☰

LaDonne Heaton Schulman - Publications

Affiliations: 
Albert Einstein College of Medicine, New York, New York, United States 
Area:
transfer RNA
Website:
http://www.nytimes.com/1992/08/13/nyregion/ladonne-h-schulman-56-dies-geneticist-studied-rna-molecule.html
Tree Info Similar researchers PubMed Report error

49 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
1994 Pak M, Willis IM, Schulman LH. Analysis of acceptor stem base pairing on tRNA(Trp) aminoacylation and function in vivo. The Journal of Biological Chemistry. 269: 2277-82. PMID 8294486  0.326
1993 Kim HY, Pelka H, Brunie S, Schulman LH. Two separate peptides in Escherichia coli methionyl-tRNA synthetase form the anticodon binding site for methionine tRNA. Biochemistry. 32: 10506-11. PMID 8399196 DOI: 10.1021/Bi00090A029  0.524
1993 Li S, Pelka H, Schulman LH. The anticodon and discriminator base are important for aminoacylation of Escherichia coli tRNA(Asn). The Journal of Biological Chemistry. 268: 18335-9. PMID 8349709  0.394
1993 Kim HY, Ghosh G, Schulman LH, Brunie S, Jakubowski H. The relationship between synthetic and editing functions of the active site of an aminoacyl-tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 90: 11553-7. PMID 8265588 DOI: 10.1073/Pnas.90.24.11553  0.613
1992 Pak M, Pallanck L, Schulman LH. Conversion of a methionine initiator tRNA into a tryptophan-inserting elongator tRNA in vivo. Biochemistry. 31: 3303-9. PMID 1554714  0.423
1992 Pallanck L, Li S, Schulman LH. The anticodon and discriminator base are major determinants of cysteine tRNA identity in vivo. The Journal of Biological Chemistry. 267: 7221-3. PMID 1373131  0.426
1991 Pallanck L, Schulman LH. Anticodon-dependent aminoacylation of a noncognate tRNA with isoleucine, valine, and phenylalanine in vivo. Proceedings of the National Academy of Sciences of the United States of America. 88: 3872-6. PMID 2023934 DOI: 10.1073/Pnas.88.9.3872  0.465
1991 Ghosh G, Pelka H, Schulman LH, Brunie S. Activation of methionine by Escherichia coli methionyl-tRNA synthetase. Biochemistry. 30: 9569-75. PMID 1911742 DOI: 10.1021/Bi00104A002  0.639
1991 Schulman LH. Recognition of tRNAs by aminoacyl-tRNA synthetases. Progress in Nucleic Acid Research and Molecular Biology. 41: 23-87. PMID 1882076 DOI: 10.1016/S0079-6603(08)60006-9  0.542
1991 Ghosh G, Kim HY, Demaret JP, Brunie S, Schulman LH. Arginine-395 is required for efficient in vivo and in vitro aminoacylation of tRNAs by Escherichia coli methionyl-tRNA synthetase. Biochemistry. 30: 11767-74. PMID 1751493 DOI: 10.1021/Bi00115A005  0.628
1991 Ghosh G, Brunie S, Schulman LH. Transition state stabilization by a phylogenetically conserved tyrosine residue in methionyl-tRNA synthetase. The Journal of Biological Chemistry. 266: 17136-41. PMID 1654323  0.582
1990 Ghosh G, Pelka H, Schulman LH. Identification of the tRNA anticodon recognition site of Escherichia coli methionyl-tRNA synthetase. Biochemistry. 29: 2220-5. PMID 2186810 DOI: 10.1021/Bi00461A003  0.642
1990 Chattapadhyay R, Pelka H, Schulman LH. Initiation of in vivo protein synthesis with non-methionine amino acids. Biochemistry. 29: 4263-8. PMID 2112406 DOI: 10.1021/Bi00470A001  0.449
1990 Schulman LH, Pelka H. An anticodon change switches the identity of E. coli tRNA(mMet) from methionine to threonine. Nucleic Acids Research. 18: 285-9. PMID 2109304 DOI: 10.1093/Nar/18.2.285  0.495
1989 Schulman LH, Pelka H. The anticodon contains a major element of the identity of arginine transfer RNAs. Science (New York, N.Y.). 246: 1595-7. PMID 2688091 DOI: 10.1126/Science.2688091  0.544
1988 Schulman LH, Pelka H. Anticodon switching changes the identity of methionine and valine transfer RNAs. Science (New York, N.Y.). 242: 765-8. PMID 3055296 DOI: 10.1126/Science.3055296  0.52
