| Year |
Citation |
Score |
| 2006 |
Rall JE, Robbins J, Edelhoch H. Iodoproteins in the thyroid. Annals of the New York Academy of Sciences. 86: 373-399. PMID 14435978 DOI: 10.1111/J.1749-6632.1960.Tb42818.X |
0.333 |
|
| 2000 |
EDELHOCH H. The metachromasia of sodium gamma-poly-glutamate and pepsin. Experimental Cell Research. 15: 412-4. PMID 13597899 DOI: 10.1016/0014-4827(58)90042-9 |
0.205 |
|
| 1998 |
METZGER H, SHARP GC, EDELHOCH H. The properties of thyroglobulin. VII. The immunoloic activity of thyroglobulin fragments. Biochemistry. 1: 205-14. PMID 14473055 DOI: 10.1021/Bi00908A003 |
0.556 |
|
| 1998 |
METZGER H, EDELHOCH H. Purification of anti-thyroglobin antibodies. Nature. 193: 275-6. PMID 14473053 DOI: 10.1038/193275A0 |
0.493 |
|
| 1998 |
STEINER RF, EDELHOCH H. The ultraviolet fluorescence of proteins. I. The influence of pH and temperature. Biochimica Et Biophysica Acta. 66: 341-55. PMID 13983752 DOI: 10.1016/0006-3002(63)91203-4 |
0.307 |
|
| 1998 |
STEINER RF, EDELHOCH H. Influence of pH and urea on the ultra-violet fluorescence of several globular proteins. Nature. 192: 873-4. PMID 13916741 DOI: 10.1038/192873A0 |
0.317 |
|
| 1998 |
STEINER RF, EDELHOCH H. Effect of thermally induced structural transitions on the ultra-violet fluorescence of proteins. Nature. 193: 375-6. PMID 13916740 DOI: 10.1038/193375A0 |
0.3 |
|
| 1998 |
EDELHOCH H, STEINER RF. Structural transitions of lysozyme in urea solution. Biochimica Et Biophysica Acta. 60: 365-72. PMID 13889149 DOI: 10.1016/0006-3002(62)90412-2 |
0.396 |
|
| 1998 |
EDELHOCH H. The denaturation of pepsin. IV. The effects of temperature. Biochimica Et Biophysica Acta. 38: 113-22. PMID 13819263 DOI: 10.1016/0006-3002(60)91200-2 |
0.214 |
|
| 1996 |
EDELHOCH H, LIPPOLDT RE. THE PROPERTIES OF THYROGLOBULIN. X. THE EFFECT OF UREA. Biochimica Et Biophysica Acta. 79: 64-75. PMID 14114530 DOI: 10.1016/0926-6577(64)90039-7 |
0.235 |
|
| 1986 |
Prasad K, Lippoldt RE, Edelhoch H, Lewis MS. An intermediate polymer in the assembly of clathrin baskets Biochemistry. 25: 5214-5219. PMID 3768341 DOI: 10.1021/Bi00366A035 |
0.393 |
|
| 1986 |
Prasad K, Yora T, Yano O, Lippoldt RE, Edelhoch H, Saroff H. Purification and characterization of a molecular weight 100,000 coat protein from coated vesicles obtained from bovine brain. Biochemistry. 25: 6942-7. PMID 2879553 DOI: 10.1021/Bi00370A030 |
0.437 |
|
| 1986 |
Pierce LR, Zurzolo C, Edelhoch H. In vivo biosynthesis of clathrin and other coated vesicle proteins from rat liver. Journal of Cellular Biochemistry. 31: 121-33. PMID 2874148 DOI: 10.1002/Jcb.240310205 |
0.414 |
|
| 1985 |
Zarrilli R, Lippoldt RE, Edelhoch H, Nandi PK. The stability and transitions of tryptic-digested clathrin. Archives of Biochemistry and Biophysics. 241: 22-7. PMID 4026317 DOI: 10.1016/0003-9861(85)90356-X |
0.414 |
|
| 1985 |
Grimaldi S, Robbins J, Edelhoch H. Interaction of carbohydrate and protein in thyroxine binding globulin. Biochemistry. 24: 3771-6. PMID 3929834 DOI: 10.1021/Bi00335A053 |
0.445 |
|
| 1985 |
Prasad K, Lippoldt RE, Edelhoch H. Coat formation in coated vesicles. Biochemistry. 24: 6421-7. PMID 2867779 DOI: 10.1021/Bi00344A017 |
0.395 |
|
| 1985 |
Pierce LR, Zurzolo C, Salvatore G, Edelhoch H. Coated vesicles from the thyroid gland: isolation, characterization, and a search for a possible role in thyroglobulin transport. Journal of Endocrinological Investigation. 8: 303-12. PMID 2866211 DOI: 10.1007/Bf03348502 |
0.423 |
|
| 1984 |
Edelhoch H, Prasad K, Lippoldt RE, Nandi PK. Stability and structure of clathrin. Biochemistry. 23: 2314-20. PMID 6733087 DOI: 10.1021/Bi00305A035 |
0.397 |
|
| 1984 |
Prasad K, Alfsen A, Lippoldt RE, Nandi PK, Edelhoch H. Structural characterization of labeled clathrin and coated vesicles. Archives of Biochemistry and Biophysics. 235: 403-10. PMID 6517598 DOI: 10.1016/0003-9861(84)90213-3 |
0.411 |
|
| 1984 |
Alfsen A, de Paillerets C, Prasad K, Nandi PK, Lippoldt RE, Edelhoch H. Organization and dynamics of lipids in bovine brain coated and uncoated vesicles. European Biophysics Journal : Ebj. 11: 129-36. PMID 6152719 DOI: 10.1007/bf00276628 |
0.274 |
|
| 1984 |
