| Year |
Citation |
Score |
| 2020 |
Mao C, Bariya P, Suo Y, Randall LL. Comparison of Single and Multiple Turnovers of SecYEG in . Journal of Bacteriology. PMID 32989086 DOI: 10.1128/JB.00462-20 |
0.788 |
|
| 2020 |
Chattrakun K, Hoogerheide DP, Mao C, Randall LL, King GM. Correction to Protein Translocation Activity in Surface-Supported Lipid Bilayers. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 32453585 DOI: 10.1021/acs.langmuir.0c01279 |
0.574 |
|
| 2019 |
Chattrakun K, Hoogerheide DP, Mao C, Randall LL, King GM. Protein Translocation Activity in Surface-Supported Lipid Bilayers. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 31448613 DOI: 10.1021/acs.langmuir.9b01928 |
0.606 |
|
| 2019 |
Sanganna Gari RR, Chattrakun K, Marsh BP, Mao C, Chada N, Randall LL, King GM. Direct visualization of the E. coli Sec translocase engaging precursor proteins in lipid bilayers Science Advances. 5: eaav9404. PMID 31206019 DOI: 10.1126/Sciadv.Aav9404 |
0.624 |
|
| 2018 |
Bariya P, Randall LL. Co-assembly of SecYEG and SecA fully restores the properties of the native translocon. Journal of Bacteriology. PMID 30275279 DOI: 10.1128/JB.00493-18 |
0.37 |
|
| 2017 |
Findik BT, Smith VF, Randall LL. Penetration into Membrane of Amino-terminal Region of SecA when Associated with SecYEG in Active Complexes. Protein Science : a Publication of the Protein Society. PMID 29247569 DOI: 10.1002/pro.3362 |
0.799 |
|
| 2017 |
Crane JM, Randall LL. The Sec System: Protein Export in Escherichia coli. Ecosal Plus. 7. PMID 29165233 DOI: 10.1128/ecosalplus.ESP-0002-2017 |
0.828 |
|
| 2017 |
Findik BT, Randall LL. Determination of the intracellular concentration of the export chaperone SecB in Escherichia coli. Plos One. 12: e0183231. PMID 28850586 DOI: 10.1371/journal.pone.0183231 |
0.803 |
|
| 2015 |
Suo Y, Hardy SJ, Randall LL. The basis of asymmetry in the SecA:SecB complex. Journal of Molecular Biology. 427: 887-900. PMID 25534082 DOI: 10.1016/j.jmb.2014.12.008 |
0.815 |
|
| 2015 |
Sanganna Gari RR, Frey N, Marsh B, Mao C, Randall L, King G. Atomic Force Microscopy of Protein Translocation Machinery in Supported Lipid Bilayers Biophysical Journal. 108: 168a. DOI: 10.1016/J.Bpj.2014.11.925 |
0.668 |
|
| 2013 |
Mao C, Cheadle CE, Hardy SJ, Lilly AA, Suo Y, Sanganna Gari RR, King GM, Randall LL. Stoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species. Proceedings of the National Academy of Sciences of the United States of America. 110: 11815-20. PMID 23818593 DOI: 10.1073/pnas.1303289110 |
0.76 |
|
| 2013 |
Sanganna Gari RR, Frey NC, Mao C, Randall LL, King GM. Dynamic structure of the translocon SecYEG in membrane: direct single molecule observations. The Journal of Biological Chemistry. 288: 16848-54. PMID 23609442 DOI: 10.1074/Jbc.M113.471870 |
0.572 |
|
| 2013 |
Sanganna Gari RR, Frey NC, Randall LL, King GM. Single Molecule Studies of the General Secretory System Biophysical Journal. 104: 222a. DOI: 10.1016/J.Bpj.2012.11.1253 |
0.371 |
|
| 2011 |
Suo Y, Hardy SJ, Randall LL. Orientation of SecA and SecB in complex, derived from disulfide cross-linking. Journal of Bacteriology. 193: 190-6. PMID 21037004 DOI: 10.1128/JB.00975-10 |
0.848 |
|
| 2010 |
Randall LL, Henzl MT. Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA. Protein Science : a Publication of the Protein Society. 19: 1173-9. PMID 20512970 DOI: 10.1002/Pro.392 |
0.467 |
|
| 2010 |
Crane JM, Lilly AA, Randall LL. Characterization of interactions between proteins using site-directed spin labeling and electron paramagnetic resonance spectroscopy. Methods in Molecular Biology (Clifton, N.J.). 619: 173-90. PMID 20419411 DOI: 10.1007/978-1-60327-412-8_11 |
0.811 |
|
| 2009 |
