1,n(6)-ethenoadenosine diphosphate and 3'-o-(n-methylanthraniloyl)adenosine 5'-diphosphate

1,n(6)-ethenoadenosine diphosphate has been researched along with 3'-o-(n-methylanthraniloyl)adenosine 5'-diphosphate in 2 studies

Compound Research Comparison

Studies (1,n(6)-ethenoadenosine diphosphate)	Trials (1,n(6)-ethenoadenosine diphosphate)	Recent Studies (post-2010) (1,n(6)-ethenoadenosine diphosphate)	Studies (3'-o-(n-methylanthraniloyl)adenosine 5'-diphosphate)	Trials (3'-o-(n-methylanthraniloyl)adenosine 5'-diphosphate)	Recent Studies (post-2010) (3'-o-(n-methylanthraniloyl)adenosine 5'-diphosphate)
37	0	0	48	0	2

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
Bujalowski, W; Klonowska, MM	1
Bujalowski, W; Jezewska, MJ	1

Other Studies

2 other study(ies) available for 1,n(6)-ethenoadenosine diphosphate and 3'-o-(n-methylanthraniloyl)adenosine 5'-diphosphate

Article	Year
Structural characteristics of the nucleotide-binding site of Escherichia coli primary replicative helicase DnaB protein. Studies with ribose and base-modified fluorescent nucleotide analogs. Biochemistry, 1994, Apr-19, Volume: 33, Issue:15 Topics: Adenine; Adenosine Diphosphate; Bacterial Proteins; Binding Sites; DNA Helicases; DnaB Helicases; Escherichia coli; Fluorescence Polarization; Fluorescent Dyes; Nucleotides; ortho-Aminobenzoates; Ribose; Spectrometry, Fluorescence	1994
Kinetic mechanism of nucleotide cofactor binding to Escherichia coli replicative helicase DnaB protein. stopped-flow kinetic studies using fluorescent, ribose-, and base-modified nucleotide analogues. Biochemistry, 2000, Feb-29, Volume: 39, Issue:8 Topics: Adenosine Diphosphate; Adenylyl Imidodiphosphate; Bacterial Proteins; Computer Simulation; DNA Helicases; DnaB Helicases; Dose-Response Relationship, Drug; Escherichia coli; Fluorescent Dyes; Kinetics; Models, Chemical; Models, Statistical; Nucleotides; ortho-Aminobenzoates; Protein Conformation; Ribose; Spectrometry, Fluorescence; Thermodynamics; Time Factors	2000

Article

Year

Structural characteristics of the nucleotide-binding site of Escherichia coli primary replicative helicase DnaB protein. Studies with ribose and base-modified fluorescent nucleotide analogs.

Biochemistry, 1994, Apr-19, Volume: 33, Issue:15

Topics: Adenine; Adenosine Diphosphate; Bacterial Proteins; Binding Sites; DNA Helicases; DnaB Helicases; Escherichia coli; Fluorescence Polarization; Fluorescent Dyes; Nucleotides; ortho-Aminobenzoates; Ribose; Spectrometry, Fluorescence

1994

Kinetic mechanism of nucleotide cofactor binding to Escherichia coli replicative helicase DnaB protein. stopped-flow kinetic studies using fluorescent, ribose-, and base-modified nucleotide analogues.

Biochemistry, 2000, Feb-29, Volume: 39, Issue:8

Topics: Adenosine Diphosphate; Adenylyl Imidodiphosphate; Bacterial Proteins; Computer Simulation; DNA Helicases; DnaB Helicases; Dose-Response Relationship, Drug; Escherichia coli; Fluorescent Dyes; Kinetics; Models, Chemical; Models, Statistical; Nucleotides; ortho-Aminobenzoates; Protein Conformation; Ribose; Spectrometry, Fluorescence; Thermodynamics; Time Factors

2000