Di Cerbo A, Nandi PK, Edelhoch H. Interaction of basic compounds with coated vesicles. Biochemistry. 23: 6036-40. PMID 6151855 DOI: 10.1021/bi00320a021 |
0.284 |
|
| 1984 |
Nandi PK, Edelhoch H. The effects of lyotropic (Hofmeister) salts on the stability of clathrin coat structure in coated vesicles and baskets Journal of Biological Chemistry. 259: 11290-11296. PMID 6147354 |
0.29 |
|
| 1983 |
Van der Walt B, Kotze B, Edelhoch H, Van Jaarsveld PP. Characterization of the major polypeptide chains of reduced bovine thyroglobulin. Biochimica Et Biophysica Acta. 744: 90-8. PMID 6830825 DOI: 10.1016/0167-4838(83)90344-8 |
0.365 |
|
| 1983 |
Nossal R, Weiss GH, Nandi PK, Lippoldt RE, Edelhoch H. Sizes and mass distributions of clathrin-coated vesicles from bovine brain. Archives of Biochemistry and Biophysics. 226: 593-603. PMID 6139088 DOI: 10.1016/0003-9861(83)90328-4 |
0.371 |
|
| 1982 |
Davoli C, Grimaldi S, Rusca G, Andreoli M, Edelhoch H. The isoelectric focusing of human thyroglobulin Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 705: 243-248. PMID 7115740 DOI: 10.1016/0167-4838(82)90184-4 |
0.359 |
|
| 1982 |
Van Jaarsveld PP, Lippoldt RE, Nandi PK, Edelhoch H. Effects of several antimalarials and phenothiazine compounds on the formation of coat structure from clathrin. Biochemical Pharmacology. 31: 793-8. PMID 7082348 DOI: 10.1016/0006-2952(82)90465-8 |
0.364 |
|
| 1982 |
Nandi PK, Irace G, Van Jaarsveld PP, Lippoldt RE, Edelhoch H. Instability of coated vesicles in concentrated sucrose solutions. Proceedings of the National Academy of Sciences of the United States of America. 79: 5881-5. PMID 6964393 DOI: 10.1073/Pnas.79.19.5881 |
0.396 |
|
| 1982 |
Grimaldi S, Edelhoch H, Robbins J. Effects of thyroxine binding on the stability, conformation, and fluorescence properties of thyroxine-binding globulin. Biochemistry. 21: 145-51. PMID 6174149 DOI: 10.1021/Bi00530A025 |
0.418 |
|
| 1982 |
Nandi PK, Prasad K, Lippoldt RE, Alfsen A, Edelhoch H. Reversibility of coated vesicle dissociation. Biochemistry. 21: 6434-40. PMID 6129893 DOI: 10.1021/Bi00268A018 |
0.383 |
|
| 1982 |
Irace G, Lippoldt RE, Edelhoch H, Nandi PK. Properties of clathrin coat structures. Biochemistry. 21: 5764-9. PMID 6129887 DOI: 10.1021/Bi00266A006 |
0.405 |
|
| 1982 |
Minton AP, Edelhoch H. Light scattering of bovine serum albumin solutions: Extension of the hard particle model to allow for electrostatic repulsion Biopolymers. 21: 451-458. DOI: 10.1002/BIP.360210215 |
0.249 |
|
| 1981 |
van Jaarsveld PP, van der Merwe MJ, van der Walt B, Edelhoch H. Enzymatic conversion of the major polypeptide chains of thyroglobulin. Endocrinology. 108: 1285-92. PMID 7472269 DOI: 10.1210/Endo-108-4-1285 |
0.378 |
|
| 1981 |
Nandi PK, Van Jaarsveld PP, Lippoldt RE, Edelhoch H. Effect of basic compounds on the polymerization of clathrin. Biochemistry. 20: 6706-10. PMID 7306530 DOI: 10.1021/Bi00526A028 |
0.394 |
|
| 1981 |
Van Jaarsveld PP, Nandi PK, Lippoldt RE, Saroff H, Edelhoch H. Polymerization of clathrin protomers into basket structures. Biochemistry. 20: 4129-35. PMID 7284315 DOI: 10.1021/bi00517a028 |
0.322 |
|
| 1981 |
Pretorius HT, Nandi PK, Lippoldt RE, Johnson ML, Keen JH, Pastan I, Edelhoch H. Molecular characterization of human clathrin. Biochemistry. 20: 2777-82. PMID 7248247 DOI: 10.1021/Bi00513A011 |
0.508 |
|
| 1981 |
Edelhoch H, Cheng S, Irace G. Spectroscopic Properties Of Rhodamine B‐Labeled Thyroid Hormone Annals of the New York Academy of Sciences. 366: 253-264. DOI: 10.1111/J.1749-6632.1981.Tb20759.X |
0.375 |
|
| 1980 |
Nandi PK, Pretorius HT, Lippoldt RE, Johnson ML, Edelhoch H. Molecular properties of the reassembled coat protein of coated vesicles. Biochemistry. 19: 5917-21. PMID 7459347 DOI: 10.1021/Bi00566A039 |
0.424 |
|
| 1980 |
Johnson ML, Lippoldt RE, Gershengorn MC, Robbins J, Edelhoch H. Molecular transitions of human thyroxine-binding globulin Archives of Biochemistry and Biophysics. 200: 288-295. PMID 6767448 DOI: 10.1016/0003-9861(80)90356-2 |
0.443 |
|
| 1979 |
Alexander SS, Colonna G, Edelhoch H. The structure and stability of human plasma cold-insoluble globulin. The Journal of Biological Chemistry. 254: 1501-5. PMID 762148 |
