Zobrazeno 1 - 10 of 18 pro vyhledávání: '"W E Kohlbrenner"'
1
Inhibitor stabilization of human immunodeficiency virus type-2 proteinase dimer formation
Autor: T F, Holzman, W E, Kohlbrenner, D, Weigl, J, Rittenhouse, D, Kempf, J, Erickson
Publikováno v: The Journal of biological chemistry. 266(29)
We report the first direct observation of the subunit self-association behavior of highly purified recombinant human immunodeficiency virus type-2 (HIV-2) proteinase. Multiple samples of enzyme were subjected to sedimentation equilibrium analytical u
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a8da36bc8d31241e5a1b246fc190e380
https://pubmed.ncbi.nlm.nih.gov/1918040
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3
Primary structure of CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) from Escherichia coli
Autor: J L Fox, R C Goldman, W E Kohlbrenner, T J Bolling, Y Kim
Publikováno v: Journal of Biological Chemistry. 261:15831-15835
The gene coding for CTP:CMP-3-deoxy-D-mannooctulosonate cytidylyltransferase (CMP-KDO synthetase), kds B, was previously cloned on a 9-kilobase Pst insert of Escherichia coli DNA into pBR 322 (Goldman, R. C., and Kohlbrenner, W. E. (1985) J. Bacterio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d83685bcafe6005e65314f4891f5fc6f
https://doi.org/10.1016/s0021-9258(18)66638-4
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4
Subunit interaction during catalysis: ammonium ion modulation of catalytic steps in the Escherichia coli glutamine synthetase reaction. Theoretical relationships for oxygen transfer catalyzed by Escherichia coli glutamine synthetase during net adenosine 5'-triphosphate cleavage
Autor: Gary S. Bild, Paul D. Boyer, W. E. Kohlbrenner
Publikováno v: Biochemistry. 19:5774-5781
A new approach for assessing if catalytic cooperativity may occur between subunits has been applied to Escherichia coli glutamine synthetase. The extent of oxygen exchange between bound [18O]glutamate and phosphate per molecule of glutamine formed wa
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::399e4ada8dbe43e303c1353acbb34873
https://doi.org/10.1021/bi00566a017
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6
Mechanism of quinolone inhibition of DNA gyrase
Autor: W E Kohlbrenner, L L Shen, D Weigl, J Baranowski
Publikováno v: Journal of Biological Chemistry. 264:2973-2978
As a means of gaining additional information on the topoisomerase-mediated cytotoxicity induced by a variety of antibacterial and antitumor compounds we have examined the interaction of the quinolone anti-bacterial agent, norfloxacin, with the bacter
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e1ab5830c24d6c2148b7aa351b5c483a
https://doi.org/10.1016/s0021-9258(19)81708-8
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7
Probes of catalytic site cooperativity during catalysis by the chloroplast adenosine triphosphate and the adenosine triphosphate synthase
Autor: W E Kohlbrenner, P D Boyer
Publikováno v: Journal of Biological Chemistry. 258:10881-10886
During net nucleoside triphosphate synthesis by chloroplast ATP synthase the extent of water oxygen incorporation into each nucleoside triphosphate released increases with decrease in ADP, GDP or IDP concentration. Likewise, during net ATP hydrolysis
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::02f3e75b6f6fcf83daa3e5fc7e2d9241
https://doi.org/10.1016/s0021-9258(17)44358-4
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8
Efrapeptin prevents modification by phenylglyoxal of an essential arginyl residue in mitochondrial adenosine triphosphatase
Autor: R L Cross, W E Kohlbrenner
Publikováno v: Journal of Biological Chemistry. 253:7609-7611
Studies of phenylglyoxal incorporation by beef-heart mitochondrial ATPase reveal one fast-reacting arginyl residue/enzyme molecule. Modification of this group proceeds at a rate which parallels the loss of enzymatic activity. Efrapeptin protects the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c5da75c38c3865232b7fd0a7ade94591
https://doi.org/10.1016/s0021-9258(17)34412-5
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9
Efrapeptin prevents modification by phenylglyoxal of an essential arginyl residue in mitochondrial adenosine triphosphatase
Autor: W E, Kohlbrenner, R L, Cross
Publikováno v: The Journal of biological chemistry. 253(21)
Studies of phenylglyoxal incorporation by beef-heart mitochondrial ATPase reveal one fast-reacting arginyl residue/enzyme molecule. Modification of this group proceeds at a rate which parallels the loss of enzymatic activity. Efrapeptin protects the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2738fff169b7820d7ea50ae3e820eb96
https://pubmed.ncbi.nlm.nih.gov/151685
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10
Probes of catalytic site cooperativity during catalysis by the chloroplast adenosine triphosphate and the adenosine triphosphate synthase
Autor: W E, Kohlbrenner, P D, Boyer
Publikováno v: The Journal of biological chemistry. 258(18)
During net nucleoside triphosphate synthesis by chloroplast ATP synthase the extent of water oxygen incorporation into each nucleoside triphosphate released increases with decrease in ADP, GDP or IDP concentration. Likewise, during net ATP hydrolysis
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9399bd7e2c9b9167bb96dbb691512b39
https://pubmed.ncbi.nlm.nih.gov/6309819
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