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High resolution NMR in vivo.

Trends in biochemical sciences

Shulman RG.
PMID: 3238747
Trends Biochem Sci. 1988 Feb;13(2):37-9. doi: 10.1016/0968-0004(88)90022-9.

No abstract available.

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Shulman RG. High resolution NMR in vivo. Trends Biochem Sci. 1988;13(2):37-9doi: 10.1016/0968-0004(88)90022-9.
Shulman, R. G. (1988). High resolution NMR in vivo. Trends in biochemical sciences, 13(2), 37-9. https://doi.org/10.1016/0968-0004(88)90022-9
Shulman, R G. "High resolution NMR in vivo." Trends in biochemical sciences vol. 13,2 (1988): 37-9. doi: https://doi.org/10.1016/0968-0004(88)90022-9
Shulman RG. High resolution NMR in vivo. Trends Biochem Sci. 1988 Feb;13(2):37-9. doi: 10.1016/0968-0004(88)90022-9. PMID: 3238747.
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New insights into metabolic pathway optimization by analogy with industrial manufacturing processes.

Biochemical Society transactions

Cascante M, Martí E, Ortega F.
PMID: 10093747
Biochem Soc Trans. 1999 Feb;27(2):276-81. doi: 10.1042/bst0270276.

No abstract available.

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Cascante M, Martí E, Ortega F. New insights into metabolic pathway optimization by analogy with industrial manufacturing processes. Biochem Soc Trans. 1999;27(2):276-81doi: 10.1042/bst0270276.
Cascante, M., Martí, E., & Ortega, F. (1999). New insights into metabolic pathway optimization by analogy with industrial manufacturing processes. Biochemical Society transactions, 27(2), 276-81. https://doi.org/10.1042/bst0270276
Cascante, M, et al. "New insights into metabolic pathway optimization by analogy with industrial manufacturing processes." Biochemical Society transactions vol. 27,2 (1999): 276-81. doi: https://doi.org/10.1042/bst0270276
Cascante M, Martí E, Ortega F. New insights into metabolic pathway optimization by analogy with industrial manufacturing processes. Biochem Soc Trans. 1999 Feb;27(2):276-81. doi: 10.1042/bst0270276. PMID: 10093747.
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Use of modified double-reciprocal plot for enzyme kinetic parameters. A pitfall.

Biochimica et biophysica acta

Karanth NG, Srivastava AK.
PMID: 7426666
Biochim Biophys Acta. 1980 Sep 09;615(1):279-82. doi: 10.1016/0005-2744(80)90032-7.

The modified double-reciprocal plot suggested by Lee and Wilson (Lee, H.J. and Wilson, I.B. (1971) Biochim. Biophys. Acta 242, 519--522) has until now been accepted as giving a simple and accurate method for the determination of enzyme kinetic parameters...

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Karanth NG, Srivastava AK. Use of modified double-reciprocal plot for enzyme kinetic parameters. A pitfall. Biochim Biophys Acta. 1980;615(1):279-82doi: 10.1016/0005-2744(80)90032-7.
Karanth, N. G., & Srivastava, A. K. (1980). Use of modified double-reciprocal plot for enzyme kinetic parameters. A pitfall. Biochimica et biophysica acta, 615(1), 279-82. https://doi.org/10.1016/0005-2744(80)90032-7
Karanth, N G, and Srivastava, A K. "Use of modified double-reciprocal plot for enzyme kinetic parameters. A pitfall." Biochimica et biophysica acta vol. 615,1 (1980): 279-82. doi: https://doi.org/10.1016/0005-2744(80)90032-7
Karanth NG, Srivastava AK. Use of modified double-reciprocal plot for enzyme kinetic parameters. A pitfall. Biochim Biophys Acta. 1980 Sep 09;615(1):279-82. doi: 10.1016/0005-2744(80)90032-7. PMID: 7426666.
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A note on the choice of substrate concentration in enzyme kinetic experiments.

Journal of theoretical biology

Weiss GH, Darvey IG.
PMID: 7311585
J Theor Biol. 1981 Jun 07;90(3):437-9. doi: 10.1016/0022-5193(81)90323-4.

No abstract available.

