Work

The human β3 alcohol dehydrogenase subunit differs from β1 by a cys for Arg-369 substitution which decreases NAD(H) binding

Year: 1987

Type: article

Source: Biochemical and Biophysical Research Communications

DOI: 10.1016/0006-291x(87)90779-0

Authors: Joe C. Burnell, Lucinda G. Carr, Francis E. Dwulet, Howard J. Edenberg, Ting-Kai Li, William F. Bosron

Institutions: Indiana University Indianapolis, Indiana University School of Medicine

Language: English

Topic: Enzyme Structure and Function

Subfield: Materials Chemistry

Field: Materials Science

Domain: Physical Sciences

Open Access status: closed

Funders: National Institutes of Health, National Institute on Alcohol Abuse and Alcoholism

Awards: G1212229999, G1374058198, G3066791320, HUMAN ALCOHOL AND ALDEHYDE DEHYDROGENASES

OpenAlex ID: W2056313629

FWCI: 4.664

Cites: 16

Cited by: 52

Related to: 10