0.331 |
|
| 1979 |
Formisano S, Johnson ML, Lee G, Aloj SM, Edelhoch H. Critical micelle concentrations of gangliosides. Biochemistry. 18: 1119-24. PMID 570850 DOI: 10.1021/Bi00573A028 |
0.387 |
|
| 1979 |
Michot JL, Nunez J, Johnson ML, Irace G, Edelhoch H. Iodide binding and regulation of lactoperoxidase activity toward thyroid goitrogens. The Journal of Biological Chemistry. 254: 2205-9. PMID 429280 |
0.271 |
|
| 1979 |
Edelhoch H, Irace G, Johnson ML, Michot JL, Nunez J. The effects of thioureylene compounds (goitrogens) on lactoperoxidase activity. The Journal of Biological Chemistry. 254: 11822-30. PMID 91609 |
0.255 |
|
| 1978 |
Irace G, Edelhoch H. Thyroxine-induced conformational changes in prealbumin. Biochemistry. 17: 5729-33. PMID 728432 DOI: 10.1021/Bi00619A020 |
0.411 |
|
| 1978 |
Henkin RI, Lippoldt RE, Bilstad J, Wolf RO, Lum CK, Edelhoch H. Fractionation of human parotid saliva proteins. The Journal of Biological Chemistry. 253: 7556-65. PMID 701270 |
0.331 |
|
| 1978 |
Formisano S, Johnson ML, Edelhoch H. Effects of Hofmeister salts on the self-association of glucagon. Biochemistry. 17: 1468-73. PMID 646994 DOI: 10.1021/Bi00601A017 |
0.392 |
|
| 1978 |
van der Walt B, Kotzé B, van Jaarsveld PP, Edelhoch H. Evidence that thyroglobulin contains nonidentical half molecule subunits. The Journal of Biological Chemistry. 253: 1853-8. PMID 632243 |
0.292 |
|
| 1978 |
Johnson ML, Formisano S, Edelhoch H. Self-association of glucagon as measured by the optical properties of rhodamine 6G. The Journal of Biological Chemistry. 253: 1353-6. PMID 627541 |
0.301 |
|
| 1978 |
Colonna G, Alexander SS, Yamada KM, Pastan I, Edelhoch H. The stability of cell surface protein to surfactants and denaturants. The Journal of Biological Chemistry. 253: 7787-90. PMID 568142 |
0.315 |
|
| 1978 |
Edelhoch H. Protein-lipid interactions and the role of water. Horizons in Biochemistry and Biophysics. 5: 241-80. PMID 355086 |
0.322 |
|
| 1978 |
Alexander SS, Colonna G, Yamada KM, Pastan I, Edelhoch H. Molecular properties of a major cell surface protein from chick embryo fibroblasts. The Journal of Biological Chemistry. 253: 5820-4. PMID 27523 |
0.348 |
|
| 1977 |
Cheng SY, Pages RA, Saroff HA, Edelhoch H, Robbins J. Analysis of thyroid hormone binding to human serum prealbumin by 8-anilinonaphthalene-1-sulfonate fluorescence. Biochemistry. 16: 3707-13. PMID 889816 DOI: 10.1021/Bi00635A031 |
0.416 |
|
| 1977 |
Formisano S, Johnson ML, Edelhoch H. Thermodynamics of the self-association of glucagon. Proceedings of the National Academy of Sciences of the United States of America. 74: 3340-4. PMID 269394 DOI: 10.1073/pnas.74.8.3340 |
0.277 |
|
| 1977 |
Frénoy JP, Bourrillon R, Lippoldt R, Edelhoch H. Stability and subunit structure of human alpha2-macroglobulin. The Journal of Biological Chemistry. 252: 1129-33. PMID 65351 |
0.314 |
|
| 1977 |
Gershengorn MC, Lippoldt RE, Edelhoch H, Robbins J. Structure and stability of human thyroxine-binding globulin Journal of Biological Chemistry. 252: 8719-8723. PMID 21882 |
0.286 |
|
| 1977 |
Palumbo G, Edelhoch H. Interaction of apoA-II from human high density lipoprotein with lysolecithin. The Journal of Biological Chemistry. 252: 3684-8. PMID 16910 |
0.286 |
|
| 1976 |
Edelhoch H, Osborne JC. The thermodynamic basis of the stability of proteins, nucleic acids, and membranes. Advances in Protein Chemistry. 30: 183-250. PMID 779430 DOI: 10.1016/S0065-3233(08)60480-5 |
0.426 |
|
| 1976 |
Ingham KC, Tylenda C, Edelhoch H. Structural studies of human chorionic gonadotropin and its subunits using tyrosine fluorescence. Archives of Biochemistry and Biophysics. 173: 680-90. PMID 5960 DOI: 10.1016/0003-9861(76)90306-4 |
0.424 |
|
| 1976 |
Osborne JC, Palumbo G, Brewer HB, Edelhoch H. The thermodynamics of the self-association of the reduced and carboxymethylated form of apo-a-II from the human high density lipoprotein complex. Biochemistry. 15: 317-20. PMID 2283 DOI: 10.1021/Bi00647A012 |
0.35 |
|
| 1975 |
Ingham KC, Saroff HA, Edelhoch H. Ligand-induced self-association of human chorionic gonadotropin. Positive cooperativity in the binding of 8-anilino-1-naphthalenesulfonate. Biochemistry. 14: 4751-8. PMID 1182114 DOI: 10.1021/Bi00692A029 |
