Page last updated: 2024-09-03

chapso and carbamates

chapso has been researched along with carbamates in 1 studies

*Carbamates: Derivatives of carbamic acid, H2NC(=O)OH. Included under this heading are N-substituted and O-substituted carbamic acids. In general carbamate esters are referred to as urethanes, and polymers that include repeating units of carbamate are referred to as POLYURETHANES. Note however that polyurethanes are derived from the polymerization of ISOCYANATES and the singular term URETHANE refers to the ethyl ester of carbamic acid. [MeSH]

*Carbamates: Derivatives of carbamic acid, H2NC(=O)OH. Included under this heading are N-substituted and O-substituted carbamic acids. In general carbamate esters are referred to as urethanes, and polymers that include repeating units of carbamate are referred to as POLYURETHANES. Note however that polyurethanes are derived from the polymerization of ISOCYANATES and the singular term URETHANE refers to the ethyl ester of carbamic acid. [MeSH]

Compound Research Comparison

Studies
(chapso)
Trials
(chapso)
Recent Studies (post-2010)
(chapso)
Studies
(carbamates)
Trials
(carbamates)
Recent Studies (post-2010) (carbamates)
650913,7179854,744

Research

Studies (1)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's1 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
DiMuzio-Mower, J; Gardell, SJ; Huang, Q; Lai, MT; Li, YM; Sardana, MK; Shafer, JA; Shi, XP; Xu, M; Yin, KC1

Other Studies

1 other study(ies) available for chapso and carbamates

ArticleYear
Presenilin 1 is linked with gamma-secretase activity in the detergent solubilized state.
    Proceedings of the National Academy of Sciences of the United States of America, 2000, May-23, Volume: 97, Issue:11

    Topics: Alzheimer Disease; Amyloid beta-Protein Precursor; Amyloid Precursor Protein Secretases; Aspartic Acid Endopeptidases; Carbamates; Cell Fractionation; Cell Membrane; Cholic Acids; Detergents; Dipeptides; Endopeptidases; HeLa Cells; Humans; Membrane Proteins; Neoplasm Proteins; Pepstatins; Presenilin-1; Protease Inhibitors; Recombinant Fusion Proteins; Solubility; Substrate Specificity

2000