Results 211 to 220 of about 122,814 (265)

Rapid, Growth Factor-Reduced Induction of Functional Neurons from hiPSCs. [PDF]

Cells Tissues Organs
Parker NA, Kolawole OE, Liao Z, Syed FS, Moquin KE, Iyer NR.   +5 more
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An improved workflow for rapid, large-scale protein production in HEK293 cells via antibiotic enrichment after lentiviral transduction

Behiels E, Nair A, Doridant A, Elegheert J.   +3 more
europepmc   +1 more source

Mechanosensing at the endoplasmic reticulum by IRE1

Farhan H, Mayr M, Garcia-Souza L, McDermott M, Horzum U, Frey Y, Haun M, Geley S, Jiang C, Luber M, Bakunts A, Pirolo C, Yakimchyk A, Liedl K, Stroberg W, Betz T, Holt L.   +16 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 ...
L B Hersh
exaly   +3 more sources

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
openaire   +2 more sources

Puromycin and Retention in the Goldfish

Science, 1967
A first experiment compared the behavior of goldfish injected with puromycin immediately after each of a weekly series of brief discriminative training sessions in the shuttlebox to that of appropriate controls. Discrimination was not prevented, nor was escape from shock impaired, but probability of response to the conditioned stimuli, both positive ...
A, Potts, M E, Bitterman
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Puromycin as an inhibitor of acetylcholinesterase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract A kinetic analysis of the interaction of puromycin, an inhibitor of protein synthesis, with bovine red cell acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) shows that puromycin is a reversible mixed inhibitor of this enzyme. Puromycin inhibition is similar to that of the pachycurares, such as d- tubocurarine , and is quite ...
D R, Moss, D E, Moss, D, Fahrney
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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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Reduction of renin-release by puromycin

Cardiovascular Research, 1970
Puromycin infused into a renal artery (10–125 μg/kg/min for 20 min) of anaesthetized dogs consistently reduced renin activity in samples of renal venous blood when kidneys were perfused at lowered pressures. It did not affect the smaller amounts of renin present in the renal venous effluent from kidneys perfused at normal pressures.
R D, Bunag, I H, Page, J W, McCubbin
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