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

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

Compound Research Comparison

Studies (3-(trifluoromethyl)-3-(3-iodophenyl)diazirine)	Trials (3-(trifluoromethyl)-3-(3-iodophenyl)diazirine)	Recent Studies (post-2010) (3-(trifluoromethyl)-3-(3-iodophenyl)diazirine)	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)
76	0	0	6	0	0

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	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Blanton, MP; McCardy, EA	1
Córsico, B; Garda, HA; Toledo, JD	1

Other Studies

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

Article	Year
Identifying the lipid-protein interface and transmembrane structural transitions of the Torpedo Na,K-ATPase using hydrophobic photoreactive probes. Biochemistry, 2000, Nov-07, Volume: 39, Issue:44 Topics: Animals; Azirines; Endopeptidases; Hydrolysis; Iodine Radioisotopes; Membrane Lipids; Membrane Proteins; Peptide Fragments; Peptide Mapping; Phosphatidylcholines; Photoaffinity Labels; Photochemistry; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Structure-Activity Relationship; Torpedo	2000
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

Identifying the lipid-protein interface and transmembrane structural transitions of the Torpedo Na,K-ATPase using hydrophobic photoreactive probes.

Biochemistry, 2000, Nov-07, Volume: 39, Issue:44

Topics: Animals; Azirines; Endopeptidases; Hydrolysis; Iodine Radioisotopes; Membrane Lipids; Membrane Proteins; Peptide Fragments; Peptide Mapping; Phosphatidylcholines; Photoaffinity Labels; Photochemistry; Protein Conformation; Sodium-Potassium-Exchanging ATPase; Structure-Activity Relationship; Torpedo

2000

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