| Year |
Citation |
Score |
| 2005 |
Ames GF, Nikaido K. Phosphate-Containing Proteins of Salmonella typhimurium and Escherichia coii Febs Journal. 115: 525-531. DOI: 10.1111/J.1432-1033.1981.Tb06234.X |
0.371 |
|
| 2001 |
Ames GF, Nikaido K, Wang IX, Liu PQ, Liu CE, Hu C. Purification and characterization of the membrane-bound complex of an ABC transporter, the histidine permease. Journal of Bioenergetics and Biomembranes. 33: 79-92. PMID 11456221 DOI: 10.1023/A:1010797029183 |
0.457 |
|
| 1999 |
Nikaido K, Ames GF. One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease. The Journal of Biological Chemistry. 274: 26727-35. PMID 10480876 DOI: 10.1074/Jbc.274.38.26727 |
0.445 |
|
| 1999 |
Liu PQ, Liu CE, Ames GF. Modulation of ATPase activity by physical disengagement of the ATP-binding domains of an ABC transporter, the histidine permease. The Journal of Biological Chemistry. 274: 18310-8. PMID 10373434 DOI: 10.1074/Jbc.274.26.18310 |
0.463 |
|
| 1999 |
Liu CE, Liu PQ, Wolf A, Lin E, Ames GF. Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. Effect of different ligands and consequences for the mechanism of action. The Journal of Biological Chemistry. 274: 739-47. PMID 9873010 DOI: 10.1074/Jbc.274.2.739 |
0.482 |
|
| 1998 |
Hung LW, Wang IX, Nikaido K, Liu PQ, Ames GF, Kim SH. Crystal structure of the ATP-binding subunit of an ABC transporter. Nature. 396: 703-7. PMID 9872322 DOI: 10.1038/25393 |
0.518 |
|
| 1998 |
Liu PQ, Ames GF. In vitro disassembly and reassembly of an ABC transporter, the histidine permease. Proceedings of the National Academy of Sciences of the United States of America. 95: 3495-500. PMID 9520394 DOI: 10.1073/Pnas.95.7.3495 |
0.468 |
|
| 1997 |
Nikaido K, Liu PQ, Ames GF. Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity. The Journal of Biological Chemistry. 272: 27745-52. PMID 9346917 DOI: 10.1074/Jbc.272.44.27745 |
0.466 |
|
| 1997 |
Liu CE, Liu PQ, Ames GF. Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter). The Journal of Biological Chemistry. 272: 21883-91. PMID 9268321 DOI: 10.1074/Jbc.272.35.21883 |
0.45 |
|
| 1997 |
Liu CE, Ames GF. Characterization of transport through the periplasmic histidine permease using proteoliposomes reconstituted by dialysis. The Journal of Biological Chemistry. 272: 859-66. PMID 8995374 DOI: 10.1074/Jbc.272.2.859 |
0.514 |
|
| 1996 |
Wolf A, Lee KC, Kirsch JF, Ames GF. Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity. The Journal of Biological Chemistry. 271: 21243-50. PMID 8702898 DOI: 10.1074/Jbc.271.35.21243 |
0.403 |
|
| 1996 |
Ames GF, Liu CE, Joshi AK, Nikaido K. Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases. The Journal of Biological Chemistry. 271: 14264-70. PMID 8662800 DOI: 10.1074/Jbc.271.24.14264 |
0.381 |
|
| 1996 |
Hecht K, Zhang S, Klopotowski T, Ames GF. D-histidine utilization in Salmonella typhimurium is controlled by the leucine-responsive regulatory protein (Lrp). Journal of Bacteriology. 178: 327-31. PMID 8550449 DOI: 10.1128/Jb.178.2.327-331.1996 |
0.367 |
|
| 1995 |
Wolf A, Shaw EW, Oh BH, De Bondt H, Joshi AK, Ames GF. Structure/function analysis of the periplasmic histidine-binding protein. Mutations decreasing ligand binding alter the properties of the conformational change and of the closed form. The Journal of Biological Chemistry. 270: 16097-106. PMID 7608172 DOI: 10.1074/Jbc.270.27.16097 |
