Year |
Citation |
Score |
2013 |
Quinlan RA, Ellis RJ. Chaperones: needed for both the good times and the bad times Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 368: 20130091. PMID 23530265 DOI: 10.1098/Rstb.2013.0091 |
0.358 |
|
2008 |
Lund PA, Ellis RJ. The chaperone function: meanings and myths. Novartis Foundation Symposium. 291: 23-44. PMID 18575264 DOI: 10.1002/9780470754030.Ch3 |
0.351 |
|
2006 |
Ellis RJ. Protein folding: inside the cage. Nature. 442: 360. PMID 16871196 DOI: 10.1038/442360A |
0.363 |
|
2006 |
Ellis RJ, Minton AP. Protein aggregation in crowded environments. Biological Chemistry. 387: 485-497. PMID 16740119 DOI: 10.1515/Bc.2006.064 |
0.345 |
|
2006 |
Ellis RJ. Molecular chaperones: assisting assembly in addition to folding Trends in Biochemical Sciences. 31: 395-401. PMID 16716593 DOI: 10.1016/J.Tibs.2006.05.001 |
0.358 |
|
2005 |
Ellis RJ. Chaperomics: In Vivo GroEL Function Defined Current Biology. 15. PMID 16139196 DOI: 10.1016/J.Cub.2005.08.025 |
0.347 |
|
2003 |
Ellis RJ. Protein Folding: Importance of the Anfinsen Cage Current Biology. 13. PMID 14614845 DOI: 10.1016/J.Cub.2003.10.051 |
0.367 |
|
2003 |
Ellis RJ. Molecular chaperones: Plugging the transport gap. Nature. 421: 801-802. PMID 12594497 DOI: 10.1038/421801A |
0.36 |
|
2002 |
Ellis RJ, Pinheiro TJT. Medicine: Danger |[mdash]| misfolding proteins Nature. 416: 483. PMID 11932723 DOI: 10.1038/416483A |
0.317 |
|
2001 |
Ellis RJ. Macromolecular crowding: obvious but underappreciated. Trends in Biochemical Sciences. 26: 597-604. PMID 11590012 DOI: 10.1016/S0968-0004(01)01938-7 |
0.345 |
|
2000 |
van den Berg B, Wain R, Dobson CM, Ellis RJ. Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. The Embo Journal. 19: 3870-5. PMID 10921869 DOI: 10.1093/Emboj/19.15.3870 |
0.343 |
|
2000 |
van den Berg B, Ellis RJ, Dobson CM. Effects of macromolecular crowding on protein folding and aggregation. The Embo Journal. 18: 6927-33. PMID 10601015 DOI: 10.1093/Emboj/18.24.6927 |
0.362 |
|
1999 |
Ellis RJ. Molecular chaperones: Pathways and networks Current Biology. 9. PMID 10074421 DOI: 10.1016/S0960-9822(99)80082-7 |
0.313 |
|
1999 |
Ellis RJ, Dobson C, Hartl U. Sequence does specify protein conformation. Trends in Biochemical Sciences. 23: 468. PMID 9868366 DOI: 10.1016/S0968-0004(98)01324-3 |
0.37 |
|
1997 |
Ellis RJ. Molecular chaperones: Avoiding the crowd Current Biology. 7. PMID 9285706 DOI: 10.1016/S0960-9822(06)00273-9 |
0.337 |
|
1996 |
Ellis RJ. Revisiting the Anfinsen cage Folding and Design. 1. PMID 9079356 DOI: 10.1016/S1359-0278(96)00004-1 |
0.354 |
|
1994 |
Ellis RJ. Chaperoning nascent proteins. Nature. 370: 96-97. PMID 8022496 DOI: 10.1038/370096A0 |
0.372 |
|
1994 |
Ellis RJ. Molecular Chaperones: Opening and closing the Anfinsen cage Current Biology. 4: 633-635. PMID 7953542 DOI: 10.1016/S0960-9822(00)00140-8 |
0.334 |
|
1994 |
Ellis RJ. Roles of molecular chaperones in protein folding Current Opinion in Structural Biology. 4: 117-122. DOI: 10.1016/S0959-440X(94)90069-8 |
0.385 |
|
1991 |
Ellis RJ. Chaperoning protein repair. Current Biology. 1: 177-178. PMID 15336159 DOI: 10.1016/0960-9822(91)90225-L |
0.337 |
|
1991 |
