Structural stability of human butyrylcholinesterase under high hydrostatic pressure-Reference-Cited by-同舟云学术

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Structural stability of human butyrylcholinesterase under high hydrostatic pressure

Published:2019-02 Issue:2 Volume:1867 Page:107-113
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Kangur Liina,Timpmann Kõu,Zeller Dominik,Masson Patrick,Peters Judith,Freiberg Arvi

Funder

Estonian Research Council

Russian Science Foundation

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference42 articles.

1. Complete amino acid sequence of human serum cholinesterase;Lockridge;J. Biol. Chem.,1987

2. Association of tetramers of human butyrylcholinesterase is mediated by conserved aromatic residues of the carboxy terminus;Altamirano;Chem. Biol. Interact.,1999

3. Conserved aromatic residues of the C-terminus of human butyrylcholinesterase mediate the association of tetramers;Altamirano;Biochemistry,1999

4. Tetramerization domain of human butyrylcholinesterase is at the C-terminus;Blong;Biochem. J.,1997

5. Lamellipodin proline rich peptides associated with native plasma butyrylcholinesterase tetramers;Li;Biochem. J.,2008

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