| Year |
Citation |
Score |
| 1992 |
Jois DS, Easwaran KR, Bednarek M, Blout ER. Conformational and ion binding properties of a cyclic octapeptide, cyclo (Ala-Leu-Pro-Gly)2. Biopolymers. 32: 993-1001. PMID 1420982 DOI: 10.1002/Bip.360320810 |
0.431 |
|
| 1990 |
Di Blasio B, Benedetti E, Pavone V, Pedone C, Saviano M, Zanotti G, Blout ER. Bicyclic peptides: solid state conformation of cyclo(Glu-Leu- Pro-Gly-Lys-Leu-Pro-Gly)cyclo(1gamma-5epsilon)Gly. Biopolymers. 30: 509-16. PMID 2265225 DOI: 10.1002/Bip.360300504 |
0.367 |
|
| 1988 |
Zanotti GC, Campbell BE, Easwaran KR, Blout ER. Bicyclic peptides. VI. Synthesis, conformation, and ion-binding of two bicyclic nonapeptides. International Journal of Peptide and Protein Research. 32: 527-35. PMID 3246477 DOI: 10.1111/J.1399-3011.1988.Tb01384.X |
0.396 |
|
| 1986 |
Campbell BE, Easwaran KR, Zanotti GC, Staples MA, Fossel ET, Blout ER. Bicyclic peptides. IV. Conformation and ion binding of cyclo(Glu1-Leu2-Pro3-Gly4-Lys5-Leu6-Pro7-Gly8)-cyclo (1 gamma----5 epsilon)Gly9. Biopolymers. 25: S47-60. PMID 3779029 |
0.306 |
|
| 1986 |
Campbell BE, Easwaran KR, Zanotti GC, Staples MA, Fossel ET, Blout ER. Bicyclic peptides. IV. Conformation and ion binding of cyclo(Glu1-Leu2-Pro3-Gly4-Lys5-Leu6-Pro7-Gly8)-cyclo (1 gamma----5 epsilon)Gly9. Biopolymers. 25: S47-60. PMID 3779029 |
0.306 |
|
| 1985 |
Ga?at A, Yang CC, Blout ER. Circular dichroism study of the unfolding-refolding of a cardiotoxin from Taiwan cobra (Naja naja atra) venom. Biochemistry. 24: 5678-85. PMID 4074722 DOI: 10.1021/Bi00341A059 |
0.304 |
|
| 1985 |
Weinstein S, Durkin JT, Veatch WR, Blout ER. Conformation of the gramicidin A channel in phospholipid vesicles: a fluorine-19 nuclear magnetic resonance study. Biochemistry. 24: 4374-82. PMID 2413886 DOI: 10.1021/Bi00337A019 |
0.747 |
|
| 1984 |
Degelaen JP, Pham P, Blout ER. Cyclic peptides. 0. Synthesis and a structural study of an ion-binding cyclic peptide analog of valinomycin, cyclo(L-Ala-Gly-D-Phe-L-Pro)3 Journal of the American Chemical Society. 106: 4882-4890. DOI: 10.1021/Ja00329A042 |
0.42 |
|
| 1984 |
DEGELAEN JP, PHAM P, BLOUT ER. ChemInform Abstract: CYCLIC PEPTIDES. 0. SYNTHESIS AND A STRUCTURAL STUDY OF AN ION-BINDING CYCLIC C PEPTIDE ANALOG OF VALINOMYCIN, CYCLO(L-ALA-GLY-D-PHE-L-PRO)3 Chemischer Informationsdienst. 15. DOI: 10.1002/CHIN.198449334 |
0.322 |
|
| 1983 |
Kosen PA, Creighton TE, Blout ER. Circular dichroism spectroscopy of the intermediates that precede the rate-limiting step of the refolding pathway of bovine pancreatic trypsin inhibitor. Relationship of conformation and the refolding pathway. Biochemistry. 22: 2433-40. PMID 6860640 DOI: 10.1021/Bi00279A020 |
0.349 |
|
| 1982 |
Wallace BA, Veatch WR, Blout ER. The effects of lipid environment, ion-binding and chemical modifications on the structure of the gramicidin transmembrane channel. Biophysical Journal. 37: 197-9. PMID 19431476 |
0.696 |
|
| 1982 |
Schultz RM, Huff JP, Anagnostaras P, Olsher U, Blout ER. Synthesis and conformational properties of a synthetic cyclic peptide for the active site of alpha-chymotrypsin. International Journal of Peptide and Protein Research. 19: 454-69. PMID 7118415 DOI: 10.1111/J.1399-3011.1982.Tb02630.X |
0.381 |
|
| 1982 |
Tolle JC, Staples MA, Blout ER. Synthesis of a new type of cyclic peptide: A bicyclic nonapeptide Journal of the American Chemical Society. 104: 6883-6884. DOI: 10.1021/Ja00388A114 |