0.412 |
|
| 1995 |
Oh BH, Kang CH, Bondt HD, Kim SH, Nikaido K, Joshi AK, Ames GF. The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins. Journal of Biological Chemistry. 269: 4135-4143. DOI: 10.2210/Pdb1Hpb/Pdb |
0.438 |
|
| 1994 |
Oh BH, Kang CH, De Bondt H, Kim SH, Nikaido K, Joshi AK, Ames GF. The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins. The Journal of Biological Chemistry. 269: 4135-43. PMID 8307974 |
0.339 |
|
| 1994 |
Ames GF. Isolation and purification of periplasmic binding proteins. Methods in Enzymology. 235: 234-41. PMID 8057897 DOI: 10.1016/0076-6879(94)35144-9 |
0.399 |
|
| 1994 |
Oh BH, Ames GF, Kim SH. Structural basis for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein. The Journal of Biological Chemistry. 269: 26323-30. PMID 7929349 DOI: 10.2210/Pdb1Laf/Pdb |
0.386 |
|
| 1994 |
Oh BH, Pandit J, Kang CH, Nikaido K, Gokcen S, Ames GF, Kim SH. Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. Journal of Biological Chemistry. 268: 11348-11355. DOI: 10.2210/Pdb1Lst/Pdb |
0.438 |
|
| 1993 |
Oh BH, Pandit J, Kang CH, Nikaido K, Gokcen S, Ames GF, Kim SH. Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. The Journal of Biological Chemistry. 268: 11348-55. PMID 8496186 |
0.339 |
|
| 1993 |
Baichwal V, Liu D, Ames GF. The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface. Proceedings of the National Academy of Sciences of the United States of America. 90: 620-4. PMID 7678461 DOI: 10.1073/Pnas.90.2.620 |
0.463 |
|
| 1992 |
Kerppola RE, Ames GF. Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family. The Journal of Biological Chemistry. 267: 2329-36. PMID 1733937 |
0.32 |
|
| 1992 |
Dimri GP, Rudd KE, Morgan MK, Bayat H, Ames GF. Physical mapping of repetitive extragenic palindromic sequences in Escherichia coli and phylogenetic distribution among Escherichia coli strains and other enteric bacteria. Journal of Bacteriology. 174: 4583-93. PMID 1624447 DOI: 10.1128/Jb.174.14.4583-4593.1992 |
0.325 |
|
| 1992 |
Kang CH, Gokcen S, Ames GF. Crystallization and preliminary X-ray studies of the liganded lysine, arginine, ornithine-binding protein from Salmonella typhimurium. Journal of Molecular Biology. 225: 1123-5. PMID 1613794 DOI: 10.1016/0022-2836(92)90109-W |
0.325 |
|
| 1992 |
Ames GF, Mimura CS, Holbrook SR, Shyamala V. Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Advances in Enzymology and Related Areas of Molecular Biology. 65: 1-47. PMID 1533298 DOI: 10.1002/9780470123119.Ch1 |
0.433 |
|
| 1992 |
Ames GF. Bacterial periplasmic permeases as model systems for the superfamily of traffic ATPases, including the multidrug resistance protein and the cystic fibrosis transmembrane conductance regulator. International Review of Cytology. 137: 1-35. PMID 1385348 DOI: 10.1016/S0074-7696(08)62672-8 |
0.485 |
|
| 1992 |
Ames GF, Lecar H. ATP-dependent bacterial transporters and cystic fibrosis: analogy between channels and transporters. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 6: 2660-6. PMID 1377140 DOI: 10.1096/Fasebj.6.9.1377140 |
0.431 |
|
| 1991 |
