Page last updated: 2024-09-03

beta-lipotropin, gln(9)- and adenosine monophosphate

beta-lipotropin, gln(9)- has been researched along with adenosine monophosphate in 2 studies

Compound Research Comparison

Studies (beta-lipotropin, gln(9)-)	Trials (beta-lipotropin, gln(9)-)	Recent Studies (post-2010) (beta-lipotropin, gln(9)-)	Studies (adenosine monophosphate)	Trials (adenosine monophosphate)	Recent Studies (post-2010) (adenosine monophosphate)
48	0	24	11,432	257	2,798

Protein Interaction Comparison

Protein	Taxonomy	adenosine monophosphate (IC50)
Fructose-1,6-bisphosphatase 1	Sus scrofa (pig)	1.3
Fructose-1,6-bisphosphatase 1	Homo sapiens (human)	2.6436
Cytochrome P450 2C9	Homo sapiens (human)	2.6
Proto-oncogene tyrosine-protein kinase Src	Homo sapiens (human)	0.1
Amine oxidase [flavin-containing] B	Rattus norvegicus (Norway rat)	0.44
Histamine H3 receptor	Rattus norvegicus (Norway rat)	0.8

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
Marahiel, MA; May, JJ; Wendrich, TM	1
Kessler, N; Marahiel, MA; May, JJ; Stubbs, MT	1

Other Studies

2 other study(ies) available for beta-lipotropin, gln(9)- and adenosine monophosphate

Article	Year
The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin. The Journal of biological chemistry, 2001, Mar-09, Volume: 276, Issue:10 Topics: Adenosine Monophosphate; Adenosine Triphosphate; Amino Acids; Bacillus subtilis; Base Sequence; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Esters; Hydroxybenzoates; Indicators and Reagents; Mass Spectrometry; Models, Genetic; Molecular Sequence Data; Oligopeptides; Operon; Plasmids; Protein Processing, Post-Translational; Protein Structure, Tertiary; Recombinant Proteins; Sequence Analysis, DNA; Sequence Homology, Nucleic Acid; Siderophores; Sulfhydryl Compounds	2001
Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases. Proceedings of the National Academy of Sciences of the United States of America, 2002, Sep-17, Volume: 99, Issue:19 Topics: Adenosine Monophosphate; Amino Acid Motifs; Amino Acid Sequence; Bacillus subtilis; Catalytic Domain; Cloning, Molecular; Crystallography, X-Ray; Esters; Models, Molecular; Molecular Sequence Data; Oligopeptides; Peptide Synthases; Protein Conformation; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Static Electricity; Substrate Specificity	2002

Article

Year

The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin.

The Journal of biological chemistry, 2001, Mar-09, Volume: 276, Issue:10

Topics: Adenosine Monophosphate; Adenosine Triphosphate; Amino Acids; Bacillus subtilis; Base Sequence; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Esters; Hydroxybenzoates; Indicators and Reagents; Mass Spectrometry; Models, Genetic; Molecular Sequence Data; Oligopeptides; Operon; Plasmids; Protein Processing, Post-Translational; Protein Structure, Tertiary; Recombinant Proteins; Sequence Analysis, DNA; Sequence Homology, Nucleic Acid; Siderophores; Sulfhydryl Compounds

2001

Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases.

Proceedings of the National Academy of Sciences of the United States of America, 2002, Sep-17, Volume: 99, Issue:19

Topics: Adenosine Monophosphate; Amino Acid Motifs; Amino Acid Sequence; Bacillus subtilis; Catalytic Domain; Cloning, Molecular; Crystallography, X-Ray; Esters; Models, Molecular; Molecular Sequence Data; Oligopeptides; Peptide Synthases; Protein Conformation; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Static Electricity; Substrate Specificity

2002