Structural characterization of sialic acid synthase by electrospray mass spectrometry—A tetrameric enzyme composed of dimeric dimers-Reference-Cited by-同舟云学术

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Structural characterization of sialic acid synthase by electrospray mass spectrometry—A tetrameric enzyme composed of dimeric dimers

Published:2005-03-01 Issue:3 Volume:16 Page:324-332
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Huang Hsin-Hung¹²,Liao Hsin-Kai¹,Chen Yu-Ju¹²,Hwang Tzann-Shun³⁴,Lin Yi-Han³,Lin Chun-Hung³⁴

Affiliation:

1. Institute of Chemistry, Academia Sinica, 128 Academia Road, Section 2, Nan-kang, 11529, Taipei, Taiwan

2. National Central University, Taoyuan, Taiwan

3. Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan

4. Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1016/j.jasms.2004.11.016

Reference40 articles.

1. Amino acid sequence of Salmonella typhimurium branched-chain amino acid aminotransferase

2. Principles of protein-protein interactions.

3. Native protein mass spectrometry: from intact oligomers to functional machineries

4. Observation of an Intact Noncovalent Homotrimer of Detergent-solubilized Rat Microsomal Glutathione Transferase-1 by Electrospray Mass Spectrometry

5. Tandem Mass Spectrometry Defines the Stoichiometry and Quaternary Structural Arrangement of Tryptophan Molecules in the Multiprotein Complex TRAP

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