| Year |
Citation |
Score |
| 2003 |
Tibbetts AS, Oesterlin L, Chan SY, Kramer G, Hardesty B, Appling DR. Mammalian mitochondrial initiation factor 2 supports yeast mitochondrial translation without formylated initiator tRNA. The Journal of Biological Chemistry. 278: 31774-80. PMID 12799364 DOI: 10.1074/Jbc.M304962200 |
0.331 |
|
| 2003 |
Garofalo C, Trinko R, Kramer G, Appling DR, Hardesty B. Purification and characterization of yeast mitochondrial initiation factor 2. Archives of Biochemistry and Biophysics. 413: 243-52. PMID 12729623 DOI: 10.1016/S0003-9861(03)00119-X |
0.367 |
|
| 2002 |
Kramer G, Ramachandiran V, Horowitz PM, Hardesty B. The molecular chaperone DnaK is not recruited to translating ribosomes that lack trigger factor. Archives of Biochemistry and Biophysics. 403: 63-70. PMID 12061803 DOI: 10.1016/S0003-9861(02)00213-8 |
0.442 |
|
| 2002 |
Ramachandiran V, Kramer G, Horowitz PM, Hardesty B. Single synonymous codon substitution eliminates pausing during chloramphenicol acetyl transferase synthesis on Escherichia coli ribosomes in vitro. Febs Letters. 512: 209-12. PMID 11852081 DOI: 10.1016/S0014-5793(02)02261-5 |
0.398 |
|
| 2001 |
Kramer G, Ramachandiran V, Hardesty B. Cotranslational folding--omnia mea mecum porto? The International Journal of Biochemistry & Cell Biology. 33: 541-53. PMID 11378437 DOI: 10.1016/S1357-2725(01)00044-9 |
0.407 |
|
| 2001 |
Kramer G, Ramachandiran V, Horowitz P, Hardesty B. An additional serine residue at the C terminus of rhodanese destabilizes the enzyme. Archives of Biochemistry and Biophysics. 385: 332-7. PMID 11368014 DOI: 10.1006/Abbi.2000.2166 |
0.383 |
|
| 2001 |
Hardesty B, Kramer G. Folding of a nascent peptide on the ribosome. Progress in Nucleic Acid Research and Molecular Biology. 66: 41-66. PMID 11051761 DOI: 10.1016/S0079-6603(00)66026-9 |
0.401 |
|
| 2000 |
Ramachandiran V, Kramer G, Hardesty B. Expression of different coding sequences in cell-free bacterial and eukaryotic systems indicates translational pausing on Escherichia coli ribosomes. Febs Letters. 482: 185-8. PMID 11024457 DOI: 10.1016/S0014-5793(00)02017-2 |
0.361 |
|
| 2000 |
McIntosh B, Ramachandiran V, Kramer G, Hardesty B. Initiation of protein synthesis with fluorophore-Met-tRNA(f) and the involvement of IF-2. Biochimie. 82: 167-74. PMID 10727773 DOI: 10.1016/S0300-9084(00)00381-3 |
0.342 |
|
| 2000 |
Ramachandiran V, Willms C, Kramer G, Hardesty B. Fluorophores at the N terminus of nascent chloramphenicol acetyltransferase peptides affect translation and movement through the ribosome. The Journal of Biological Chemistry. 275: 1781-6. PMID 10636875 DOI: 10.1074/Jbc.275.3.1781 |
0.413 |
|
| 1999 |
Shibatani T, Kramer G, Hardesty B, Horowitz PM. Domain separation precedes global unfolding of rhodanese. The Journal of Biological Chemistry. 274: 33795-9. PMID 10559274 DOI: 10.1074/Jbc.274.47.33795 |
0.326 |
|
| 1999 |
Kramer G, Kudlicki W, McCarthy D, Tsalkova T, Simmons D, Hardesty B. N-terminal and C-terminal modifications affect folding, release from the ribosomes and stability of in vitro synthesized proteins. The International Journal of Biochemistry & Cell Biology. 31: 231-41. PMID 10216956 DOI: 10.1016/S1357-2725(98)00143-5 |
0.371 |
|
| 1999 |
Hardesty B, Tsalkova T, Kramer G. Co-translational folding. Current Opinion in Structural Biology. 9: 111-4. PMID 10047581 DOI: 10.1016/S0959-440X(99)80014-1 |
0.402 |
|
| 1999 |
Tsalkova T, Kramer G, Hardesty B. The effect of a hydrophobic N-terminal probe on translational pausing of chloramphenicol acetyl transferase and rhodanese. Journal of Molecular Biology. 286: 71-81. PMID 9931250 DOI: 10.1006/Jmbi.1998.2481 |
0.396 |
|
| 1998 |
Trevino RJ, Tsalkova T, Kramer G, Hardesty B, Chirgwin JM, Horowitz PM. Truncations at the NH2 terminus of rhodanese destabilize the enzyme and decrease its heterologous expression. The Journal of Biological Chemistry. 273: 27841-7. PMID 9774394 DOI: 10.1074/Jbc.273.43.27841 |
