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Items: 16

1.

Rapid, directed transport of DC-SIGN clusters in the plasma membrane.

Liu P, Weinreb V, Ridilla M, Betts L, Patel P, de Silva AM, Thompson NL, Jacobson K.

Sci Adv. 2017 Nov 8;3(11):eaao1616. doi: 10.1126/sciadv.aao1616. eCollection 2017 Nov.

2.

Combining multi-mutant and modular thermodynamic cycles to measure energetic coupling networks in enzyme catalysis.

Carter CW Jr, Chandrasekaran SN, Weinreb V, Li L, Williams T.

Struct Dyn. 2017 Jan 26;4(3):032101. doi: 10.1063/1.4974218. eCollection 2017 May.

3.

Functional Class I and II amino acid-activating enzymes can be coded by opposite strands of the same gene.

Martinez-Rodriguez L, Erdogan O, Jimenez-Rodriguez M, Gonzalez-Rivera K, Williams T, Li L, Weinreb V, Collier M, Chandrasekaran SN, Ambroggio X, Kuhlman B, Carter CW Jr.

J Biol Chem. 2016 Nov 4;291(45):23830-23831. No abstract available.

4.

Functional Class I and II Amino Acid-activating Enzymes Can Be Coded by Opposite Strands of the Same Gene.

Martinez-Rodriguez L, Erdogan O, Jimenez-Rodriguez M, Gonzalez-Rivera K, Williams T, Li L, Weinreb V, Collier M, Chandrasekaran SN, Ambroggio X, Kuhlman B, Carter CW Jr.

J Biol Chem. 2015 Aug 7;290(32):19710-25. doi: 10.1074/jbc.M115.642876. Epub 2015 Jun 18. Erratum in: J Biol Chem. 2016 Nov 4;291(45):23830-23831.

5.

The Rodin-Ohno hypothesis that two enzyme superfamilies descended from one ancestral gene: an unlikely scenario for the origins of translation that will not be dismissed.

Carter CW Jr, Li L, Weinreb V, Collier M, Gonzalez-Rivera K, Jimenez-Rodriguez M, Erdogan O, Kuhlman B, Ambroggio X, Williams T, Chandrasekharan SN.

Biol Direct. 2014 Jun 14;9:11. doi: 10.1186/1745-6150-9-11.

6.

Enhanced amino acid selection in fully evolved tryptophanyl-tRNA synthetase, relative to its urzyme, requires domain motion sensed by the D1 switch, a remote dynamic packing motif.

Weinreb V, Li L, Chandrasekaran SN, Koehl P, Delarue M, Carter CW Jr.

J Biol Chem. 2014 Feb 14;289(7):4367-76. doi: 10.1074/jbc.M113.538660. Epub 2014 Jan 6.

7.

A master switch couples Mg²⁺-assisted catalysis to domain motion in B. stearothermophilus tryptophanyl-tRNA Synthetase.

Weinreb V, Li L, Carter CW Jr.

Structure. 2012 Jan 11;20(1):128-38. doi: 10.1016/j.str.2011.10.020.

8.

Histidyl-tRNA synthetase urzymes: Class I and II aminoacyl tRNA synthetase urzymes have comparable catalytic activities for cognate amino acid activation.

Li L, Weinreb V, Francklyn C, Carter CW Jr.

J Biol Chem. 2011 Mar 25;286(12):10387-95. doi: 10.1074/jbc.M110.198929. Epub 2011 Jan 26.

9.

Tryptophanyl-tRNA synthetase Urzyme: a model to recapitulate molecular evolution and investigate intramolecular complementation.

Pham Y, Kuhlman B, Butterfoss GL, Hu H, Weinreb V, Carter CW Jr.

J Biol Chem. 2010 Dec 3;285(49):38590-601. doi: 10.1074/jbc.M110.136911. Epub 2010 Sep 23.

10.

Mg2+-assisted catalysis by B. stearothermophilus TrpRS is promoted by allosteric effects.

Weinreb V, Li L, Campbell CL, Kaguni LS, Carter CW Jr.

Structure. 2009 Jul 15;17(7):952-64. doi: 10.1016/j.str.2009.05.007.

11.

Mg2+-free Bacillus stearothermophilus tryptophanyl-tRNA synthetase retains a major fraction of the overall rate enhancement for tryptophan activation.

Weinreb V, Carter CW Jr.

J Am Chem Soc. 2008 Jan 30;130(4):1488-94. doi: 10.1021/ja076557x. Epub 2008 Jan 4.

12.

A conformational transition state accompanies tryptophan activation by B. stearothermophilus tryptophanyl-tRNA synthetase.

Kapustina M, Weinreb V, Li L, Kuhlman B, Carter CW Jr.

Structure. 2007 Oct;15(10):1272-84.

14.

A minimal TrpRS catalytic domain supports sense/antisense ancestry of class I and II aminoacyl-tRNA synthetases.

Pham Y, Li L, Kim A, Erdogan O, Weinreb V, Butterfoss GL, Kuhlman B, Carter CW Jr.

Mol Cell. 2007 Mar 23;25(6):851-62.

15.

Optimization of apolipoprotein B mRNA editing by APOBEC1 apoenzyme and the role of its auxiliary factor, ACF.

Chester A, Weinreb V, Carter CW Jr, Navaratnam N.

RNA. 2004 Sep;10(9):1399-411. Epub 2004 Jul 23.

16.

Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations.

Retailleau P, Huang X, Yin Y, Hu M, Weinreb V, Vachette P, Vonrhein C, Bricogne G, Roversi P, Ilyin V, Carter CW Jr.

J Mol Biol. 2003 Jan 3;325(1):39-63.

PMID:
12473451

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