Linking Distinct Conformations of Nicotinamide Adenine Dinucleotide with Protein Fold/Function-Reference-Cited by-同舟云学术

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Linking Distinct Conformations of Nicotinamide Adenine Dinucleotide with Protein Fold/Function

Published:2011-05-25 Issue:24 Volume:115 Page:7932-7939
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Kuppuraj Gopi¹,Sargsyan Karen²,Hua Yun-Hao²,Merrill A. Rod³,Lim Carmay²

Affiliation:

1. Chemical Biology & Molecular Biophysics, Taiwan International Graduate Program, Academia Sinica, Taipei 115, Taiwan

2. Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan

3. Department of Molecular & Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp1118663

Reference51 articles.

1. The power to reduce: pyridine nucleotides – small molecules with a multitude of functions

2. NADH/NAD+ interaction with NADH: Ubiquinone oxidoreductase (complex I)

3. ADP-Ribosylation of Proteins

4. Crystal Structure of Diphtheria Toxin Bound to Nicotinamide Adenine Dinucleotide

5. ADP-Ribose Transfer Reactions

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4. Structure–function analyses of a pertussis-like toxin from pathogenic Escherichia coli reveal a distinct mechanism of inhibition of trimeric G-proteins;Journal of Biological Chemistry;2017-09

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