proline and coenzyme f420

proline has been researched along with coenzyme f420 in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	1 (50.00)	2.80

Authors

Authors	Studies
Aufhammer, SW; Ermler, U; Hagemeier, CH; Shima, S; Thauer, RK; Warkentin, E	1
Bashiri, G; Gazak, R; Janata, J; Kadlcik, S; Kamenik, Z; Kuzma, M; Man, P; Pavlikova, M; Steiningerova, L	1

Other Studies

2 other study(ies) available for proline and coenzyme f420

Article	Year
Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420: Architecture of the F420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family. Protein science : a publication of the Protein Society, 2005, Volume: 14, Issue:7 Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalysis; Crystallography, X-Ray; Flavin Mononucleotide; Flavins; Luciferases; Methanobacterium; Models, Molecular; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Peptides; Proline; Protein Binding; Protein Conformation; Riboflavin; Sequence Homology, Amino Acid	2005
Different Reaction Specificities of F Journal of the American Chemical Society, 2020, 02-19, Volume: 142, Issue:7 Topics: Benzodiazepines; Catalysis; Depsipeptides; Lincomycin; Models, Molecular; Oxidoreductases; Peptides, Cyclic; Proline; Pyrroles; Riboflavin; Substrate Specificity; Tyrosine	2020

Article

Year

Crystal structure of methylenetetrahydromethanopterin reductase (Mer) in complex with coenzyme F420: Architecture of the F420/FMN binding site of enzymes within the nonprolyl cis-peptide containing bacterial luciferase family.

Protein science : a publication of the Protein Society, 2005, Volume: 14, Issue:7

Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Bacterial Proteins; Binding Sites; Catalysis; Crystallography, X-Ray; Flavin Mononucleotide; Flavins; Luciferases; Methanobacterium; Models, Molecular; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Peptides; Proline; Protein Binding; Protein Conformation; Riboflavin; Sequence Homology, Amino Acid

2005

Different Reaction Specificities of F

Journal of the American Chemical Society, 2020, 02-19, Volume: 142, Issue:7

Topics: Benzodiazepines; Catalysis; Depsipeptides; Lincomycin; Models, Molecular; Oxidoreductases; Peptides, Cyclic; Proline; Pyrroles; Riboflavin; Substrate Specificity; Tyrosine

2020