Speiser DM, Ames GF. Salmonella typhimurium histidine periplasmic permease mutations that allow transport in the absence of histidine-binding proteins. Journal of Bacteriology. 173: 1444-51. PMID 1995591 DOI: 10.1128/Jb.173.4.1444-1451.1991 |
0.512 |
|
| 1991 |
Petronilli V, Ames GF. Binding protein-independent histidine permease mutants. Uncoupling of ATP hydrolysis from transmembrane signaling. The Journal of Biological Chemistry. 266: 16293-6. PMID 1885562 |
0.363 |
|
| 1991 |
Shyamala V, Ames GF. Use of exonuclease for rapid polymerase-chain-reaction-based in vitro mutagenesis. Gene. 97: 1-6. PMID 1825304 DOI: 10.1016/0378-1119(91)90002-S |
0.313 |
|
| 1991 |
Kang CH, Shin WC, Yamagata Y, Gokcen S, Ames GF, Kim SH. Crystal structure of the lysine-, arginine-, ornithine-binding protein (LAO) from Salmonella typhimurium at 2.7-A resolution. The Journal of Biological Chemistry. 266: 23893-9. PMID 1748660 |
0.402 |
|
| 1990 |
Shyamala V, Schneider E, Ames GF. Tandem chromosomal duplications: role of REP sequences in the recombination event at the join-point. The Embo Journal. 9: 939-46. PMID 2178927 DOI: 10.1002/J.1460-2075.1990.Tb08192.X |
0.328 |
|
| 1990 |
Ames GF, Joshi AK. Energy coupling in bacterial periplasmic permeases. Journal of Bacteriology. 172: 4133-7. PMID 2142937 DOI: 10.1128/Jb.172.8.4133-4137.1990 |
0.508 |
|
| 1989 |
Shyamala V, Ames GF. Genome walking by single-specific-primer polymerase chain reaction: SSP-PCR. Gene. 84: 1-8. PMID 2691331 DOI: 10.1016/0378-1119(89)90132-7 |
0.336 |
|
| 1989 |
Bishop L, Agbayani R, Ambudkar SV, Maloney PC, Ames GF. Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport. Proceedings of the National Academy of Sciences of the United States of America. 86: 6953-7. PMID 2674940 DOI: 10.1073/Pnas.86.18.6953 |
0.484 |
|
| 1989 |
Prossnitz E, Gee A, Ames GF. Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and interaction between the binding protein and the membrane complex. The Journal of Biological Chemistry. 264: 5006-14. PMID 2647746 |
0.598 |
|
| 1989 |
Shyamala V, Ames GF. Amplification of bacterial genomic DNA by the polymerase chain reaction and direct sequencing after asymmetric amplification: application to the study of periplasmic permeases. Journal of Bacteriology. 171: 1602-8. PMID 2646290 DOI: 10.1128/Jb.171.3.1602-1608.1989 |
0.336 |
|
| 1989 |
Schneider E, Bishop L, Schneider E, Alfandary V, Ames GF. Fine-structure genetic map of the maltose transport operon of Salmonella typhimurium. Journal of Bacteriology. 171: 5860-5. PMID 2553663 DOI: 10.1128/Jb.171.11.5860-5865.1989 |
0.431 |
|
| 1988 |
Ames GF. Structure and mechanism of bacterial periplasmic transport systems. Journal of Bioenergetics and Biomembranes. 20: 1-18. PMID 3279024 DOI: 10.1007/Bf00762135 |
0.506 |
|
| 1988 |
Stern MJ, Prossnitz E, Ames GF. Role of the intercistronic region in post-transcriptional control of gene expression in the histidine transport operon of Salmonella typhimurium: involvement of REP sequences. Molecular Microbiology. 2: 141-52. PMID 3130541 DOI: 10.1111/J.1365-2958.1988.Tb00015.X |
0.511 |
|
| 1988 |
Yang Y, Ames GF. DNA gyrase binds to the family of prokaryotic repetitive extragenic palindromic sequences. Proceedings of the National Academy of Sciences of the United States of America. 85: 8850-4. PMID 2848243 DOI: 10.1073/Pnas.85.23.8850 |