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Weiss GH, Darvey IG. A note on the choice of substrate concentration in enzyme kinetic experiments. J Theor Biol. 1981;90(3):437-9doi: 10.1016/0022-5193(81)90323-4.
Weiss, G. H., & Darvey, I. G. (1981). A note on the choice of substrate concentration in enzyme kinetic experiments. Journal of theoretical biology, 90(3), 437-9. https://doi.org/10.1016/0022-5193(81)90323-4
Weiss, G H, and Darvey, I G. "A note on the choice of substrate concentration in enzyme kinetic experiments." Journal of theoretical biology vol. 90,3 (1981): 437-9. doi: https://doi.org/10.1016/0022-5193(81)90323-4
Weiss GH, Darvey IG. A note on the choice of substrate concentration in enzyme kinetic experiments. J Theor Biol. 1981 Jun 07;90(3):437-9. doi: 10.1016/0022-5193(81)90323-4. PMID: 7311585.
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Two new schematic rules for rate laws of enzyme-catalysed reactions.

Journal of theoretical biology

Chou KC.
PMID: 7289637
J Theor Biol. 1981 Apr 21;89(4):581-92. doi: 10.1016/0022-5193(81)90030-8.

No abstract available.

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Chou KC. Two new schematic rules for rate laws of enzyme-catalysed reactions. J Theor Biol. 1981;89(4):581-92doi: 10.1016/0022-5193(81)90030-8.
Chou, K. C. (1981). Two new schematic rules for rate laws of enzyme-catalysed reactions. Journal of theoretical biology, 89(4), 581-92. https://doi.org/10.1016/0022-5193(81)90030-8
Chou, K C. "Two new schematic rules for rate laws of enzyme-catalysed reactions." Journal of theoretical biology vol. 89,4 (1981): 581-92. doi: https://doi.org/10.1016/0022-5193(81)90030-8
Chou KC. Two new schematic rules for rate laws of enzyme-catalysed reactions. J Theor Biol. 1981 Apr 21;89(4):581-92. doi: 10.1016/0022-5193(81)90030-8. PMID: 7289637.
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Analysis of progress curves in enzyme kinetics: bias and convergent set in the differential and in the integral method.

Journal of biochemical and biophysical methods

Markus M, Plesser T, Kohlmeier M.
PMID: 7229264
J Biochem Biophys Methods. 1981 Feb;4(2):81-90. doi: 10.1016/0165-022x(81)90021-x.

Two problems encountered in the analysis of progress curves are examined: 1. Systematic deviations due to errors in the initial solute concentrations make the least-squares method unsuitable. The improvements accomplished by the introduction of a proper weighting matrix are...

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Markus M, Plesser T, Kohlmeier M. Analysis of progress curves in enzyme kinetics: bias and convergent set in the differential and in the integral method. J Biochem Biophys Methods. 1981;4(2):81-90doi: 10.1016/0165-022x(81)90021-x.
Markus, M., Plesser, T., & Kohlmeier, M. (1981). Analysis of progress curves in enzyme kinetics: bias and convergent set in the differential and in the integral method. Journal of biochemical and biophysical methods, 4(2), 81-90. https://doi.org/10.1016/0165-022x(81)90021-x
Markus, M, et al. "Analysis of progress curves in enzyme kinetics: bias and convergent set in the differential and in the integral method." Journal of biochemical and biophysical methods vol. 4,2 (1981): 81-90. doi: https://doi.org/10.1016/0165-022x(81)90021-x
Markus M, Plesser T, Kohlmeier M. Analysis of progress curves in enzyme kinetics: bias and convergent set in the differential and in the integral method. J Biochem Biophys Methods. 1981 Feb;4(2):81-90. doi: 10.1016/0165-022x(81)90021-x. PMID: 7229264.
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Biochemical systems analysis. I. Some mathematical properties of the rate law for the component enzymatic reactions.

Journal of theoretical biology

Savageau MA.
PMID: 5387046
J Theor Biol. 1969 Dec;25(3):365-9. doi: 10.1016/s0022-5193(69)80026-3.

No abstract available.