Lilly AA, Crane JM, Randall LL. Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands. Protein Science : a Publication of the Protein Society. 18: 1860-8. PMID 19569227 DOI: 10.1002/pro.197 |
0.84 |
|
| 2009 |
Mao C, Hardy SJ, Randall LL. Maximal efficiency of coupling between ATP hydrolysis and translocation of polypeptides mediated by SecB requires two protomers of SecA. Journal of Bacteriology. 191: 978-84. PMID 18978043 DOI: 10.1128/JB.01321-08 |
0.583 |
|
| 2008 |
Cooper DB, Smith VF, Crane JM, Roth HC, Lilly AA, Randall LL. SecA, the motor of the secretion machine, binds diverse partners on one interactive surface. Journal of Molecular Biology. 382: 74-87. PMID 18602400 DOI: 10.1016/j.jmb.2008.06.049 |
0.738 |
|
| 2006 |
Crane JM, Suo Y, Lilly AA, Mao C, Hubbell WL, Randall LL. Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling. Journal of Molecular Biology. 363: 63-74. PMID 16962134 DOI: 10.1016/J.Jmb.2006.07.021 |
0.807 |
|
| 2006 |
Patel CN, Smith VF, Randall LL. Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export. Protein Science : a Publication of the Protein Society. 15: 1379-86. PMID 16731972 DOI: 10.1110/ps.062141006 |
0.856 |
|
| 2005 |
Crane JM, Mao C, Lilly AA, Smith VF, Suo Y, Hubbell WL, Randall LL. Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export. Journal of Molecular Biology. 353: 295-307. PMID 16169560 DOI: 10.1016/J.Jmb.2005.08.022 |
0.786 |
|
| 2005 |
Randall LL, Crane JM, Lilly AA, Liu G, Mao C, Patel CN, Hardy SJ. Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export. Journal of Molecular Biology. 348: 479-89. PMID 15811382 DOI: 10.1016/j.jmb.2005.02.036 |
0.769 |
|
| 2004 |
Randall LL, Crane JM, Liu G, Hardy SJ. Sites of interaction between SecA and the chaperone SecB, two proteins involved in export. Protein Science : a Publication of the Protein Society. 13: 1124-33. PMID 15010547 DOI: 10.1110/ps.03410104 |
0.785 |
|
| 2002 |
Randall LL, Hardy SJ. SecB, one small chaperone in the complex milieu of the cell. Cellular and Molecular Life Sciences : Cmls. 59: 1617-23. PMID 12475171 |
0.485 |
|
| 2002 |
Woodbury RL, Hardy SJ, Randall LL. Complex behavior in solution of homodimeric SecA. Protein Science : a Publication of the Protein Society. 11: 875-82. PMID 11910030 DOI: 10.1110/ps.4090102 |
0.842 |
|
| 2000 |
Woodbury RL, Topping TB, Diamond DL, Suciu D, Kumamoto CA, Hardy SJ, Randall LL. Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions. The Journal of Biological Chemistry. 275: 24191-8. PMID 10807917 DOI: 10.1074/Jbc.M002885200 |
0.458 |
|
| 1999 |
Murén EM, Suciu D, Topping TB, Kumamoto CA, Randall LL. Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers. The Journal of Biological Chemistry. 274: 19397-402. PMID 10383453 DOI: 10.1074/Jbc.274.27.19397 |
0.387 |
|
| 1998 |
Randall LL, Hardy SJ, Topping TB, Smith VF, Bruce JE, Smith RD. The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding. Protein Science : a Publication of the Protein Society. 7: 2384-90. PMID 9828004 DOI: 10.1002/Pro.5560071115 |
0.496 |
|
| 1998 |
Randall LL, Topping TB, Suciu D, Hardy SJ. Calorimetric analyses of the interaction between SecB and its ligands. Protein Science : a Publication of the Protein Society. 7: 1195-200. PMID 9605324 DOI: 10.1002/pro.5560070514 |
0.416 |
|
| 1998 |
de Cock H, Randall LL. Correlation between requirement for SecA during export and folding properties of precursor polypeptides. Molecular Microbiology. 27: 469-76. PMID 9484900 DOI: 10.1046/j.1365-2958.1998.00695.x |
0.317 |
|
| 1997 |
Diamond DL, Randall LL. Kinetic partitioning: Poising SecB to favor association with a rapidly folding ligand Journal of Biological Chemistry. 272: 28994-28998. PMID 9360972 DOI: 10.1074/jbc.272.46.28994 |
0.393 |
|
| 1997 |
