Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 101

1.

Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan.

Floor SN, Borja MS, Gross JD.

Proc Natl Acad Sci U S A. 2012 Feb 21;109(8):2872-7. doi: 10.1073/pnas.1113620109. Epub 2012 Feb 9.

2.

Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformation.

Valkov E, Muthukumar S, Chang CT, Jonas S, Weichenrieder O, Izaurralde E.

Nat Struct Mol Biol. 2016 Jun;23(6):574-9. doi: 10.1038/nsmb.3232. Epub 2016 May 16.

PMID:
27183195
3.

A split active site couples cap recognition by Dcp2 to activation.

Floor SN, Jones BN, Hernandez GA, Gross JD.

Nat Struct Mol Biol. 2010 Sep;17(9):1096-101. doi: 10.1038/nsmb.1879. Epub 2010 Aug 15.

4.

The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex.

Fromm SA, Truffault V, Kamenz J, Braun JE, Hoffmann NA, Izaurralde E, Sprangers R.

EMBO J. 2012 Jan 18;31(2):279-90. doi: 10.1038/emboj.2011.408. Epub 2011 Nov 15.

5.

Structural basis of mRNA-cap recognition by Dcp1-Dcp2.

Mugridge JS, Ziemniak M, Jemielity J, Gross JD.

Nat Struct Mol Biol. 2016 Nov;23(11):987-994. doi: 10.1038/nsmb.3301. Epub 2016 Oct 3.

6.

Structural basis of dcp2 recognition and activation by dcp1.

She M, Decker CJ, Svergun DI, Round A, Chen N, Muhlrad D, Parker R, Song H.

Mol Cell. 2008 Feb 15;29(3):337-49. doi: 10.1016/j.molcel.2008.01.002.

7.

Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition.

Borja MS, Piotukh K, Freund C, Gross JD.

RNA. 2011 Feb;17(2):278-90. doi: 10.1261/rna.2382011. Epub 2010 Dec 10.

8.

Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.

Wurm JP, Holdermann I, Overbeck JH, Mayer PHO, Sprangers R.

Proc Natl Acad Sci U S A. 2017 Jun 6;114(23):6034-6039. doi: 10.1073/pnas.1704496114. Epub 2017 May 22.

9.

The S. pombe mRNA decapping complex recruits cofactors and an Edc1-like activator through a single dynamic surface.

Wurm JP, Overbeck J, Sprangers R.

RNA. 2016 Sep;22(9):1360-72. doi: 10.1261/rna.057315.116. Epub 2016 Jun 28.

10.

mRNA decapping is promoted by an RNA-binding channel in Dcp2.

Deshmukh MV, Jones BN, Quang-Dang DU, Flinders J, Floor SN, Kim C, Jemielity J, Kalek M, Darzynkiewicz E, Gross JD.

Mol Cell. 2008 Feb 15;29(3):324-36. doi: 10.1016/j.molcel.2007.11.027.

11.

The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1.

Chang CT, Bercovich N, Loh B, Jonas S, Izaurralde E.

Nucleic Acids Res. 2014 Apr;42(8):5217-33. doi: 10.1093/nar/gku129. Epub 2014 Feb 8.

12.

Two-headed tetraphosphate cap analogs are inhibitors of the Dcp1/2 RNA decapping complex.

Ziemniak M, Mugridge JS, Kowalska J, Rhoads RE, Gross JD, Jemielity J.

RNA. 2016 Apr;22(4):518-29. doi: 10.1261/rna.055152.115. Epub 2016 Jan 29.

13.

Control of mRNA decapping by Dcp2: An open and shut case?

Floor SN, Jones BN, Gross JD.

RNA Biol. 2008 Oct-Dec;5(4):189-92. Epub 2008 Oct 26.

14.

Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme Dcp2.

Aglietti RA, Floor SN, McClendon CL, Jacobson MP, Gross JD.

Structure. 2013 Sep 3;21(9):1571-80. doi: 10.1016/j.str.2013.06.021. Epub 2013 Aug 1.

15.

Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to m7GDP and its Edc3 activator.

Charenton C, Taverniti V, Gaudon-Plesse C, Back R, Séraphin B, Graille M.

Nat Struct Mol Biol. 2016 Nov;23(11):982-986. doi: 10.1038/nsmb.3300. Epub 2016 Oct 3.

PMID:
27694841
16.

In vitro reconstitution of a cellular phase-transition process that involves the mRNA decapping machinery.

Fromm SA, Kamenz J, Nöldeke ER, Neu A, Zocher G, Sprangers R.

Angew Chem Int Ed Engl. 2014 Jul 7;53(28):7354-9. doi: 10.1002/anie.201402885. Epub 2014 May 26.

17.

Structural and functional insights into eukaryotic mRNA decapping.

Ling SH, Qamra R, Song H.

Wiley Interdiscip Rev RNA. 2011 Mar-Apr;2(2):193-208. doi: 10.1002/wrna.44. Epub 2010 Sep 2. Review.

PMID:
21957006
18.

Competition between Decapping Complex Formation and Ubiquitin-Mediated Proteasomal Degradation Controls Human Dcp2 Decapping Activity.

Erickson SL, Corpuz EO, Maloy JP, Fillman C, Webb K, Bennett EJ, Lykke-Andersen J.

Mol Cell Biol. 2015 Jun;35(12):2144-53. doi: 10.1128/MCB.01517-14. Epub 2015 Apr 13.

19.

Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe.

She M, Decker CJ, Chen N, Tumati S, Parker R, Song H.

Nat Struct Mol Biol. 2006 Jan;13(1):63-70. Epub 2005 Dec 11.

20.

Insights into the molecular determinants involved in cap recognition by the vaccinia virus D10 decapping enzyme.

Soulière MF, Perreault JP, Bisaillon M.

Nucleic Acids Res. 2010 Nov;38(21):7599-610. doi: 10.1093/nar/gkq628. Epub 2010 Jul 17.

Supplemental Content

Support Center