Michalska K, Gale J, Joachimiak G, Chang C, Hatzos-Skintges C, Nocek B
IUCrJ. 2019; 6(Pt 4):649-664.
PMID: 31316809
PMC: 6608616.
DOI: 10.1107/S2052252519005955.
ONeill C, Skilton R, Pearson S, Filardo S, Andersson P, Clarke I
Front Cell Infect Microbiol. 2019; 8:434.
PMID: 30619780
PMC: 6302012.
DOI: 10.3389/fcimb.2018.00434.
Portin P, Wilkins A
Genetics. 2017; 205(4):1353-1364.
PMID: 28360126
PMC: 5378099.
DOI: 10.1534/genetics.116.196956.
Hilario E, Caulkins B, Huang Y, You W, Chang C, Mueller L
Biochim Biophys Acta. 2015; 1864(3):268-279.
PMID: 26708480
PMC: 4732270.
DOI: 10.1016/j.bbapap.2015.12.006.
Caulkins B, Yang C, Hilario E, Fan L, Dunn M, Mueller L
Biochim Biophys Acta. 2015; 1854(9):1194-9.
PMID: 25688830
PMC: 4506891.
DOI: 10.1016/j.bbapap.2015.02.003.
Molecular analysis of intragenic recombination at the tryptophan synthetase locus in Neurospora crassa.
Wiest A, Barchers D, Eaton M, Henderson R, Schnittker R, McCluskey K
J Genet. 2013; 92(3):523-8.
PMID: 24371173
DOI: 10.1007/s12041-013-0305-4.
The tryptophan synthase α2β2 complex: a model for substrate channeling, allosteric communication, and pyridoxal phosphate catalysis.
Miles E
J Biol Chem. 2013; 288(14):10084-10091.
PMID: 23426371
PMC: 3617248.
DOI: 10.1074/jbc.X113.463331.
Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex.
Dunn M
Arch Biochem Biophys. 2012; 519(2):154-66.
PMID: 22310642
PMC: 3702454.
DOI: 10.1016/j.abb.2012.01.016.
Indole and 7-hydroxyindole diminish Pseudomonas aeruginosa virulence.
Lee J, Attila C, Cirillo S, Cirillo J, Wood T
Microb Biotechnol. 2011; 2(1):75-90.
PMID: 21261883
PMC: 3815423.
DOI: 10.1111/j.1751-7915.2008.00061.x.
Characterisation of the tryptophan synthase alpha subunit in maize.
Kriechbaumer V, Weigang L, Fiesselmann A, Letzel T, Frey M, Gierl A
BMC Plant Biol. 2008; 8:44.
PMID: 18430213
PMC: 2395261.
DOI: 10.1186/1471-2229-8-44.
Mutants of Drosophila Melanogaster Deficient in Xanthine Dehydrogenase.
Glassman E, MITCHELL H
Genetics. 1959; 44(2):153-62.
PMID: 17247815
PMC: 1209939.
DOI: 10.1093/genetics/44.2.153.
A technique for the assay of enzymes in intact plant cells in the presence of dimethylsulfoxide.
Delmer D, Mills S
Plant Physiol. 1969; 44(1):153-5.
PMID: 16657027
PMC: 396053.
DOI: 10.1104/pp.44.1.153.
STUDIES ON NORMAL AND GENETICALLY ALTERED TRYPTOPHAN SYNTHETASE FROM NEUROSPORA CRASSA.
Demoss J, Bonner D
Proc Natl Acad Sci U S A. 1959; 45(9):1405-12.
PMID: 16590520
PMC: 222729.
DOI: 10.1073/pnas.45.9.1405.
THE FORMATION OF A NEW ENZYMATICALLY ACTIVE PROTEIN AS A RESULT OF SUPPRESSION.
Crawford I, Yanofsky C
Proc Natl Acad Sci U S A. 1959; 45(8):1280-7.
PMID: 16590505
PMC: 222711.
DOI: 10.1073/pnas.45.8.1280.
THE EFFECTS OF DELETIONS, POINT MUTATIONS, REVERSIONS AND SUPPRESSOR MUTATIONS ON THE TWO COMPONENTS OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI.
Yanofsky C, Crawford I
Proc Natl Acad Sci U S A. 1959; 45(7):1016-26.
PMID: 16590470
PMC: 222680.
DOI: 10.1073/pnas.45.7.1016.
ENZYME COMPLEMENTATION IN VITRO BETWEEN ADENYLOSUCCINASELESS MUTANTS OF NEUROSPORA CRASSA.
Woodward D
Proc Natl Acad Sci U S A. 1959; 45(6):846-50.
PMID: 16590454
PMC: 222647.
DOI: 10.1073/pnas.45.6.846.
The favorable features of tryptophan synthase for proving Beadle and Tatum's one gene-one enzyme hypothesis.
Yanofsky C
Genetics. 2005; 169(2):511-6.
PMID: 15731515
PMC: 1449131.
DOI: 10.1093/genetics/169.2.511.
An inducible tryptophan synthetase in tryptophan auxotrophs of Escherichia coli.
NEWTON W, Snell E
Proc Natl Acad Sci U S A. 1962; 48:1431-9.
PMID: 14479374
PMC: 220970.
DOI: 10.1073/pnas.48.8.1431.
THE RIBOSOMAL ASSOCIATION OF THE DISSIMILAR POLYPEPTIDE CHAINS OF TRYPTOPHAN SYNTHETASE.
HORIBATA K, Kern M
Proc Natl Acad Sci U S A. 1964; 51:218-26.
PMID: 14124319
PMC: 300052.
DOI: 10.1073/pnas.51.2.218.
COMPLEMENTATION OF LECITHINASE ACTIVITIES BY CLOSELY RELATED PSEUDOMONADS: ITS TAXONOMIC IMPLICATION.
Bates J, LIU P
J Bacteriol. 1963; 86:585-92.
PMID: 14066442
PMC: 278477.
DOI: 10.1128/jb.86.3.585-592.1963.