0.374 |
|
| 1987 |
Schmitz G, Dürre P, Mullenbach G, Ames GF. Nitrogen regulation of transport operons: analysis of promoters argTr and dhuA. Molecular & General Genetics : Mgg. 209: 403-7. PMID 3118148 DOI: 10.1007/Bf00329673 |
0.387 |
|
| 1985 |
Payne GM, Spudich EN, Ames GF. A mutational hot-spot in the hisM gene of the histidine transport operon in Salmonella typhimurium is due to deletion of repeated sequences and results in an altered specificity of transport. Molecular & General Genetics : Mgg. 200: 493-6. PMID 3900641 DOI: 10.1007/Bf00425737 |
0.514 |
|
| 1985 |
Ames GF. Chapter 6 The Histidine Transport System of Salmonella typhimurium Current Topics in Membranes and Transport. 23: 103-119. DOI: 10.1016/S0070-2161(08)60152-5 |
0.496 |
|
| 1984 |
Stern MJ, Ames GF, Smith NH, Robinson EC, Higgins CF. Repetitive extragenic palindromic sequences: a major component of the bacterial genome. Cell. 37: 1015-26. PMID 6378385 DOI: 10.1016/0092-8674(84)90436-7 |
0.536 |
|
| 1984 |
Hobson AC, Weatherwax R, Ames GF. ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system. Proceedings of the National Academy of Sciences of the United States of America. 81: 7333-7. PMID 6239289 |
0.365 |
|
| 1984 |
Stern MJ, Higgins CF, Ames GF. Isolation and characterization of lac fusions to two nitrogen-regulated promoters. Molecular & General Genetics : Mgg. 195: 219-27. PMID 6092849 DOI: 10.1007/Bf00332750 |
0.573 |
|
| 1983 |
Ames GF, Higgins CF. The organization, mechanism of action, and evolution of periplasmic transport systems Trends in Biochemical Sciences. 8: 97-100. DOI: 10.1016/0968-0004(83)90259-1 |
0.594 |
|
| 1982 |
Higgins CF, Haag PD, Nikaido K, Ardeshir F, Garcia G, Ames GF. Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium Nature. 298: 723-727. PMID 7050725 DOI: 10.1038/298723a0 |
0.648 |
|
| 1982 |
Higgins CF, Ames GF. Regulatory regions of two transport operons under nitrogen control: nucleotide sequences. Proceedings of the National Academy of Sciences of the United States of America. 79: 1083-7. PMID 7041112 DOI: 10.1073/pnas.79.4.1083 |
0.614 |
|
| 1981 |
Higgins CF, Ames GF. Two periplasmic transport proteins which interact with a common membrane receptor show extensive homology: complete nucleotide sequences. Proceedings of the National Academy of Sciences of the United States of America. 78: 6038-42. PMID 6273842 DOI: 10.1073/Pnas.78.10.6038 |
0.64 |
|
| 1981 |
Ardeshir F, Higgins CF, Ames GF. Physical map of the Salmonella typhimurium histidine transport operon: correlation with the genetic map. Journal of Bacteriology. 147: 401-9. PMID 6267009 DOI: 10.1128/Jb.147.2.401-409.1981 |
0.58 |
|
| 1980 |
Ardeshir F, Ames GF. Cloning of the histidine transport genes from Salmonella typhimurium and characterization of an analogous transport system in Escherichia coli. Journal of Supramolecular Structure. 13: 117-30. PMID 6449635 DOI: 10.1002/Jss.400130111 |
0.485 |
|
| 1980 |
LeVine SM, Ardeshir F, Ames GF. Isolation and Characterization of acetate kinase and phosphotransacetylase mutants of Escherichia coli and Salmonella typhimurium. Journal of Bacteriology. 143: 1081-5. PMID 6259116 |
0.301 |
|
| 1979 |
