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

HCR1 Hcr1p

eIF3j, HCR1, Hcr1p
Eukaryotic initiation factor-3 (EIF3) has a molecular mass of about 600 kD and contains 13 nonidentical protein subunits, including EIF3J. EIF3 plays a central role in binding of initiator methionyl-tRNA and mRNA to the 40S ribosomal subunit to form the 40S initiation complex (Fraser et al., 2004 [PubMed 14688252]; Fraser et al., 2007 [PubMed 17588516]).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: PRT1, 110-kDa, CAN, eIF3g, eIF5
Papers using eIF3j antibodies
Influence of Ionic Strength, pH, and Chelation of Divalent Metals on Isolation of Polyribosomes from Tobacco Leaves.
Renne Rolf, In PLoS Pathogens, 1975
... 10e10 anti-PABPC (1∶2000, Santa Cruz Biotechnology), rabbit polyclonal anti-eIF2α (1∶1000, Cell Signaling) or rabbit polyclonal anti-eIF3j (1∶1000, Cell Signaling).
Papers on eIF3j
Protein kinase CK2 potentiates translation efficiency by phosphorylating eIF3j at Ser127.
Donella-Deana et al., Padova, Italy. In Biochim Biophys Acta, Jul 2015
Mammalian eIF3 consists of 13 subunits, including the loosely associated eIF3j subunit that plays a stabilizing role in the eIF3 complex formation and interaction with the 40S ribosomal subunit.
Structure of a yeast 40S-eIF1-eIF1A-eIF3-eIF3j initiation complex.
Ban et al., Zürich, Switzerland. In Nat Struct Mol Biol, Mar 2015
Our structure highlights differences in initiation-complex binding to the ribosome compared to that of mammalian eIF3, demonstrates a direct contact between eIF3j and eIF1A and reveals the network of interactions between eIF3 subunits.
Human eukaryotic initiation factor 2 (eIF2)-GTP-Met-tRNAi ternary complex and eIF3 stabilize the 43 S preinitiation complex.
Fraser et al., Davis, United States. In J Biol Chem, 2014
We have reconstituted the human 43 S PIC and used fluorescence anisotropy to systematically measure the affinity of eIF1, eIF1A, and eIF3j in the presence of different combinations of 43 S PIC components.
Functional and biochemical characterization of human eukaryotic translation initiation factor 3 in living cells.
Valášek et al., Praha, Czech Republic. In Mol Cell Biol, 2014
We knocked down expression of the PCI domain-containing eIF3c and eIF3a subunits and of eIF3j in human HeLa and HEK293 cells and analyzed the functional consequences.
The translation initiation complex eIF3 in trypanosomatids and other pathogenic excavates--identification of conserved and divergent features based on orthologue analysis.
de Melo Neto et al., Recife, Brazil. In Bmc Genomics, 2013
The biochemical data indicates a lack of association of the eIF3j subunit to the complex whilst highlighting the strong interaction between eIF3 and eIF1.
Translation initiation factors eIF3 and HCR1 control translation termination and stop codon read-through in yeast cells.
Valášek et al., Praha, Czech Republic. In Plos Genet, 2013
Here, we uncover roles for HCR1 and eIF3 in translation termination in vivo.
Spectrin domain of eukaryotic initiation factor 3a is the docking site for formation of the a:b:i:g subcomplex.
Zhang et al., Indianapolis, United States. In J Biol Chem, 2013
The binding of eIF3b to the spectrin domain of eIF3a occurs in its RNA recognition motif domain where eIF3j also binds in a mutually exclusive manner.
Prognostic factors and outcomes of unrelated bone marrow transplantation for Philadelphia chromosome positive acute lymphoblastic leukemia (Ph+ALL) pre-treated with tyrosine kinase inhibitors.
Hino et al., Ōsaka, Japan. In Osaka City Med J, 2013
Univariate analysis revealed that first hematological complete remission (HCR1) and MCR at transplant were significantly related to better OS and LFS.
Human-like eukaryotic translation initiation factor 3 from Neurospora crassa.
Cate et al., Berkeley, United States. In Plos One, 2012
N. crassa eIF3 forms a stable 12-subunit complex linked genetically and biochemically to the 13(th) subunit, eIF3j, which in humans modulates mRNA start codon selection.
Eukaryotic translation initiation factor 3, subunit a, regulates the extracellular signal-regulated kinase pathway.
Kolch et al., Glasgow, United Kingdom. In Mol Cell Biol, 2012
Beta-Arrestin 2 modulates binding of eIF-3-alpha to selected components of the extracellular signal-regulated kinase pathway.
Components of the multifactor complex needed for internal initiation by the IRES of hepatitis C virus in Saccharomyces cerevisiae.
Racaniello et al., New York City, United States. In Rna Biol, 2010
Internal initiation dependent upon the HCV IRES was abrogated in strains lacking eIF5B, and reduced in strains with altered eIF3, either lacking the Hcr1p subunit, a component of eIF3 not previously known to interact with HCV RNA, or possessing an amino acid change in the Rpg1p subunit.
The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons.
Hinnebusch et al., Bethesda, United States. In Mol Cell Biol, 2010
Data suggest that the eIF3b-eIF3j/eIF3a module binds near the mRNA entry channel and regulates the transition between scanning-conducive and initiation-competent conformations of the preinitiation complex.
The indispensable N-terminal half of eIF3j/HCR1 cooperates with its structurally conserved binding partner eIF3b/PRT1-RRM and with eIF1A in stringent AUG selection.
Valásek et al., Cambridge, United Kingdom. In J Mol Biol, 2010
a conserved tryptophan residue in the human eIF3j N-terminal acidic motif (NTA) is held in the helix alpha1 and loop 5 hydrophobic pocket of the human eIF3b RNA recognition motif (RRM)
The iron-sulphur protein RNase L inhibitor functions in translation termination.
Krebber et al., Göttingen, Germany. In Embo Rep, 2010
although the Fe-S cluster is not required for the interaction of Rli1 with eRF1 or its other interacting partner, Hcr1, from the initiation complex eIF3, it is required for its activity in translation termination
Crystal structure of the RNA recognition motif of yeast translation initiation factor eIF3b reveals differences to human eIF3b.
Ficner et al., Göttingen, Germany. In Plos One, 2009
It harbors an RNA Recognition Motif (RRM), which is shown to be a non-canonical RRM in human as it is not capable to interact with oligonucleotides, but rather interacts with eIF3j, a sub-stoichiometric subunit of eIF3.
Human initiation factor eIF3 subunit b interacts with HCV IRES RNA through its N-terminal RNA recognition motif.
Baudin et al., Grenoble, France. In Febs Lett, 2009
Because eIF3b was previously shown to be involved in eIF3j binding, biological implications are discussed.
Recycling of eukaryotic posttermination ribosomal complexes.
Pestova et al., United States. In Cell, 2007
We investigated eukaryotic recycling using post-TCs assembled on a model mRNA encoding a tetrapeptide followed by a UAA stop codon and report that initiation factors eIF3, eIF1, eIF1A, and eIF3j, a loosely associated subunit of eIF3, can promote recycling of eukaryotic post-TCs.
Structure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunit.
Lukavsky et al., Cambridge, United Kingdom. In J Biol Chem, 2007
structural analysis of the eIF3b RNA recognition motif and its interaction with eIF3j
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