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n-epsilon-acetyllysine and chlorine

n-epsilon-acetyllysine has been researched along with chlorine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	2 (100.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Crowley, JR; d'Avignon, A; Gaut, JP; Hazen, SL; Heinecke, JW; Hsu, FF	1
Anderson, MM; d'Avignon, A; Hazen, SL; Heinecke, JW; Hsu, FF	1

Other Studies

2 other study(ies) available for n-epsilon-acetyllysine and chlorine

Article	Year
p-Hydroxyphenylacetaldehyde, the major product of L-tyrosine oxidation by the myeloperoxidase-H2O2-chloride system of phagocytes, covalently modifies epsilon-amino groups of protein lysine residues. The Journal of biological chemistry, 1997, Jul-04, Volume: 272, Issue:27 Topics: Acetaldehyde; Amino Acids; Animals; Cattle; Chlorides; Chromatography, High Pressure Liquid; Humans; Hydrogen Peroxide; Inflammation; Lysine; Magnetic Resonance Spectroscopy; Neutrophils; Peroxidase; Phagocytes; Phenol; Proteins; Schiff Bases; Serum Albumin, Bovine; Tyrosine	1997
Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway. The Journal of biological chemistry, 1998, Feb-27, Volume: 273, Issue:9 Topics: Aldehydes; Amino Acids; Chloramines; Chlorides; Humans; Hypochlorous Acid; Lysine; Mass Spectrometry; Models, Chemical; Neutrophils; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Peroxidase; Phenylalanine; Tyrosine	1998

Article

Year

p-Hydroxyphenylacetaldehyde, the major product of L-tyrosine oxidation by the myeloperoxidase-H2O2-chloride system of phagocytes, covalently modifies epsilon-amino groups of protein lysine residues.

The Journal of biological chemistry, 1997, Jul-04, Volume: 272, Issue:27

Topics: Acetaldehyde; Amino Acids; Animals; Cattle; Chlorides; Chromatography, High Pressure Liquid; Humans; Hydrogen Peroxide; Inflammation; Lysine; Magnetic Resonance Spectroscopy; Neutrophils; Peroxidase; Phagocytes; Phenol; Proteins; Schiff Bases; Serum Albumin, Bovine; Tyrosine

1997

Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway.

The Journal of biological chemistry, 1998, Feb-27, Volume: 273, Issue:9

Topics: Aldehydes; Amino Acids; Chloramines; Chlorides; Humans; Hypochlorous Acid; Lysine; Mass Spectrometry; Models, Chemical; Neutrophils; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Peroxidase; Phenylalanine; Tyrosine

1998