| Year |
Citation |
Score |
| 2013 |
Vo J, Inwood W, Hayes JM, Kustu S. Mechanism for nitrogen isotope fractionation during ammonium assimilation by Escherichia coli K12. Proceedings of the National Academy of Sciences of the United States of America. 110: 8696-701. PMID 23650377 DOI: 10.1073/Pnas.1216683110 |
0.324 |
|
| 2012 |
Hall J, Yan D, Kustu S. The Pivotal Twin-Histidine Element of the Escherichia Coli Ammonium Channel AmtB Functions as a Substrate Selectivity Filter Biophysical Journal. 102: 682a. DOI: 10.1016/J.Bpj.2011.11.3707 |
0.372 |
|
| 2010 |
Kim KS, Pelton JG, Inwood WB, Andersen U, Kustu S, Wemmer DE. The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. Journal of Bacteriology. 192: 4089-102. PMID 20400551 DOI: 10.1128/Jb.00201-10 |
0.362 |
|
| 2009 |
Inwood WB, Hall JA, Kim KS, Fong R, Kustu S. Genetic evidence for an essential oscillation of transmembrane-spanning segment 5 in the Escherichia coli ammonium channel AmtB. Genetics. 183: 1341-55. PMID 19884311 DOI: 10.1534/Genetics.109.109579 |
0.41 |
|
| 2009 |
Inwood WB, Hall JA, Kim KS, Demirkhanyan L, Wemmer D, Zgurskaya H, Kustu S. Epistatic effects of the protease/chaperone HflB on some damaged forms of the Escherichia coli ammonium channel AmtB. Genetics. 183: 1327-40. PMID 19596908 DOI: 10.1534/Genetics.109.103747 |
0.444 |
|
| 2008 |
Yoshihara C, Inoue K, Schichnes D, Ruzin S, Inwood W, Kustu S. An Rh1-GFP fusion protein is in the cytoplasmic membrane of a white mutant strain of Chlamydomonas reinhardtii. Molecular Plant. 1: 1007-20. PMID 19825599 DOI: 10.1093/Mp/Ssn074 |
0.405 |
|
| 2008 |
Inwood W, Yoshihara C, Zalpuri R, Kim KS, Kustu S. The ultrastructure of a Chlamydomonas reinhardtii mutant strain lacking phytoene synthase resembles that of a colorless alga. Molecular Plant. 1: 925-37. PMID 19825593 DOI: 10.1093/Mp/Ssn046 |
0.302 |
|
| 2007 |
Fong RN, Kim KS, Yoshihara C, Inwood WB, Kustu S. The W148L substitution in the Escherichia coli ammonium channel AmtB increases flux and indicates that the substrate is an ion. Proceedings of the National Academy of Sciences of the United States of America. 104: 18706-11. PMID 17998534 DOI: 10.1073/Pnas.0709267104 |
0.406 |
|
| 2006 |
Loh KD, Gyaneshwar P, Markenscoff Papadimitriou E, Fong R, Kim KS, Parales R, Zhou Z, Inwood W, Kustu S. A previously undescribed pathway for pyrimidine catabolism. Proceedings of the National Academy of Sciences of the United States of America. 103: 5114-9. PMID 16540542 DOI: 10.1073/Pnas.0600521103 |
0.363 |
|
| 2005 |
Kim KS, Feild E, King N, Yaoi T, Kustu S, Inwood W. Spontaneous mutations in the ammonium transport gene AMT4 of Chlamydomonas reinhardtii. Genetics. 170: 631-44. PMID 15802504 DOI: 10.1534/Genetics.105.041574 |
0.355 |
|
| 2005 |
Altman S, Bassler BL, Beckwith J, Belfort M, Berg HC, Bloom B, Brenchley JE, Campbell A, Collier RJ, Connell N, Cozzarelli NR, Craig NL, Darst S, Ebright RH, Elledge SJ, ... ... Kustu SG, et al. An open letter to Elias Zerhouni. Science (New York, N.Y.). 307: 1409-10. PMID 15746409 DOI: 10.1126/Science.307.5714.1409C |
0.447 |
|
| 2005 |
Gyaneshwar P, Paliy O, McAuliffe J, Jones A, Jordan MI, Kustu S. Lessons from Escherichia coli genes similarly regulated in response to nitrogen and sulfur limitation. Proceedings of the National Academy of Sciences of the United States of America. 102: 3453-8. PMID 15716358 DOI: 10.1073/Pnas.0500141102 |
0.347 |
|
| 2005 |
