Inhibition of activity and quenching of intrinsic fluorescence of transglutaminase by acrylamide are independent events
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference19 articles.
1. Fluorescence quenching studies with proteins
2. TIME-RESOLVED FLUORESCENCE OF PROTEINS
3. THE PHOTOPHYSICS AND PHOTOCHEMISTRY OF THE NEAR-UV ABSORBING AMINO ACIDS-I. TRYPTOPHAN AND ITS SIMPLE DERIVATIVES
4. Does the fluorescence quencher acrylamide bind to proteins?
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1. Nε-Acryloyllysine Piperazides as Irreversible Inhibitors of Transglutaminase 2: Synthesis, Structure–Activity Relationships, and Pharmacokinetic Profiling;Journal of Medicinal Chemistry;2018-04-17
2. Effects of acrylamide on creatine kinase from rabbit muscle;The International Journal of Biochemistry & Cell Biology;2001-11
3. Effect of acrylamide on aldolase structure. II. Characterization of aldolase unfolding intermediates;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1999-05
4. THE INTERACTION OF ACRYLAMIDE WITH GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE. STRUCTURAL MODIFICATIONS IN THE ENZYME STUDIED BY FLUORESCENCE TECHNIQUES;Photochemistry and Photobiology;1990-06
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