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Items: 47

1.

Non-coding RNAs: what are we missing?

Carvalho Barbosa C, Calhoun SH, Wieden HJ.

Biochem Cell Biol. 2019 May 31. doi: 10.1139/bcb-2019-0037. [Epub ahead of print]

PMID:
31150585
2.

Elongation Factor Tu's Nucleotide Binding Is Governed by a Thermodynamic Landscape Unique among Bacterial Translation Factors.

Girodat D, Mercier E, Gzyl KE, Wieden HJ.

J Am Chem Soc. 2019 May 28. doi: 10.1021/jacs.9b01522. [Epub ahead of print]

PMID:
31058500
3.

Cellular roles of the human Obg-like ATPase 1 (hOLA1) and its YchF homologs 1.

Balasingam N, Brandon HE, Ross JA, Wieden HJ, Thakor N.

Biochem Cell Biol. 2019 Feb 11:1-11. doi: 10.1139/bcb-2018-0353. [Epub ahead of print]

PMID:
30742486
4.

sdAb-DB: The Single Domain Antibody Database.

Wilton EE, Opyr MP, Kailasam S, Kothe RF, Wieden HJ.

ACS Synth Biol. 2018 Nov 16;7(11):2480-2484. doi: 10.1021/acssynbio.8b00407.

PMID:
30441908
5.

Viruses, IRESs, and a universal translation initiation mechanism.

Roberts L, Wieden HJ.

Biotechnol Genet Eng Rev. 2018 Apr;34(1):60-75. doi: 10.1080/02648725.2018.1471567. Epub 2018 May 28. Review.

PMID:
29804514
6.

Molecular Determinants for 23S rRNA Recognition and Modification by the E. coli Pseudouridine Synthase RluE.

Tillault AS, Schultz SK, Wieden HJ, Kothe U.

J Mol Biol. 2018 Apr 27;430(9):1284-1294. doi: 10.1016/j.jmb.2018.03.011. Epub 2018 Mar 16.

7.

The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion.

Tanzawa T, Kato K, Girodat D, Ose T, Kumakura Y, Wieden HJ, Uchiumi T, Tanaka I, Yao M.

Nucleic Acids Res. 2018 Apr 6;46(6):3232-3244. doi: 10.1093/nar/gky115.

8.

The Emergency Medical Service Microbiome.

Hudson AJ, Glaister GD, Wieden HJ.

Appl Environ Microbiol. 2018 Feb 14;84(5). pii: e02098-17. doi: 10.1128/AEM.02098-17. Print 2018 Mar 1. Review.

9.

Characterization of Fluorescein Arsenical Hairpin (FlAsH) as a Probe for Single-Molecule Fluorescence Spectroscopy.

Fernandes DD, Bamrah J, Kailasam S, Gomes GW, Li Y, Wieden HJ, Gradinaru CC.

Sci Rep. 2017 Oct 12;7(1):13063. doi: 10.1038/s41598-017-13427-8.

10.

Streamlined purification of fluorescently labeled Escherichia coli phosphate-binding protein (PhoS) suitable for rapid-kinetics applications.

Smith DD, Girodat D, Wieden HJ, Selinger LB.

Anal Biochem. 2017 Nov 15;537:106-113. doi: 10.1016/j.ab.2017.09.012. Epub 2017 Sep 21.

PMID:
28941789
11.

A synthetic biology approach to integrative high school STEM training.

Dubé S, Orr D, Dempsey B, Wieden HJ.

Nat Biotechnol. 2017 Jun 7;35(6):591-595. doi: 10.1038/nbt.3896. No abstract available.

PMID:
28591116
12.

Tetracycline does not directly inhibit the function of bacterial elongation factor Tu.

Gzyl KE, Wieden HJ.

PLoS One. 2017 May 26;12(5):e0178523. doi: 10.1371/journal.pone.0178523. eCollection 2017.

13.

Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function.

Heller JLE, Kamalampeta R, Wieden HJ.

Mol Cell Biol. 2017 May 31;37(12). pii: e00653-16. doi: 10.1128/MCB.00653-16. Print 2017 Jun 15. Review.

14.

Engineering bacterial translation initiation - Do we have all the tools we need?

Vigar JRJ, Wieden HJ.

Biochim Biophys Acta Gen Subj. 2017 Nov;1861(11 Pt B):3060-3069. doi: 10.1016/j.bbagen.2017.03.008. Epub 2017 Mar 14. Review.

PMID:
28315412
15.

In Vivo Cleavage Map Illuminates the Central Role of RNase E in Coding and Non-coding RNA Pathways.

