Thermal inactivation and conformational lock studies on horse liver alcohol dehydrogenase: Structural mechanism-Reference-Cited by-同舟云学术

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Thermal inactivation and conformational lock studies on horse liver alcohol dehydrogenase: Structural mechanism

Published:2013-07 Issue: Volume:58 Page:66-72
ISSN:0141-8130
Container-title:International Journal of Biological Macromolecules
language:en
Short-container-title:International Journal of Biological Macromolecules

Author:

Moosavi-Movahedi Faezeh,Saboury Ali A.,Alijanvand H. Hadi,Bohlooli M.,Salami M.,Moosavi-Movahedi Ali A.

Funder

Iran National Science Foundation

University of Tehran

Publisher

Elsevier BV

Subject

Molecular Biology,General Medicine,Biochemistry,Structural Biology

Reference27 articles.

1. Structural studies of horse liver alcohol dehydrogenase: Coenzyme, substrate and inhibitor binding

2. Biocatalytic Reduction of Carbonyl Groups

3. The Molecular Weight of Horse Liver Alcohol Dehydrogenase.

4. Structure of the complex of active site metal-depleted horse liver alcohol dehydrogenase and NADH.

5. Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution

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3. Insight Into The Structural Characteristics of Self-Assembled Liposome Nanoparticles With Epigallocatechin Gallate/Alcohol Dehydrogenase;2024

4. Prevention of Swelling Phenomenon of Alginate Beads To Improve the Stability and Recyclability of Encapsulated Horse Liver Alcohol Dehydrogenase;ChemBioChem;2023-08-11

5. Molecular Mechanisms Underlying the Stimulatory Effects of Epigallocatechin-3-O-Gallate on the Enzyme Activity of Alcohol Dehydrogenase: Multi-Spectroscopic Analysis and Molecular Docking;2023

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