0.357 |
|
| 1998 |
Tsalkova T, Odom OW, Kramer G, Hardesty B. Different conformations of nascent peptides on ribosomes. Journal of Molecular Biology. 278: 713-23. PMID 9614937 DOI: 10.1006/Jmbi.1998.1721 |
0.385 |
|
| 1998 |
McCarthy D, Kramer G, Hardesty B. Reactivation of thermally inactivated pre-beta-lactamase by DnaK, DnaJ, and GrpE. Protein Science : a Publication of the Protein Society. 7: 1164-71. PMID 9605320 DOI: 10.1002/Pro.5560070510 |
0.34 |
|
| 1998 |
Kramer G, Zhang T, Kudlicki W, Hardesty B. Preparation and application of chaperone-deficient Escherichia coli cell-free translation systems. Methods in Enzymology. 290: 18-26. PMID 9534148 DOI: 10.1016/S0076-6879(98)90004-0 |
0.406 |
|
| 1997 |
Kudlicki W, Coffman A, Kramer G, Hardesty B. Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing. The Journal of Biological Chemistry. 272: 32206-10. PMID 9405422 DOI: 10.1074/Jbc.272.51.32206 |
0.397 |
|
| 1997 |
Kudlicki W, Coffman A, Kramer G, Hardesty B. Ribosomes and ribosomal RNA as chaperones for folding of proteins. Folding & Design. 2: 101-8. PMID 9135982 DOI: 10.1016/S1359-0278(97)00014-X |
0.411 |
|
| 1996 |
Kudlicki W, Odom OW, Kramer G, Hardesty B. Binding of an N-terminal rhodanese peptide to DnaJ and to ribosomes. The Journal of Biological Chemistry. 271: 31160-5. PMID 8940114 DOI: 10.1074/Jbc.271.49.31160 |
0.423 |
|
| 1995 |
Hardesty B, Kudlicki W, Odom OW, Zhang T, McCarthy D, Kramer G. Cotranslational folding of nascent proteins on Escherichia coli ribosomes. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 73: 1199-207. PMID 8722037 DOI: 10.1139/O95-129 |
0.491 |
|
| 1995 |
Kudlicki W, Odom OW, Kramer G, Hardesty B, Merrill GA, Horowitz PM. The importance of the N-terminal segment for DnaJ-mediated folding of rhodanese while bound to ribosomes as peptidyl-tRNA. The Journal of Biological Chemistry. 270: 10650-7. PMID 7738002 DOI: 10.1074/Jbc.270.18.10650 |
0.415 |
|
| 1995 |
Kudlicki W, Kitaoka Y, Odom OW, Kramer G, Hardesty B. Elongation and folding of nascent ricin chains as peptidyl-tRNA on ribosomes: the effect of amino acid deletions on these processes. Journal of Molecular Biology. 252: 203-12. PMID 7674301 DOI: 10.1006/Jmbi.1995.0488 |
0.424 |
|
| 1995 |
Kudlicki W, Chirgwin J, Kramer G, Hardesty B. Folding of an enzyme into an active conformation while bound as peptidyl-tRNA to the ribosome. Biochemistry. 34: 14284-7. PMID 7578030 DOI: 10.1021/Bi00044A003 |
0.441 |
|
| 1995 |
Kudlicki W, Odom OW, Merrill G, Kramer G, Hardesty B. Inhibition of the release factor-dependent termination reaction on ribosomes by DnaJ and the N-terminal peptide of rhodanese. Journal of Bacteriology. 177: 5517-22. PMID 7559337 DOI: 10.1128/Jb.177.19.5517-5522.1995 |
0.407 |
|
| 1994 |
Kudlicki W, Odom OW, Kramer G, Hardesty B. Chaperone-dependent folding and activation of ribosome-bound nascent rhodanese. Analysis by fluorescence. Journal of Molecular Biology. 244: 319-31. PMID 7966342 DOI: 10.1006/Jmbi.1994.1732 |
0.404 |
|
| 1994 |
Kudlicki W, Mouat M, Walterscheid JP, Kramer G, Hardesty B. Development of a chaperone-deficient system by fractionation of a prokaryotic coupled transcription/translation system. Analytical Biochemistry. 217: 12-9. PMID 7911283 DOI: 10.1006/Abio.1994.1077 |
0.409 |
|
| 1993 |
Ma C, Kudlicki W, Odom OW, Kramer G, Hardesty B. In vitro protein engineering using synthetic tRNA(Ala) with different anticodons. Biochemistry. 32: 7939-45. PMID 8347599 DOI: 10.1021/Bi00082A015 |
0.411 |
|
| 1993 |
Tsalkova T, Zardeneta G, Kudlicki W, Kramer G, Horowitz PM, Hardesty B. GroEL and GroES increase the specific enzymatic activity of newly-synthesized rhodanese if present during in vitro transcription/translation. Biochemistry. 32: 3377-80. PMID 8096394 DOI: 10.1021/Bi00064A022 |
0.453 |
|
| 1992 |