Noel D, Nikaido K, Ames GF. A single amino acid substitution in a histidine-transport protein drastically alters its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochemistry. 18: 4159-65. PMID 385047 DOI: 10.1021/Bi00586A017 |
0.456 |
|
| 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 |
0.422 |
|
| 1978 |
Noel KD, Ames GF. Evidence for a common mechanism for the insertion of the Tn10 transposon and for the generation of Tn10-stimulated deletions. Molecular & General Genetics : Mgg. 166: 217-23. PMID 370547 DOI: 10.1007/Bf00285924 |
0.405 |
|
| 1978 |
Ames GF, Biek DP, Spudich EN. Duplications of histidine transport genes in Salmonella typhimurium and their use for the selection of deletion mutants. Journal of Bacteriology. 136: 1094-108. PMID 363688 DOI: 10.1128/JB.136.3.1094-1108.1978 |
0.325 |
|
| 1977 |
Ames GF, Noel KD, Taber H, Spudich EN, Nikaido K, Afong J. Fine-structure map of the histidine transport genes in Salmonella typhimurium. Journal of Bacteriology. 129: 1289-97. PMID 321422 DOI: 10.1128/Jb.129.3.1289-1297.1977 |
0.428 |
|
| 1976 |
Ames GF, Spurich EN. Protein-protein interaction in transport: periplasmic histidine-binding protein J interacts with P protein. Proceedings of the National Academy of Sciences of the United States of America. 73: 1877-81. PMID 778848 DOI: 10.1073/pnas.73.6.1877 |
0.39 |
|
| 1976 |
Ames GF. Protein‐protein interaction in transport Journal of Cellular Physiology. 89: 543-543. DOI: 10.1002/Jcp.1040890408 |
0.472 |
|
| 1974 |
Ames GF. Isolation of transport mutants in bacteria. Methods in Enzymology. 32: 849-56. PMID 4614010 DOI: 10.1016/0076-6879(74)32086-1 |
0.461 |
|
| 1974 |
Ames GF. Two methods for the assay of amino acid transport in bacteria. Methods in Enzymology. 32: 843-9. PMID 4614009 DOI: 10.1016/0076-6879(74)32085-X |
0.354 |
|
| 1974 |
Ames GF, Spudich EN, Nikaido H. Protein Composition of the Outer Membrane of Salmonella typhimurium: Effect of Lipopolysaccharide Mutations Journal of Bacteriology. 117: 406-416. PMID 4590466 DOI: 10.1128/Jb.117.2.406-416.1974 |
0.386 |
|
| 1974 |
Kustu SG, Ames GF. The histidine-binding protein J, a histidine transport component, has two different functional sites. The Journal of Biological Chemistry. 249: 6976-83. PMID 4213931 |
0.365 |
|
| 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 |
0.423 |
|
| 1973 |
Ames BN, Ames GF, Young JD, Tsuchiya D, Lecocq J. Illicit transport: the oligopeptide permease. Proceedings of the National Academy of Sciences of the United States of America. 70: 456-8. PMID 4568730 DOI: 10.1073/Pnas.70.2.456 |
0.419 |
|
| 1973 |
Kaback HR, Hong J, Ames G. Membranes and Transport Crc Critical Reviews in Microbiology. 2: 333-376. DOI: 10.3109/10408417309108389 |
0.309 |
|
| 1972 |
Ames GF, Lever JE. The histidine-binding protein J is a component of histidine transport. Identification of its structural gene, hisJ. The Journal of Biological Chemistry. 247: 4309-16. PMID 4556307 |
0.416 |
|
| 1970 |
Ames GF, Lever J. Components of histidine transport: histidine-binding proteins and hisP protein. Proceedings of the National Academy of Sciences of the United States of America. 66: 1096-103. PMID 4920090 DOI: 10.1073/Pnas.66.4.1096 |
0.506 |
|
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