Quantification of the d-Ala-d-Lac-Terminated Peptidoglycan Structure in Vancomycin-Resistant Enterococcus faecalis Using a Combined Solid-State Nuclear Magnetic Resonance and Mass Spectrometry Analysis-Reference-Cited by-同舟云学术

Quantification of the d-Ala-d-Lac-Terminated Peptidoglycan Structure in Vancomycin-Resistant Enterococcus faecalis Using a Combined Solid-State Nuclear Magnetic Resonance and Mass Spectrometry Analysis

Published:2017-01-17 Issue:4 Volume:56 Page:612-622
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Chang James D.¹,Foster Erin E.¹,Yang Hao²,Kim Sung Joon¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, Baylor University, Waco, Texas 76798, United States

2. Department of Chemistry, Washington University, St. Louis, Missouri 63130, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00774

Reference42 articles.

1. The rise of the Enterococcus: beyond vancomycin resistance

2. REDOR constraints on the peptidoglycan lattice architecture of Staphylococcus aureus and its FemA mutant

3. Cross-Link Formation and Peptidoglycan Lattice Assembly in the FemA Mutant of Staphylococcus aureus

4. Identification of the UDP-MurNAc-Pentapeptide: l -Alanine Ligase for Synthesis of Branched Peptidoglycan Precursors in Enterococcus faecalis

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