Mascagni P, Tonolo M, Ball H, Lim M, Ellis RJ, Coates A. Chemical synthesis of 10 kDa chaperonin. Biological activity suggests chaperonins do not require other molecular chaperones. Febs Letters. 286: 201-3. PMID 1677897 DOI: 10.1016/0014-5793(91)80973-7 |
0.373 |
|
1990 |
Ellis RJ. Impropriety in proteins. Nature. 345: 484-484. PMID 2348858 DOI: 10.1038/345484A0 |
0.362 |
|
1989 |
Ellis RJ, Robinson C, van der Vies SM, Kirwin PM. Processing and assembly of chloroplast proteins. Biochemical Society Transactions. 16: 703-4. PMID 3069516 DOI: 10.1042/Bst0160703 |
0.482 |
|
1989 |
Ellis RJ, Hemmingsen SM. Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures Trends in Biochemical Sciences. 14: 339-342. PMID 2572080 DOI: 10.1016/0968-0004(89)90168-0 |
0.331 |
|
1988 |
Ellis RJ, Vies SMVD. The Rubisco subunit binding protein Photosynthesis Research. 16: 661-675. PMID 24430994 DOI: 10.1007/Bf00039488 |
0.368 |
|
1988 |
Hemmingsen SM, Woolford C, Van Der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ. Homologous plant and bacterial proteins chaperone oligomeric protein assembly Nature. 333: 330-334. PMID 2897629 DOI: 10.1038/333330A0 |
0.389 |
|
1987 |
Musgrove JE, Johnson RA, Ellis RJ. Dissociation of the ribulosebisphosphate-carboxylase large-subunit binding protein into dissimilar subunits. Febs Journal. 163: 529-534. PMID 3549295 DOI: 10.1111/J.1432-1033.1987.Tb10900.X |
0.341 |
|
1986 |
Hemmingsen SM, Ellis RJ. Purification and Properties of Ribulosebisphosphate Carboxylase Large Subunit Binding Protein Plant Physiology. 80: 269-276. PMID 16664596 DOI: 10.1104/Pp.80.1.269 |
0.349 |
|
1986 |
Lennox CR, Ellis RJ. The carboxylase-large-subunit-binding protein: photoregulation and reversible dissociation Biochemical Society Transactions. 14: 9-11. PMID 3956850 DOI: 10.1042/Bst0140009 |
0.334 |
|
1985 |
Robinson C, Ellis RJ. Transport of proteins into chloroplasts. The effect of incorporation of amino acid analogues on the import and processing of chloroplast polypeptides. European Journal of Biochemistry. 152: 67-73. PMID 4043086 DOI: 10.1111/J.1432-1033.1985.TB09164.X |
0.477 |
|
1984 |
Robinson C, Ellis RJ. Transport of proteins into chloroplasts. Partial purification of a chloroplast protease involved in the processing of important precursor polypeptides. European Journal of Biochemistry. 142: 337-42. PMID 6430703 DOI: 10.1111/J.1432-1033.1984.Tb08291.X |
0.515 |
|
1984 |
Robinson C, Ellis RJ. Transport of proteins into chloroplasts. The precursor of small subunit of ribulose bisphosphate carboxylase is processed to the mature size in two steps. European Journal of Biochemistry. 142: 343-6. PMID 6378638 DOI: 10.1111/J.1432-1033.1984.TB08292.X |
0.473 |
|
1980 |
Barraclough R, Ellis RJ. Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bishopshate carboxylase in isolated intact pea chloroplasts Biochimica Et Biophysica Acta. 608: 19-31. PMID 7388030 DOI: 10.1016/0005-2787(80)90129-X |
0.344 |
|
1980 |
Silverthorne J, Ellis RJ. Protein synthesis in chloroplasts. VIII. Differential synthesis of chloroplast proteins during spinach leaf development. Biochimica Et Biophysica Acta. 607: 319-330. PMID 6154482 DOI: 10.1016/0005-2787(80)90084-2 |
0.33 |
|
1980 |
Bedbrook JR, Smith SM, Ellis RJ. Molecular cloning and sequencing of cDNA encoding the precursor to the small subunit of chloroplast ribulose-1,5-bisphosphate carboxylase Nature. 287: 692-697. DOI: 10.1038/287692A0 |