Chao Y, Li L, Girodat D, Förstner KU, Said N, Corcoran C, Śmiga M, Papenfort K, Reinhardt R, Wieden HJ, Luisi BF, Vogel J.

Mol Cell. 2017 Jan 5;65(1):39-51. doi: 10.1016/j.molcel.2016.11.002.

16.

The C-terminal Helix of Pseudomonas aeruginosa Elongation Factor Ts Tunes EF-Tu Dynamics to Modulate Nucleotide Exchange.

De Laurentiis EI, Mercier E, Wieden HJ.

J Biol Chem. 2016 Oct 28;291(44):23136-23148. Epub 2016 Sep 13.

17.

Cellular mRNA recruits the ribosome via eIF3-PABP bridge to initiate internal translation.

Thakor N, Smith MD, Roberts L, Faye MD, Patel H, Wieden HJ, Cate JHD, Holcik M.

RNA Biol. 2017 May 4;14(5):553-567. doi: 10.1080/15476286.2015.1137419. Epub 2016 Feb 1.

18.

Introducing a class of standardized and interchangeable parts utilizing programmed ribosomal frameshifts for synthetic biology applications.

Brandon HE, Friedt JR, Glaister GD, Kharey SK, Smith DD, Stinson ZK, Wieden HJ.

Translation (Austin). 2015 Nov 3;3(2):e1112458. doi: 10.1080/21690731.2015.1112458. eCollection 2015 Jul-Dec.

19.

The conserved GTPase HflX is a ribosome splitting factor that binds to the E-site of the bacterial ribosome.

Coatham ML, Brandon HE, Fischer JJ, Schümmer T, Wieden HJ.

Nucleic Acids Res. 2016 Feb 29;44(4):1952-61. doi: 10.1093/nar/gkv1524. Epub 2016 Jan 4.

20.

Histidine 114 Is Critical for ATP Hydrolysis by the Universally Conserved ATPase YchF.

Rosler KS, Mercier E, Andrews IC, Wieden HJ.

J Biol Chem. 2015 Jul 24;290(30):18650-61. doi: 10.1074/jbc.M114.598227. Epub 2015 May 27.

21.

Contribution of two conserved histidines to the dual activity of archaeal RNA guide-dependent and -independent pseudouridine synthase Cbf5.

Tillault AS, Fourmann JB, Loegler C, Wieden HJ, Kothe U, Charpentier B.

RNA. 2015 Jul;21(7):1233-9. doi: 10.1261/rna.051425.115. Epub 2015 May 19.

22.
23.

A conserved P-loop anchor limits the structural dynamics that mediate nucleotide dissociation in EF-Tu.

Mercier E, Girodat D, Wieden HJ.

Sci Rep. 2015 Jan 8;5:7677. doi: 10.1038/srep07677.

24.

The ABC-F protein EttA gates ribosome entry into the translation elongation cycle.

Boël G, Smith PC, Ning W, Englander MT, Chen B, Hashem Y, Testa AJ, Fischer JJ, Wieden HJ, Frank J, Gonzalez RL Jr, Hunt JF.

Nat Struct Mol Biol. 2014 Feb;21(2):143-51. doi: 10.1038/nsmb.2740. Epub 2014 Jan 5.

25.

An arginine-aspartate network in the active site of bacterial TruB is critical for catalyzing pseudouridine formation.

Friedt J, Leavens FM, Mercier E, Wieden HJ, Kothe U.

Nucleic Acids Res. 2014 Apr;42(6):3857-70. doi: 10.1093/nar/gkt1331. Epub 2013 Dec 26.

26.

GTPase of the immune-associated nucleotide-binding protein 5 (GIMAP5) regulates calcium influx in T-lymphocytes by promoting mitochondrial calcium accumulation.

Chen XL, Serrano D, Mayhue M, Wieden HJ, Stankova J, Boulay G, Ilangumaran S, Ramanathan S.

Biochem J. 2013 Jan 15;449(2):353-64. doi: 10.1042/BJ20120516.

PMID:
23098229
27.

The 70S ribosome modulates the ATPase activity of Escherichia coli YchF.

Becker M, Gzyl KE, Altamirano AM, Vuong A, Urban K, Wieden HJ.

RNA Biol. 2012 Oct;9(10):1288-301. doi: 10.4161/rna.22131. Epub 2012 Sep 20.

28.

The ribosome modulates the structural dynamics of the conserved GTPase HflX and triggers tight nucleotide binding.

Fischer JJ, Coatham ML, Bear SE, Brandon HE, De Laurentiis EI, Shields MJ, Wieden HJ.