0.358 |
|
| 1981 |
Gierasch LM, Deber CM, Madison V, Niu CH, Blout ER. Conformations of (X-L-Pro-Y)2 cyclic hexapeptides. Preferred beta-turn conformers and implications for beta turns in proteins. Biochemistry. 20: 4730-8. PMID 7295645 DOI: 10.1021/Bi00519A032 |
0.632 |
|
| 1981 |
Wallace BA, Veatch WR, Blout ER. Conformation of gramicidin A in phospholipid vesicles: circular dichroism studies of effects of ion binding, chemical modification, and lipid structure. Biochemistry. 20: 5754-60. PMID 6170328 DOI: 10.1021/Bi00523A018 |
0.726 |
|
| 1981 |
Blout ER. Cyclic peptides: Past, present, and future Biopolymers. 20: 1901-1912. DOI: 10.1002/Bip.1981.360200913 |
0.361 |
|
| 1979 |
Easwaran KR, Pease LG, Blout ER. Conformations of an ion-binding cyclic peptide analogue of valinomycin, cyclo(L-Val-Gly-Gly-L-Pro)3. Biochemistry. 18: 61-7. PMID 420778 DOI: 10.1021/Bi00568A010 |
0.437 |
|
| 1979 |
Wallace BA, Blout ER. Conformation of an oligopeptide in phospholipid vesicles. Proceedings of the National Academy of Sciences of the United States of America. 76: 1775-9. PMID 287016 |
0.383 |
|
| 1979 |
Weinstein S, Wallace BA, Blout ER, Morrow JS, Veatch W. Conformation of gramicidin A channel in phospholipid vesicles: a 13C and 19F nuclear magnetic resonance study. Proceedings of the National Academy of Sciences of the United States of America. 76: 4230-4. PMID 92025 DOI: 10.1073/Pnas.76.9.4230 |
0.739 |
|
| 1978 |
Dreyfuss G, Schwartz KJ, Blout ER. Compartmentalization of cyclic AMP-dependent protein kinases in human erythrocytes. Proceedings of the National Academy of Sciences of the United States of America. 75: 5926-30. PMID 216002 DOI: 10.1073/Pnas.75.12.5926 |
0.383 |
|
| 1978 |
Dreyfuss G, Schwartz K, Blout ER, Barrio JR, Liu FT, Leonard NJ. Fluorescent photoaffinity labeling: adenosine 3',5'-cyclic monophosphate receptor sites. Proceedings of the National Academy of Sciences of the United States of America. 75: 1199-203. PMID 206888 DOI: 10.1073/Pnas.75.3.1199 |
0.539 |
|
| 1978 |
Madison V, Deber C, Blout E. Additions and Corrections - Cyclic Peptides. 17. Metal and Amino Acid Complexes of cyclo(Pro-Gly)4and Analogues Studies by Nuclear Magnetic Resonance and Circular Dichroism Journal of the American Chemical Society. 100: 1326-1326. DOI: 10.1021/Ja00472A601 |
0.6 |
|
| 1978 |
Niu C, Madison V, Pease LG, Blout ER. Cyclic peptides. XXII. Cation binding by a cyclic hexapeptide: Cyclo(D-Ala-Pro-Gly)2 Biopolymers. 17: 2747-2751. DOI: 10.1002/Bip.1978.360171120 |
0.391 |
|
| 1978 |
Meraldi JP, Blout ER, Boni R, Verdini AS. Solution conformations of some azetidine cyclic peptides Biopolymers. 17: 2401-2413. DOI: 10.1002/Bip.1978.360171009 |
0.384 |
|
| 1978 |
Boni R, Verdini AS, Deber CM, Blout ER. Synthesis and circular dichroism characterization of L-azetidine-2-carboxylic acid cyclic peptides Biopolymers. 17: 2385-2399. DOI: 10.1002/Bip.1978.360171008 |
0.601 |
|
| 1978 |
Niu CH, Pease LG, Blout ER. Cyclic peptides. XVIII. 13C spin-lattice relaxation times of (X-pro-Y)2 cyclic hexapeptides Biopolymers. 17: 115-123. DOI: 10.1002/Bip.1978.360170109 |
0.36 |
|
| 1977 |
Madison V, Deber CM, Blout ER. Cyclic peptides. 17. Metal and amino acid complexes of cyclo(pro-gly)4 and analogues studied by nuclear magnetic resonance and circular dichroism. Journal of the American Chemical Society. 99: 4788-98. PMID 874230 DOI: 10.1002/Chin.197741092 |
0.556 |
|
| 1977 |