Hardesty B, Odom OW, Picking W. Ribosome function determined by fluorescence. Biochimie. 74: 391-401. PMID 1637864 DOI: 10.1016/0300-9084(92)90117-W |
0.344 |
|
| 1992 |
Picking WD, Picking WL, Odom OW, Hardesty B. Fluorescence characterization of the environment encountered by nascent polyalanine and polyserine as they exit Escherichia coli ribosomes during translation. Biochemistry. 31: 2368-75. PMID 1540593 DOI: 10.1021/Bi00123A023 |
0.429 |
|
| 1992 |
Kudlicki W, Kramer G, Hardesty B. High efficiency cell-free synthesis of proteins: refinement of the coupled transcription/translation system. Analytical Biochemistry. 206: 389-93. PMID 1332549 DOI: 10.1016/0003-2697(92)90383-I |
0.355 |
|
| 1992 |
Picking WD, Odom OW, Hardesty B. Evidence for RNA in the peptidyl transferase center of Escherichia coli ribosomes as indicated by fluorescence. Biochemistry. 31: 12565-70. PMID 1282033 DOI: 10.1021/Bi00165A004 |
0.424 |
|
| 1991 |
Kudlicki W, Picking WD, Kramer G, Hardesty B, Smailov SK, Mukhamedzhanov BG, Lee AV, Iskakov BK. Eukaryotic protein synthesis initiation factor 2. A target for inactivation by proanthocyanidin. European Journal of Biochemistry / Febs. 197: 623-9. PMID 2029895 DOI: 10.1111/J.1432-1033.1991.Tb15952.X |
0.383 |
|
| 1991 |
Czworkowski J, Odom OW, Hardesty B. Fluorescence study of the topology of messenger RNA bound to the 30S ribosomal subunit of Escherichia coli. Biochemistry. 30: 4821-30. PMID 2029524 DOI: 10.1021/Bi00233A026 |
0.39 |
|
| 1991 |
Picking WL, Picking WD, Ma CH, Hardesty B. A synthetic alanyl-initiator tRNA with initiator tRNA properties as determined by fluorescence measurements: comparison to a synthetic alanyl-elongator tRNA. Nucleic Acids Research. 19: 5749-54. PMID 1945852 DOI: 10.1093/Nar/19.20.5749 |
0.447 |
|
| 1991 |
Odom OW, Picking WD, Tsalkova T, Hardesty B. The synthesis of polyphenylalanine on ribosomes to which erythromycin is bound. European Journal of Biochemistry / Febs. 198: 713-22. PMID 1904819 DOI: 10.1111/J.1432-1033.1991.Tb16071.X |
0.452 |
|
| 1991 |
Picking W, Picking WD, Hardesty B. The use of synthetic tRNAs as probes for examining nascent peptides on Escherichia coli ribosomes. Biochimie. 73: 1101-7. PMID 1742354 DOI: 10.1016/0300-9084(91)90152-Q |
0.414 |
|
| 1991 |
Picking WD, Kudlicki W, Kramer G, Hardesty B, Vandenheede JR, Merlevede W, Park IK, DePaoli-Roach A. Fluorescence studies on the interaction of inhibitor 2 and okadaic acid with the catalytic subunit of type 1 phosphoprotein phosphatases. Biochemistry. 30: 10280-7. PMID 1657143 DOI: 10.1021/Bi00106A028 |
0.351 |
|
| 1990 |
Ovchinnikov LP, Motuz LP, Natapov PG, Averbuch LJ, Wettenhall RE, Szyszka R, Kramer G, Hardesty B. Three phosphorylation sites in elongation factor 2. Febs Letters. 275: 209-12. PMID 2261989 DOI: 10.1016/0014-5793(90)81473-2 |
0.364 |
|
| 1990 |
Hardesty B, Picking WD, Odom OW. The extension of polyphenylalanine and polylysine peptides on Escherichia coli ribosomes. Biochimica Et Biophysica Acta. 1050: 197-202. PMID 2207144 DOI: 10.1016/0167-4781(90)90166-Y |
0.431 |
|
| 1990 |
Odom OW, Picking WD, Hardesty B. Movement of tRNA but not the nascent peptide during peptide bond formation on ribosomes. Biochemistry. 29: 10734-44. PMID 1703007 DOI: 10.1021/Bi00500A004 |
0.404 |
|
| 1989 |
Szyszka R, Kramer G, Hardesty B. The phosphorylation state of the reticulocyte 90-kDa heat shock protein affects its ability to increase phosphorylation of peptide initiation factor 2 alpha subunit by the heme-sensitive kinase. Biochemistry. 28: 1435-8. PMID 2719907 DOI: 10.1021/Bi00430A001 |
0.326 |
|
| 1989 |
Hardesty B, Kramer G. The 90,000 dalton heat shock protein, a lot of smoke but no function as yet. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 67: 749-50. PMID 2695143 DOI: 10.1139/O89-112 |
0.36 |
|
| 1988 |
Zardeneta G, Kramer G, Hardesty B. Quantification and characterization of regulin, a Mr-230,000 highly elongated protein of rabbit reticulocytes. European Journal of Biochemistry / Febs. 178: 267-76. PMID 3203693 DOI: 10.1111/J.1432-1033.1988.Tb14452.X |