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Savageau MA. Biochemical systems analysis. I. Some mathematical properties of the rate law for the component enzymatic reactions. J Theor Biol. 1969;25(3):365-9doi: 10.1016/s0022-5193(69)80026-3.
Savageau, M. A. (1969). Biochemical systems analysis. I. Some mathematical properties of the rate law for the component enzymatic reactions. Journal of theoretical biology, 25(3), 365-9. https://doi.org/10.1016/s0022-5193(69)80026-3
Savageau, M A. "Biochemical systems analysis. I. Some mathematical properties of the rate law for the component enzymatic reactions." Journal of theoretical biology vol. 25,3 (1969): 365-9. doi: https://doi.org/10.1016/s0022-5193(69)80026-3
Savageau MA. Biochemical systems analysis. I. Some mathematical properties of the rate law for the component enzymatic reactions. J Theor Biol. 1969 Dec;25(3):365-9. doi: 10.1016/s0022-5193(69)80026-3. PMID: 5387046.
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Diffusion-controlled reactions of enzymes. A comparison between Chou's model and Alberty-Hammes-Eigen's model.

European journal of biochemistry

Zhou GQ, Zhong WZ.
PMID: 7151785
Eur J Biochem. 1982 Nov 15;128(2):383-7.
Free Article

In the study of enzyme-catalysed mechanisms, it is often necessary to calculate the upper limit of enzyme reaction, which is usually used as an important criterion to identify whether an assumed enzyme-catalysed mechanism is reasonable or not. Basically, in...

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Zhou GQ, Zhong WZ. Diffusion-controlled reactions of enzymes. A comparison between Chou's model and Alberty-Hammes-Eigen's model. Eur J Biochem. 1982;128(2):383-7
Zhou, G. Q., & Zhong, W. Z. (1982). Diffusion-controlled reactions of enzymes. A comparison between Chou's model and Alberty-Hammes-Eigen's model. European journal of biochemistry, 128(2), 383-7.
Zhou, G Q, and Zhong, W Z. "Diffusion-controlled reactions of enzymes. A comparison between Chou's model and Alberty-Hammes-Eigen's model." European journal of biochemistry vol. 128,2 (1982): 383-7.
Zhou GQ, Zhong WZ. Diffusion-controlled reactions of enzymes. A comparison between Chou's model and Alberty-Hammes-Eigen's model. Eur J Biochem. 1982 Nov 15;128(2):383-7. PMID: 7151785.
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IV. Transient phase of the uni-bi mechanisms.

Journal of theoretical biology

Galvez J, Varon R, Garcia Canovas F, Garcia Carmona F.
PMID: 7078213
J Theor Biol. 1982 Jan 21;94(2):413-20. doi: 10.1016/0022-5193(82)90319-8.

No abstract available.

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Galvez J, Varon R, Garcia Canovas F, et al. IV. Transient phase of the uni-bi mechanisms. J Theor Biol. 1982;94(2):413-20doi: 10.1016/0022-5193(82)90319-8.
Galvez, J., Varon, R., Garcia Canovas, F., & Garcia Carmona, F. (1982). IV. Transient phase of the uni-bi mechanisms. Journal of theoretical biology, 94(2), 413-20. https://doi.org/10.1016/0022-5193(82)90319-8
Galvez, J, et al. "IV. Transient phase of the uni-bi mechanisms." Journal of theoretical biology vol. 94,2 (1982): 413-20. doi: https://doi.org/10.1016/0022-5193(82)90319-8
Galvez J, Varon R, Garcia Canovas F, Garcia Carmona F. IV. Transient phase of the uni-bi mechanisms. J Theor Biol. 1982 Jan 21;94(2):413-20. doi: 10.1016/0022-5193(82)90319-8. PMID: 7078213.
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The identification of unbranched enzyme kinetic mechanisms by computer analysis of qualitative information: logic of the method.

Journal of theoretical biology

Ainsworth S, Kinderlerer J.
PMID: 7121029
J Theor Biol. 1982 May 21;96(2):253-79. doi: 10.1016/0022-5193(82)90224-7.

No abstract available.

