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adenosine monophosphate and formycins

adenosine monophosphate has been researched along with formycins in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19905 (62.50)18.7374
1990's3 (37.50)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
DeWolf, WE; Fullin, FA; Schramm, VL1
Ikehara, M; Tezuka, T; Uesugi, S1
Jahngen, EG; Rossomando, EF1
Fromm, HJ; Scheffler, JE1
Dovey, HF; McKerrow, JH; Wang, CC1
Schobert, B1
Derbyshire, DJ; Pauptit, RA; Thatcher, DR; Tucker, AD; Weston, SA1
Corton, J; Hardie, DG; Hawley, SA; Shugar, D; Weekes, J1

Other Studies

8 other study(ies) available for adenosine monophosphate and formycins

ArticleYear
The catalytic site of AMP nucleosidase. Substrate specificity and pH effects with AMP and formycin 5'-PO4.
    The Journal of biological chemistry, 1979, Nov-10, Volume: 254, Issue:21

    Topics: Adenosine Monophosphate; Antibiotics, Antineoplastic; Azotobacter; Binding Sites; Formycins; Hydrogen-Ion Concentration; Kinetics; N-Glycosyl Hydrolases; Protein Binding; Ribonucleotides; Structure-Activity Relationship; Substrate Specificity

1979
Hybridization of polymers of antibiotic C-nucleoside phosphates, poly(formycin phosphate) and poly(laurusin phosphate)
    Biochemistry, 1975, Volume: 14, Issue:13

    Topics: Adenosine Monophosphate; Antibiotics, Antineoplastic; Chemical Phenomena; Chemistry; Cytosine Nucleotides; Formycins; Inosine Nucleotides; Nucleic Acid Conformation; Poly U; Polynucleotides

1975
AMP deaminase in Dictyostelium discoideum: increase in activity following nutrient deprivation induced by starvation or hadacidin.
    Molecular and cellular biochemistry, 1986, Volume: 71, Issue:1

    Topics: Adenosine Kinase; Adenosine Monophosphate; Adenosine Triphosphate; AMP Deaminase; Cell Division; Culture Media; Dictyostelium; Enzyme Activation; Formycins; Glycine; Guanosine Monophosphate; Hypoxanthine Phosphoribosyltransferase; Nucleotide Deaminases; Ribonucleotides; Substrate Specificity

1986
Regulation of rabbit liver fructose-1,6-bisphosphatase by metals, nucleotides, and fructose 2,6-bisphosphate as determined from fluorescence studies.
    Biochemistry, 1986, Oct-21, Volume: 25, Issue:21

    Topics: Adenosine Monophosphate; Animals; Cations, Divalent; Formycins; Fructose-Bisphosphatase; Fructosediphosphates; Hexosediphosphates; Kinetics; Liver; Magnesium; Manganese; Rabbits; Ribonucleotides; Spectrometry, Fluorescence; Zinc

1986
Action of tubercidin and other adenosine analogs on Schistosoma mansoni schistosomules.
    Molecular and biochemical parasitology, 1985, Volume: 16, Issue:2

    Topics: Adenosine; Adenosine Kinase; Adenosine Monophosphate; Animals; Antibiotics, Antineoplastic; Formycins; Movement; Nucleotides; Purine-Nucleoside Phosphorylase; Ribonucleosides; Schistosoma mansoni; Substrate Specificity; Tubercidin; Vidarabine

1985
Enzymatic synthesis of ATP analogs and their purification by reverse-phase high-performance liquid chromatography.
    Analytical biochemistry, 1995, Apr-10, Volume: 226, Issue:2

    Topics: Adenine Nucleotides; Adenosine Diphosphate; Adenosine Monophosphate; Adenosine Triphosphate; Adenylate Kinase; Chromatography, High Pressure Liquid; Ethenoadenosine Triphosphate; Formycins; Nucleoside-Phosphate Kinase; Pyruvate Kinase; Ribonucleotides; Tubercidin

1995
X-ray structure of recombinant ricin A-chain at 1.8 A resolution.
    Journal of molecular biology, 1994, Dec-09, Volume: 244, Issue:4

    Topics: Adenosine Monophosphate; Crystallography, X-Ray; Formycins; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Ribonucleotides; Ricin

1994
Activation of rat liver AMP-activated protein kinase by kinase kinase in a purified, reconstituted system. Effects of AMP and AMP analogues.
    European journal of biochemistry, 1994, Feb-01, Volume: 219, Issue:3

    Topics: Adenosine Monophosphate; AMP-Activated Protein Kinase Kinases; AMP-Activated Protein Kinases; Animals; Binding Sites; Dinucleoside Phosphates; Enzyme Activation; Formycins; Liver; Molecular Weight; Multienzyme Complexes; Phosphorylation; Protein Kinases; Protein Serine-Threonine Kinases; Rats; Ribonucleotides

1994