Compounds > 6-chloropurine 9-beta-d-ribofuranosyl 5'-monophosphate
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6-chloropurine 9-beta-d-ribofuranosyl 5'-monophosphate and iodoacetamide

6-chloropurine 9-beta-d-ribofuranosyl 5'-monophosphate has been researched along with iodoacetamide in 3 studies

*Iodoacetamide: An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate. [MeSH]

*Iodoacetamide: An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate. [MeSH]

Compound Research Comparison

Studies
(6-chloropurine 9-beta-d-ribofuranosyl 5'-monophosphate)		Trials
(6-chloropurine 9-beta-d-ribofuranosyl 5'-monophosphate)		Recent Studies (post-2010)
(6-chloropurine 9-beta-d-ribofuranosyl 5'-monophosphate)		Studies
(iodoacetamide)		Trials
(iodoacetamide)		Recent Studies (post-2010) (iodoacetamide)
14021,5020130

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19901 (33.33)18.7374
1990's2 (66.67)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Drabble, WT; Gilbert, HJ1
Huete-Pérez, JA; Wang, CC; Whitby, FG; Wu, JC1
Antonino, LC; Straub, K; Wu, JC1

Other Studies

3 other study(ies) available for 6-chloropurine 9-beta-d-ribofuranosyl 5'-monophosphate and iodoacetamide

ArticleYear
Active-site modification of native and mutant forms of inosine 5'-monophosphate dehydrogenase from Escherichia coli K12.
    The Biochemical journal, 1980, Nov-01, Volume: 191, Issue:2

    Topics: Binding Sites; Enzyme Activation; Escherichia coli; IMP Dehydrogenase; Inosine Monophosphate; Iodoacetamide; Isoenzymes; Ketone Oxidoreductases; Kinetics; Mutation; Nucleotides; Purine Nucleotides; Spectrophotometry

1980
Identification of the IMP binding site in the IMP dehydrogenase from Tritrichomonas foetus.
    Biochemistry, 1995, Oct-24, Volume: 34, Issue:42

    Topics: Animals; Base Sequence; Binding Sites; Chromatography, High Pressure Liquid; Cysteine; Electrophoresis, Polyacrylamide Gel; Enzyme Inhibitors; IMP Dehydrogenase; Inosine Monophosphate; Iodoacetamide; Kinetics; Molecular Sequence Data; Recombinant Proteins; Substrate Specificity; Thionucleotides; Tritrichomonas foetus; Trypsin

1995
Probing the active site of human IMP dehydrogenase using halogenated purine riboside 5'-monophosphates and covalent modification reagents.
    Biochemistry, 1994, Feb-22, Volume: 33, Issue:7

    Topics: Binding Sites; Chromatography, High Pressure Liquid; Humans; IMP Dehydrogenase; Indicators and Reagents; Inosine Monophosphate; Iodoacetamide; Kinetics; Mass Spectrometry; NAD; Trypsin

1994