Gyaneshwar P, Paliy O, McAuliffe J, Popham DL, Jordan MI, Kustu S. Sulfur and nitrogen limitation in Escherichia coli K-12: specific homeostatic responses. Journal of Bacteriology. 187: 1074-90. PMID 15659685 DOI: 10.1128/Jb.187.3.1074-1090.2005 |
0.315 |
|
| 2004 |
Soupene E, Inwood W, Kustu S. Lack of the Rhesus protein Rh1 impairs growth of the green alga Chlamydomonas reinhardtii at high CO2. Proceedings of the National Academy of Sciences of the United States of America. 101: 7787-92. PMID 15096599 DOI: 10.1073/Pnas.0401809101 |
0.406 |
|
| 2003 |
Lee SY, De La Torre A, Yan D, Kustu S, Nixon BT, Wemmer DE. Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains. Genes & Development. 17: 2552-63. PMID 14561776 DOI: 10.1101/Gad.1125603 |
0.475 |
|
| 2003 |
Soupene E, van Heeswijk WC, Plumbridge J, Stewart V, Bertenthal D, Lee H, Prasad G, Paliy O, Charernnoppakul P, Kustu S. Physiological studies of Escherichia coli strain MG1655: growth defects and apparent cross-regulation of gene expression. Journal of Bacteriology. 185: 5611-26. PMID 12949114 DOI: 10.1128/Jb.185.18.5611-5626.2003 |
0.303 |
|
| 2003 |
Hastings CA, Lee SY, Cho HS, Yan D, Kustu S, Wemmer DE. High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain. Biochemistry. 42: 9081-90. PMID 12885241 DOI: 10.1021/Bi0273866 |
0.431 |
|
| 2003 |
Corbin RW, Paliy O, Yang F, Shabanowitz J, Platt M, Lyons CE, Root K, McAuliffe J, Jordan MI, Kustu S, Soupene E, Hunt DF. Toward a protein profile of Escherichia coli: comparison to its transcription profile. Proceedings of the National Academy of Sciences of the United States of America. 100: 9232-7. PMID 12878731 DOI: 10.1073/Pnas.1533294100 |
0.423 |
|
| 2003 |
Hastings CA, Lee S-, Cho HS, Yan D, Kustu S, Wemmer DE. Solution structure and backbone dynamics of beryllofluoride-activated NTRC receiver domain Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb1Krw/Pdb |
0.326 |
|
| 2002 |
Soupene E, King N, Lee H, Kustu S. Aquaporin Z of Escherichia coli: reassessment of its regulation and physiological role. Journal of Bacteriology. 184: 4304-7. PMID 12107150 DOI: 10.1128/Jb.184.15.4304-4307.2002 |
0.34 |
|
| 2002 |
Soupene E, King N, Feild E, Liu P, Niyogi KK, Huang CH, Kustu S. Rhesus expression in a green alga is regulated by CO(2). Proceedings of the National Academy of Sciences of the United States of America. 99: 7769-73. PMID 12032358 DOI: 10.1073/Pnas.112225599 |
0.322 |
|
| 2002 |
Soupene E, Chu T, Corbin RW, Hunt DF, Kustu S. Gas channels for NH(3): proteins from hyperthermophiles complement an Escherichia coli mutant. Journal of Bacteriology. 184: 3396-400. PMID 12029058 DOI: 10.1128/Jb.184.12.3396-3400.2002 |
0.433 |
|
| 2002 |
Soupene E, Lee H, Kustu S. Ammonium/methylammonium transport (Amt) proteins facilitate diffusion of NH3 bidirectionally. Proceedings of the National Academy of Sciences of the United States of America. 99: 3926-31. PMID 11891327 DOI: 10.1073/Pnas.062043799 |
0.388 |
|
| 2001 |
Cho HS, Pelton JG, Yan D, Kustu S, Wemmer DE. Phosphoaspartates in bacterial signal transduction. Current Opinion in Structural Biology. 11: 679-84. PMID 11751048 DOI: 10.1016/S0959-440X(01)00271-8 |
0.407 |
|
| 2001 |
Soupene E, Ramirez RM, Kustu S. Evidence that fungal MEP proteins mediate diffusion of the uncharged species NH(3) across the cytoplasmic membrane. Molecular and Cellular Biology. 21: 5733-41. PMID 11486013 DOI: 10.1128/Mcb.21.17.5733-5741.2001 |
0.383 |
|
| 2001 |