0.429 |
|
| 1975 |
Ingham KC, Saroff HA, Edelhoch H. Ligand-induced self-association of human luteinizing hormone. Negative cooperativity in the binding of 8-anilino-1-naphthalensulfonate. Biochemistry. 14: 4745-51. PMID 1182113 DOI: 10.1021/Bi00692A028 |
0.42 |
|
| 1975 |
Haeberli A, Salvatore G, Edelhoch H, Rall JE. Relationship between iodination and the polypeptide chain composition of thyroglobulin. The Journal of Biological Chemistry. 250: 7836-41. PMID 1176451 |
0.289 |
|
| 1975 |
Haeberli A, Bilstad J, Edelhoch H, Rall JE. Elementary chain composition of guinea pig thyroglobulin. The Journal of Biological Chemistry. 250: 7294-9. PMID 1165242 |
0.296 |
|
| 1975 |
Ferguson RN, Edelhoch H, Saroff HA, Robbins J, Cahnmann HJ. Negative cooperativity in the binding of thyroxine to human serum prealbumin. Preparation of tritium-labeled 8-anilino-1-naphthalenesulfonic acid. Biochemistry. 14: 282-9. PMID 1120103 DOI: 10.1021/Bi00673A014 |
0.371 |
|
| 1975 |
Henkin RI, Lippoldt RE, Bilstad J, Edelhoch H. A zinc protein isolated from human parotid saliva. Proceedings of the National Academy of Sciences of the United States of America. 72: 488-92. PMID 1054831 DOI: 10.1073/pnas.72.2.488 |
0.312 |
|
| 1975 |
Osborne JC, Palumbo G, Brewer HB, Edelhoch H. The self-association of the reduced ApoA-II apoprotein from the human high density lipoprotein complex. Biochemistry. 14: 3741-6. PMID 240392 DOI: 10.1021/Bi00688A004 |
0.385 |
|
| 1975 |
Gwynne J, Brewer HB, Edelhoch H. The molecular behavior of apoA-I in human high density lipoproteins. The Journal of Biological Chemistry. 250: 2269-74. PMID 234964 |
0.236 |
|
| 1975 |
Gwynne J, Palumbo G, Brewer HB, Edelhoch H. The interaction of apoA-I from human high density lipoprotein with lysolecithin. The Journal of Biological Chemistry. 250: 7300-6. PMID 170259 |
0.235 |
|
| 1975 |
Gwynne J, Palumbo G, Osborne JC, Brewer HB, Edelhoch H. The self-association of apoA-II, an apoprotein of the human high density lipoprotein complex. Archives of Biochemistry and Biophysics. 170: 204-12. PMID 169745 DOI: 10.1016/0003-9861(75)90111-3 |
0.417 |
|
| 1974 |
Frati L, Bilstad J, Edelhoch H, Rall JE, Salvatore G. Biosynthesis of the 27 S thyroid iodoprotein. Archives of Biochemistry and Biophysics. 162: 126-34. PMID 4831328 DOI: 10.1016/0003-9861(74)90111-8 |
0.358 |
|
| 1974 |
Lamas L, Taurog A, Salvatore G, Edelhoch H. Preferential syntheisi of thyroxine from early iodinated tyrosyl residues in thyroglobulin. The Journal of Biological Chemistry. 249: 2732-7. PMID 4828318 |
0.247 |
|
| 1974 |
Pollet R, Edelhoch H. Changes in optical parameters of myeloma proteins with phosphorylcholine binding. The Journal of Biological Chemistry. 249: 5188-94. PMID 4604203 |
0.262 |
|
| 1974 |
Cohn DV, Macgregor RR, Sinha D, Huang DW, Edelhoch H, Hamilton JW. The migration behavior of proparathyroid hormone, parathyroid hormone, and their peptide fragments during gel filtration. Archives of Biochemistry and Biophysics. 164: 669-73. PMID 4477704 DOI: 10.1016/0003-9861(74)90079-4 |
0.413 |
|
| 1974 |
Ui N, Lippoldt RE, Edelhoch H. Acid-induced conformational change in hog thyroglobulin. Archives of Biochemistry and Biophysics. 164: 202-9. PMID 4473957 DOI: 10.1016/0003-9861(74)90023-X |
0.465 |
|
| 1974 |
Ingham KC, Aloj SM, Edelhoch H. Rates of dissociation and recombination of the subunits of bovine thyrotropin. Archives of Biochemistry and Biophysics. 163: 589-99. PMID 4472276 DOI: 10.1016/0003-9861(74)90518-9 |
0.444 |
|
| 1974 |
Gwynne J, Brewer B, Edelhoch H. The molecular properties of ApoA-I from human high density lipoprotein. The Journal of Biological Chemistry. 249: 2411-6. PMID 4362678 |
0.266 |
|
| 1973 |
Edelhoch H, Schneider AB. Conformational changes of protected glucogon fragments bound to lysolecithin Archives of Biochemistry and Biophysics. 157: 470-475. PMID 4798757 DOI: 10.1016/0003-9861(73)90664-4 |
0.311 |
|
| 1973 |