Madison V, Deber CM, Blout ER. Cyclic peptides. 17. Metal and amino acid complexes of cyclo(pro-gly)4 and analogues studied by nuclear magnetic resonance and circular dichroism. Journal of the American Chemical Society. 99: 4788-98. PMID 874230 DOI: 10.1002/Chin.197741092 |
0.556 |
|
| 1977 |
Bartman B, Deber CM, Blout ER. 13C NMR relaxation studies of complexes between cyclo(L-Pro-Gly)3 and amino acids. Conformational aspects of stepwise binding. Journal of the American Chemical Society. 99: 1028-33. PMID 833392 |
0.534 |
|
| 1977 |
BARTMAN B, DEBER CM, BLOUT ER. ChemInform Abstract: CYCLIC PEPTIDES. 16. CARBON-13 NMR RELAXATION STUDIES OF COMPLEXES BETWEEN CYCLO(L-PRO-GLY)3 AND AMINO ACIDS. CONFORMATIONAL ASPECTS OF STEPWISE BINDING Chemischer Informationsdienst. 8: no-no. DOI: 10.1002/chin.197718085 |
0.574 |
|
| 1976 |
Young PE, Madison V, Blout ER. Cyclic peptides. 15. Lanthanide-assisted 13C and 1H NMR analysis of preferred side-chain rotamers in proline-containing cyclic dipeptides. Journal of the American Chemical Society. 98: 5365-71. PMID 956561 DOI: 10.1021/Ja00433A051 |
0.418 |
|
| 1976 |
Madison V, Young PE, Blout ER. Cyclic peptides. 14. Conformational energy and circular dichroism of proline-containing cyclic dipeptides. Journal of the American Chemical Society. 98: 5358-64. PMID 956560 DOI: 10.1002/Chin.197646074 |
0.419 |
|
| 1976 |
Veatch WR, Blout ER. Preparation and properties of O-dansyltyrosine gramicidin C. Biochemistry. 15: 3026-30. PMID 60127 |
0.716 |
|
| 1976 |
Deber CM, Madison V, Blout ER. Why cyclic peptides? Complementary approaches to conformations Accounts of Chemical Research. 9: 106-113. DOI: 10.1021/Ar50099A005 |
0.604 |
|
| 1976 |
Eisenman G, Deber C, Blout ER. Cyclic octapeptides are selective carriers of cations across lipid bilayers Biophysical Journal. 16: 81A. |
0.443 |
|
| 1975 |
Fossel ET, Easwaran KR, Blout ER. A 13C spin-lattice relaxation study of dipeptides containing glycine and proline: mobility of the cyclic proline side chain. Biopolymers. 14: 927-35. PMID 1156651 DOI: 10.1002/Bip.1975.360140504 |
0.348 |
|
| 1975 |
DEBER CM, BLOUT ER. ChemInform Abstract: CYCLIC PEPTIDES PART 7, THE SYNTHESIS AND CHARACTERIZATION OF CYCLIC PEPTIDES WITH REPEATING PRO-GLY SEQUENCES Chemischer Informationsdienst. 6: no-no. DOI: 10.1002/Chin.197509434 |
0.587 |
|
| 1975 |
DEBER CM, BLOUT ER. ChemInform Abstract: CYCLIC PEPTIDES PART 10, AMINO ACID-CYCLIC PEPTIDE COMPLEXES Chemischer Informationsdienst. 6: no-no. DOI: 10.1002/Chin.197506433 |
0.607 |
|
| 1974 |
Dober CM, Fossel ET, Blout ER. Cyclic peptides. 8. 13C and 1H nuclear magnetic resonance evidence for slow cis'-trans' rotation in a cyclic tetrapeptide. Journal of the American Chemical Society. 96: 4015-7. PMID 4851238 DOI: 10.1021/Ja00819A051 |
0.304 |
|
| 1974 |
Dober CM, Fossel ET, Blout ER. Cyclic peptides. 8. 13C and 1H nuclear magnetic resonance evidence for slow cis'-trans' rotation in a cyclic tetrapeptide. Journal of the American Chemical Society. 96: 4015-7. PMID 4851238 DOI: 10.1021/Ja00819A051 |
0.304 |
|
| 1974 |
Deber CM, Blout ER. Letter: Amino acid-cyclic peptide complexes. Journal of the American Chemical Society. 96: 7566-8. PMID 4427067 DOI: 10.1021/Ja00831A037 |
0.57 |
|
| 1974 |
Madison V, Atreyi M, Deber CM, Blout ER. Cyclic peptides. IX. Conformations of a synthetic ion-binding cyclic peptide, cyclo-(pro-gly)3, from circular dichroism and 1H and 13C nuclear magnetic resonance. Journal of the American Chemical Society. 96: 6725-34. PMID 4412689 DOI: 10.1021/Ja00828A031 |