0.35 |
|
| 1988 |
Odom OW, Deng HY, Hardesty B. Fluorescence labeling and isolation of labeled RNA and ribosomal proteins. Methods in Enzymology. 164: 174-87. PMID 3071661 DOI: 10.1016/S0076-6879(88)64042-0 |
0.316 |
|
| 1987 |
Kudlicki W, Wettenhall RE, Kemp BE, Szyszka R, Kramer G, Hardesty B. Evidence for a second phosphorylation site on eIF-2 alpha from rabbit reticulocytes. Febs Letters. 215: 16-20. PMID 3569538 DOI: 10.1016/0014-5793(87)80105-9 |
0.313 |
|
| 1987 |
Kramer G, Kudlicki W, Fullilove S, Hardesty B. Association of the heme-controlled eIF-2 alpha kinase with spectrin-derived peptides. Haematology and Blood Transfusion. 31: 265-7. PMID 3443393 DOI: 10.1007/978-3-642-72624-8_56 |
0.4 |
|
| 1987 |
Rose DW, Wettenhall RE, Kudlicki W, Kramer G, Hardesty B. The 90-kilodalton peptide of the heme-regulated eIF-2 alpha kinase has sequence similarity with the 90-kilodalton heat shock protein. Biochemistry. 26: 6583-7. PMID 3427028 DOI: 10.1021/Bi00395A003 |
0.383 |
|
| 1987 |
Odom OW, Hardesty B. An apparent conformational change in tRNA(Phe) that is associated with the peptidyl transferase reaction. Biochimie. 69: 925-38. PMID 3126830 DOI: 10.1016/0300-9084(87)90226-4 |
0.415 |
|
| 1987 |
Hardesty B, Kudlicki W, Chen SC, Fullilove S, Kramer G. Involvement of the membrane skeleton in the regulation of the cAMP-independent protein kinase and a protein phosphatase that control protein synthesis. Haematology and Blood Transfusion. 31: 268-73. PMID 2832271 DOI: 10.1007/978-3-642-72624-8_57 |
0.338 |
|
| 1986 |
Kudlicki W, Kramer G, Hardesty B. Inhibition of protein synthesis by the beta-subunit of spectrin. Febs Letters. 200: 271-4. PMID 3709793 DOI: 10.1016/0014-5793(86)81150-4 |
0.365 |
|
| 1986 |
Deng HY, Odom OW, Hardesty B. Localization of L11 on the Escherichia coli ribosome by singlet-singlet energy transfer. European Journal of Biochemistry / Febs. 156: 497-503. PMID 3516693 DOI: 10.1111/J.1432-1033.1986.Tb09608.X |
0.343 |
|
| 1985 |
Kramer G, Wollny E, Fullilove S, Tipper J, Kudlicki W, Hardesty B. Regulin, a cytoskeleton-associated protein affecting phosphorylation-dephosphorylation. Haematology and Blood Transfusion. 29: 302-5. PMID 2993121 DOI: 10.1007/978-3-642-70385-0_62 |
0.339 |
|
| 1985 |
Kudlicki W, Fullilove S, Kramer G, Hardesty B. The 90-kDa component of reticulocyte heme-regulated eIF-2 alpha (initiation factor 2 alpha-subunit) kinase is derived from the beta subunit of spectrin. Proceedings of the National Academy of Sciences of the United States of America. 82: 5332-6. PMID 2410920 DOI: 10.1073/Pnas.82.16.5332 |
0.343 |
|
| 1984 |
Odom OW, Deng HY, Dabbs ER, Hardesty B. Binding of S21 to the 50S subunit and the effect of the 50S subunit on nonradiative energy transfer between the 3' end of 16S RNA and S21. Biochemistry. 23: 5069-76. PMID 6388639 DOI: 10.1021/Bi00316A037 |
0.414 |
|
| 1984 |
Odom OW, Stöffler G, Hardesty B. Movement of the 3'-end of 16 S RNA towards S21 during activation of 30 S ribosomal subunits. Febs Letters. 173: 155-8. PMID 6378660 DOI: 10.1016/0014-5793(84)81037-6 |
0.367 |
|
| 1984 |
Odom OW, Deng HY, Subramanian AR, Hardesty B. Relaxation time, interthiol distance, and mechanism of action of ribosomal protein S1. Archives of Biochemistry and Biophysics. 230: 178-93. PMID 6201138 DOI: 10.1016/0003-9861(84)90099-7 |
0.388 |
|
| 1983 |
Rychlik W, Odom OW, Hardesty B. Localization of the elongation factor Tu binding site on Escherichia coli ribosomes. Biochemistry. 22: 85-93. PMID 6338919 DOI: 10.1021/Bi00270A012 |
0.455 |
|
| 1983 |
Robbins D, Hardesty B. Comparison of ribosomal entry and acceptor transfer ribonucleic acid binding sites on Escherichia coli 70S ribosomes. Fluorescence energy transfer measurements from Phe-tRNAPhe to the 3' end of 16S ribonucleic acid. Biochemistry. 22: 5675-9. PMID 6197085 DOI: 10.1021/Bi00293A034 |
