| Year |
Citation |
Score |
| 1990 |
DeLange RJ, Glazer AN. Bile acids: antioxidants or enhancers of peroxidation depending on lipid concentration. Archives of Biochemistry and Biophysics. 276: 19-25. PMID 2297222 DOI: 10.1016/0003-9861(90)90004-I |
0.453 |
|
| 1990 |
Wakim BT, Picken MM, DeLange RJ. Identification and partial purification of a chromatin bound calmodulin activated histone 3 kinase from calf thymus. Biochemical and Biophysical Research Communications. 171: 84-90. PMID 2168180 DOI: 10.1016/0006-291X(90)91359-Z |
0.302 |
|
| 1989 |
DeLange RJ, Glazer AN. Phycoerythrin fluorescence-based assay for peroxy radicals: a screen for biologically relevant protective agents. Analytical Biochemistry. 177: 300-6. PMID 2567129 DOI: 10.1016/0003-2697(89)90056-0 |
0.401 |
|
| 1988 |
Seeler BJ, Horton MJ, Szego CM, DeLange RJ. Monoclonal antibody toward lysosomal cathepsin B cross-reacts preferentially with distinct histone classes. The International Journal of Biochemistry. 20: 1089-106. PMID 2470626 DOI: 10.1016/0020-711X(88)90254-6 |
0.333 |
|
| 1984 |
Lundell DJ, Glazer AN, DeLange RJ, Brown DM. Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Amino acid sequence studies. The Journal of Biological Chemistry. 259: 5472-80. PMID 6715353 |
0.509 |
|
| 1984 |
Urist MR, Huo YK, Brownell AG, Hohl WM, Buyske J, Lietze A, Tempst P, Hunkapiller M, DeLange RJ. Purification of bovine bone morphogenetic protein by hydroxyapatite chromatography. Proceedings of the National Academy of Sciences of the United States of America. 81: 371-5. PMID 6320184 DOI: 10.1073/Pnas.81.2.371 |
0.303 |
|
| 1983 |
Selsted ME, Brown DM, DeLange RJ, Lehrer RI. Primary structures of MCP-1 and MCP-2, natural peptide antibiotics of rabbit lung macrophages. The Journal of Biological Chemistry. 258: 14485-9. PMID 6643497 |
0.312 |
|
| 1981 |
DeLange RJ, Williams LC, Glazer AN. The amino acid sequence of the beta subunit of allophycocyanin. The Journal of Biological Chemistry. 256: 9558-66. PMID 6793571 |
0.494 |
|
| 1980 |
Searcy DG, Delange RJ. Thermoplasma acidophilum histone-like protein. Partial amino acid sequence suggestive of homology to eukaryotic histones. Biochimica Et Biophysica Acta. 609: 197-200. PMID 7407184 DOI: 10.1016/0005-2787(80)90212-9 |
0.435 |
|
| 1979 |
DeLange RJ, Williams LC, Drazin RE, Collier RJ. The amino acid sequence of fragment A, an enzymically active fragment of diphtheria toxin. III. The chymotryptic peptides, the peptides derived by cleavage at tryptophan residues, and the complete sequence of the protein. The Journal of Biological Chemistry. 254: 5838-42. PMID 221484 |
0.318 |
|
| 1979 |
Glazer AN, Hixson CS, DeLange RJ. Determination of the number of thioether-linked cysteine residues in cytochromes c and phycobiliproteins. Analytical Biochemistry. 92: 489-96. PMID 220892 DOI: 10.1016/0003-2697(79)90689-4 |
0.523 |
|
| 1978 |
Delange RJ. Peptide mapping and amino acid sequencing of histones. Methods in Cell Biology. 18: 169-88. PMID 355788 DOI: 10.1016/S0091-679X(08)60139-9 |
0.39 |
|
| 1976 |
