Crystal Structure of N-Acetylornithine Transcarbamylase from Xanthomonas campestris-Reference-Cited by-同舟云学术

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Crystal Structure of N-Acetylornithine Transcarbamylase from Xanthomonas campestris

Published:2005-04 Issue:15 Volume:280 Page:14366-14369
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Shi Dashuang,Morizono Hiroki,Yu Xiaolin,Roth Lauren,Caldovic Ljubica,Allewell Norma M.,Malamy Michael H.,Tuchman Mendel

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference19 articles.

1. Comparison of the genomes of two Xanthomonas pathogens with differing host specificities

2. Crystal Structure of a Transcarbamylase-like Protein from the Anaerobic Bacterium Bacteroides fragilis at 2.0Å Resolution

3. Human ornithine transcarbamylase: crystallographic insights into substrate recognition and conformational changes

4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

5. [20] Processing of X-ray diffraction data collected in oscillation mode

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1. Structural analysis and molecular substrate recognition properties of Arabidopsis thaliana ornithine transcarbamylase, the molecular target of phaseolotoxin produced by Pseudomonas syringae;Frontiers in Plant Science;2023-12-18

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3. HPLC-MS-based untargeted metabolomic analysis of differential plasma metabolites and their associated metabolic pathways in reproductively anosmic black porgy, Acanthopagrus schlegelii;Comparative Biochemistry and Physiology Part D: Genomics and Proteomics;2023-06

4. De novo arginine synthesis is required for full virulence of Xanthomonas arboricola pv. juglandis during Walnut Bacterial Blight Disease;Phytopathology®;2021-12-23

5. Regulation of arginine biosynthesis, catabolism and transport in Escherichia coli;Amino Acids;2019-07-03

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