0.404 |
|
| 1982 |
Zardeneta G, Kramer G, Hardesty B. Structure and function of peptide initiation factor 2: differential loss of activities during proteolysis and generation of a terminal fragment containing the phosphorylation sites of the alpha subunit. Proceedings of the National Academy of Sciences of the United States of America. 79: 3158-61. PMID 6954466 DOI: 10.1073/Pnas.79.10.3158 |
0.398 |
|
| 1982 |
Dionne CA, Stearns GB, Kramer G, Hardesty B. Inhibition of peptide initiation by a low molecular weight RNA from rabbit reticulocytes. The Journal of Biological Chemistry. 257: 12373-9. PMID 6181066 |
0.316 |
|
| 1981 |
Kramer G, Hardesty B. Phosphorylation reactions that influence the activity of elF-2 Current Topics in Cellular Regulation. 20: 185-203. PMID 6276082 DOI: 10.1016/B978-0-12-152820-1.50009-2 |
0.365 |
|
| 1981 |
Robbins CH, Kramer G, Saneto R, Hardesty B, Johnson HM. Dissociation of protein kinase activity and the induction of the antiviral state in a cell line responsive to the antiviral effects of interferon. Biochemical and Biophysical Research Communications. 103: 103-10. PMID 6172123 DOI: 10.1016/0006-291X(81)91666-1 |
0.312 |
|
| 1981 |
Robbins D, Odom OW, Lynch J, Kramer G, Hardesty B, Liou R, Ofengand J. Position of transfer ribonucleic acid on Escherichia coli ribosomes. Distance from the 3′ end of 16S ribonucleic acid to three points on phenylalanine-accepting transfer ribonucleic acid in the donor site of 70S ribosomes Biochemistry. 20: 5301-5309. PMID 6170320 DOI: 10.1021/Bi00521A033 |
0.398 |
|
| 1981 |
Digweed M, Erdmann VA, Odom OW, Hardesty B. Fluorescence modification of Escherichia coli 5S RNA Nucleic Acids Research. 9: 3187-3198. PMID 6169004 DOI: 10.1093/Nar/9.13.3187 |
0.371 |
|
| 1981 |
Stoffler-Meilicke M, Stoffler G, Odom OW, Zinn A, Kramer G, Hardesty B. Localization of 3' ends of 5S and 23S rRNAs in reconstituted subunits of Escherichia coli ribosomes. Proceedings of the National Academy of Sciences. 78: 5538-5542. DOI: 10.1073/Pnas.78.9.5538 |
0.363 |
|
| 1980 |
Grankowski N, Lehmusvirta D, Kramer G, Hardesty B. Partial purification and characterization of reticulocyte phosphatase with activity for phosphorylated peptide initiation factor 2 Journal of Biological Chemistry. 255: 310-317. PMID 6243124 |
0.314 |
|
| 1980 |
Odom OW, Robbins DJ, Lynch J, Dottavio-Martin D, Kramer G, Hardesty B. Distances between 3′ ends of ribosomal ribonucleic acids reassembled into Escherichia coli ribosomes Biochemistry. 19: 5947-5954. PMID 6162473 DOI: 10.1021/Bi00567A001 |
0.352 |
|
| 1980 |
Wallis MH, Kramer G, Hardesty B. Partial purification and characterization of a 90000-dalton peptide involved in activation of the eIF-2.alpha. protein kinase of the hemin-controlled translational repressor Biochemistry. 19: 798-804. DOI: 10.1021/Bi00545A028 |
0.449 |
|
| 1979 |
Kramer G, Pinphanichakarn P, Hardesty B. Control of eukaryotic protein synthesis by phosphorylation Hamatologie Und Bluttransfusion. 23: 283-290. PMID 544364 DOI: 10.1007/978-3-642-67057-2_35 |
0.332 |
|
| 1979 |
Grankowski N, Kramer G, Hardesty B. Purification and partial characterization of the catalytic subunit of cAMP-dependent protein kinases from reticulocytes Archives of Biochemistry and Biophysics. 197: 618-629. PMID 228603 DOI: 10.1016/0003-9861(79)90286-8 |
0.38 |
|
| 1979 |
Kramer G, Odom OW, Hardesty B. [51] Polyamines in eukaryotic peptide initiation Methods in Enzymology. 60: 555-566. DOI: 10.1016/S0076-6879(79)60053-8 |
0.324 |
|
| 1979 |
Henderson AB, Kramer G, Hardesty B. [36] Binding of iodine-labeled mRNA to 40 S ribosomal subunits Methods in Enzymology. 60: 401-410. DOI: 10.1016/S0076-6879(79)60038-1 |
0.364 |
|
| 1977 |
Pinphanichakarn P, Kramer G, Hardesty B. Partial purification and characterization of a translational inhibitor from Friend leukemia cells Journal of Biological Chemistry. 252: 2106-2112. PMID 845164 |