1988 Schulman LH, Abelson J. Recent excitement in understanding transfer RNA identity. Science (New York, N.Y.). 240: 1591-2. PMID 2454505 DOI: 10.1126/Science.2454505  0.46
1987 Schulman LH, Pelka H, Leon O. Peptides at the tRNA binding site of the crystallizable monomeric form of E. coli methionyl-tRNA synthetase. Nucleic Acids Research. 15: 10523-30. PMID 3320968 DOI: 10.1093/Nar/15.24.10523  0.444
1987 Leon O, Schulman LH. Covalent coupling of 4-thiouridine in the initiator methionine tRNA to specific lysine residues in Escherichia coli methionyl-tRNA synthetase. Biochemistry. 26: 7113-21. PMID 3122828 DOI: 10.1021/Bi00396A037  0.46
1987 Leon O, Schulman LH. tRNA recognition site of Escherichia coli methionyl-tRNA synthetase. Biochemistry. 26: 5416-22. PMID 3118944 DOI: 10.1021/Bi00391A030  0.499
1987 Leon O, Schulman LH. Covalent coupling of the variable loop of the elongator methionine tRNA to a specific lysine residue in Escherichia coli methionyl-tRNA synthetase Biochemistry. 26: 1933-1940. PMID 3109475 DOI: 10.1021/Bi00381A022  0.497
1986 Valenzuela D, Schulman LH. Identification of peptide sequences at the tRNA binding site of Escherichia coli methionyl-tRNA synthetase. Biochemistry. 25: 4555-61. PMID 3094575 DOI: 10.1021/Bi00364A015  0.458
1986 Pelka H, Schulman LH. Study of the interaction of Escherichia coli methionyl-tRNA synthetase with tRNAfMet using chemical and enzymatic probes. Biochemistry. 25: 4450-6. PMID 3092857 DOI: 10.1021/Bi00363A042  0.508
1985 Schulman LH, Pelka H. In vitro conversion of a methionine to a glutamine-acceptor tRNA. Biochemistry. 24: 7309-14. PMID 3910101 DOI: 10.1021/Bi00346A043  0.544
1984 Valenzuela D, Leon O, Schulman LH. Modification of specific lysine residues in E. coli methionyl-tRNA synthetase by crosslinking to E. coli formylmethionine tRNA. Biochemical and Biophysical Research Communications. 119: 677-84. PMID 6424668 DOI: 10.1016/S0006-291X(84)80303-4  0.505
1984 Schulman LH, Pelka H. Recognition of tRNAs by aminoacyl-tRNA synthetases: Escherichia coli tRNAMet and E. coli methionyl-tRNA synthetase. Federation Proceedings. 43: 2977-80. PMID 6389181  0.459
1983 Schulman LH, Pelka H. Anticodon loop size and sequence requirements for recognition of formylmethionine tRNA by methionyl-tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 80: 6755-9. PMID 6359155 DOI: 10.1073/Pnas.80.22.6755  0.499
1983 Schulman LH, Pelka H, Susani M. Base substitutions in the wobble position of the anticodon inhibit aminoacylation of E. coli tRNAfMet by E. coli Met-tRNA synthetase. Nucleic Acids Research. 11: 1439-55. PMID 6338482 DOI: 10.1093/Nar/11.5.1439  0.521
1981 Schulman LH, Valenzuela D, Pelka H. Reversible inactivation of Escherichia coli methionyl-tRNA synthetase by covalent attachment of formylmethionine tRNA to the tRNA binding site with a cleavable cross-linker. Biochemistry. 20: 6018-23. PMID 7030381 DOI: 10.1021/Bi00524A015  0.52
1981 Schulman LH, Pelka H, Reines SA. Attachment of protein affinity-labeling reagents of variable length and amino acid specificity to E. coli tRNAfMet. Nucleic Acids Research. 9: 1203-17. PMID 6164986 DOI: 10.1093/Nar/9.5.1203  0.406
1979 Reines SA, Schulman LH. A new method for attachment of fluorescent probes to tRNA. Methods in Enzymology. 59: 146-56. PMID 440078 DOI: 10.1016/0076-6879(79)59076-4  0.417
1978 Stern L, Schulman LH. The role of the minor base N4-acetylcytidine in the function of the Escherichia coli noninitiator methionine transfer RNA. The Journal of Biological Chemistry. 253: 6132-9. PMID 355249  0.309
1977 Schulman LH, Pelka H. Structural requirements for aminoacylation of Escherichia coli formylmethionine transfer RNA. Biochemistry. 16: 4256-65. PMID 332227 DOI: 10.1021/Bi00638A020  0.443
1977 Stern L, Schulman LH. Role of anticodon bases in aminoacylation of Escherichia coli methionine transfer RNAs. The Journal of Biological Chemistry. 252: 6403-8. PMID 330530  0.36