0.639 |
|
| 1974 |
Fossel ET, Veatch WR, Ovchinnikov UA, Blout ER. A 13C nuclear magnetic resonance study of gramicidin A in monomer and dimer forms. Biochemistry. 13: 5264-75. PMID 4139973 DOI: 10.1021/bi00723a003 |
0.712 |
|
| 1974 |
Veatch WR, Blout ER. The aggregation of gramicidin A in solution. Biochemistry. 13: 5257-64. PMID 4139972 DOI: 10.1021/Bi00723A002 |
0.691 |
|
| 1974 |
Veatch WR, Fossel ET, Blout ER. The conformation of gramicidin A. Biochemistry. 13: 5249-56. PMID 4139971 DOI: 10.1021/Bi00723A001 |
0.731 |
|
| 1974 |
Deber CM, Blout ER. Cyclic Peptides VII. The Synthesis and Characterization of Cyclic Peptides with Repeating Pro-Gly Sequences Israel Journal of Chemistry. 12: 15-29. DOI: 10.1002/Ijch.197400004 |
0.602 |
|
| 1974 |
MADISON V, ATREYI M, DEBER CM, BLOUT ER. ChemInform Abstract: CYCLIC PEPTIDES PART 9, CONFORMATIONS OF A SYNTHETIC ION-BINDING CYCLIC PEPTIDE, CYCLO-(PRO-GLY)3, FROM CIRCULAR DICHROISM AND (1)H AND (13)C NUCLEAR MAGNETIC RESONANCE Chemischer Informationsdienst. 5. DOI: 10.1002/Chin.197452453 |
0.64 |
|
| 1974 |
Deber CM, Fossel ET, Blout ER. Cyclic Peptides Part 8, (13)C And (1)H Nuclear Magnetic Resonance Evidence For Slow Cis′-Trans′ Rotation In A Cyclic Tetrapeptide Cheminform. 5. DOI: 10.1002/Chin.197433103 |
0.416 |
|
| 1973 |
Thompson RC, Blout ER. Dependence of the kinetic parameters for elastase-catalyzed amide hydrolysis on the length of peptide substrates. Biochemistry. 12: 57-65. PMID 4734226 DOI: 10.1021/Bi00725A011 |
0.351 |
|
| 1973 |
Thompson RC, Blout ER. Restrictions on the binding of proline-containing peptides to elastase. Biochemistry. 12: 51-7. PMID 4734225 DOI: 10.1021/Bi00725A010 |
0.395 |
|
| 1973 |
Thompson RC, Blout ER. Peptide chloromethyl ketones as irreversible inhibitors of elastase. Biochemistry. 12: 44-7. PMID 4734223 DOI: 10.1021/Bi00725A008 |
0.373 |
|
| 1973 |
Young PE, Madison V, Blout ER. Cyclic peptides. VI. Europium-assisted nuclear magnetic resonance study of the solution conformations of cyclo(L-Pro-L-Pro) and cyclo(L-Pro-D-Pro). Journal of the American Chemical Society. 95: 6142-4. PMID 4733838 DOI: 10.1021/Ja00799A065 |
0.408 |
|
| 1973 |
Pease LG, Deber CM, Blout ER. Cyclic peptides. V. 1 H and 13 C nuclear magnetic resonance determination of the preferred beta conformation for proline-containing cyclic hexapeptides. Journal of the American Chemical Society. 95: 258-60. PMID 4682895 DOI: 10.1021/Ja00782A056 |
0.614 |
|
| 1973 |
Young PE, Madison V, Blout ER. Cyclic Peptides Part 6, Europium-Assisted Nuclear Magnetic Resonance Study Of The Solution Conformations Of Cyclo(L-Pro-L-Pro) And Cyclo(L-Pro-D-Pro) Cheminform. 4. DOI: 10.1002/Chin.197345110 |
0.407 |
|
| 1973 |
PEASE LG, DEBER CM, BLOUT ER. ChemInform Abstract: CYCLISCHE PEPTIDE 5. MITT. (1)H- UND (13)C-NMR-BESTIMMUNG DER BEVORZUGTEN BETA-KONFORM. FUER PROLIN ENTHALTENDE CYCLISCHE HEXAPEPTIDE Chemischer Informationsdienst. 4. DOI: 10.1002/Chin.197311088 |
0.582 |
|
| 1972 |
Torchia DA, Wong SC, Deber CM, Blout ER. Cyclic peptides. 3. Solution conformations of cyclo(serylprolylglycylserylprolylglycyl) from nuclear magnetic resonance. Journal of the American Chemical Society. 94: 616-20. PMID 5060992 DOI: 10.1021/Ja00757A049 |
0.625 |
|
| 1972 |