Biochimie. 2012 Aug;94(8):1647-59. doi: 10.1016/j.biochi.2012.04.016. Epub 2012 Apr 25.

PMID:
22554723
29.

Substrate binding in protein-tyrosine phosphatase-like inositol polyphosphatases.

Gruninger RJ, Dobing S, Smith AD, Bruder LM, Selinger LB, Wieden HJ, Mosimann SC.

J Biol Chem. 2012 Mar 23;287(13):9722-30. doi: 10.1074/jbc.M111.309872. Epub 2011 Dec 2.

30.

Construction of a fully active Cys-less elongation factor Tu: functional role of conserved cysteine 81.

De Laurentiis EI, Mo F, Wieden HJ.

Biochim Biophys Acta. 2011 May;1814(5):684-92. doi: 10.1016/j.bbapap.2011.02.007. Epub 2011 Feb 19.

PMID:
21338717
31.

A combined molecular dynamics and rapid kinetics approach to identify conserved three-dimensional communication networks in elongation factor Tu.

Wieden HJ, Mercier E, Gray J, Steed B, Yawney D.

Biophys J. 2010 Dec 1;99(11):3735-43. doi: 10.1016/j.bpj.2010.10.013.

32.

Toward understanding the function of the universally conserved GTPase HflX from Escherichia coli: a kinetic approach.

Shields MJ, Fischer JJ, Wieden HJ.

Biochemistry. 2009 Nov 17;48(45):10793-802. doi: 10.1021/bi901074h.

PMID:
19824612
33.

The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange.

Dahl LD, Wieden HJ, Rodnina MV, Knudsen CR.

J Biol Chem. 2006 Jul 28;281(30):21139-46. Epub 2006 May 22.

34.

Conformations of the signal recognition particle protein Ffh from Escherichia coli as determined by FRET.

Buskiewicz I, Peske F, Wieden HJ, Gryczynski I, Rodnina MV, Wintermeyer W.

J Mol Biol. 2005 Aug 12;351(2):417-30.

PMID:
16005894
35.

Recognition and selection of tRNA in translation.

Rodnina MV, Gromadski KB, Kothe U, Wieden HJ.

FEBS Lett. 2005 Feb 7;579(4):938-42. Review.

36.

Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosome.

Kothe U, Wieden HJ, Mohr D, Rodnina MV.

J Mol Biol. 2004 Mar 5;336(5):1011-21.

PMID:
15037065
37.

Essential role of histidine 84 in elongation factor Tu for the chemical step of GTP hydrolysis on the ribosome.

Daviter T, Wieden HJ, Rodnina MV.

J Mol Biol. 2003 Sep 19;332(3):689-99.

PMID:
12963376
38.

The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome.

Gu SQ, Peske F, Wieden HJ, Rodnina MV, Wintermeyer W.

RNA. 2003 May;9(5):566-73.

39.
40.

Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.

Stark H, Rodnina MV, Wieden HJ, Zemlin F, Wintermeyer W, van Heel M.

Nat Struct Biol. 2002 Nov;9(11):849-54.

PMID:
12379845
41.

Inactivation of the elongation factor Tu by mosquitocidal toxin-catalyzed mono-ADP-ribosylation.

Schirmer J, Wieden HJ, Rodnina MV, Aktories K.

Appl Environ Microbiol. 2002 Oct;68(10):4894-9.

42.

Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor Tu.

Gromadski KB, Wieden HJ, Rodnina MV.

Biochemistry. 2002 Jan 8;41(1):162-9.

PMID:
11772013
43.

Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine base.

Wieden HJ, Gromadski K, Rodnin D, Rodnina MV.

J Biol Chem. 2002 Feb 22;277(8):6032-6. Epub 2001 Dec 13.

44.

The importance of structural transitions of the switch II region for the functions of elongation factor Tu on the ribosome.

Knudsen C, Wieden HJ, Rodnina MV.

J Biol Chem. 2001 Jun 22;276(25):22183-90. Epub 2001 Apr 13.

45.
46.

GTPases mechanisms and functions of translation factors on the ribosome.

Rodnina MV, Stark H, Savelsbergh A, Wieden HJ, Mohr D, Matassova NB, Peske F, Daviter T, Gualerzi CO, Wintermeyer W.

Biol Chem. 2000 May-Jun;381(5-6):377-87. Review.

PMID:
10937868
47.

Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation.

Stark H, Rodnina MV, Wieden HJ, van Heel M, Wintermeyer W.

Cell. 2000 Feb 4;100(3):301-9.

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