A new method for analysis of disulfide-containing proteins by matrix-assisted laser desorption ionization (MALDI) mass spectrometry-Reference-Cited by-同舟云学术

A new method for analysis of disulfide-containing proteins by matrix-assisted laser desorption ionization (MALDI) mass spectrometry

Published:2009-12-01 Issue:12 Volume:20 Page:2284-2293
ISSN:1044-0305
Container-title:Journal of the American Society for Mass Spectrometry
language:en
Short-container-title:J. Am. Soc. Mass Spectrom.

Author:

Yang Hongmei¹²,Liu Ning¹³,Qiu Xiaoyan¹,Liu Shuying¹⁴

Affiliation:

1. Changchun Center of Mass Spectrometry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, 5625 Renmin Street, 130022, Changchun, P.R. China

2. Graduate School of the Chinese Academy of Sciences, Beijing, P.R. China

3. Jilin University, Changchun, P.R. China

4. Changchun University of Chinese Medicine, Changchun, P.R. China

Publisher

American Chemical Society (ACS)

Subject

Spectroscopy,Structural Biology

Link

https://pubs.acs.org/doi/pdf/10.1016/j.jasms.2009.08.020

Reference38 articles.

1. Effect of disulfide bonds on the structure, function, and stability of the trypsin/tPA inhibitor from Erythrina caffra: Site-directed mutagenesis, expression, and physiochemical characterization

2. Disulfide Bonds and Protein Folding

3. Modificomics: Posttranslational modifications beyond protein phosphorylation and glycosylation

4. NMR-Based Mapping of Disulfide Bridges in Cysteine-Rich Peptides: Application to the μ-Conotoxin SxIIIA

5. Peptide Binding and NMR Analysis of the Interaction between SAP97 PDZ2 and GluR-A: Potential Involvement of a Disulfide Bond

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