0.37 |
|
1979 |
Barraclough R, Ellis RJ. The biosynthesis of ribulose bisphosphate carboxylase. Uncoupling of the synthesis of the large and small subunits in isolated soybean leaf cells. Febs Journal. 94: 165-177. PMID 571334 DOI: 10.1111/J.1432-1033.1979.Tb12883.X |
0.32 |
|
1979 |
Smith SM, Ellis RJ. Processing of small subunit precursor of ribulose bisphosphate carboxylase and its assembly into whole enzyme are stromal events Nature. 278: 662-664. DOI: 10.1038/278662A0 |
0.43 |
|
1979 |
Ellis RJ. The most abundant protein in the world Trends in Biochemical Sciences. 4: 241-244. DOI: 10.1016/0968-0004(79)90212-3 |
0.379 |
|
1978 |
Highfield PE, Ellis RJ. Synthesis and transport of the small subunit of chloroplast ribulose bisphosphate carboxylase Nature. 271: 420-424. DOI: 10.1038/271420A0 |
0.349 |
|
1977 |
Siddell SG, Ellis RJ. Protein synthesis by etioplasts. Biochemical Society Transactions. 5: 98-102. PMID 892212 DOI: 10.1042/Bst0050098 |
0.353 |
|
1977 |
Ellis RJ. Protein synthesis by isolated chloroplasts Biochimica Et Biophysica Acta. 463: 185-215. DOI: 10.1016/0304-4173(77)90008-8 |
0.347 |
|
1976 |
Highfield PE, Ellis RJ. Protein synthesis in chloroplasts. VII. Initiation of protein synthesis in isolated intact pea chloroplasts. Biochimica Et Biophysica Acta. 447: 20-27. PMID 963079 DOI: 10.1016/0005-2787(76)90091-5 |
0.329 |
|
1975 |
Joy KW, Ellis RJ. Protein synthesis in chloroplasts. IV. Polypeptides of the chloroplast envelope. Biochimica Et Biophysica Acta. 378: 143-51. PMID 1120134 DOI: 10.1016/0005-2787(75)90145-8 |
0.307 |
|
1975 |
Hartley MR, Wheeler A, Ellis RJ. Protein synthesis in chloroplasts. V. Translation of messenger RNA for the large subunit of fraction I protein in a heterologous cell-free system. Journal of Molecular Biology. 91: 67-77. PMID 1102697 DOI: 10.1016/0022-2836(75)90372-1 |
0.349 |
|
1975 |
Ellis RJ. Inhibition of chloroplast protein synthesis by lincomycin and 2-(4-methyl-2,6- dinitroanilino)-N-methylpropionamide Phytochemistry. 14: 89-93. DOI: 10.1016/0031-9422(75)85015-1 |
0.375 |
|
1974 |
Ellis RJ. The Biogenesis of Chloroplasts: Protein Synthesis by Isolated Chloroplasts Biochemical Society Transactions. 2: 179-182. DOI: 10.1042/Bst0020179 |
0.35 |
|
1974 |
Eaglesham ARJ, Ellis RJ. Protein synthesis in chloroplasts: II. Light-driven synthesis of membrane proteins by isolated pea chloroplasts Biochimica Et Biophysica Acta. 335: 396-407. DOI: 10.1016/0005-2787(74)90162-2 |
0.335 |
|
1973 |
Blair GE, Ellis RJ. Protein synthesis in chloroplasts I. Light-driven synthesis of the large subunit of Fraction I protein by isolated pea chloroplasts Biochimica Et Biophysica Acta. 319: 223-234. PMID 4748357 DOI: 10.1016/0005-2787(73)90013-0 |
0.375 |
|
1961 |
ELLIS RJ, DAVIES DD. Glutamic-oxaloacetic transaminase of cauliflower. 1. Purification and specificity. The Biochemical Journal. 78: 615-23. PMID 13726498 DOI: 10.1042/bj0780615 |
0.417 |
|
1961 |
DAVIES DD, ELLIS RJ. Glutamic-oxaloacetic transaminase of cauliflower. 2. Kinetics and mechanism of action. The Biochemical Journal. 78: 623-30. PMID 13720088 DOI: 10.1042/bj0780623 |
0.414 |
|
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