Aloj SM, Edelhoch H, Ingham KC, Morgan FJ, Canfield RE, Ross GT. The rates of dissociation and reassociation of the subunits of human chorionic gonadotropin. Archives of Biochemistry and Biophysics. 159: 497-504. PMID 4784469 DOI: 10.1016/0003-9861(73)90480-3 |
0.432 |
|
| 1973 |
Edelhoch H, Schneider AB. Conformational changes of protected glucagon fragments bound to lysolecithin. Archives of Biochemistry and Biophysics. 157: 470-5. PMID 4738379 DOI: 10.1016/0003-9861(73)90664-4 |
0.406 |
|
| 1973 |
Aloj SM, Ingham KC, Edelhoch H. Interaction of 1,8-ANS with human luteinizing hormones: A probe for subunit interactions of hCG and hLH Archives of Biochemistry and Biophysics. 155: 478-479. PMID 4735854 DOI: 10.1016/0003-9861(73)90141-0 |
0.371 |
|
| 1973 |
van Jaarsveld PP, Edelhoch H, Goodman DS, Robbins J. The interaction of human plasma retinol-binding protein and prealbumin. The Journal of Biological Chemistry. 248: 4698-705. PMID 4718739 |
0.274 |
|
| 1973 |
Pages RA, Robbins J, Edelhoch H. Binding of thyroxine and thyroxine analogs to human serum prealbumin. Biochemistry. 12: 2773-9. PMID 4711480 DOI: 10.1021/Bi00738A034 |
0.383 |
|
| 1973 |
Rossi G, Edelhoch H, Tenore A, Van Middlesworth L, Salvatore G. Characterization and properties of thyroid iodoproteins from severely iodine-deficient rats. Endocrinology. 92: 1241-9. PMID 4686320 DOI: 10.1210/endo-92-4-1241 |
0.238 |
|
| 1973 |
Pollet R, Edelhoch H. The binding peoperties of anti-phosphorylcholine mouse myeloma proteins as measured by protein fluorescence. The Journal of Biological Chemistry. 248: 5443-7. PMID 4588682 |
0.309 |
|
| 1973 |
Aloj S, Bruni CB, Edelhoch H, Rechler MM. Physical studies comparing a genetically fused enzyme of the histidine operon with its component enzymes. The Journal of Biological Chemistry. 248: 5880-6. PMID 4579430 |
0.213 |
|
| 1973 |
van Jaarsveld PP, Branch WT, Edelhoch H, Robbins J. Polymorphism of rhesus monkey serum prealbumin. Molecular properties and binding of thyroxine and retinol-binding protein. The Journal of Biological Chemistry. 248: 4706-12. PMID 4198061 |
0.311 |
|
| 1973 |
Ingham KC, Aloj SM, Edelhoch H. The rates of dissociation and recombination of the subunits of human luteinizing hormone Archives of Biochemistry and Biophysics. 159: 596-605. DOI: 10.1016/0003-9861(73)90496-7 |
0.43 |
|
| 1972 |
Aloj S, Edelhoch H. Structural studies on polypeptide hormones. II. Parathyroid hormone. Archives of Biochemistry and Biophysics. 150: 782-5. PMID 5065143 DOI: 10.1016/0003-9861(72)90098-7 |
0.441 |
|
| 1972 |
Aloj S, Edelhoch H. The molecular properties of human growth hormone. The Journal of Biological Chemistry. 247: 1146-52. PMID 5062240 |
0.278 |
|
| 1972 |
Pollet R, Rossi G, Edelhoch H. Fluorescence and circular dichroism of Bence-Jones proteins at high temperature. The Journal of Biological Chemistry. 247: 5921-7. PMID 5057089 |
0.29 |
|
| 1972 |
Bilstad JM, Edelhoch H, Lippoldt R, Rall JE, Salvatore G. Isolation and characterization of discrete fragments of 27 S thyroid iodoprotein. Archives of Biochemistry and Biophysics. 151: 341-50. PMID 5044523 DOI: 10.1016/0003-9861(72)90505-x |
0.249 |
|
| 1972 |
Aloj AM, Edelhoch H, Handwerger S, Sherwood LM. Correlations in the structure and function of human placental lactogen and human growth hormone. 2. The effects of disulfide bond modification on the conformation of human placental lactogen. Endocrinology. 91: 728-37. PMID 5041205 DOI: 10.1210/Endo-91-3-728 |
0.419 |
|
| 1972 |
Branch WT, Robbins J, Edelhoch H. Thyroxine-binding prealbumin. Conformation in urea and guanidine. Archives of Biochemistry and Biophysics. 152: 144-51. PMID 4627354 DOI: 10.1016/0003-9861(72)90202-0 |
0.438 |
|
| 1972 |
Schneider AB, Edelhoch H. Polypeptide hormone interaction. 3. Conformational changes of glucagon bound to lysolecithin Journal of Biological Chemistry. 247: 4992-4995. PMID 4341534 |
0.28 |
|
| 1972 |
Schneider AB, Edelhoch H. Polypeptide hormone interaction. II. Glucagon binding to lysolecithin Journal of Biological Chemistry. 247: 4986-4991. PMID 4341533 |
0.267 |
|
| 1971 |
Covelli I, Van Zyl A, Edelhoch H. Spectrophotometric determination of monoiodotyrosine, diiodotyrosine, and thyroxine in iodoproteins. Analytical Biochemistry. 42: 82-90. PMID 5556420 DOI: 10.1016/0003-2697(71)90012-1 |
