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Roles of dom34:hbs1 in nonstop protein clearance from translocators for normal organelle protein influx.

Izawa T, Tsuboi T, Kuroha K, Inada T, Nishikawa S, Endo T.

Cell Rep. 2012 Sep 27;2(3):447-53. doi: 10.1016/j.celrep.2012.08.010. Epub 2012 Sep 13.


Dom34:hbs1 plays a general role in quality-control systems by dissociation of a stalled ribosome at the 3' end of aberrant mRNA.

Tsuboi T, Kuroha K, Kudo K, Makino S, Inoue E, Kashima I, Inada T.

Mol Cell. 2012 May 25;46(4):518-29. doi: 10.1016/j.molcel.2012.03.013. Epub 2012 Apr 11.


Protein quality control systems associated with no-go and nonstop mRNA surveillance in yeast.

Matsuda R, Ikeuchi K, Nomura S, Inada T.

Genes Cells. 2014 Jan;19(1):1-12. doi: 10.1111/gtc.12106. Epub 2013 Nov 21.


Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay.

Shoemaker CJ, Eyler DE, Green R.

Science. 2010 Oct 15;330(6002):369-72. doi: 10.1126/science.1192430.


Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome.

Becker T, Armache JP, Jarasch A, Anger AM, Villa E, Sieber H, Motaal BA, Mielke T, Berninghausen O, Beckmann R.

Nat Struct Mol Biol. 2011 Jun;18(6):715-20. doi: 10.1038/nsmb.2057. Epub 2011 May 29.


Dom34-Hbs1 mediated dissociation of inactive 80S ribosomes promotes restart of translation after stress.

van den Elzen AM, Schuller A, Green R, Séraphin B.

EMBO J. 2014 Feb 3;33(3):265-76. doi: 10.1002/embj.201386123. Epub 2014 Jan 14.


Structure of yeast Dom34: a protein related to translation termination factor Erf1 and involved in No-Go decay.

Graille M, Chaillet M, van Tilbeurgh H.

J Biol Chem. 2008 Mar 14;283(11):7145-54. doi: 10.1074/jbc.M708224200. Epub 2008 Jan 7.


Dissection of Dom34-Hbs1 reveals independent functions in two RNA quality control pathways.

van den Elzen AM, Henri J, Lazar N, Gas ME, Durand D, Lacroute F, Nicaise M, van Tilbeurgh H, Séraphin B, Graille M.

Nat Struct Mol Biol. 2010 Dec;17(12):1446-52. doi: 10.1038/nsmb.1963. Epub 2010 Nov 21.


Novel G-protein complex whose requirement is linked to the translational status of the cell.

Carr-Schmid A, Pfund C, Craig EA, Kinzy TG.

Mol Cell Biol. 2002 Apr;22(8):2564-74.


Release factor eRF3 mediates premature translation termination on polylysine-stalled ribosomes in Saccharomyces cerevisiae.

Chiabudini M, Tais A, Zhang Y, Hayashi S, Wölfle T, Fitzke E, Rospert S.

Mol Cell Biol. 2014 Nov;34(21):4062-76. doi: 10.1128/MCB.00799-14. Epub 2014 Aug 25.


The protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membrane.

Gillece P, Pilon M, Römisch K.

Proc Natl Acad Sci U S A. 2000 Apr 25;97(9):4609-14.


Protein transport: two translocons are better than one.

Robb A, Brown JD.

Mol Cell. 2001 Sep;8(3):484-6.


Ribosome-associated complex and Ssb are required for translational repression induced by polylysine segments within nascent chains.

Chiabudini M, Conz C, Reckmann F, Rospert S.

Mol Cell Biol. 2012 Dec;32(23):4769-79. doi: 10.1128/MCB.00809-12. Epub 2012 Sep 24.


The Hbs1-Dom34 protein complex functions in non-stop mRNA decay in mammalian cells.

Saito S, Hosoda N, Hoshino S.

J Biol Chem. 2013 Jun 14;288(24):17832-43. doi: 10.1074/jbc.M112.448977. Epub 2013 May 10.


Why Dom34 stimulates growth of cells with defects of 40S ribosomal subunit biosynthesis.

Bhattacharya A, McIntosh KB, Willis IM, Warner JR.

Mol Cell Biol. 2010 Dec;30(23):5562-71. doi: 10.1128/MCB.00618-10. Epub 2010 Sep 27.


Dom34 rescues ribosomes in 3' untranslated regions.

Guydosh NR, Green R.

Cell. 2014 Feb 27;156(5):950-62. doi: 10.1016/j.cell.2014.02.006.


Two novel proteins in the mitochondrial outer membrane mediate beta-barrel protein assembly.

Ishikawa D, Yamamoto H, Tamura Y, Moritoh K, Endo T.

J Cell Biol. 2004 Aug 30;166(5):621-7. Epub 2004 Aug 23.


The mitochondrial morphology protein Mdm10 functions in assembly of the preprotein translocase of the outer membrane.

Meisinger C, Rissler M, Chacinska A, Szklarz LK, Milenkovic D, Kozjak V, Schönfisch B, Lohaus C, Meyer HE, Yaffe MP, Guiard B, Wiedemann N, Pfanner N.

Dev Cell. 2004 Jul;7(1):61-71.


Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.

Griesemer M, Young C, Robinson A, Petzold L.

IET Syst Biol. 2012 Apr;6(2):54-63. doi: 10.1049/iet-syb.2011.0006.

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