0.308 |
|
| 1977 |
Ussery MA, Tanaka WK, Hardesty B. Subcellular distribution of aminoacyl tRNA synthetases in various eukaryotic cells European Journal of Biochemistry. 72: 491-500. PMID 837925 DOI: 10.1111/J.1432-1033.1977.Tb11272.X |
0.389 |
|
| 1977 |
Kramer G, Henderson AB, Pinphanichakarn P, Wallis MH, Hardesty B. Partial reaction of peptide initiation inhibited by phosphorylation of either initiation factor eIF 2 or 40S ribosomal proteins Proceedings of the National Academy of Sciences of the United States of America. 74: 1445-1449. PMID 193100 DOI: 10.1073/Pnas.74.4.1445 |
0.459 |
|
| 1976 |
Pinphanichakarn P, Kramer G, Hardesty B. Partial reaction of peptide initiation inhibited by the reticulocyte hemin-controlled repressor Biochemical and Biophysical Research Communications. 73: 625-631. PMID 1008879 DOI: 10.1016/0006-291X(76)90856-1 |
0.398 |
|
| 1976 |
Kramer G, Konecki D, Cimadevilla JM, Hardesty B. ATP requirement for binding of 125I-labeled globin mRNA to Artemia salina ribosomes Archives of Biochemistry and Biophysics. 174: 355-358. PMID 938054 DOI: 10.1016/0003-9861(76)90356-8 |
0.392 |
|
| 1976 |
Kramer G, Cimadevilla JM, Hardesty B. Specificity of the protein kinase activity associated with the hemin controlled repressor of rabbit reticulocyte Proceedings of the National Academy of Sciences of the United States of America. 73: 3078-3082. PMID 184458 DOI: 10.1073/Pnas.73.9.3078 |
0.341 |
|
| 1975 |
Cimadevilla JM, Kramer G, Pinphanichakarn P, Konecki D, Hardesty B. Inhibition of peptide chain initiation by a nonhemin-regulated translational repressor from friend leukemia cells Archives of Biochemistry and Biophysics. 171: 145-153. PMID 1190790 DOI: 10.1016/0003-9861(75)90017-X |
0.419 |
|
| 1975 |
Konecki D, Kramer G, Pinphanichakarn P, Hardesty B. Polyamines are necessary for maximum in vitro synthesis of globin peptides and play a role in chain initiation Archives of Biochemistry and Biophysics. 169: 192-198. PMID 1155944 DOI: 10.1016/0003-9861(75)90332-X |
0.406 |
|
| 1975 |
Cimadevilla JM, Hardesty B. Isolation and partial characterization of a 40 S ribosomal subunit transfer ribonucleic acid binding factor from rabbit reticulocytes Journal of Biological Chemistry. 250: 4389-4397. PMID 1141214 |
0.324 |
|
| 1975 |
Cimadevilla JM, Hardesty B. Aminoacyl-tRNA specificity of a 40S ribosomal subunit binding factor from rabbit reticulocytes Biochemical and Biophysical Research Communications. 63: 16-23. PMID 1125008 DOI: 10.1016/S0006-291X(75)80004-0 |
0.417 |
|
| 1975 |
Som K, Hardesty B. Isolation and partial characterization of an aminoacyl-tRNA synthetase complex from rabbit reticulocytes Archives of Biochemistry and Biophysics. 166: 507-517. PMID 1119806 DOI: 10.1016/0003-9861(75)90414-2 |
0.345 |
|
| 1975 |
Odom OW, Hardesty B, Wintermeyer W, Zachau HG. Efficient polyphenylalanine synthesis with proflavine and ethidium labeled tRNAPhe from yeast in the reticulocyte ribosomal system Bba Section Nucleic Acids and Protein Synthesis. 378: 159-163. PMID 1091290 DOI: 10.1016/0005-2787(75)90147-1 |
0.371 |
|
| 1974 |
Morrisey H, Hardesty B. [60] Assay and purification of met-tRNA hydrolase from rabbit reticulocytes Methods in Enzymology. 29: 726-739. PMID 4850661 DOI: 10.1016/0076-6879(74)29065-7 |
0.425 |
|
| 1974 |
Cimadevilla JM, Morrisey J, Hardesty B. A functional interaction between methionyl-transfer RNA hydrolase and a transfer RNA binding factor Journal of Molecular Biology. 83: 437-446. PMID 4830855 DOI: 10.1016/0022-2836(74)90505-1 |
0.425 |
|
| 1974 |
Odom OW, Hardesty B, Wintermeyer W, Zachau HG. The effect of removal or replacement with proflavine of the Y base in the anticodon loop of yeast tRNAPhe on binding into the acceptor or donor sites of reticulocyte ribosomes Archives of Biochemistry and Biophysics. 162: 536-551. PMID 4600956 DOI: 10.1016/0003-9861(74)90214-8 |