0.342 |
|
| 1971 |
Schneider AB, Bornet H, Edelhoch H. The effects of low temperature on the conformation of thyroglobulin Journal of Biological Chemistry. 246: 2835-2841. PMID 5554296 |
0.236 |
|
| 1971 |
Schneider AB, Edelhoch H. Equilibrium density centrifugation of thyroglobulin in RbCl. Effect of iodine Journal of Biological Chemistry. 246: 6592-6598. PMID 5132673 |
0.229 |
|
| 1971 |
Aloj S, Edelhoch H. The molecular properties of human chorionic somatomammotropin. The Journal of Biological Chemistry. 246: 5047-52. PMID 5106224 |
0.284 |
|
| 1971 |
Bornet H, Edelhoch H. Polypeptide hormone interaction. I. Glucagon detergent interaction. The Journal of Biological Chemistry. 246: 1785-92. PMID 5102150 |
0.239 |
|
| 1971 |
Cramarossa L, Andreoli M, Schneider A, Edelhoch H. Effect of freezing in methylmercaptoimidazole on the structure of thyroglobulin. Endocrinology. 89: 741-8. PMID 4105306 DOI: 10.1210/Endo-89-3-741 |
0.394 |
|
| 1970 |
Edelhoch H, Lippoldt RE. The properties of bovine growth hormone. IV. Circular dichroism of native and iodinated molecules. The Journal of Biological Chemistry. 245: 4199-203. PMID 5533922 |
0.291 |
|
| 1970 |
Malan PG, Edelhoch H. Nitration of human serum albumin and bovine and human goiter thyroglobulins with tetranitromethane. Biochemistry. 9: 3205-14. PMID 5530843 DOI: 10.1021/Bi00818A013 |
0.362 |
|
| 1970 |
Schneider AB, Bornet H, Edelhoch H. Properties of thyroglobulin. XX. The biosynthesis of thyroglobulin. Effect of temperature on subunit species Journal of Biological Chemistry. 245: 2673-2678. PMID 5463049 |
0.254 |
|
| 1970 |
Brewer HB, Edelhoch H. A conformational study of porcine thyrocalcitonin. The Journal of Biological Chemistry. 245: 2402-8. PMID 5462539 |
0.254 |
|
| 1970 |
Schneider AB, Edelhoch H. The properties of thyroglobulin. XIX. The equilibrium between guinea pig thyroglobulin and its subunits Journal of Biological Chemistry. 245: 885-890. PMID 5416670 |
0.283 |
|
| 1970 |
Aloj SM, Edelhoch H. Conformational similarity of ovine prolactin and bovine growth hormone. Proceedings of the National Academy of Sciences of the United States of America. 66: 830-6. PMID 5269246 DOI: 10.1073/pnas.66.3.830 |
0.341 |
|
| 1969 |
Nissley P, Cittanova N, Edelhoch H. The properties of thyroglobulin. 18. Isolation of thyroglobulin subunits. Biochemistry. 8: 443-8. PMID 5777340 DOI: 10.1021/Bi00829A060 |
0.364 |
|
| 1969 |
Andreoli M, Sena L, Edelhoch H, Salvatore G. The noncovalent subunit structure of human thyroglobulin Archives of Biochemistry and Biophysics. 134: 242-248. PMID 5388089 DOI: 10.1016/0003-9861(69)90272-0 |
0.416 |
|
| 1969 |
Edelhoch H, Carlomagno MS, Salvatore G. Iodine and the structure of thyroglobulin. Archives of Biochemistry and Biophysics. 134: 264-5. PMID 5345593 DOI: 10.1016/0003-9861(69)90279-3 |
0.254 |
|
| 1969 |
Bernstein RS, Wilchek M, Edelhoch H. Structural studies on polypeptide hormones. II. Polarization of fluorescence. The Journal of Biological Chemistry. 244: 4398-405. PMID 4308859 |
0.294 |
|
| 1969 |
Edelhoch H, Lippoldt RE. Structural studies on polypeptide hormones. I. Fluorescence. The Journal of Biological Chemistry. 244: 3876-83. PMID 4308740 |
0.31 |
|
| 1969 |
Edelhoch H, Perlman RL, Wilchek M. Tyrosine fluorescence in proteins Annals of the New York Academy of Sciences. 158: 391-409. PMID 4308073 DOI: 10.1111/J.1749-6632.1969.Tb56233.X |
0.624 |
|
| 1968 |
Edelhoch H, Perlman RL, Wilchek M. Fluorescence studies with tyrosyl peptides Biochemistry. 7: 3893-3900. PMID 5722258 DOI: 10.1021/Bi00851A016 |
0.554 |
|
| 1968 |
Edelhoch H, Bernstein RS, Wilchek M. The fluorescence of tyrosyl and tryptophanyl diketopiperazines. The Journal of Biological Chemistry. 243: 5985-92. PMID 5696631 |
0.257 |
|
| 1968 |
Edelhoch H, Lippoldt RE, Wilchek M. The circular dichroism of tryosyl and tryptophanyl diketopiperazines. The Journal of Biological Chemistry. 243: 4799-805. PMID 5687722 |
0.228 |
|
| 1968 |
Perlman RL, Van Zyl A, Edelhoch H. The properties of thyroglobulin. XVI. Energy transfer to iodoamino acids Journal of the American Chemical Society. 90: 2168-2172. PMID 5644190 DOI: 10.1021/JA01010A040 |