Cho H, Wang W, Kim R, Yokota H, Damo S, Kim SH, Wemmer D, Kustu S, Yan D. BeF3 - acts as a phosphate analog in proteins phosphorylated on aspartate: Structure of a BeF3 - complex with phosphoserine phosphatase Proceedings of the National Academy of Sciences of the United States of America. 98: 8525-8530. PMID 11438683 DOI: 10.1073/Pnas.131213698 |
0.464 |
|
| 2001 |
Lee SY, Cho HS, Pelton JG, Yan D, Henderson RK, King DS, Huang L, Kustu S, Berry EA, Wemmer DE. Crystal structure of an activated response regulator bound to its target. Nature Structural Biology. 8: 52-6. PMID 11135671 DOI: 10.1038/83053 |
0.338 |
|
| 2000 |
Zimmer DP, Soupene E, Lee HL, Wendisch VF, Khodursky AB, Peter BJ, Bender RA, Kustu S. Nitrogen regulatory protein C-controlled genes of Escherichia coli: scavenging as a defense against nitrogen limitation. Proceedings of the National Academy of Sciences of the United States of America. 97: 14674-9. PMID 11121068 DOI: 10.1073/Pnas.97.26.14674 |
0.43 |
|
| 2000 |
Lee J, Owens JT, Hwang I, Meares C, Kustu S. Phosphorylation-induced signal propagation in the response regulator NtrC Journal of Bacteriology. 182: 5188-5195. PMID 10960104 DOI: 10.1128/Jb.182.18.5188-5195.2000 |
0.625 |
|
| 2000 |
Cho HS, Lee SY, Yan D, Pan X, Parkinson JS, Kustu S, Wemmer DE, Pelton JG. NMR structure of activated CheY. Journal of Molecular Biology. 297: 543-51. PMID 10731410 DOI: 10.1006/Jmbi.2000.3595 |
0.448 |
|
| 1999 |
Kern D, Volkman BF, Luginbühl P, Nohaile MJ, Kustu S, Wemmer DE. Structure of a transiently phosphorylated switch in bacterial signal transduction. Nature. 402: 894-8. PMID 10622255 DOI: 10.1038/47273 |
0.47 |
|
| 1999 |
Yan D, Cho HS, Hastings CA, Igo MM, Lee SY, Pelton JG, Stewart V, Wemmer DE, Kustu S. Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators. Proceedings of the National Academy of Sciences of the United States of America. 96: 14789-94. PMID 10611291 DOI: 10.1073/Pnas.96.26.14789 |
0.443 |
|
| 1999 |
Yan D, Kustu S. "Switch I" mutant forms of the bacterial enhancer-binding protein NtrC that perturb the response to DNA. Proceedings of the National Academy of Sciences of the United States of America. 96: 13142-6. PMID 10557287 DOI: 10.1073/Pnas.96.23.13142 |
0.542 |
|
| 1999 |
Pelton JG, Kustu S, Wemmer DE. Solution structure of the DNA-binding domain of NtrC with three alanine substitutions. Journal of Molecular Biology. 292: 1095-110. PMID 10512705 DOI: 10.1006/Jmbi.1999.3140 |
0.489 |
|
| 1999 |
Li J, Passaglia L, Rombel I, Yan D, Kustu S. Mutations affecting motifs of unknown function in the central domain of nitrogen regulatory protein C. Journal of Bacteriology. 181: 5443-54. PMID 10464219 DOI: 10.1128/Jb.181.17.5443-5454.1999 |
0.561 |
|
| 1999 |
Hu P, Leighton T, Ishkhanova G, Kustu S. Sensing of nitrogen limitation by Bacillus subtilis: comparison to enteric bacteria. Journal of Bacteriology. 181: 5042-50. PMID 10438777 DOI: 10.1128/Jb.181.16.5042-5050.1999 |
0.302 |
|
| 1999 |
Rombel I, Peters-Wendisch P, Mesecar A, Thorgeirsson T, Shin YK, Kustu S. MgATP binding and hydrolysis determinants of NtrC, a bacterial enhancer-binding protein. Journal of Bacteriology. 181: 4628-38. PMID 10419963 DOI: 10.1128/Jb.181.15.4628-4638.1999 |
0.461 |
|
| 1999 |
Hwang I, Thorgeirsson T, Lee J, Kustu S, Shin YK. Physical evidence for a phosphorylation-dependent conformational change in the enhancer-binding protein NtrC. Proceedings of the National Academy of Sciences of the United States of America. 96: 4880-5. PMID 10220387 DOI: 10.1073/Pnas.96.9.4880 |
0.676 |
|
| 1998 |