0.455 |
|
| 1974 |
Prather N, Ravel JM, Hardesty B, Shive W. Evidence for activities of rabbit reticulocyte elongation factor 1 analogous to bacterial factors EF-Ts and EF-Tu. Biochemical and Biophysical Research Communications. 57: 578-83. PMID 4597319 DOI: 10.1016/0006-291X(74)90585-3 |
0.322 |
|
| 1973 |
Hardesty B, Obrig T, Irvin J, Culp W. The effect of sodium fluoride, edeine, and cycloheximide on peptide synthesis with reticulocyte ribosomes Basic Life Sciences. 1: 377-392. PMID 4773153 DOI: 10.1007/978-1-4684-0877-5_30 |
0.359 |
|
| 1973 |
Obrig TG, Irvin JD, Hardesty B. The effect of an antiviral peptide on the ribosomal reactions of the peptide elongation enzymes, EF-I and EF-II Archives of Biochemistry and Biophysics. 155: 278-289. PMID 4705425 DOI: 10.1016/0003-9861(73)90116-1 |
0.457 |
|
| 1973 |
Ravel JM, Dawkins RC, Lax S, Odom OW, Hardesty B. Interaction of rabbit reticulocyte elongation factor 1 with guanosine-triphosphate and aminoacyl-transfer ribonucleic acid. Archives of Biochemistry and Biophysics. 155: 332-41. PMID 4574542 DOI: 10.1016/0003-9861(73)90122-7 |
0.37 |
|
| 1973 |
Culp W, Odom OW, Hardesty B. The effect of GTP hydrolysis by the peptide elongation enzymes on the sedimentation of ribosomes bearing peptidyl-tRNA and on the susceptibility of ribosome-bound tRNA to hydrolysis by ribonuclease Archives of Biochemistry and Biophysics. 155: 225-236. PMID 4350250 |
0.332 |
|
| 1972 |
Morrisey J, Hardesty B. Met-tRNA hydrolase from reticulocytes specific for Met-tRNAf Met on 40S ribosomal subunits Archives of Biochemistry and Biophysics. 152: 385-397. PMID 5072706 DOI: 10.1016/0003-9861(72)90228-7 |
0.457 |
|
| 1972 |
Irvin JD, Hardesty B. Binding of aminoacyl transfer ribonucleic acid synthetases to ribosomes from rabbit reticulocytes Biochemistry. 11: 1915-1920. PMID 5025634 DOI: 10.1021/Bi00760A028 |
0.374 |
|
| 1971 |
Obrig T, Irvin J, Culp W, Hardesty B. Inhibition of peptide initiation on reticulocyte ribosomes by edeine European Journal of Biochemistry. 21: 31-41. PMID 5568674 DOI: 10.1111/J.1432-1033.1971.Tb01436.X |
0.465 |
|
| 1971 |
Obrig TG, Culp WJ, McKeehan WL, Hardesty B. The mechanism by which cycloheximide and related glutarimide antibiotics inhibit peptide synthesis on reticulocyte ribosomes. The Journal of Biological Chemistry. 246: 174-81. PMID 5541758 |
0.47 |
|
| 1971 |
Hardesty B, McKeehan W. [34] Transfer factor II (T-II) from rabbit reticulocytes Methods in Enzymology. 20: 330-337. DOI: 10.1016/S0076-6879(71)20036-7 |
0.649 |
|
| 1971 |
Hardesty B, McKeehan W, Culp W. [33] Aminoacyl transfer RNA binding enzyme (T-I) from rabbit reticulocytes Methods in Enzymology. 20: 316-330. DOI: 10.1016/S0076-6879(71)20035-5 |
0.573 |
|
| 1970 |
McKeehan W, Irvin J, Hardesty B. A factor in the salt wash of reticulocyte ribosomes that can interact with acetylphenylalanyl-tRNA Biochemical and Biophysical Research Communications. 41: 757-764. PMID 5479299 DOI: 10.1016/0006-291X(70)90078-1 |
0.743 |
|
| 1970 |
Culp W, Morrisey J, Hardesty B. Initiator tRNA for the synthesis of globin peptides Biochemical and Biophysical Research Communications. 40: 777-785. PMID 4322105 DOI: 10.1016/0006-291X(70)90970-8 |
0.408 |
|
| 1969 |
Lin SY, McKeehan WL, Culp W, Hardesty B. Partial characterization of the enzymatic properties of the aminoacyl transfer ribonucleic acid binding enzyme. The Journal of Biological Chemistry. 244: 4340-50. PMID 5806580 |
0.469 |
|
| 1969 |
Hardesty B, Culp W, McKeehan W. The sequence of reactions leading to the synthesis of a peptide bond on reticulocyte ribosomes Cold Spring Harbor Symposia On Quantitative Biology. 34: 331-345. PMID 5266171 DOI: 10.1101/Sqb.1969.034.01.040 |
0.505 |
|
| 1969 |
Culp W, McKeehan W, Hardesty B. The mechanism of messenger RNA translocation through ribosomes Proceedings of the National Academy of Sciences of the United States of America. 64: 388-395. PMID 5263021 DOI: 10.1073/Pnas.64.1.388 |
