N-terminal acetylation and protonation of individual hemoglobin subunits: Position-dependent effects on tetramer strength and cooperativity-Reference-Cited by-同舟云学术

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N-terminal acetylation and protonation of individual hemoglobin subunits: Position-dependent effects on tetramer strength and cooperativity

Published:2009-01-01 Issue:6 Volume:14 Page:1458-1471
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Ashiuchi Makoto,Yagami Takeshi,Willey Ronald J.,Padovan Julio C.,Chait Brian T.,Popowicz Anthony,Manning Lois R.,Manning James M.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference37 articles.

1. Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis;Allfrey;Proc. Natl. Acad. Sci.,1964

2. Tetramer-dimer dissociation in hemoglobin and the Bohr effect;Atha;J. Biol. Chem.,1976

3. Matrix-assisted laser desorption ionization mass-spectrometry of proteins;Beavis;Methods Enzymol.,1996

4. N-terminal processing: The methionine aminopeptidase and N-acetyl transferase families;Bradshaw;Trends Biochem. Sci.,1998

5. The interaction of 2,3-diphosphoglycerate with various human hemoglobins;Bunn;J. Clin. Invest.,1970

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3. Contributions to nucleosome dynamics in chromatin from interactive propagation of phosphorylation/acetylation and inducible histone lysine basicities;Protein Science;2018-01-05

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