Smith VF, Hardy SJ, Randall LL. Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein. Protein Science : a Publication of the Protein Society. 6: 1746-55. PMID 9260287 DOI: 10.1002/pro.5560060815 |
0.417 |
|
| 1997 |
Topping TB, Randall LL. Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands. The Journal of Biological Chemistry. 272: 19314-8. PMID 9235927 |
0.4 |
|
| 1997 |
Randall LL, Topping TB, Hardy SJ, Pavlov MY, Freistroffer DV, Ehrenberg M. Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins. Proceedings of the National Academy of Sciences of the United States of America. 94: 802-7. PMID 9023337 |
0.437 |
|
| 1995 |
Powers EL, Randall LL. Export of periplasmic galactose-binding protein in Escherichia coli depends on the chaperone SecB. Journal of Bacteriology. 177: 1906-7. PMID 7896722 |
0.431 |
|
| 1995 |
Khisty VJ, Randall LL. Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning. Journal of Bacteriology. 177: 3277-82. PMID 7768828 |
0.445 |
|
| 1995 |
Randall LL, Hardy SJ. High selectivity with low specificity: how SecB has solved the paradox of chaperone binding. Trends in Biochemical Sciences. 20: 65-9. PMID 7701564 |
0.36 |
|
| 1995 |
Khisty VJ, Munske GR, Randall LL. Mapping of the binding frame for the chaperone SecB within a natural ligand, galactose-binding protein. The Journal of Biological Chemistry. 270: 25920-7. PMID 7592780 |
0.376 |
|
| 1995 |
Diamond DL, Strobel S, Chun SY, Randall LL. Interaction of SecB with intermediates along the folding pathway of maltose-binding protein Protein Science. 4: 1118-1123. PMID 7549876 |
0.454 |
|
| 1994 |
Topping TB, Randall LL. Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Science : a Publication of the Protein Society. 3: 730-6. PMID 8061603 DOI: 10.1002/pro.5560030502 |
0.434 |
|
| 1994 |
Chun SY, Randall LL. In vivo studies of the role of SecA during protein export in Escherichia coli. Journal of Bacteriology. 176: 4197-203. PMID 8021205 |
0.427 |
|
| 1993 |
Chun SY, Strobel S, Bassford P, Randall LL. Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro. The Journal of Biological Chemistry. 268: 20855-62. PMID 8407916 |
0.369 |
|
| 1993 |
Hardy SJ, Randall LL. Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 339: 343-52; discussion 3. PMID 8098539 DOI: 10.1098/rstb.1993.0033 |
0.502 |
|
| 1991 |
Hardy SJ, Randall LL. A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB. Science (New York, N.Y.). 251: 439-43. PMID 1989077 |
0.427 |
|
| 1991 |
Teschke CM, Kim J, Song T, Park S, Park C, Randall LL. Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli. The Journal of Biological Chemistry. 266: 11789-96. PMID 1904869 |
0.667 |
|
| 1990 |
Randall LL, Topping TB, Hardy SJ. No specific recognition of leader peptide by SecB, a chaperone involved in protein export. Science (New York, N.Y.). 248: 860-3. PMID 2188362 |
0.44 |
|
| 1989 |
Hardy SJ, Randall LL. Biochemical investigation of protein export in Escherichia coli. Journal of Cell Science. Supplement. 11: 29-43. PMID 2693459 |
0.396 |
|
| 1989 |
Liu G, Topping TB, Randall LL. Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein. Proceedings of the National Academy of Sciences of the United States of America. 86: 9213-7. PMID 2687876 |
0.437 |
|
| 1988 |
Park S, Liu G, Topping TB, Cover WH, Randall LL. Modulation of folding pathways of exported proteins by the leader sequence. Science (New York, N.Y.). 239: 1033-5. PMID 3278378 |
0.824 |
|
| 1988 |
Thom JR, Randall LL. Role of the leader peptide of maltose-binding protein in two steps of the export process. Journal of Bacteriology. 170: 5654-61. PMID 3056909 |
0.314 |
|
| 1988 |
Liu GP, Topping TB, Cover WH, Randall LL. Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported protein. The Journal of Biological Chemistry. 263: 14790-3. PMID 3049590 |