0.517 |
|
| 1968 |
Pharo RL, Sordahl LA, Edelhoch H, Sanadi DR. Studies on dihydronicotinamide adenine dinucleotide ubiquinone reductase. II. Purication and properties. Archives of Biochemistry and Biophysics. 125: 416-428. PMID 4172972 DOI: 10.1016/0003-9861(68)90598-5 |
0.373 |
|
| 1967 |
Edelhoch H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry. 6: 1948-1954. PMID 6049437 DOI: 10.1021/Bi00859A010 |
0.396 |
|
| 1967 |
Edelhoch H, Brand L, Wilchek M. Fluorescence studies with tryptophyl peptides. Biochemistry. 6: 547-59. PMID 6047638 DOI: 10.1021/Bi00854A024 |
0.243 |
|
| 1967 |
Vecchio G, Edelhoch H, Robbins J, Weathers B. Studies on the structure of 27S thyroid iodoprotein. Biochemistry. 5: 2617-23. PMID 5968572 DOI: 10.1021/BI00872A020 |
0.26 |
|
| 1967 |
Cuatrecasas P, Edelhoch H, Anfinsen CB. Fluorescence studies of the interaction of nucleotides with the active site of the nuclease of Staphylococcus aureus. Proceedings of the National Academy of Sciences of the United States of America. 58: 2043-50. PMID 5237497 DOI: 10.1073/Pnas.58.5.2043 |
0.304 |
|
| 1967 |
de Crombrugghe B, Edelhoch H. The properties of thyroglobulin. XIV. The structure of reoxidized thyroglobulin. Biochemistry. 5: 2238-45. PMID 4959961 DOI: 10.1021/Bi00871A012 |
0.573 |
|
| 1967 |
Salvatore G, Aloj S, Salvatore M, Edelhoch H. Hybridization of Half Molecules of Guinea Pig Thyroglobulin Journal of Biological Chemistry. 242: 5002-5007. DOI: 10.1016/s0021-9258(18)99468-8 |
0.219 |
|
| 1967 |
Perlman RL, Edelhoch H. The Formation of Diiodotyrosine in Iodinated Human Serum Albumin Journal of Biological Chemistry. 242: 2416-2422. DOI: 10.1016/s0021-9258(18)95977-6 |
0.268 |
|
| 1966 |
Burger HG, Edelhoch H, Condliffe PG. Fluorescence in the characterization of bovine growth hormone. Endocrinology. 78: 98-102. PMID 5948430 DOI: 10.1210/Endo-78-1-98 |
0.393 |
|
| 1966 |
Edelhoch H, Steiner RF. Properties of thyroglobulin. XII. Comparison of the configurational states of reduced and unreduced thyroglobulin. Biopolymers. 4: 999-1014. PMID 5927650 DOI: 10.1002/bip.1966.360040905 |
0.232 |
|
| 1966 |
Jakoby WB, Labaw L, Edelhoch H, Pastan I, Rall JE. Thyroglobulin: evidence for crystallization and association. Science (New York, N.Y.). 153: 1671-2. PMID 5917084 DOI: 10.1126/Science.153.3744.1671 |
0.442 |
|
| 1965 |
Edelhoch H, Steiner R. Changes in Physical Properties Accompanying the Interaction of Trypsin with Protein Inhibitors Journal of Biological Chemistry. 240: 2877-2882. DOI: 10.1016/S0021-9258(18)97262-5 |
0.274 |
|
| 1963 |
FRATTALI V, STEINER RF, MILLAR DB, EDELHOCH H. REDUCTION AND REOXIDATION OF THE DISULPHIDE BONDS OF PEPSINOGEN. Nature. 199: 1186-7. PMID 14072043 DOI: 10.1038/1991186A0 |
0.307 |
|
| 1963 |
Edelhoch H, Schlaff S. Structural Transitions in Antibody and Normal γ-Globulins Journal of Biological Chemistry. 238: 244-250. DOI: 10.1016/S0021-9258(19)83987-X |
0.241 |
|
| 1962 |
Steiner RF, Edelhoch H. Structural Transitions in Antibody and Normal γ-Globulins. II. Fluorescence Polarization Studies Journal of the American Chemical Society. 84: 2139-2148. DOI: 10.1021/ja00870a028 |
0.282 |
|
| 1962 |
Edelhoch H, Lippoldt RE, Steiner RF. Structural Transitions in Antibody and Normal γ-Globulins. I. Molecular Properties Journal of the American Chemical Society. 84: 2133-2138. DOI: 10.1021/ja00870a027 |
0.282 |
|
| 1962 |
Steiner RF, Edelhoch H. Fluorescent Protein Conjugates. Chemical Reviews. 62: 457-483. DOI: 10.1021/cr60219a004 |
0.299 |
|
| 1961 |
Edsall J, Edelhoch H, Lontie R, Morrison P. Additions and Corrections-Light Scattering in Solutions of Serum Albumin: Effects of Charge and Ionic Strength Journal of the American Chemical Society. 83: 5045-5045. DOI: 10.1021/Ja01485A602 |
0.619 |
|
| 1961 |
Steiner RF, Edelhoch H. The Properties of Thyroglobulin. VI. The Internal Rigidity of Native and Denatured Thyroglobulin Journal of the American Chemical Society. 83: 1435-1444. DOI: 10.1021/ja01467a040 |
0.31 |
|
| 1961 |
Edelhoch H, Metzger H. The Properties of Thyroglobulin. V. The Properties of Denatured Thyroglobulin Journal of the American Chemical Society. 83: 1428-1435. DOI: 10.1021/JA01467A039 |