Torchia DA, Di Corato A, Wong SC, Deber CM, Blout ER. Cyclic peptides. II. Solution conformations of cyclo(ProlyLserylglycylprolylserylglycyl) from nuclear magnetic resonance. Journal of the American Chemical Society. 94: 609-15. PMID 5060991 DOI: 10.1021/Ja00757A048 |
0.62 |
|
| 1972 |
Deber CM, Torchia DA, Wong SC, Blout ER. Conformational interconversions of the cyclic hexapeptide cyclo(Pro-Gly) 3 . Proceedings of the National Academy of Sciences of the United States of America. 69: 1825-9. PMID 4505660 DOI: 10.1073/Pnas.69.7.1825 |
0.639 |
|
| 1972 |
TORCHIA DA, DI CORATO A, WONG SCK, DEBER CM, BLOUT ER. ChemInform Abstract: CYCLISCHE PEPTIDE 2. UND 3. MITT. ERMITTLUNG DER KONFORM. VON CYCLO-(PYROLYLSERYLGLYCYLPROLYLSERYLGLYCYL) UND VON CYCLO-(SERYLPROLYLGLYCYLSERYLPROLYLGLYCYL) IN LOESUNG DURCH KERNMAGNETISCHE RESONANZ Chemischer Informationsdienst. 3. DOI: 10.1002/Chin.197213082 |
0.592 |
|
| 1971 |
Parrish JR, Blout ER. Spectroscopic studies of random chain and -helical polypeptides in hexafluoroisopropanol. Biopolymers. 10: 1491-512. PMID 5126122 DOI: 10.1002/Bip.360100906 |
0.355 |
|
| 1971 |
Deber CM, Torchia DA, Blout ER. Cyclic peptides. I. Cyclo(tri-l-prolyl) and derivatives. Synthesis and molecular conformation from nuclear magnetic resonance. Journal of the American Chemical Society. 93: 4893-7. PMID 5118215 DOI: 10.1021/Ja00748A038 |
0.633 |
|
| 1971 |
Ceber C, Bovey F, Carvey J, Blout E. Additions and Corrections - Nuclear Magnetic Resonance Evidence for cis-Peptide Bonds in Proline Oligomers Journal of the American Chemical Society. 93: 3310-3310. DOI: 10.1021/JA00742A602 |
0.3 |
|
| 1971 |
DEBER CM, TORCHIA DA, BLOUT ER. ChemInform Abstract: CYCLISCHE PEPTIDE 1. MITT. CYCLO(TRI-L-PROLYL) UND DERIVATE, SYNTH. UND MOLEKUELKONFORM. MITTELS KERNMAGNETISCHER RESONANZ Chemischer Informationsdienst. Organische Chemie. 2: no-no. DOI: 10.1002/Chin.197149362 |
0.594 |
|
| 1971 |
DEBER CM, BOVEY FA, CARVER JP, BLOUT ER. ChemInform Abstract: NMR-NACHWEIS VON CIS-PEPTIDBINDUNGEN IN DIMEREN BIS HEXAMEREN PROLIN-OLIGOMEREN Chemischer Informationsdienst. Organische Chemie. 2: no-no. DOI: 10.1002/chin.197101159 |
0.629 |
|
| 1970 |
Deber CM, Bovey FA, Carver JP, Blout ER. Nuclear magnetic resonance evidence for cis-peptide bonds in proline oligomers. Journal of the American Chemical Society. 92: 6191-8. PMID 5505620 DOI: 10.1021/ja00724a016 |
0.688 |
|
| 1969 |
Brown FR, Carver JP, Blout ER. Low temperature circular dichroism of poly (glycyl-L-prolyl-L-alanine). Journal of Molecular Biology. 39: 307-13. PMID 5391435 |
0.502 |
|
| 1966 |
Carver JP, Shechter E, Blout ER. Analysis of the Optical Rotatory Dispersion of Polypeptides and Proteins. V. A Comparison of Methods1 Journal of the American Chemical Society. 88: 2562-2573. DOI: 10.1021/ja00963a035 |
0.473 |
|
| 1966 |
Carver JP, Shechter E, Blout ER. Analysis of the Optical Rotatory Dispersion of Polypeptides and Proteins. IV. A Digital Computer Analysis for the Region 190-600 mμ1,2 Journal of the American Chemical Society. 88: 2550-2561. DOI: 10.1021/ja00963a034 |
0.473 |
|
| 1964 |
SHECHTER E, CARVER JP, BLOUT ER. AN ANALYSIS OF THE OPTICAL ROTATORY DISPERSION OF POLYPEPTIDES AND PROTEINS, 3. Proceedings of the National Academy of Sciences of the United States of America. 51: 1029-36. PMID 14215623 |
0.475 |
|
| 1963 |
Blout ER, Carver JP, Gross J. Intrinsic Cotton Effects In Collagen And Poly-L-Proline Journal of the American Chemical Society. 85: 644-646. DOI: 10.1021/ja00888a041 |