1977 Sundari RM, Pelka H, Schulman LH. Structural requirements of Escherichia coli formylmethionyl transfer ribonucleic acid for ribosome binding and initiation of protein synthesis. The Journal of Biological Chemistry. 252: 3941-4. PMID 325000  0.302
1977 Schulman LH, Pelka H. Alteration of the kinetic parameters for aminoacylation of Escherichia coli formylmethionine transfer RNA by modification of an anticodon base. The Journal of Biological Chemistry. 252: 814-9. PMID 14133  0.466
1976 Schulman LH, Pelka H. Location of accessible bases in Escherichia coli formylmethionine transfer RNA as determined by chemical modification. Biochemistry. 15: 5769-75. PMID 827308 DOI: 10.1021/Bi00671A013  0.431
1976 Sundari RM, Stringer EA, Schulman LH, Maitra U. Interaction of bacterial initiation factor 2 with initiator tRNA. The Journal of Biological Chemistry. 251: 3338-45. PMID 776966  0.34
1975 Schulman LH, Pelka H. The structural basis for the resistance of Escherichia coli formylmethionyl transfer ribonucleic acid to cleavage by Escherichia coli peptidyl transfer ribonucleic acid hydrolase. The Journal of Biological Chemistry. 250: 542-7. PMID 1089645  0.48
1974 Schulman LH, Shapiro R, Law DC, Louis JB. A simplified method for study of RNA conformation--reaction of formylmethionine transfer RNA with [14C]methylamine-bisulfite. Nucleic Acids Research. 1: 1305-16. PMID 10793691 DOI: 10.1093/Nar/1.10.1305  0.416
1973 Schulman LH, Ku?an I, Edelman B, Chambers RW. Photoreactions of pseudouridine 3'-phosphate. Biochemistry. 12: 201-8. PMID 4682993 DOI: 10.1021/Bi00726A004  0.536
1973 Schulman LH, Her MO. Recognition of altered E. coli formylmethionine transfer RNA by bacterial T factor. Biochemical and Biophysical Research Communications. 51: 275-82. PMID 4571402 DOI: 10.1016/0006-291X(73)91253-9  0.417
1973 Silber R, Malathi VG, Schulman LH, Hurwitz J, Duesberg PH. Studies of the Rous sarcoma virus RNA: characterization of the 5'-terminus. Biochemical and Biophysical Research Communications. 50: 467-72. PMID 4347521 DOI: 10.1016/0006-291X(73)90863-2  0.376
1972 Schulman LH. Structure and function of Escherichia coli formylmethionine transfer RNA: loss of methionine acceptor activity by modification of a specific guanosine residue in the acceptor stem of formylmethionine transfer RNA from Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America. 69: 3594-7. PMID 4566450 DOI: 10.1073/Pnas.69.12.3594  0.484
1972 Goddard JP, Schulman LH. Conversion of exposed cytidine residues to uridine residues in Escherichia coli formylmethionine transfer ribonucleic acid. The Journal of Biological Chemistry. 247: 3864-7. PMID 4338231  0.369
1971 Schulman LH. Structure and function of Escherichia coli formylmethionine transfer RNA. II. Effect of modification of guanosine residues on aminoacyl synthetase recognition. Journal of Molecular Biology. 58: 117-31. PMID 4932653 DOI: 10.1016/0022-2836(71)90236-1  0.521
1970 Schulman LH. Structure and function of E. coli formylmethionyl tRNA. I. Effect of modification of pyrimidine residues on aminoacyl synthetase recognition. Proceedings of the National Academy of Sciences of the United States of America. 66: 507-14. PMID 4917443 DOI: 10.1073/Pnas.66.2.507  0.472
1968 Schulman LH, Chambers RW. Transfer RNA, II. A structural basis for alanine acceptor activity. Proceedings of the National Academy of Sciences of the United States of America. 61: 308-15. PMID 5246927  0.549
1968 Reeves RH, Imura N, Schwam H, Weiss GB, Schulman LH, Chambers RW. Transfer RNA, I. Isolation and characterization of a new yeast alanine transfer RNA. Proceedings of the National Academy of Sciences of the United States of America. 60: 1450-7. PMID 5244751 DOI: 10.1073/Pnas.60.4.1450  0.568
Show low-probability matches.