Structure of the prolyl-tRNA synthetase from the eukaryotic pathogenGiardia lamblia-Reference-Cited by-同舟云学术

Structure of the prolyl-tRNA synthetase from the eukaryotic pathogenGiardia lamblia

Published:2012-08-18 Issue:9 Volume:68 Page:1194-1200
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Larson Eric T.,Kim Jessica E.,Napuli Alberto J.,Verlinde Christophe L. M. J.,Fan Erkang,Zucker Frank H.,Van Voorhis Wesley C.,Buckner Frederick S.,Hol Wim G. J.,Merritt Ethan A.

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2012/09/00/cb5011/cb5011.pdf

Reference41 articles.

1. Cysteine Activation Is an Inherent in Vitro Property of Prolyl-tRNA Synthetases

2. Methanocaldococcus jannaschii Prolyl-tRNA Synthetase Charges tRNAPro with Cysteine

3. Asymmetric behavior of archaeal prolyl-tRNA synthetase

4. Trans-editing of Cys-tRNAPro by Haemophilus influenzae YbaK Protein

5. GiardiaDB and TrichDB: integrated genomic resources for the eukaryotic protist pathogens Giardia lamblia and Trichomonas vaginalis

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