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Ainsworth S, Kinderlerer J. The identification of unbranched enzyme kinetic mechanisms by computer analysis of qualitative information: logic of the method. J Theor Biol. 1982;96(2):253-79doi: 10.1016/0022-5193(82)90224-7.
Ainsworth, S., & Kinderlerer, J. (1982). The identification of unbranched enzyme kinetic mechanisms by computer analysis of qualitative information: logic of the method. Journal of theoretical biology, 96(2), 253-79. https://doi.org/10.1016/0022-5193(82)90224-7
Ainsworth, S, and Kinderlerer, J. "The identification of unbranched enzyme kinetic mechanisms by computer analysis of qualitative information: logic of the method." Journal of theoretical biology vol. 96,2 (1982): 253-79. doi: https://doi.org/10.1016/0022-5193(82)90224-7
Ainsworth S, Kinderlerer J. The identification of unbranched enzyme kinetic mechanisms by computer analysis of qualitative information: logic of the method. J Theor Biol. 1982 May 21;96(2):253-79. doi: 10.1016/0022-5193(82)90224-7. PMID: 7121029.
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A kinetic analysis of enzyme systems involving four substrates.

The Biochemical journal

Elliott KR, Tipton KF.
PMID: 4463962
Biochem J. 1974 Sep;141(3):789-805. doi: 10.1042/bj1410789.
Free PMC Article

A treatment of kinetic data for enzyme mechanisms involving four substrates is described. The initial-rate equations and product-inhibition patterns for such mechanisms are presented. The treatment is extended to include analysis of enzyme mechanisms involving three substrates in which...

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Elliott KR, Tipton KF. A kinetic analysis of enzyme systems involving four substrates. Biochem J. 1974;141(3):789-805doi: 10.1042/bj1410789.
Elliott, K. R., & Tipton, K. F. (1974). A kinetic analysis of enzyme systems involving four substrates. The Biochemical journal, 141(3), 789-805. https://doi.org/10.1042/bj1410789
Elliott, K R, and Tipton, K F. "A kinetic analysis of enzyme systems involving four substrates." The Biochemical journal vol. 141,3 (1974): 789-805. doi: https://doi.org/10.1042/bj1410789
Elliott KR, Tipton KF. A kinetic analysis of enzyme systems involving four substrates. Biochem J. 1974 Sep;141(3):789-805. doi: 10.1042/bj1410789. PMID: 4463962; PMCID: PMC1168185.
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Efficient Synthesis of Single-Chain Globules Mimicking the Morphology and Polymerase Activity of Metalloenzymes.

Macromolecular rapid communications

Sanchez-Sanchez A, Arbe A, Kohlbrecher J, Colmenero J, Pomposo JA.
PMID: 26139198
Macromol Rapid Commun. 2015 Sep;36(17):1592-7. doi: 10.1002/marc.201500252. Epub 2015 Jul 02.

Endowing unimolecular soft nanoobjects with biomimetic functions is attracting significant interest in the emerging field of single-chain technology. Inspired by the compartmentalized structure and polymerase activity of metalloenzymes, copper-containing compact nanoglobules have been designed, synthesized, and characterized endowed with...

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Sanchez-Sanchez A, Arbe A, Kohlbrecher J, et al. Efficient Synthesis of Single-Chain Globules Mimicking the Morphology and Polymerase Activity of Metalloenzymes. Macromol Rapid Commun. 2015;36(17):1592-7doi: 10.1002/marc.201500252.
Sanchez-Sanchez, A., Arbe, A., Kohlbrecher, J., Colmenero, J., & Pomposo, J. A. (2015). Efficient Synthesis of Single-Chain Globules Mimicking the Morphology and Polymerase Activity of Metalloenzymes. Macromolecular rapid communications, 36(17), 1592-7. https://doi.org/10.1002/marc.201500252
Sanchez-Sanchez, Ana, et al. "Efficient Synthesis of Single-Chain Globules Mimicking the Morphology and Polymerase Activity of Metalloenzymes." Macromolecular rapid communications vol. 36,17 (2015): 1592-7. doi: https://doi.org/10.1002/marc.201500252
Sanchez-Sanchez A, Arbe A, Kohlbrecher J, Colmenero J, Pomposo JA. Efficient Synthesis of Single-Chain Globules Mimicking the Morphology and Polymerase Activity of Metalloenzymes. Macromol Rapid Commun. 2015 Sep;36(17):1592-7. doi: 10.1002/marc.201500252. Epub 2015 Jul 02. PMID: 26139198.
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Showing 13 to 24 of 75 entries