Page last updated: 2024-09-03

1,4-diamino-2-butyne and phenylhydrazine

1,4-diamino-2-butyne has been researched along with phenylhydrazine in 2 studies

Compound Research Comparison

Studies (1,4-diamino-2-butyne)	Trials (1,4-diamino-2-butyne)	Recent Studies (post-2010) (1,4-diamino-2-butyne)	Studies (phenylhydrazine)	Trials (phenylhydrazine)	Recent Studies (post-2010) (phenylhydrazine)
9	0	1	921	0	110

Protein Interaction Comparison

Protein	Taxonomy	phenylhydrazine (IC50)
Cytochrome P450 1A2	Homo sapiens (human)	8
Cytochrome P450 3A4	Homo sapiens (human)	0.9
Cytochrome P450 2D6	Homo sapiens (human)	3
Cytochrome P450 2C9	Homo sapiens (human)	6
Polyunsaturated fatty acid lipoxygenase ALOX15	Oryctolagus cuniculus (rabbit)	1.666
Indoleamine 2,3-dioxygenase 1	Homo sapiens (human)	0.5933
Indoleamine 2,3-dioxygenase 1	Mus musculus (house mouse)	0.2
Cytochrome P450 2C19	Homo sapiens (human)	5
Prostaglandin G/H synthase 2	Homo sapiens (human)	1.514
Mu-type opioid receptor	Mus musculus (house mouse)	0.25

Research

Studies (2)

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

Authors

Authors	Studies
Adachi, O; Frébort, I; Luhová, L; Matsushita, K; Pec, P; Toyama, H	1
Dooley, DM; Elmore, BO; Kuchar, JA; Sayre, LM; Shepard, EM; Smith, J	1

Other Studies

2 other study(ies) available for 1,4-diamino-2-butyne and phenylhydrazine

Article	Year
Active-site covalent modifications of quinoprotein amine oxidases from Aspergillus niger. Evidence for binding of the mechanism-based inhibitor, 1,4-diamino-2-butyne, to residue Lys356 involved in the catalytic cycle. European journal of biochemistry, 1994, Nov-01, Volume: 225, Issue:3 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Aspergillus niger; Binding Sites; Diamines; Diethyl Pyrocarbonate; Kinetics; Lysine; Models, Chemical; Molecular Sequence Data; Phenylhydrazines; Schiff Bases; Sequence Homology, Amino Acid; Spectrophotometry; Substrate Specificity	1994
Towards the development of selective amine oxidase inhibitors. Mechanism-based inhibition of six copper containing amine oxidases. European journal of biochemistry, 2002, Volume: 269, Issue:15 Topics: Amine Oxidase (Copper-Containing); Animals; Bacteria; Diamines; Dihydroxyphenylalanine; Drug Design; Enzyme Inhibitors; Mammals; Models, Molecular; Naphthalenes; Phenylhydrazines; Protein Conformation; Protein-Lysine 6-Oxidase; Species Specificity; Time Factors; Titrimetry	2002

Article

Year

Active-site covalent modifications of quinoprotein amine oxidases from Aspergillus niger. Evidence for binding of the mechanism-based inhibitor, 1,4-diamino-2-butyne, to residue Lys356 involved in the catalytic cycle.

European journal of biochemistry, 1994, Nov-01, Volume: 225, Issue:3

Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Aspergillus niger; Binding Sites; Diamines; Diethyl Pyrocarbonate; Kinetics; Lysine; Models, Chemical; Molecular Sequence Data; Phenylhydrazines; Schiff Bases; Sequence Homology, Amino Acid; Spectrophotometry; Substrate Specificity

1994

Towards the development of selective amine oxidase inhibitors. Mechanism-based inhibition of six copper containing amine oxidases.

European journal of biochemistry, 2002, Volume: 269, Issue:15

Topics: Amine Oxidase (Copper-Containing); Animals; Bacteria; Diamines; Dihydroxyphenylalanine; Drug Design; Enzyme Inhibitors; Mammals; Models, Molecular; Naphthalenes; Phenylhydrazines; Protein Conformation; Protein-Lysine 6-Oxidase; Species Specificity; Time Factors; Titrimetry

2002