0.577 |
|
| 1969 |
Culp WJ, McKeehan WL, Hardesty B. Deacylated tRNA-phe binding to a reticulocyte ribosomal site for the initiation of polyphenylalanine synthesis. Proceedings of the National Academy of Sciences of the United States of America. 63: 1431-8. PMID 5260946 DOI: 10.1073/Pnas.63.4.1431 |
0.587 |
|
| 1969 |
McKeehan WL, Hardesty B. Purification and partial characterization of the aminoacyl transfer ribonucleic acid binding enzyme from rabbit reticulocytes. The Journal of Biological Chemistry. 244: 4330-9. PMID 4308855 |
0.481 |
|
| 1969 |
McKeehan W, Sepulveda P, Lin SY, Hardesty B. Two distinct transfer enzymes from rabbit reticulocytes with ribosome dependent guanosine triphosphate phosphohydrolase activity Biochemical and Biophysical Research Communications. 34: 668-672. PMID 4305066 DOI: 10.1016/0006-291X(69)90790-6 |
0.632 |
|
| 1969 |
Culp W, McKeehan W, Hardesty B. THE MECHANISM OF MESSENGER RNA TRANSLOCATION THROUGH RIBOSOMES Proceedings of the National Academy of Sciences. 64: 388-395. DOI: 10.1073/pnas.64.1.388 |
0.433 |
|
| 1969 |
Culp W, McKeehan W, Hardesty B. THE MECHANISM OF MESSENGER RNA TRANSLOCATION THROUGH RIBOSOMES Proceedings of the National Academy of Sciences. 64: 388-395. DOI: 10.1073/pnas.64.1.388 |
0.433 |
|
| 1969 |
McKeehan W, Hardesty B. The mechanism of cycloheximide inhibition of protein synthesis in rabbit reticulocytes Biochemical and Biophysical Research Communications. 36: 625-630. DOI: 10.1016/0006-291X(69)90351-9 |
0.44 |
|
| 1969 |
McKeehan W, Hardesty B. The mechanism of cycloheximide inhibition of protein synthesis in rabbit reticulocytes Biochemical and Biophysical Research Communications. 36: 625-630. DOI: 10.1016/0006-291X(69)90351-9 |
0.453 |
|
| 1969 |
McKeehan W, Hardesty B. The mechanism of cycloheximide inhibition of protein synthesis in rabbit reticulocytes Biochemical and Biophysical Research Communications. 36: 625-630. DOI: 10.1016/0006-291X(69)90351-9 |
0.453 |
|
| 1969 |
McKeehan W, Hardesty B. The mechanism of cycloheximide inhibition of protein synthesis in rabbit reticulocytes Biochemical and Biophysical Research Communications. 36: 625-630. DOI: 10.1016/0006-291X(69)90351-9 |
0.453 |
|
| 1968 |
Culp WJ, Mosteller RD, Hardesty B. Involvement of transfer ribonucleic acid in early reactions of polyphenylalanine synthesis Archives of Biochemistry and Biophysics. 125: 658-670. DOI: 10.1016/0003-9861(68)90624-3 |
0.402 |
|
| 1967 |
Mosteller RD, Culp WJ, Hardesty B. A reaction associated with nonenzymatic binding in the reticulocyte transfer system. Proceedings of the National Academy of Sciences. 57: 1817-1824. DOI: 10.1073/Pnas.57.6.1817 |
0.314 |
|
| 1966 |
Mosteller R, Ravel JM, Hardesty B. Differential inactivation of soluble reticulocyte transfer factors with N-ethylmaleimide. Biochemical and Biophysical Research Communications. 24: 714-9. PMID 5970503 DOI: 10.1016/0006-291X(66)90383-4 |
0.309 |
|
| 1966 |
Mosteller R, Ravel JM, Hardesty B. Differential inactivation of soluble reticulocyte transfer factors with N-ethylmaleimide. Biochemical and Biophysical Research Communications. 24: 714-9. PMID 5970503 DOI: 10.1016/0006-291X(66)90383-4 |
0.309 |
|
| 1966 |
Lin S, Mosteller RD, Hardesty B. The mechanism of sodium fluoride and cycloheximide inhibition of hemoglobin biosynthesis in the cell-free reticulocyte system Journal of Molecular Biology. 21: 51-69. DOI: 10.1016/0022-2836(66)90079-9 |
0.396 |
|
| 1963 |
HARDESTY BA, MITCHELL HK. The interaction of fatty acids with mammalian cytochrome c. Archives of Biochemistry and Biophysics. 100: 1-8. PMID 13952740 |
0.455 |
|
| 1963 |
HARDESTY BA, MITCHELL HK. The accumulation of free fatty acids in poky, a maternally inherited mutant of Neurospora crassa. Archives of Biochemistry and Biophysics. 100: 330-4. PMID 13952739 |
0.469 |
|
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