methionine sulfoxide and Inflammation

methionine sulfoxide has been researched along with Inflammation in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	1 (50.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Barbasz, A; Golda, A; Kozik, A; Mak, P; Rapala-Kozik, M; Silberring, J; Suder, P	1
Belaaouaj, A; Fu, X; Heinecke, JW; Shao, B; Verlinde, CL	1

Other Studies

2 other study(ies) available for methionine sulfoxide and Inflammation

Article	Year
Myeloperoxidase-catalyzed oxidative inactivation of human kininogens: the impairment of kinin-precursor and prekallikrein-binding functions. Biological chemistry, 2011, Volume: 392, Issue:3 Topics: Amino Acid Sequence; Bradykinin; Humans; Inflammation; Kininogens; Kinins; Methionine; Molecular Sequence Data; Peroxidase; Phagocytes; Prekallikrein; Reactive Oxygen Species; Tryptophan	2011
Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: an oxidative mechanism for regulation of serine proteinases by myeloperoxidase. The Journal of biological chemistry, 2005, Aug-12, Volume: 280, Issue:32 Topics: Animals; Catalytic Domain; Cathepsin G; Cathepsins; Chromatography, High Pressure Liquid; Dose-Response Relationship, Drug; Humans; Hydrogen Peroxide; Hypochlorous Acid; Inflammation; Mass Spectrometry; Methionine; Mice; Models, Chemical; Models, Molecular; Neutrophils; Oxidants; Oxygen; Peptides; Peroxidase; Protein Binding; Serine Endopeptidases; Spectrometry, Mass, Electrospray Ionization; Time Factors	2005

Article

Year

Myeloperoxidase-catalyzed oxidative inactivation of human kininogens: the impairment of kinin-precursor and prekallikrein-binding functions.

Biological chemistry, 2011, Volume: 392, Issue:3

Topics: Amino Acid Sequence; Bradykinin; Humans; Inflammation; Kininogens; Kinins; Methionine; Molecular Sequence Data; Peroxidase; Phagocytes; Prekallikrein; Reactive Oxygen Species; Tryptophan

2011

Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: an oxidative mechanism for regulation of serine proteinases by myeloperoxidase.

The Journal of biological chemistry, 2005, Aug-12, Volume: 280, Issue:32

Topics: Animals; Catalytic Domain; Cathepsin G; Cathepsins; Chromatography, High Pressure Liquid; Dose-Response Relationship, Drug; Humans; Hydrogen Peroxide; Hypochlorous Acid; Inflammation; Mass Spectrometry; Methionine; Mice; Models, Chemical; Models, Molecular; Neutrophils; Oxidants; Oxygen; Peptides; Peroxidase; Protein Binding; Serine Endopeptidases; Spectrometry, Mass, Electrospray Ionization; Time Factors

2005