0.503 |
|
| 1961 |
Simmons NS, Cohen C, Szent-Gyorgyi AG, Wetlaufer DB, Blout ER. A Conformation-dependent Cotton Effect in α-Helical Polypeptides and Proteins1,2 Journal of the American Chemical Society. 83: 4766-4769. DOI: 10.1021/JA01484A017 |
0.62 |
|
| 1950 |
Leonard NJ, Blout ER. The Ultraviolet Absorption Spectra of Hindered Benzils Journal of the American Chemical Society. 72: 484-487. DOI: 10.1021/Ja01157A126 |
0.36 |
|
| 1949 |
Leonard NJ, Rapala RT, Herzog HL, Blout ER. The Ultraviolet Absorption Spectra of Alkoxy- and Hydroxybenzils Journal of the American Chemical Society. 71: 2997-3002. DOI: 10.1021/Ja01177A014 |
0.359 |
|
| 1943 |
Blout ER, Fried J, Elderfield RC. Studies on lactones related to the cardiac aglycones. XII. The condensation of ethyl oxalate with ethyl γ-cyclohexylcrotonate and a method for predicting the products from such condensations Journal of Organic Chemistry. 8: 37-42. DOI: 10.1021/Jo01189A007 |
0.552 |
|
| 1941 |
Paist WD, Blout ER, Uhle FC, Elderfield RC. Studies on lactones related to the cardiac aglycones. III. The properties of β-substituted Δα,β-butenolides and a suggested revision of the structure of the side chain of the digitalis-strophanthus aglycones Journal of Organic Chemistry. 6: 273-288. DOI: 10.1021/Jo01202A012 |
0.465 |
|
| Low-probability matches (unlikely to be authored by this person) |
| 1972 |
Parrish JR, Blout ER. The conformation of poly-L-alanine in hexafluoroisopropanol. Biopolymers. 11: 1001-20. PMID 5035096 DOI: 10.1002/Bip.1972.360110506 |
0.295 |
|
| 1972 |
Parrish JR, Blout ER. The conformation of poly-L-alanine in hexafluoroisopropanol. Biopolymers. 11: 1001-20. PMID 5035096 DOI: 10.1002/Bip.1972.360110506 |
0.295 |
|
| 1973 |
Thompson RC, Blout ER. Elastase-catalyzed amide hydrolysis of tri- and tetrapeptide amides. Biochemistry. 12: 66-71. PMID 4734227 DOI: 10.1021/Bi00725A012 |
0.293 |
|
| 1980 |
Degelaen J, Pham P, Blout E. Conformational and dynamic aspects of an ion- binding cyclic peptide analogue of valinomycine, cyclo(LAla-Gly-DPhe-LPro)3 Inorganica Chimica Acta. 40: X76. DOI: 10.1016/S0020-1693(00)92148-0 |
0.29 |
|
| 2003 |
Leonard NJ, Blout E. Josef Fried. July 21, 1914-August 17, 2001. Biographical Memoirs. National Academy of Sciences (U.S.). 82: 143-56. PMID 15046027 |
0.289 |
|
| 1987 |
Bednarek MA, Campbell BE, Easwaran KR, Blout ER. Bicyclic peptides. V. Conformation and ion binding of an undeca and a dodeca bicyclic peptide. Biopolymers. 26: S11-23. PMID 3619997 DOI: 10.1002/Bip.360260006 |
0.289 |
|
| 1987 |
Bednarek MA, Campbell BE, Easwaran KR, Blout ER. Bicyclic peptides. V. Conformation and ion binding of an undeca and a dodeca bicyclic peptide. Biopolymers. 26: S11-23. PMID 3619997 DOI: 10.1002/Bip.360260006 |
0.289 |
|
| 1976 |
YOUNG PE, MADISON V, BLOUT ER. ChemInform Abstract: CYCLIC PEPTIDES. 15. LANTHANIDE-ASSISTED CARBON-13 AND PROTON NMR ANALYSIS OF F PREFERRED SIDE-CHAIN ROTAMERS IN PROLINE-CONTAINING CYCLIC DIPEPTIDES Chemischer Informationsdienst. 7: no-no. DOI: 10.1002/chin.197646075 |
0.279 |
|
| 1977 |
Baron D, Pease LG, Blout ER. Cyclic peptides. 19. Cation binding of a cyclic dodecapeptide cyclo-(L-Val-Gly-Gly-L-Pro)3 in an aprotic medium. Journal of the American Chemical Society. 99: 8299-8366. PMID 925266 DOI: 10.1002/Chin.197812355 |
0.277 |
|
| 1977 |
