1-palmitoyl-2-(decanedioyl mono-(2-iodo-4-(3-trifluoromethyl-3h-diazirin-3-yl)benzyl)ester)glycero-3-phosphocholine and hydroxylamine

1-palmitoyl-2-(decanedioyl mono-(2-iodo-4-(3-trifluoromethyl-3h-diazirin-3-yl)benzyl)ester)glycero-3-phosphocholine has been researched along with hydroxylamine in 1 studies

*Hydroxylamine: A colorless inorganic compound (HONH2) used in organic synthesis and as a reducing agent, due to its ability to donate nitric oxide. [MeSH]

Compound Research Comparison

Studies (1-palmitoyl-2-(decanedioyl mono-(2-iodo-4-(3-trifluoromethyl-3h-diazirin-3-yl)benzyl)ester)glycero-3-phosphocholine)	Trials (1-palmitoyl-2-(decanedioyl mono-(2-iodo-4-(3-trifluoromethyl-3h-diazirin-3-yl)benzyl)ester)glycero-3-phosphocholine)	Recent Studies (post-2010) (1-palmitoyl-2-(decanedioyl mono-(2-iodo-4-(3-trifluoromethyl-3h-diazirin-3-yl)benzyl)ester)glycero-3-phosphocholine)	Studies (hydroxylamine)	Trials (hydroxylamine)	Recent Studies (post-2010) (hydroxylamine)
6	0	0	1,711	3	363

Research

Studies (1)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	1 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Córsico, B; Garda, HA; Toledo, JD	1

Other Studies

1 other study(ies) available for 1-palmitoyl-2-(decanedioyl mono-(2-iodo-4-(3-trifluoromethyl-3h-diazirin-3-yl)benzyl)ester)glycero-3-phosphocholine and hydroxylamine

Article	Year
Evidence for a central apolipoprotein A-I domain loosely bound to lipids in discoidal lipoproteins that is capable of penetrating the bilayer of phospholipid vesicles. The Journal of biological chemistry, 2001, May-18, Volume: 276, Issue:20 Topics: Amino Acid Sequence; Apolipoprotein A-I; Azirines; Binding Sites; Cyanogen Bromide; Humans; Hydroxylamine; Iodine Radioisotopes; Lipid Bilayers; Models, Biological; Models, Molecular; Molecular Conformation; Molecular Sequence Data; Peptide Fragments; Phosphatidylcholines; Photoaffinity Labels; Protein Structure, Secondary	2001

Article

Year

Evidence for a central apolipoprotein A-I domain loosely bound to lipids in discoidal lipoproteins that is capable of penetrating the bilayer of phospholipid vesicles.

The Journal of biological chemistry, 2001, May-18, Volume: 276, Issue:20

Topics: Amino Acid Sequence; Apolipoprotein A-I; Azirines; Binding Sites; Cyanogen Bromide; Humans; Hydroxylamine; Iodine Radioisotopes; Lipid Bilayers; Models, Biological; Models, Molecular; Molecular Conformation; Molecular Sequence Data; Peptide Fragments; Phosphatidylcholines; Photoaffinity Labels; Protein Structure, Secondary

2001