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Lennick, M., Allewell, N. M. (1981) Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association. Proceedings of the National Academy of Sciences, 78 (11) 6759-6763 doi:10.1073/pnas.78.11.6759

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Reference TypeJournal (article/letter/editorial)
TitleChanges in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.
JournalProceedings of the National Academy of Sciences
AuthorsLennick, M.Author
Allewell, N. M.Author
Year1981 (November 1)Volume78
Issue11
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.78.11.6759Search in ResearchGate
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Mindat Ref. ID1414816Long-form Identifiermindat:1:5:1414816:1
GUID0
Full ReferenceLennick, M., Allewell, N. M. (1981) Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association. Proceedings of the National Academy of Sciences, 78 (11) 6759-6763 doi:10.1073/pnas.78.11.6759
Plain TextLennick, M., Allewell, N. M. (1981) Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association. Proceedings of the National Academy of Sciences, 78 (11) 6759-6763 doi:10.1073/pnas.78.11.6759
In(1981, November) Proceedings of the National Academy of Sciences Vol. 78 (11) Proceedings of the National Academy of Sciences

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McCarthy, M. P., Allewell, N. M. (1983) Thermodynamics of assembly of Escherichia coli aspartate transcarbamoylase. Proceedings of the National Academy of Sciences, 80 (22) 6824-6828 doi:10.1073/pnas.80.22.6824
Luhrmann, R., Bald, R., Stoffler-Meilicke, M., Stoffler, G. (1981) Localization of the puromycin binding site on the large ribosomal subunit of Escherichia coli by immunoelectron microscopy. Proceedings of the National Academy of Sciences, 78 (12) 7276-7280 doi:10.1073/pnas.78.12.7276
Bethell, M. R., Smith, K. E., White, J. S., Jones, M. E. (1968) Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli. Proceedings of the National Academy of Sciences, 60 (4) 1442-1449 doi:10.1073/pnas.60.4.1442
Klotz, I. M., Hunston, D. L. (1977) Analytical and graphical examination of strong binding by half-of-sites in proteins: Illustration with aspartate transcarbamylase. Proceedings of the National Academy of Sciences, 74 (11) 4959-4963 doi:10.1073/pnas.74.11.4959
Kastner, B., Stoffler-Meilicke, M., Stoffler, G. (1981) Arrangement of the subunits in the ribosome of Escherichia coli: demonstration by immunoelectron microscopy. Proceedings of the National Academy of Sciences, 78 (11) 6652-6656 doi:10.1073/pnas.78.11.6652
Burgers, P. M., Kornberg, A., Sakakibara, Y. (1981) The dnaN gene codes for the beta subunit of DNA polymerase III holoenzyme of escherichia coli. Proceedings of the National Academy of Sciences, 78 (9) 5391-5395 doi:10.1073/pnas.78.9.5391
Chang, F. N., Flaks, J. G. (1970) Topography of the Escherichia coli 30S Ribosomal Subunit and Streptomycin Binding. Proceedings of the National Academy of Sciences, 67 (3) 1321-1328 doi:10.1073/pnas.67.3.1321
Flower, A. M., McHenry, C. S. (1990) The gamma subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting. Proceedings of the National Academy of Sciences, 87 (10) 3713-3717 doi:10.1073/pnas.87.10.3713
Konigsberg, W. H., Henderson, L. (1983) Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli. Proceedings of the National Academy of Sciences, 80 (9) 2467-2471 doi:10.1073/pnas.80.9.2467
Irbe, R. M., Morin, L. M., Oishi, M. (1981) Prophage (phi 80) induction in Escherichia coli K-12 by specific deoxyoligonucleotides. Proceedings of the National Academy of Sciences, 78 (1) 138-142 doi:10.1073/pnas.78.1.138
Cox, M. M., Lehman, I. R. (1981) recA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange. Proceedings of the National Academy of Sciences, 78 (6) 3433-3437 doi:10.1073/pnas.78.6.3433
 
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