Page last updated: 2024-09-05

n-acetylglucosaminitol and muramidase

n-acetylglucosaminitol has been researched along with muramidase in 3 studies

Compound Research Comparison

Studies
(n-acetylglucosaminitol)
Trials
(n-acetylglucosaminitol)
Recent Studies (post-2010)
(n-acetylglucosaminitol)
Studies
(muramidase)
Trials
(muramidase)
Recent Studies (post-2010) (muramidase)
70023,7772075,249

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19901 (33.33)18.7374
1990's1 (33.33)18.2507
2000's1 (33.33)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Segawa, S; Sugihara, M1
Imoto, T; Kainosho, M; Mine, S; Tate, S; Ueda, T1
Imoto, T; Kino, S; Ohkuri, T; Ueda, T; Yoshida, Y1

Other Studies

3 other study(ies) available for n-acetylglucosaminitol and muramidase

ArticleYear
Characterization of the transition state of lysozyme unfolding. II. Effects of the intrachain crosslinking and the inhibitor binding on the transition state.
    Biopolymers, 1984, Volume: 23, Issue:11 Pt 2

    Topics: Acetylglucosamine; Animals; Chickens; Egg White; Kinetics; Muramidase; Oligosaccharides; Protein Conformation; Trisaccharides

1984
Analysis of the relationship between enzyme activity and its internal motion using nuclear magnetic resonance: 15N relaxation studies of wild-type and mutant lysozyme.
    Journal of molecular biology, 1999, Mar-12, Volume: 286, Issue:5

    Topics: Acetylglucosamine; Anisotropy; Binding Sites; Escherichia coli; Hydrogen Bonding; Kinetics; Models, Molecular; Muramidase; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protons; Structure-Activity Relationship; Trisaccharides

1999
Elucidation of the relationship between enzyme activity and internal motion using a lysozyme stabilized by cavity-filling mutations.
    Cellular and molecular life sciences : CMLS, 2005, Volume: 62, Issue:9

    Topics: Acetylglucosamine; Animals; Chickens; Chitin; Enzyme Stability; Genotype; Kinetics; Models, Molecular; Muramidase; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Tertiary; Temperature

2005