Compounds > sf 2197
Page last updated: 2024-09-03

sf 2197 and acetylcysteine

sf 2197 has been researched along with acetylcysteine in 4 studies

Compound Research Comparison

Studies
(sf 2197)		Trials
(sf 2197)		Recent Studies (post-2010)
(sf 2197)		Studies
(acetylcysteine)		Trials
(acetylcysteine)		Recent Studies (post-2010) (acetylcysteine)
60114,5801,0465,960

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's3 (75.00)18.2507
2000's0 (0.00)29.6817
2010's1 (25.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Ishii, M; Ogita, T; Shimada, K; Tanzawa, K1
Enokita, R; Ishii, M; Negishi, T; Ogita, T; Okazaki, T; Sato, A; Suzuki, K; Tamaki, K; Tanzawa, K1
Kurihara, S; Monma, S; Oikawa, T; Shimada, K; Sugimura, Y; Tamaki, K; Tanzawa, K1
Bekiesch, P; Gross, H; Kaysser, L; Keinhörster, D; Kirchner, N; Kulik, A; Lacret, R; Leipoldt, F; Popadić, D; Santos-Aberturas, J; Stegmann, DP; Truman, AW; Wolf, F1

Other Studies

4 other study(ies) available for sf 2197 and acetylcysteine

ArticleYear
Matlystatins, new inhibitors of typeIV collagenases from Actinomadura atramentaria. II. Biological activities.
    The Journal of antibiotics, 1992, Volume: 45, Issue:11

    Topics: Acetylcysteine; Actinomycetales; Aminopeptidases; Anti-Bacterial Agents; Bacteria; Basement Membrane; Binding, Competitive; CD13 Antigens; Fibrosarcoma; Fungi; Gelatin; Humans; Matrix Metalloproteinase 9; Matrix Metalloproteinase Inhibitors; Molecular Weight; Pyridazines; Thermolysin; Tumor Cells, Cultured

1992
Matlystatins, new inhibitors of typeIV collagenases from Actinomadura atramentaria. I. Taxonomy, fermentation, isolation, and physico-chemical properties of matlystatin-group compounds.
    The Journal of antibiotics, 1992, Volume: 45, Issue:11

    Topics: Acetylcysteine; Actinomycetales; Anti-Bacterial Agents; Chromatography; Chromatography, High Pressure Liquid; Fermentation; Magnetic Resonance Spectroscopy; Matrix Metalloproteinase 9; Matrix Metalloproteinase Inhibitors; Molecular Structure; Pyridazines; Spectrometry, Mass, Fast Atom Bombardment

1992
Synthesis and structure-activity relationships of gelatinase inhibitors derived from matlystatins.
    Chemical & pharmaceutical bulletin, 1995, Volume: 43, Issue:11

    Topics: Acetylcysteine; Chromatography, High Pressure Liquid; Dipeptides; Fibrosarcoma; Gelatinases; Humans; Magnetic Resonance Spectroscopy; Metalloendopeptidases; Protease Inhibitors; Pyridazines; Structure-Activity Relationship; Substrate Specificity; Succinates; Thermolysin; Tumor Cells, Cultured

1995
Warhead biosynthesis and the origin of structural diversity in hydroxamate metalloproteinase inhibitors.
    Nature communications, 2017, 12-06, Volume: 8, Issue:1

    Topics: Acetylcysteine; Actinobacteria; Acyl Coenzyme A; Biosynthetic Pathways; Carboxy-Lyases; Gene Deletion; Gene Expression Profiling; Gene Expression Regulation, Bacterial; Genes, Bacterial; Hydroxamic Acids; Matrix Metalloproteinase Inhibitors; Metalloproteases; Multigene Family; Ornithine; Oxidoreductases; Propionates; Protease Inhibitors; Pyridazines; Sequence Deletion; Streptomyces

2017