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Refinado por: Nome da Publicação: Journal Of Biological Chemistry remover assunto: Kinetics remover assunto: Molecular Biology remover
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1
1-beta-D-Arabinofuranosylcytosine stimulates ceramide and diglyceride formation in HL-60 cells
1-beta-D-Arabinofuranosylcytosine stimulates ceramide and diglyceride formation in HL-60 cells
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1-beta-D-Arabinofuranosylcytosine stimulates ceramide and diglyceride formation in HL-60 cells

Strum, J C ; Small, G W ; Pauig, S B ; Daniel, L W

The Journal of biological chemistry, 1994-06, Vol.269 (22), p.15493-15497 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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2
1,2-Diacylglycerol, protein kinase C, and pancreatic enzyme secretion
1,2-Diacylglycerol, protein kinase C, and pancreatic enzyme secretion
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1,2-Diacylglycerol, protein kinase C, and pancreatic enzyme secretion

Pandol, S J ; Schoeffield, M S

The Journal of biological chemistry, 1986-04, Vol.261 (10), p.4438-4444 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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3
1,3-Butadiene oxidation by human myeloperoxidase. Role of chloride ion in catalysis of divergent pathways
1,3-Butadiene oxidation by human myeloperoxidase. Role of chloride ion in catalysis of divergent pathways
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1,3-Butadiene oxidation by human myeloperoxidase. Role of chloride ion in catalysis of divergent pathways

DUESCHER, RJ ; ELFARRA, AA

The Journal of biological chemistry, 1992-10, Vol.267 (28), p.19859-19865 [Periódico revisado por pares]

BETHESDA: American Society for Biochemistry and Molecular Biology

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4
14-3-3 Isoforms Are Induced by Aldosterone and Participate in Its Regulation of Epithelial Sodium Channels
14-3-3 Isoforms Are Induced by Aldosterone and Participate in Its Regulation of Epithelial Sodium Channels
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14-3-3 Isoforms Are Induced by Aldosterone and Participate in Its Regulation of Epithelial Sodium Channels

Liang, Xiubin ; Peters, Kathryn W. ; Butterworth, Michael B. ; Frizzell, Raymond A.

The Journal of biological chemistry, 2006-06, Vol.281 (24), p.16323-16332 [Periódico revisado por pares]

United States: Elsevier Inc

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5
1400W Is a Slow, Tight Binding, and Highly Selective Inhibitor of Inducible Nitric-oxide Synthase in Vitro and in Vivo
1400W Is a Slow, Tight Binding, and Highly Selective Inhibitor of Inducible Nitric-oxide Synthase in Vitro and in Vivo
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1400W Is a Slow, Tight Binding, and Highly Selective Inhibitor of Inducible Nitric-oxide Synthase in Vitro and in Vivo

Garvey, E P ; Oplinger, J A ; Furfine, E S ; Kiff, R J ; Laszlo, F ; Whittle, B J ; Knowles, R G

The Journal of biological chemistry, 1997-02, Vol.272 (8), p.4959-4963 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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6
14C2H2- and 14CO2-labeling studies of the de novo synthesis of polypeptides by Nitrosomonas europaea during recovery from acetylene and light inactivation of ammonia monooxygenase
14C2H2- and 14CO2-labeling studies of the de novo synthesis of polypeptides by Nitrosomonas europaea during recovery from acetylene and light inactivation of ammonia monooxygenase
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14C2H2- and 14CO2-labeling studies of the de novo synthesis of polypeptides by Nitrosomonas europaea during recovery from acetylene and light inactivation of ammonia monooxygenase

Hyman, M R ; Arp, D J

The Journal of biological chemistry, 1992-01, Vol.267 (3), p.1534-1545 [Periódico revisado por pares]

United States: Elsevier Inc

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7
15N-tracer and NMR studies on the pathway of denitrification. Evidence against trioxodinitrate but for nitroxyl as an intermediate
15N-tracer and NMR studies on the pathway of denitrification. Evidence against trioxodinitrate but for nitroxyl as an intermediate
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15N-tracer and NMR studies on the pathway of denitrification. Evidence against trioxodinitrate but for nitroxyl as an intermediate

Garber, E A ; Wehrli, S ; Hollocher, T C

The Journal of biological chemistry, 1983-03, Vol.258 (6), p.3587-3591 [Periódico revisado por pares]

Bethesda, MD: Elsevier Inc

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8
15N,18O tracer studies on the activation of nitrite by denitrifying bacteria. Nitrite/water-oxygen exchange and nitrosation reactions as indicators of electrophilic catalysis
15N,18O tracer studies on the activation of nitrite by denitrifying bacteria. Nitrite/water-oxygen exchange and nitrosation reactions as indicators of electrophilic catalysis
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15N,18O tracer studies on the activation of nitrite by denitrifying bacteria. Nitrite/water-oxygen exchange and nitrosation reactions as indicators of electrophilic catalysis

Garber, E A ; Hollocher, T C

The Journal of biological chemistry, 1982-07, Vol.257 (14), p.8091-8097 [Periódico revisado por pares]

United States: Elsevier Inc

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9
18O-Labeling of guanosine monophosphate upon hydrolysis of cyclic guanosine 3':5'-monophosphate by phosphodiesterase
18O-Labeling of guanosine monophosphate upon hydrolysis of cyclic guanosine 3':5'-monophosphate by phosphodiesterase
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18O-Labeling of guanosine monophosphate upon hydrolysis of cyclic guanosine 3':5'-monophosphate by phosphodiesterase

Goldberg, N D ; Walseth, T F ; Stephenson, J H ; Krick, T P ; Graff, G

The Journal of biological chemistry, 1980-11, Vol.255 (21), p.10344-10347 [Periódico revisado por pares]

United States: American Society for Biochemistry and Molecular Biology

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10
2-Keto-3-deoxy-d-glycero-d-galacto-nononic Acid (KDN)- and N-Acetylneuraminic Acid-cleaving Sialidase (KDN-sialidase) and KDN-cleaving Hydrolase (KDNase) from the Hepatopancreas of Oyster, Crassostrea virginica
2-Keto-3-deoxy-d-glycero-d-galacto-nononic Acid (KDN)- and N-Acetylneuraminic Acid-cleaving Sialidase (KDN-sialidase) and KDN-cleaving Hydrolase (KDNase) from the Hepatopancreas of Oyster, Crassostrea virginica
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2-Keto-3-deoxy-d-glycero-d-galacto-nononic Acid (KDN)- and N-Acetylneuraminic Acid-cleaving Sialidase (KDN-sialidase) and KDN-cleaving Hydrolase (KDNase) from the Hepatopancreas of Oyster, Crassostrea virginica

Pavlova, Nadejda V. ; Yuziuk, Jeffrey A. ; Nakagawa, Hiroki ; Kiso, Makoto ; Li, Su-Chen ; Li, Yu-Teh

The Journal of biological chemistry, 1999-11, Vol.274 (45), p.31974-31980 [Periódico revisado por pares]

United States: Elsevier Inc

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