Baron D, Pease LG, Blout ER. Cyclic peptides. 19. Cation binding of a cyclic dodecapeptide cyclo-(L-Val-Gly-Gly-L-Pro)3 in an aprotic medium. Journal of the American Chemical Society. 99: 8299-8366. PMID 925266 DOI: 10.1002/Chin.197812355 |
0.277 |
|
| 1984 |
Degelaen JP, Pham P, Blout ER. Synthesis and a structural study of an ion-binding cyclic peptide analogue of valinomycin, cyclo( L-Ala-Gly-D-Phe-L-Pro)3 Journal of the American Chemical Society. 106: 4882-4890. |
0.27 |
|
| 1968 |
Morita K, Simons ER, Blout ER. Polypeptides. LVI. Effect of lithium bromide and of temperature on the conformation of a copolymer of glutamic acid and lysine. Biopolymers. 6: 181-8. PMID 5644148 DOI: 10.1002/Bip.1968.360060203 |
0.26 |
|
| 1968 |
Laufer DA, Chapman TM, Marlborough DI, Vaidya VM, Blout ER. A reagent for peptide synthesis. Copoly(ethylene-N-hydroxymaleimide). Journal of the American Chemical Society. 90: 2696-8. PMID 5646894 |
0.237 |
|
| 1968 |
Laufer DA, Chapman TM, Marlborough DI, Vaidya VM, Blout ER. A reagent for peptide synthesis. Copoly(ethylene-N-hydroxymaleimide). Journal of the American Chemical Society. 90: 2696-8. PMID 5646894 |
0.237 |
|
| 1978 |
Rosenthal SL, Parola AH, Blout ER, Davidson RL. Membrane alterations associated with "transformation" by BUdR in BUdR-dependent cells. Fluorescence Polarization studies with a lipid probe. Experimental Cell Research. 112: 419-29. PMID 631226 DOI: 10.1016/0014-4827(78)90224-0 |
0.228 |
|
| 1979 |
Parola AH, Robbins PW, Blout ER. Membrane dynamic alterations associated with viral transformation and reversion. Decay of fluorescence emission and anisotropy studies of 3T3 cells. Experimental Cell Research. 118: 205-14. PMID 215422 DOI: 10.1016/0014-4827(79)90598-6 |
0.228 |
|
| 1965 |
Cheung HT, Blout ER. The hydrazide as a carboxylie-protecting group in peptide synthesis. The Journal of Organic Chemistry. 30: 315-6. PMID 5870713 |
0.227 |
|
| 1975 |
Fuchs P, Parola A, Robbins PW, Blout ER. Fluorescence polarization and viscosities of membrane lipids of 3T3 cells. Proceedings of the National Academy of Sciences of the United States of America. 72: 3351-4. PMID 1059120 DOI: 10.1073/Pnas.72.9.3351 |
0.225 |
|
| 1981 |
Kosen PA, Creighton TE, Blout ER. Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor. Biochemistry. 20: 5744-54. PMID 7295701 DOI: 10.1021/Bi00523A017 |
0.223 |
|
| 1981 |
Kosen PA, Creighton TE, Blout ER. Circular dichroism spectroscopy of bovine pancreatic trypsin inhibitor and five altered conformational states. Relationship of conformation and the refolding pathway of the trypsin inhibitor. Biochemistry. 20: 5744-54. PMID 7295701 DOI: 10.1021/Bi00523A017 |
0.223 |
|
| 1972 |
Visser L, Blout ER. The use of p-nitrophenyl N-tert-butyloxycarbonyl-L-alaninate as substrate for elastase. Biochimica Et Biophysica Acta. 268: 257-60. PMID 5062949 DOI: 10.1016/0005-2744(72)90223-9 |
0.221 |
|
| 1964 |
BLOUT ER. DISCUSSION: THE ROLE OF SYNTHETIC PEPTIDES IN ELUCIDATION OF BIOLOGICAL PROBLEMS. Metabolism: Clinical and Experimental. 13: SUPPL:1290-6. PMID 14228774 |
0.218 |
|
| 1971 |
Visser L, Blout ER. Elastase. II. Optical properties and the effects of sodium dodecyl sulfate. Biochemistry. 10: 743-52. PMID 5544664 DOI: 10.1021/Bi00781A004 |
0.212 |
|
| 1981 |
Galat A, Creighton TE, Lord RC, Blout ER. Circular dichroism, Raman spectroscopy, and gel filtration of trapped folding intermediates of ribonuclease. Biochemistry. 20: 594-601. PMID 7213596 DOI: 10.1021/Bi00506A023 |
