Structural analysis of glutathionyl hemoglobin using native mass spectrometry-Reference-Cited by-同舟云学术

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Structural analysis of glutathionyl hemoglobin using native mass spectrometry

Published:2019-12 Issue:3 Volume:208 Page:107386
ISSN:1047-8477
Container-title:Journal of Structural Biology
language:en
Short-container-title:Journal of Structural Biology

Author:

Muralidharan Monita,Mitra Amrita,Maity Dibyajyoti^ORCID,Pal Debnath,Mandal Amit Kumar

Funder

DST

Publisher

Elsevier BV

Subject

Structural Biology

Reference25 articles.

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2. Protein complexes in the gas phase: technology for structural genomics and proteomics;Benesch;Chem. Rev.,2007

3. Comparison of human hemoglobin A carrying glutathione as a mixed disulfide with the naturally occurring human hemoglobin A;Birchmeier;Biochemistry,1973

4. Covalent binding of glutathione to hemoglobin. II. Functional consequences and structural changes reflected in NMR spectra;Craescu;J. Biol. Chem.,1986

5. Covalent binding of glutathione to hemoglobin. I. Inhibition of hemoglobin S polymerization;Garel;J. Biol. Chem.,1986

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3. Hemoglobin is an oxygen-dependent glutathione buffer adapting the intracellular reduced glutathione levels to oxygen availability;Redox Biology;2022-12

4. The Redox Potential of the β-93-Cysteine Thiol Group in Human Hemoglobin Estimated from In Vitro Oxidant Challenge Experiments;Molecules;2021-04-26

5. Characterization of cellular oxidative stress response by stoichiometric redox proteomics;American Journal of Physiology-Cell Physiology;2021-02-01

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