DeLange RJ, Chang JY, Shaper JH, Glazer AN. Amino acid sequence of flagellin of Bacillus subtilis 168. III. Tryptic peptides, N-bromosuccinimide peptides, and the complete amino acid sequence. The Journal of Biological Chemistry. 251: 705-11. PMID 814121 |
0.577 |
|
| 1976 |
Shaper JH, DeLange RJ, Martinez RJ, Glazer AN. Amino acid sequence of flagellin of Bacillus subtilis 168. II. Tryptic peptides from maleylated flagellin. The Journal of Biological Chemistry. 251: 701-4. PMID 814120 |
0.53 |
|
| 1976 |
Chang JY, DeLange RJ, Shaper JH, Glazer AN. Amino acid sequence of flagellin of Bacillus subtilis 168. I. Cyanogen bromide peptides. The Journal of Biological Chemistry. 251: 695-700. PMID 814119 |
0.571 |
|
| 1976 |
Glazer AN, DeLange RJ, Sigman DS. Chemical Modification of Proteins. Selected methods and analytical procedures Laboratory Techniques in Biochemistry and Molecular Biology. 4: 1. DOI: 10.1016/S0075-7535(08)70259-6 |
0.434 |
|
| 1973 |
DeLange RJ, Hooper JA, Smith EL. Histone 3. 3. Sequence studies on the cyanogen bromide peptides; complete amino acid sequence of calf thymus histone 3. The Journal of Biological Chemistry. 248: 3261-74. PMID 4735580 |
0.605 |
|
| 1973 |
DeLange RJ, Smith EL. Histone 3. I. Isolation and sequences of the tryptic peptides from the maleylated calf thymus protein. The Journal of Biological Chemistry. 248: 3248-54. PMID 4735579 |
0.569 |
|
| 1973 |
Delange RJ, Chang JY, Shaper JH, Martinez RJ, Komatsu SK, Glazer AN. On the amino-acid sequence of flagellin from Bacillus subtilis 168: comparison with other bacterial flagellins. Proceedings of the National Academy of Sciences of the United States of America. 70: 3428-31. PMID 4202846 DOI: 10.1073/Pnas.70.12.3428 |
0.613 |
|
| 1972 |
DeLange RJ, Hooper JA, Smith EL. Complete amino-acid sequence of calf-thymus histone 3. Proceedings of the National Academy of Sciences of the United States of America. 69: 882-4. PMID 4502939 DOI: 10.1073/Pnas.69.4.882 |
0.625 |
|
| 1972 |
DeLange RJ, Smith EL. Structures of histones Accounts of Chemical Research. 5: 368-373. DOI: 10.1021/Ar50059A002 |
0.535 |
|
| 1971 |
DeLange RJ, Huang TS. Egg white avidin. 3. Sequence of the 78-residue middle cyanogen bromide peptide. Complete amino acid sequence of the protein subunit. The Journal of Biological Chemistry. 246: 698-709. PMID 5100763 |
0.346 |
|
| 1971 |
Huang TS, DeLange RJ. Egg white avidin. II. Isolation, composition, and amino acid sequences of the tryptic peptides. The Journal of Biological Chemistry. 246: 686-97. PMID 5100762 |
0.304 |
|
| 1971 |
DeLange RJ, Smith EL. Histones: structure and function. Annual Review of Biochemistry. 40: 279-314. PMID 4941236 DOI: 10.1146/annurev.bi.40.070171.001431 |
0.48 |
|
| 1971 |
Delange RJ, Smith EL. 3 Leucine Aminopeptidase and Other N-Terminal Exopeptidases Enzymes. 3: 81-118. DOI: 10.1016/S1874-6047(08)60394-7 |
0.533 |
|
| 1970 |
DeLange RJ, Smith EL, Bonner J. Calf thymus histone 3: sequences of the amino-and carboxyl-terminal regions and of the regions containing lysyl residues modified by acetylation and methylation. Biochemical and Biophysical Research Communications. 40: 989-93. PMID 5531405 DOI: 10.1016/0006-291X(70)91001-6 |
0.628 |
|
| 1970 |
