n-propyl 2-pyridyl disulfide and 2,2'-dipyridyl

n-propyl 2-pyridyl disulfide has been researched along with 2,2'-dipyridyl in 2 studies

*2,2'-Dipyridyl: A reagent used for the determination of iron. [MeSH]

Compound Research Comparison

Studies (n-propyl 2-pyridyl disulfide)	Trials (n-propyl 2-pyridyl disulfide)	Recent Studies (post-2010) (n-propyl 2-pyridyl disulfide)	Studies (2,2'-dipyridyl)	Trials (2,2'-dipyridyl)	Recent Studies (post-2010) (2,2'-dipyridyl)
5	0	1	2,251	0	894

Protein Interaction Comparison

Protein	Taxonomy	n-propyl 2-pyridyl disulfide (IC50)	2,2'-dipyridyl (IC50)
Deoxyhypusine hydroxylase	Homo sapiens (human)		5

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	2 (100.00)	18.7374
1990's	0 (0.00)	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
Brocklehurst, K; Kowlessur, D; O'Driscoll, M; Patel, G; Quenby, S; Salih, E; Templeton, W; Thomas, EW; Willenbrock, F	1
Brocklehurst, K; Malthouse, JP	1

Other Studies

2 other study(ies) available for n-propyl 2-pyridyl disulfide and 2,2'-dipyridyl

Article	Year
Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding. The Biochemical journal, 1987, May-15, Volume: 244, Issue:1 Topics: 2,2'-Dipyridyl; Acetamides; Binding Sites; Cysteine Endopeptidases; Disulfides; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Phenylalanine; Pyridines; Structure-Activity Relationship; Substrate Specificity; Sulfhydryl Compounds	1987
Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin. The Biochemical journal, 1980, Dec-01, Volume: 191, Issue:3 Topics: 2,2'-Dipyridyl; Benzoxazoles; Binding Sites; Chemical Phenomena; Chemistry; Disulfides; Endopeptidases; Ficain; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Papain; Protein Conformation; Pyridines	1980

Article

Year

Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding.

The Biochemical journal, 1987, May-15, Volume: 244, Issue:1

Topics: 2,2'-Dipyridyl; Acetamides; Binding Sites; Cysteine Endopeptidases; Disulfides; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Phenylalanine; Pyridines; Structure-Activity Relationship; Substrate Specificity; Sulfhydryl Compounds

1987

Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin.

The Biochemical journal, 1980, Dec-01, Volume: 191, Issue:3

Topics: 2,2'-Dipyridyl; Benzoxazoles; Binding Sites; Chemical Phenomena; Chemistry; Disulfides; Endopeptidases; Ficain; Hydrogen-Ion Concentration; Kinetics; Models, Chemical; Papain; Protein Conformation; Pyridines

1980