Polyproline-rich peptides associated with Torpedo californica acetylcholinesterase tetramers-Reference-Cited by-同舟云学术

Polyproline-rich peptides associated with Torpedo californica acetylcholinesterase tetramers

Published:2020-03 Issue: Volume:319 Page:109007
ISSN:0009-2797
Container-title:Chemico-Biological Interactions
language:en
Short-container-title:Chemico-Biological Interactions

Author:

Toker Lilly,Silman Israel,Zeev-Ben-Mordehai Tzviya,Sussman Joel L.,Schopfer Lawrence M.,Lockridge Oksana

Funder

National Institutes of Health

Fred & Pamela Buffet Cancer Center

Publisher

Elsevier BV

Subject

Toxicology,General Medicine

Reference39 articles.

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3. Structural characterization of the asymmetric (17 + 13) S species of acetylcholinesterase from Torpedo. II. Component peptides obtained by selective proteolysis and disulfide bond reduction;Lee;J. Biol. Chem.,1982

4. Bovine brain acetylcholinesterase primary sequence involved in intersubunit disulfide linkages;Roberts;J. Biol. Chem.,1991

5. Structure of 18S and 14S acetylcholinesterase. Identification of collagen-like subunits that are linked by disulfide bonds to catalytic subunits;Rosenberry;Biochemistry,1977

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