0.269 |
|
| 1961 |
Metzger H, Edelhoch H. The Properties of Thyroglobulin. IV. Denaturation Kinetics Journal of the American Chemical Society. 83: 1423-1427. DOI: 10.1021/ja01467a038 |
0.544 |
|
| 1960 |
Edelhoch H, Lippoldt RE. The optical rotatory and viscometric properties of γ-poly-D-glutamate Biochimica Et Biophysica Acta. 45: 205-216. PMID 13725656 DOI: 10.1016/0006-3002(60)91445-1 |
0.37 |
|
| 1960 |
Edelhoch H. THE PROPERTIES OF THYROGLOBULIN. III. THE TITRATION OF THYROGLOBULIN IN SODIUM DODECYL SULFATE The Journal of Physical Chemistry. 64: 1771-1773. DOI: 10.1021/J100840A510 |
0.305 |
|
| 1960 |
Raijman L, Grisolia S, Edelhoch H. Further Purification and Properties of Brain Acyl Phosphatase Journal of Biological Chemistry. 235: 2340-2342. DOI: 10.1016/s0021-9258(18)64623-x |
0.232 |
|
| 1959 |
Edelhoch H. The Denaturization of Pepsin. V. The Electrostatic Free Energy of Native and Denatured Pepsin The Journal of Physical Chemistry. 63: 1535-1536. DOI: 10.1021/J150579A602 |
0.235 |
|
| 1958 |
Edelhoch H, Lippoldt RE. The optical rotatory properties of bacterial γ-poly-d-glutamate Biochimica Et Biophysica Acta. 30: 657-658. PMID 13618287 DOI: 10.1016/0006-3002(58)90127-6 |
0.33 |
|
| 1958 |
Edelhoch H. The Denaturation of Pepsin. III. The Effects of Various Protein Denaturants on the Kinetics of Pepsin Inactivation1 Journal of the American Chemical Society. 80: 6648-6655. DOI: 10.1021/JA01557A048 |
0.301 |
|
| 1958 |
Edelhoch H. The Denaturation of Pepsin. II. Hydrogen Ion Equilibria of Native and Denatured Pepsin1 Journal of the American Chemical Society. 80: 6640-6647. DOI: 10.1021/JA01557A047 |
0.217 |
|
| 1957 |
Edelhoch H. The Denaturation of Pepsin. I. Macromolecular Changes1 Journal of the American Chemical Society. 79: 6100-6109. DOI: 10.1021/JA01580A002 |
0.31 |
|
| 1957 |
Edelhoch H, Bateman JB. The Behavior of a Bacterial Polypeptide as a Polyelectrolyte Journal of the American Chemical Society. 79: 6093-6100. DOI: 10.1021/JA01580A001 |
0.195 |
|
| 1957 |
Edelhoch H, Rodwell VW, Grisolia S. The Molecular Properties Of Yeast And Muscle Phosphoglyceric Acid Mutase Journal of Biological Chemistry. 228: 891-903. DOI: 10.1016/S0021-9258(18)70668-6 |
0.24 |
|
| 1956 |
Edelhoch H. The effect of urea analogues and metals on the rate of pepsin denaturation. Biochimica Et Biophysica Acta. 22: 401-402. PMID 13382865 DOI: 10.1016/0006-3002(56)90173-1 |
0.322 |
|
| 1956 |
COLEMAN J, EDELHOCH H. Macromolecular interactions: proteins and nucleic acids Archives of Biochemistry and Biophysics. 63: 382-393. PMID 13355463 DOI: 10.1016/0003-9861(56)90053-4 |
0.513 |
|
| 1956 |
Edelhoch H. THE MECHANISM OF PEPSIN DENATURATION1 Journal of the American Chemical Society. 78: 2644-2645. DOI: 10.1021/JA01592A087 |
0.208 |
|
| 1956 |
Edelhoch H, Coleman J. THE KINETICS OF THE ENZYMATIC HYDROLYSIS OF RIBONUCLEIC ACID Journal of Biological Chemistry. 219: 351-363. DOI: 10.1016/s0021-9258(18)65800-4 |
0.248 |
|
| 1954 |
Edelhoch H, Taylor HS. The Adsorption of Gases on Calcium Fluoride The Journal of Physical Chemistry. 58: 344-350. DOI: 10.1021/J150514A014 |
0.188 |
|
| 1953 |
Hartman RS, Bateman JB, Edelhoch HE. Divergent Electrophoretic Properties of Dissolved and Adsorbed Trypsin Journal of the American Chemical Society. 75: 5748-5749. DOI: 10.1021/JA01118A517 |
0.286 |
|
| 1953 |
Edelhoch H, Katchalski E, Maybury RH, Hughes WL, Edsall JT. Dimerization of serum mercaptalbumin in presence of mercurials. I. Kinetic and equilibrium studies with mercuric salts Journal of the American Chemical Society. 75: 5058-5072. DOI: 10.1021/Ja01116A050 |
0.638 |
|
| 1952 |
Edelhoch H, Hayaishi O, Teply L. THE PREPARATION AND PROPERTIES OF A SOLUBLE DIPHOSPHOPYRIDINE NUCLEOTIDE CYTOCHROME c REDUCTASE Journal of Biological Chemistry. 197: 97-104. DOI: 10.1016/s0021-9258(18)55657-x |
0.248 |
|
| 1950 |
Edsall JT, Edelhoch H, Lontie R, Morrison PR. Light scattering in solutions of serum albumin: Effects of charge and ionic strength Journal of the American Chemical Society. 72: 4641-4656. DOI: 10.1021/Ja01166A085 |
0.619 |
|
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