He L, Soupene E, Ninfa A, Kustu S. Physiological role for the GlnK protein of enteric bacteria: relief of NifL inhibition under nitrogen-limiting conditions. Journal of Bacteriology. 180: 6661-7. PMID 9852012 DOI: 10.1128/Jb.180.24.6661-6667.1998 |
0.408 |
|
| 1998 |
Soupene E, He L, Yan D, Kustu S. Ammonia acquisition in enteric bacteria: physiological role of the ammonium/methylammonium transport B (AmtB) protein. Proceedings of the National Academy of Sciences of the United States of America. 95: 7030-4. PMID 9618533 DOI: 10.1073/Pnas.95.12.7030 |
0.375 |
|
| 1997 |
He L, Soupene E, Kustu S. NtrC is required for control of Klebsiella pneumoniae NifL activity. Journal of Bacteriology. 179: 7446-55. PMID 9393710 DOI: 10.1128/Jb.179.23.7446-7455.1997 |
0.417 |
|
| 1997 |
Nohaile M, Kern D, Wemmer D, Stedman K, Kustu S. Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: Evidence for an activating surface Journal of Molecular Biology. 273: 299-316. PMID 9367763 DOI: 10.1006/Jmbi.1997.1296 |
0.696 |
|
| 1997 |
North AK, Kustu S. Mutant forms of the enhancer-binding protein NtrC can activate transcription from solution. Journal of Molecular Biology. 267: 17-36. PMID 9096204 DOI: 10.1006/Jmbi.1996.0838 |
0.541 |
|
| 1997 |
Wyman C, Rombel I, North AK, Bustamante C, Kustu S. Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein. Science (New York, N.Y.). 275: 1658-61. PMID 9054362 DOI: 10.1126/Science.275.5306.1658 |
0.498 |
|
| 1996 |
North AK, Weiss DS, Suzuki H, Flashner Y, Kustu S. Repressor forms of the enhancer-binding protein NrtC: some fail in coupling ATP hydrolysis to open complex formation by sigma 54-holoenzyme. Journal of Molecular Biology. 260: 317-31. PMID 8757796 DOI: 10.1006/Jmbi.1996.0403 |
0.605 |
|
| 1995 |
Berger DK, Narberhaus F, Lee HS, Kustu S. In vitro studies of the domains of the nitrogen fixation regulatory protein NIFA. Journal of Bacteriology. 177: 191-9. PMID 8002617 DOI: 10.1128/Jb.177.1.191-199.1995 |
0.547 |
|
| 1995 |
Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE. Three-dimensional solution structure of the N-terminal receiver domain of NTRC. Biochemistry. 34: 1413-24. PMID 7827089 DOI: 10.1021/Bi00004A036 |
0.406 |
|
| 1995 |
Narberhaus F, Lee HS, Schmitz RA, He L, Kustu S. The C-terminal domain of NifL is sufficient to inhibit NifA activity. Journal of Bacteriology. 177: 5078-87. PMID 7665487 DOI: 10.1128/Jb.177.17.5078-5087.1995 |
0.511 |
|
| 1995 |
Wedel A, Kustu S. The bacterial enhancer-binding protein NTRC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation. Genes & Development. 9: 2042-52. PMID 7649482 DOI: 10.1101/Gad.9.16.2042 |
0.451 |
|
| 1995 |
Flashner Y, Weiss DS, Keener J, Kustu S. Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain. Journal of Molecular Biology. 249: 700-13. PMID 7602583 DOI: 10.1006/Jmbi.1995.0330 |
0.6 |
|
| 1994 |
Berger DK, Narberhaus F, Kustu S. The isolated catalytic domain of NIFA, a bacterial enhancer-binding protein, activates transcription in vitro: activation is inhibited by NIFL. Proceedings of the National Academy of Sciences of the United States of America. 91: 103-7. PMID 8278350 DOI: 10.1073/Pnas.91.1.103 |
0.52 |
|
| 1994 |
Klose KE, North AK, Stedman KM, Kustu S. The major dimerization determinants of the nitrogen regulatory protein NTRC from enteric bacteria lie in its carboxy-terminal domain. Journal of Molecular Biology. 241: 233-45. PMID 8057363 DOI: 10.1006/Jmbi.1994.1492 |
0.753 |
|
| 1994 |
