traditional coding exon sequencing of positional candidate genes, we identified three different mutations in the gene encoding ORC4, a component of the eukaryotic origin recognition complex, in five individuals with Meier-Gorlin syndrome.
Structural basis of DNA replication origin recognition by an ORC protein.
Wigley et al., Potters Bar, United Kingdom. In Science, 2007
We report the structure of an archaeal origin recognition complex protein, ORC1, bound to an origin recognition box, a DNA sequence that is found in multiple copies at replication origins.
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