Rossmann Folds
Rossmann Fold is a structural motif characterized by a repeated β-α-β pattern that forms a conserved nucleotide-binding domain primarily involved in binding dinucleotide cofactors such as NAD+ or FAD in dehydrogenases and other oxidoreductases.
164
Publications
9.7K
Citations
844
Authors
296
Institutions
Publications per year
2017–2026
32
164
Enzyme Structure with Two Catalytic Sites for Double-Sieve Selection of Substrate
Osamu Nureki, Dmitry G. Vassylyev, Masaru Tateno et al. · Science · 1998 · 320 citations
1–5 of 164
844
The University of Texas Southwestern Medical Center, United States
6 publications · 552 citations
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4
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3
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National Center for Biotechnology Information, United States
3 publications · 432 citations
3
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3
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1–5 of 844
296

Howard Hughes Medical Institute
Chevy Chase, United States
9 h-index
16 publications
1.6K citations

Centre National de la Recherche Scientifique
Paris, France
8 h-index
41 publications
2.5K citations

Chinese Academy of Sciences
Beijing, China
7 h-index
24 publications
525 citations
The University of Texas Southwestern Medical Center
Dallas, United States
6 h-index
19 publications
1.6K citations
The University of Tokyo
Tokyo, Japan
5 h-index
20 publications
3.5K citations
National Institutes of Health
Bethesda, United States
4 h-index
14 publications
1.6K citations
Scripps Research Institute
San Diego, United States
4 h-index
17 publications
3.9K citations
Argonne National Laboratory
Lemont, United States
4 h-index
6 publications
343 citations
1–8 of 296
JBC · 20 publications · 1.3K citations
18
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18 publications · 859 citations
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PNAS · 12 publications · 890 citations
12
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10 publications · 430 citations
10
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10 publications · 431 citations
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