Li J, Kustu S, Stewart V. In vitro interaction of nitrate-responsive regulatory protein NarL with DNA target sequences in the fdnG, narG, narK and frdA operon control regions of Escherichia coli K-12. Journal of Molecular Biology. 241: 150-65. PMID 8057356 DOI: 10.1006/Jmbi.1994.1485 |
0.506 |
|
| 1993 |
Lee HS, Berger DK, Kustu S. Activity of purified NIFA, a transcriptional activator of nitrogen fixation genes. Proceedings of the National Academy of Sciences of the United States of America. 90: 2266-70. PMID 8460132 DOI: 10.1073/Pnas.90.6.2266 |
0.507 |
|
| 1993 |
Klose KE, Weiss DS, Kustu S. Glutamate at the site of phosphorylation of nitrogen-regulatory protein NTRC mimics aspartyl-phosphate and activates the protein. Journal of Molecular Biology. 232: 67-78. PMID 8331671 DOI: 10.1006/Jmbi.1993.1370 |
0.705 |
|
| 1993 |
North AK, Klose KE, Stedman KM, Kustu S. Prokaryotic enhancer-binding proteins reflect eukaryote-like modularity: the puzzle of nitrogen regulatory protein C. Journal of Bacteriology. 175: 4267-73. PMID 8331061 DOI: 10.1128/Jb.175.14.4267-4273.1993 |
0.731 |
|
| 1993 |
Lee HS, Narberhaus F, Kustu S. In vitro activity of NifL, a signal transduction protein for biological nitrogen fixation. Journal of Bacteriology. 175: 7683-8. PMID 8244938 DOI: 10.1128/Jb.175.23.7683-7688.1993 |
0.467 |
|
| 1993 |
Lee HS, Ishihama A, Kustu S. The C terminus of the alpha subunit of RNA polymerase is not essential for transcriptional activation of sigma 54 holoenzyme. Journal of Bacteriology. 175: 2479-82. PMID 8096842 DOI: 10.1128/Jb.175.8.2479-2482.1993 |
0.464 |
|
| 1993 |
Porter SC, North AK, Wedel AB, Kustu S. Oligomerization of NTRC at the glnA enhancer is required for transcriptional activation. Genes & Development. 7: 2258-73. PMID 7901122 DOI: 10.1101/Gad.7.11.2258 |
0.543 |
|
| 1992 |
Santero E, Hoover TR, North AK, Berger DK, Porter SC, Kustu S. Role of integration host factor in stimulating transcription from the sigma 54-dependent nifH promoter. Journal of Molecular Biology. 227: 602-20. PMID 1404379 DOI: 10.1016/0022-2836(92)90211-2 |
0.465 |
|
| 1992 |
Weiss DS, Klose KE, Hoover TR, North AK, Porter SC, Wedel AB, Kustu S. 25 Prokaryotic Transcriptional Enhancers Cold Spring Harbor Monograph Archive. 667-694. DOI: 10.1101/087969425.22B.667 |
0.515 |
|
| 1991 |
Popham D, Keener J, Kustu S. Purification of the alternative σ factor, σ54, from Salmonella typhimurium and characterization of σ54-holoenzyme Journal of Biological Chemistry. 266: 19510-19518. PMID 1918063 |
0.336 |
|
| 1991 |
Batut J, Santero E, Kustu S. In vitro activity of the nitrogen fixation regulatory protein FIXJ from Rhizobium meliloti. Journal of Bacteriology. 173: 5914-7. PMID 1885556 DOI: 10.1128/Jb.173.18.5914-5917.1991 |
0.465 |
|
| 1991 |
Weiss DS, Batut J, Klose KE, Keener J, Kustu S. The phosphorylated form of the enhancer-binding protein NTRC has an ATPase activity that is essential for activation of transcription. Cell. 67: 155-67. PMID 1833069 DOI: 10.1016/0092-8674(91)90579-N |
0.686 |
|
| 1991 |
Kustu S, North AK, Weiss DS. Prokaryotic transcriptional enhancers and enhancer-binding proteins. Trends in Biochemical Sciences. 16: 397-402. PMID 1776167 DOI: 10.1016/0968-0004(91)90163-P |
0.489 |
|
| 1990 |
Hoover TR, Santero E, Porter S, Kustu S. The integration host factor stimulates interaction of RNA polymerase with NIFA, the transcriptional activator for nitrogen fixation operons Cell. 63: 11-22. PMID 2208275 DOI: 10.1016/0092-8674(90)90284-L |
0.45 |
|
| 1990 |
