"Schiff Bases" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Condensation products of aromatic amines and aldehydes forming azomethines substituted on the N atom, containing the general formula R-N:CHR. (From Grant & Hackh's Chemical Dictionary, 5th ed)
| Descriptor ID |
D012545
|
| MeSH Number(s) |
D02.491.784
|
| Concept/Terms |
Schiff Bases- Schiff Bases
- Bases, Schiff
- Schiff Base
- Base, Schiff
|
Below are MeSH descriptors whose meaning is more general than "Schiff Bases".
Below are MeSH descriptors whose meaning is more specific than "Schiff Bases".
This graph shows the total number of publications written about "Schiff Bases" by people in this website by year, and whether "Schiff Bases" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1994 | 0 | 1 | 1 |
| 1995 | 0 | 3 | 3 |
| 1996 | 0 | 3 | 3 |
| 1997 | 0 | 1 | 1 |
| 1999 | 0 | 1 | 1 |
| 2002 | 0 | 1 | 1 |
| 2005 | 0 | 1 | 1 |
| 2008 | 0 | 1 | 1 |
| 2010 | 0 | 1 | 1 |
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Below are the most recent publications written about "Schiff Bases" by people in Profiles.
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Identification of the structural determinants for the stability of substrate and aminoacrylate external Schiff bases in O-acetylserine sulfhydrylase-A. Biochemistry. 2010 Jul 27; 49(29):6093-103.
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Role of Histidine-152 in cofactor orientation in the PLP-dependent O-acetylserine sulfhydrylase reaction. Arch Biochem Biophys. 2008 Apr 15; 472(2):115-25.
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Tertiary structure and spectral tuning of UV and violet pigments in vertebrates. Gene. 2006 Jan 03; 365:95-103.
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Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate. Biochemistry. 2005 Dec 06; 44(48):15930-6.
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Detection of intermediates in reactions catalyzed by PLP-dependent enzymes: O-acetylserine sulfhydrylase and serine-glyoxalate aminotransferase. Methods Enzymol. 2002; 354:223-37.
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Time-resolved fluorescence of O-acetylserine sulfhydrylase. Biochim Biophys Acta. 1999 Jan 11; 1429(2):317-30.
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Time-resolved fluorescence of O-acetylserine sulfhydrylase catalytic intermediates. Biochemistry. 1997 Dec 09; 36(49):15419-27.
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A change in the internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst. Biochemistry. 1996 Oct 15; 35(41):13485-93.
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Kinetic isotope effects as a probe of the beta-elimination reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 1996 May 21; 35(20):6358-65.
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Formation of the alpha-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase. Biochemistry. 1996 Apr 16; 35(15):4776-83.