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Instability of Puromycin

Nature, 1966
PUROMYCIN dihydrochloride is being extensively used as an inhibitor of protein synthesis. This antibiotic inhibitor is valuable because its mode of action on protein biosynthesis has been elucidated in precise molecular terms1. Examination of the literature shows, however, that there is a considerable range in the reported potencies of different ...
G P, Studzinski, R, Baserga
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Biosynthesis of puromycin by Streptomyces alboniger: Characterization of puromycin N-acetyltransferase

Biochemistry, 1985
Puromycin N-acetyltransferase from Streptomyces alboniger inactivates puromycin by acetylating the amino position of its tyrosinyl moiety. This enzyme has been partially purified by column chromatography through DEAE-cellulose and Affigel Blue and characterized. It has an Mr of 23 000, as determined by gel filtration.
J, Vara, J A, Perez-Gonzalez, A, Jimenez
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Streptomycinoid Antibiotics: Synergism by Puromycin

Science, 1964
Puromycin synergizes the lethal action of streptomycin and related antibiotics. This is interpreted to mean that puromycin action uncovers a sensitive site (or sites) on the 30 S ribosome. The streptomycinoid antibiotics can then associate more readily with the ribosome and inhibit further synthesis of valid protein.
J R, WHITE, H L, WHITE
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Synthesis of L,L‐Puromycin.

ChemInform, 2005
Abstract l , l -Puromycin, a diastereomer of the natural peptidyl nucleoside antibiotic puromycin, has been synthesized from l -xylose in 13 steps.
Carrie L.K. Gilbert   +3 more
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Inhibition of Aminopeptidase and Acetylcholinesterase by Puromycin and Puromycin Analogs

Journal of Neurochemistry, 1981
Abstract: Puromycin analogs in which the O‐methyl‐L‐tyrosine moiety was substituted by a number of amino acids were examined as inhibitors of the puromycin‐sensitive rat brain aminopeptidase and bovine erythrocyte acetyl‐cholinesterase. In the case of the aminopeptidase, the structure and stereochemistry of the amino acid substituent were important ...
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Puromycin: Action on Neuronal Mitochondria

Science, 1968
Puromycin, in dosages that inhibit cerebral protein synthesis and expression of memory in mice, produces swelling of neuronal mitochondria. Acetoxycycloheximide, which inhibits cerebral protein synthesis to the same extent as puromycin, fails to produce swelling of neuronal mitochondria.
P, Gambetti, N K, Gonatas, L B, Flexner
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Puromycin analogs. Effect of aryl-substituted puromycin analogs on the ribosomal peptidyltransferase reaction

Journal of Medicinal Chemistry, 1981
A series of ortho- and para-substituted L-phenylalanylpuromycin analogues were synthesized and evaluated as substrates for the peptidyltransferase reaction of Escherichia coli ribosomes. Kinetic results reveal that substitution of the p-methoxy group of the puromycin molecule alters the peptidyltransferase activity of the molecule with the following ...
H, Lee, K L, Fong, R, Vince
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Selecting Transgenic Mosquito Larvae with Puromycin

Cold Spring Harbor Protocols, 2023
The selection of mosquito transgenic larvae using a nonfluorescent approach can be advantageous to reserve fluorophores for downstream applications, such as immunostaining or for the study of promoter activity by cloning a fluorescence reporter gene under the control of that promoter.
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Structure of puromycin aminonucleoside

Acta Crystallographica Section C Crystal Structure Communications, 1988
3'-Amino-3'-deoxy-N,N-dimethyladenosine, $C_{12}H_{18}N_6O_3$, $M_r = 294.3$, monoclinic, $P2_1$, a = 4.684(1), b= 10.252(1), c= 14.381 (3)\AA, \beta = 91.16 (2)°, V= 690.49 $\AA^3$, Z = 2, $D_x = 1.39$ Mg $m^{-3}$, \lambda(Cu K\alpha) = 1.5418 \AA, \mu = 0.84 $mm^{-1}$, F(000) = 312, T= 295 K, R =0.045 for 986 observed reflections with I > 1.5\sigma(I)
Padmaja, N, Ramakumar, S, Viswamitra, MA
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Stereochemistry of the puromycin reaction

Biochemical and Biophysical Research Communications, 1971
Summary Space-filling models have shown that peptidyl-puromycin cannot be formed if puromycin is displacing the end of aminoacyl-tRNA. Instead, the models show that puromycin “hugs” the terminus of peptidyl-tRNA in such a way that the free amino group of the antibiotic is in a perfect position for a nucleophylic attack on the carbonyl carbon of the ...
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