0.786 |
|
| 1987 |
Cover WH, Ryan JP, Bassford PJ, Walsh KA, Bollinger J, Randall LL. Suppression of a signal sequence mutation by an amino acid substitution in the mature portion of the maltose-binding protein. Journal of Bacteriology. 169: 1794-800. PMID 3553148 DOI: 10.1128/Jb.169.5.1794-1800.1987 |
0.793 |
|
| 1986 |
Randall LL, Hardy SJ. Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli. Cell. 46: 921-8. PMID 3530497 |
0.348 |
|
| 1985 |
Iida A, Groarke JM, Park S, Thom J, Zabicky JH, Hazelbauer GL, Randall LL. A signal sequence mutant defective in export of ribose-binding protein and a corresponding pseudorevertant isolated without imposed selection. The Embo Journal. 4: 1875-80. PMID 3928371 |
0.31 |
|
| 1983 |
Randall LL. Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation. Cell. 33: 231-40. PMID 6380753 |
0.342 |
|
| 1983 |
Randall LL, Hardy SJ. Preparation of free and membrane-bound polysomes from Escherichia coli. Methods in Enzymology. 97: 70-6. PMID 6361483 |
0.309 |
|
| 1982 |
Randall LL. Studies of export of protein in Escherichia coli. Progress in Clinical and Biological Research. 91: 15-21. PMID 6755483 |
0.301 |
|
| 1981 |
Josefsson LG, Randall LL. Processing in vivo of precursor maltose-binding protein in Escherichia coli occurs post-translationally as well as co-translationally. The Journal of Biological Chemistry. 256: 2504-7. PMID 7007385 |
0.388 |
|
| 1980 |
Randall LL, Josefsson LG, Hardy SJ. Processing of exported proteins in Escherichia coli. Biochemical Society Transactions. 8: 413-5. PMID 7004934 |
0.363 |
|
| 1980 |
Randall LL, Josefsson LG, Hardy SJ. Novel intermediates in the synthesis of maltose-binding protein in Escherichia coli. European Journal of Biochemistry / Febs. 107: 375-9. PMID 6995119 |
0.459 |
|
| 1979 |
Ferenci T, Randall LL. Precursor maltose-binding protein is active in binding substrate. The Journal of Biological Chemistry. 254: 9979-81. PMID 385604 |
0.398 |
|
| 1979 |
Palva ET, Randall LL. Cross-linking analysis of the two forms of protein I, a major outer membrane protein of Escherichia coli. Journal of Bacteriology. 138: 254-6. PMID 374368 |
0.37 |
|
| 1978 |
Randall LL, Josefsson LG, Hardy SJ. Processing in vitro of precursor periplasmic proteins from Escherichia coli. European Journal of Biochemistry / Febs. 92: 411-5. PMID 367780 |
0.443 |
|
| 1978 |
Randall LL, Hardy SJ, Josefsson LG. Precursors of three exported proteins in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 75: 1209-12. PMID 349560 |
0.435 |
|
| 1978 |
Palva ET, Randall LL. Arrangement of protein I in Escherichia coli outer membrane: cross-linking study. Journal of Bacteriology. 133: 279-86. PMID 338582 |
0.345 |
|
| 1977 |
Randall LL, Hardy SJ. Synthesis of exported proteins by membrane-bound polysomes from Escherichia coli. European Journal of Biochemistry / Febs. 75: 43-53. PMID 405218 |
0.418 |
|
| 1976 |
Palva ET, Randall LL. Nearest-neighbor analysis of Escherichia coli outer membrane proteins using cleavable cross-links. Journal of Bacteriology. 127: 1558-60. PMID 783148 |
0.35 |
|
| 1975 |
Randall LL, Hardy AJ. Analysis of the ribosomes engaged in the synthesis of the outer membrane proteins of Escherichia coli. Molecular & General Genetics : Mgg. 137: 151-60. PMID 1102914 |
0.362 |
|
| 1975 |
Randall LL. Insertion of a minor protein into the outer membrane of Escherichia coli during inhibition of lipid synthesis. Journal of Bacteriology. 122: 347-51. PMID 1092644 |
0.331 |
|
| 1969 |
Kurland CG, Voynow P, Hardy SJ, Randall L, Lutter L. Physical and functional heterogeneity of E. coli ribosomes Cold Spring Harbor Symposia On Quantitative Biology. 34: 17-24. PMID 4909497 |
0.488 |
|
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