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Items: 1 to 20 of 134

1.

NAC functions as a modulator of SRP during the early steps of protein targeting to the endoplasmic reticulum.

Zhang Y, Berndt U, Gölz H, Tais A, Oellerer S, Wölfle T, Fitzke E, Rospert S.

Mol Biol Cell. 2012 Aug;23(16):3027-40. doi: 10.1091/mbc.E12-02-0112. Epub 2012 Jun 27.

2.

A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel.

Berndt U, Oellerer S, Zhang Y, Johnson AE, Rospert S.

Proc Natl Acad Sci U S A. 2009 Feb 3;106(5):1398-403. doi: 10.1073/pnas.0808584106. Epub 2009 Jan 21.

3.
5.

Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens.

Flanagan JJ, Chen JC, Miao Y, Shao Y, Lin J, Bock PE, Johnson AE.

J Biol Chem. 2003 May 16;278(20):18628-37. Epub 2003 Mar 5.

7.

Cotranslational signal-independent SRP preloading during membrane targeting.

Chartron JW, Hunt KC, Frydman J.

Nature. 2016 Aug 11;536(7615):224-8. Epub 2016 Aug 3.

8.

Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.

Mircheva M, Boy D, Weiche B, Hucke F, Graumann P, Koch HG.

BMC Biol. 2009 Nov 13;7:76. doi: 10.1186/1741-7007-7-76.

9.

Signal recognition particle-ribosome binding is sensitive to nascent chain length.

Noriega TR, Tsai A, Elvekrog MM, Petrov A, Neher SB, Chen J, Bradshaw N, Puglisi JD, Walter P.

J Biol Chem. 2014 Jul 11;289(28):19294-305. doi: 10.1074/jbc.M114.563239. Epub 2014 May 7.

11.

Sec62 protein mediates membrane insertion and orientation of moderately hydrophobic signal anchor proteins in the endoplasmic reticulum (ER).

Reithinger JH, Kim JE, Kim H.

J Biol Chem. 2013 Jun 21;288(25):18058-67. doi: 10.1074/jbc.M113.473009. Epub 2013 Apr 30.

13.

A network of cytosolic factors targets SRP-independent proteins to the endoplasmic reticulum.

Ast T, Cohen G, Schuldiner M.

Cell. 2013 Feb 28;152(5):1134-45. doi: 10.1016/j.cell.2013.02.003.

15.

Defining the specificity of cotranslationally acting chaperones by systematic analysis of mRNAs associated with ribosome-nascent chain complexes.

del Alamo M, Hogan DJ, Pechmann S, Albanese V, Brown PO, Frydman J.

PLoS Biol. 2011 Jul;9(7):e1001100. doi: 10.1371/journal.pbio.1001100. Epub 2011 Jul 12.

16.

Analysis of the interplay of protein biogenesis factors at the ribosome exit site reveals new role for NAC.

Nyathi Y, Pool MR.

J Cell Biol. 2015 Jul 20;210(2):287-301. doi: 10.1083/jcb.201410086.

17.

Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting.

Bacher G, Lütcke H, Jungnickel B, Rapoport TA, Dobberstein B.

Nature. 1996 May 16;381(6579):248-51.

PMID:
8622769
18.

Cotranslational Intersection between the SRP and GET Targeting Pathways to the Endoplasmic Reticulum of Saccharomyces cerevisiae.

Zhang Y, Schäffer T, Wölfle T, Fitzke E, Thiel G, Rospert S.

Mol Cell Biol. 2016 Aug 26;36(18):2374-83. doi: 10.1128/MCB.00131-16. Print 2016 Sep 15.

19.

The principle of antagonism ensures protein targeting specificity at the endoplasmic reticulum.

Gamerdinger M, Hanebuth MA, Frickey T, Deuerling E.

Science. 2015 Apr 10;348(6231):201-7. doi: 10.1126/science.aaa5335.

20.

Access to ribosomal protein Rpl25p by the signal recognition particle is required for efficient cotranslational translocation.

Dalley JA, Selkirk A, Pool MR.

Mol Biol Cell. 2008 Jul;19(7):2876-84. doi: 10.1091/mbc.E07-10-1074. Epub 2008 Apr 30.

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