DeLange RJ, Glazer AN, Smith EL. Identification and location of episilon-N-trimethyllysine in yeast cytochromes c. The Journal of Biological Chemistry. 245: 3325-7. PMID 5459636 |
0.578 |
|
| 1970 |
DeLange RJ. Egg white avidin. I. Amino acid composition; sequence of the amino- and carboxyl-terminal cyanogen bromide peptides. The Journal of Biological Chemistry. 245: 907-16. PMID 5417264 |
0.324 |
|
| 1970 |
Smith EL, DeLange RJ, Bonner J. Chemistry and biology of the histones. Physiological Reviews. 50: 159-70. PMID 4908087 DOI: 10.1152/Physrev.1970.50.2.159 |
0.486 |
|
| 1969 |
DeLange RJ, Fambrough DM, Smith EL, Bonner J. Calf and pea histone IV. II. The complete amino acid sequence of calf thymus histone IV; presence of epsilon-N-acetyllysine. The Journal of Biological Chemistry. 244: 319-34. PMID 5773298 |
0.583 |
|
| 1969 |
DeLange RJ, Fambrough DM, Smith EL, Bonner J. Calf and pea histone IV. 3. Complete amino acid sequence of pea seedling histone IV; comparison with the homologous calf thymus histone. The Journal of Biological Chemistry. 244: 5669-79. PMID 5388597 |
0.573 |
|
| 1969 |
DeLange RJ, Glazer AN, Smith EL. Presence and location of an unusual amino acid, epsilon-N-trimethyllysine, in cytochrome c of wheat germ and Neurospora. The Journal of Biological Chemistry. 244: 1385-8. PMID 4304194 |
0.634 |
|
| 1968 |
Olaitan SA, DeLange RJ, Smith EL. The structure of subtilisin Novo. The Journal of Biological Chemistry. 243: 5296-301. PMID 5702048 |
0.423 |
|
| 1968 |
DeLange RJ, Fambrough DM, Smith EL, Bonner J. Calf and pea histone IV. I. Amino acid compositions and the identical COOH-terminal 19-residue sequence. The Journal of Biological Chemistry. 243: 5906-13. PMID 5696625 |
0.597 |
|
| 1968 |
Smith EL, DeLange RJ, Evans WH, Landon M, Markland FS. Subtilisin Carlsberg. V. The complete sequence; comparison with subtilisin BPN'; evolutionary relationships. The Journal of Biological Chemistry. 243: 2184-91. PMID 4967581 |
0.474 |
|
| 1968 |
DeLange RJ, Smith EL. Subtilisin Carlsberg. II. Sequences of the tryptic ptpeides. The Journal of Biological Chemistry. 243: 2143-64. PMID 4967578 |
0.486 |
|
| 1968 |
DeLange RJ, Smith EL. Subtilisin Carlsberg. I. Amino acid composition; isolation and composition of peptides from the tryptic hydrolysate. The Journal of Biological Chemistry. 243: 2134-42. PMID 4967577 |
0.52 |
|
| 1968 |
Riley WD, DeLange RJ, Bratvold GE, Krebs EG. Reversal of phosphorylase kinase activation. The Journal of Biological Chemistry. 243: 2209-15. PMID 4296833 |
0.363 |
|
| 1968 |
DeLange RJ, Kemp RG, Riley WD, Cooper RA, Krebs EG. Activation of skeletal muscle phosphorylase kinase by adenosine triphosphate and adenosine 3',5'-monophosphate. The Journal of Biological Chemistry. 243: 2200-8. PMID 4296832 |
0.364 |
|
| 1966 |
Krebs EG, DeLange RJ, Kemp RG, Riley WD. Activation of skeletal muscle phosphorylase. Pharmacological Reviews. 18: 163-71. PMID 5904134 |
0.362 |
|
| 1966 |
Smith EL, Markland FS, Kasper CB, DeLange RJ, Landon M, Evans WH. The complete amino acid sequence of two types of subtilisin, BPN' and Carlsberg. The Journal of Biological Chemistry. 241: 5974-6. PMID 4959323 |
0.546 |
|
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