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Liu, K. D., Roseman, S. (1983) Kinetic characterization and regulation of phosphoenolpyruvate-dependent methyl alpha-D-glucopyranoside transport by Salmonella typhimurium membrane vesicles. Proceedings of the National Academy of Sciences, 80 (23) 7142-7145 doi:10.1073/pnas.80.23.7142

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Reference TypeJournal (article/letter/editorial)
TitleKinetic characterization and regulation of phosphoenolpyruvate-dependent methyl alpha-D-glucopyranoside transport by Salmonella typhimurium membrane vesicles.
JournalProceedings of the National Academy of Sciences
AuthorsLiu, K. D.Author
Roseman, S.Author
Year1983 (December 1)Volume80
Issue23
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.80.23.7142Search in ResearchGate
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Mindat Ref. ID1431707Long-form Identifiermindat:1:5:1431707:1
GUID0
Full ReferenceLiu, K. D., Roseman, S. (1983) Kinetic characterization and regulation of phosphoenolpyruvate-dependent methyl alpha-D-glucopyranoside transport by Salmonella typhimurium membrane vesicles. Proceedings of the National Academy of Sciences, 80 (23) 7142-7145 doi:10.1073/pnas.80.23.7142
Plain TextLiu, K. D., Roseman, S. (1983) Kinetic characterization and regulation of phosphoenolpyruvate-dependent methyl alpha-D-glucopyranoside transport by Salmonella typhimurium membrane vesicles. Proceedings of the National Academy of Sciences, 80 (23) 7142-7145 doi:10.1073/pnas.80.23.7142
In(1983, December) Proceedings of the National Academy of Sciences Vol. 80 (23) Proceedings of the National Academy of Sciences

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Stock, A., Koshland, D. E., Stock, J. (1985) Homologies between the Salmonella typhimurium CheY protein and proteins involved in the regulation of chemotaxis, membrane protein synthesis, and sporulation. Proceedings of the National Academy of Sciences, 82 (23) 7989-7993 doi:10.1073/pnas.82.23.7989
Yusuf, H. K., Pohlentz, G., Sandhoff, K. (1983) Tunicamycin inhibits ganglioside biosynthesis in rat liver Golgi apparatus by blocking sugar nucleotide transport across the membrane vesicles. Proceedings of the National Academy of Sciences, 80 (23) 7075-7079 doi:10.1073/pnas.80.23.7075
Biek, D., Roth, J. R. (1980) Regulation of Tn5 transposition in Salmonella typhimurium. Proceedings of the National Academy of Sciences, 77 (10) 6047-6051 doi:10.1073/pnas.77.10.6047
Mulford, C. A., Osborn, M. J. (1983) An intermediate step in translocation of lipopolysaccharide to the outer membrane of Salmonella typhimurium. Proceedings of the National Academy of Sciences, 80 (5) 1159-1163 doi:10.1073/pnas.80.5.1159
Lever, J. E. (1976) Regulation of active alpha-aminoisobutyric acid transport expressed in membrane vesicles from mouse fibroblasts. Proceedings of the National Academy of Sciences, 73 (8) 2614-2618 doi:10.1073/pnas.73.8.2614
Ames, G. F., Nikaido, K. (1978) Identification of a membrane protein as a histidine transport component in Salmonella typhimurium. Proceedings of the National Academy of Sciences, 75 (11) 5447-5451 doi:10.1073/pnas.75.11.5447
Hall, C. L., Munford, R. S. (1983) Enzymatic deacylation of the lipid A moiety of Salmonella typhimurium lipopolysaccharides by human neutrophils. Proceedings of the National Academy of Sciences, 80 (21) 6671-6675 doi:10.1073/pnas.80.21.6671
Fan, C. C., Powell, D. W. (1983) Calcium/calmodulin inhibition of coupled NaCl transport in membrane vesicles from rabbit ileal brush border. Proceedings of the National Academy of Sciences, 80 (17) 5248-5252 doi:10.1073/pnas.80.17.5248
Jones, B. D., Paterson, H. F., Hall, A., Falkow, S. (1993) Salmonella typhimurium induces membrane ruffling by a growth factor-receptor-independent mechanism. Proceedings of the National Academy of Sciences, 90 (21) 10390-10394 doi:10.1073/pnas.90.21.10390
Cronenwett, C. S., Wagner, R. P. (1965) Over-all synthesis of isoleucine by membrane fractions of Salmonella typhimurium. Proceedings of the National Academy of Sciences, 54 (6) 1643-1650 doi:10.1073/pnas.54.6.1643
Inui, K.-i., Moller, D. E., Tillotson, L. G., Isselbacher, K. J. (1979) Stereospecific hexose transport by membrane vesicles from mouse fibroblasts: Membrane vesicles retain increased hexose transport associated with viral transformation. Proceedings of the National Academy of Sciences, 76 (8) 3972-3976 doi:10.1073/pnas.76.8.3972
 
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