Su W, Porter S, Kustu S, Echols H. DNA-looping and enhancer activity: association between DNA-bound NtrC activator and RNA polymerase at the bacterial glnA promoter. Proceedings of the National Academy of Sciences of the United States of America. 87: 5504-8. PMID 2164685 DOI: 10.1073/Pnas.87.14.5504 |
0.39 |
|
| 1990 |
Wedel A, Weiss DS, Popham D, Dröge P, Kustu S. A bacterial enhancer functions to tether a transcriptional activator near a promoter. Science (New York, N.Y.). 248: 486-90. PMID 1970441 DOI: 10.1126/Science.1970441 |
0.432 |
|
| 1989 |
Santero E, Hoover T, Keener J, Kustu S. In vitro activity of the nitrogen fixation regulatory protein NIFA Proceedings of the National Academy of Sciences of the United States of America. 86: 7346-7350. PMID 2678099 DOI: 10.1073/Pnas.86.19.7346 |
0.452 |
|
| 1989 |
Popham DL, Szeto D, Keener J, Kustu S. Function of a bacterial activator protein that binds to transcriptional enhancers Science. 243: 629-635. PMID 2563595 DOI: 10.1126/Science.2563595 |
0.509 |
|
| 1988 |
Keener J, Dale EC, Kustu S, Calendar R. In vitro transcription from the late promoter of bacteriophage P4. Journal of Bacteriology. 170: 3543-6. PMID 3403508 DOI: 10.1128/Jb.170.8.3543-3546.1988 |
0.401 |
|
| 1988 |
Keener J, Kustu S. Protein kinase and phosphoprotein phosphatase activities of nitrogen regulatory proteins NTRB and NTRC of enteric bacteria: roles of the conserved amino-terminal domain of NTRC Proceedings of the National Academy of Sciences of the United States of America. 85: 4976-4980. PMID 2839825 |
0.459 |
|
| 1987 |
Wong PK, Popham D, Keener J, Kustu S. In vitro transcription of the nitrogen fixation regulatory operon nifLA of Klebsiella pneumoniae Journal of Bacteriology. 169: 2876-2880. PMID 3294810 DOI: 10.1128/Jb.169.6.2876-2880.1987 |
0.468 |
|
| 1985 |
Ames GF, Prody C, Kustu S. Simple, rapid, and quantitative release of periplasmic proteins by chloroform. Journal of Bacteriology. 160: 1181-3. PMID 6501229 DOI: 10.1128/JB.160.3.1181-1183.1984 |
0.313 |
|
| 1985 |
Hirschman J, Wong PK, Sei K, Keener J, Kustu S. Products of nitrogen regulatory genes ntrA and ntrC of enteric bacteria activate glnA transcription in vitro: evidence that the ntrA product is a sigma factor. Proceedings of the National Academy of Sciences of the United States of America. 82: 7525-9. PMID 2999766 DOI: 10.1073/pnas.82.22.7525 |
0.32 |
|
| 1981 |
McFarland N, McCarter L, Artz S, Kustu S. Nitrogen regulatory locus "glnR" of enteric bacteria is composed of cistrons ntrB and ntrC: identification of their protein products. Proceedings of the National Academy of Sciences of the United States of America. 78: 2135-9. PMID 6113591 DOI: 10.1073/Pnas.78.4.2135 |
0.437 |
|
| 1980 |
Kustu S, Burton D, Garcia E, McCarter L, McFarland N. Nitrogen control in Salmonella: regulation by the glnR and glnF gene products. Proceedings of the National Academy of Sciences of the United States of America. 76: 4576-80. PMID 41244 DOI: 10.1073/Pnas.76.9.4576 |
0.387 |
|
| 1979 |
Kustu SG, McFarland NC, Hui SP, Esmon B, Ames GF. Nitrogen control of Salmonella typhimurium: co-regulation of synthesis of glutamine synthetase and amino acid transport systems. Journal of Bacteriology. 138: 218-34. PMID 35521 DOI: 10.1128/Jb.138.1.218-234.1979 |
0.421 |
|
| 1973 |
Kustu SG, Ames GF. The hisP protein, a known histidine transport component in Salmonella typhimurium, is also an arginine transport component. Journal of Bacteriology. 116: 107-13. PMID 4583201 DOI: 10.1128/Jb.116.1.107-113.1973 |
0.386 |
|
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