0.21 |
|
| 1981 |
Galat A, Creighton TE, Lord RC, Blout ER. Circular dichroism, Raman spectroscopy, and gel filtration of trapped folding intermediates of ribonuclease. Biochemistry. 20: 594-601. PMID 7213596 DOI: 10.1021/Bi00506A023 |
0.21 |
|
| 1963 |
Blout ER, Shechter E. A new technique for producing oriented synthetic polypeptides: Some initial results Biopolymers. 1: 565-568. DOI: 10.1002/Bip.360010608 |
0.203 |
|
| 1976 |
Blout ER. The neurobiology of lithium. III. Physicial chemistry and transport. Ion complexing with natural and synthetic peptides. Neurosciences Research Program Bulletin. 14: 137-9. PMID 1272521 |
0.201 |
|
| 1970 |
Quinn RS, Blout ER. Spectrofluorometric assay for elastolytic enzymes. Biochemical and Biophysical Research Communications. 40: 328-33. PMID 5529031 DOI: 10.1016/0006-291X(70)91013-2 |
0.201 |
|
| 1961 |
Miyazawa T, Blout ER. The Infrared Spectra of Polypeptides in Various Conformations: Amide I and II Bands1 Journal of the American Chemical Society. 83: 712-719. DOI: 10.1021/JA01464A042 |
0.199 |
|
| 1970 |
Thompson RC, Blout ER. Evidence for an extended active center in elastase. Proceedings of the National Academy of Sciences of the United States of America. 67: 1734-40. PMID 5275373 |
0.188 |
|
| 1970 |
Thompson RC, Blout ER. Evidence for an extended active center in elastase. Proceedings of the National Academy of Sciences of the United States of America. 67: 1734-40. PMID 5275373 |
0.188 |
|
| 1960 |
Blout ER, de Lozé C, Bloom SM, Fasman GD. THE DEPENDENCE OF THE CONFORMATIONS OF SYNTHETIC POLYPEPTIDES ON AMINO ACID COMPOSITION1,2 Journal of the American Chemical Society. 82: 3787-3789. DOI: 10.1021/Ja01499A080 |
0.188 |
|
| 1975 |
Doyle BB, Bendit EG, Blout ER. Infrared spectroscopy of collagen and collagen-like polypeptides. Biopolymers. 14: 937-57. PMID 1156652 DOI: 10.1002/Bip.1975.360140505 |
0.185 |
|
| 1975 |
Doyle BB, Bendit EG, Blout ER. Infrared spectroscopy of collagen and collagen-like polypeptides. Biopolymers. 14: 937-57. PMID 1156652 DOI: 10.1002/Bip.1975.360140505 |
0.185 |
|
| 1966 |
Oriel PJ, Blout ER. On the structure of gly-pro-gly and gly-pro-ala oligopeptides and sequential polypeptides Journal of the American Chemical Society. 88: 2041-2045. |
0.182 |
|
| 1981 |
Ga?at A, Degelaen JP, Yang CC, Blout ER. Reversed unfolding-refolding process of cobra neurotoxin. Biochemistry. 20: 7415-23. PMID 7326234 DOI: 10.1021/Bi00529A015 |
0.175 |
|
| 1981 |
Ga?at A, Degelaen JP, Yang CC, Blout ER. Reversed unfolding-refolding process of cobra neurotoxin. Biochemistry. 20: 7415-23. PMID 7326234 DOI: 10.1021/Bi00529A015 |
0.175 |
|
| 1987 |
Blout E. To honor Ephraim Katchalski-Katzir Biopolymers. 26: Siii-Siv. DOI: 10.1002/Bip.360260003 |
0.17 |
|
| 1982 |
Sugihara T, Blout ER, Wallace BA. Hydrophobic oligopeptides in solution and in phospholipid vesicles: synthetic fragments of bacteriorhodopsin. Biochemistry. 21: 3444-52. PMID 7115678 DOI: 10.1021/Bi00257A030 |
0.169 |
|
| 1982 |
Sugihara T, Blout ER, Wallace BA. Hydrophobic oligopeptides in solution and in phospholipid vesicles: synthetic fragments of bacteriorhodopsin. Biochemistry. 21: 3444-52. PMID 7115678 DOI: 10.1021/Bi00257A030 |
0.169 |
|
| 1965 |
HARRISON SC, BLOUT ER. REVERSIBLE CONFORMATIONAL CHANGES OF MYOGLOBIN AND APOMYOGLOBIN. The Journal of Biological Chemistry. 240: 299-303. PMID 14253427 |
0.166 |
|
| 1972 |
Griffin JH, Rosenbusch JP, Weber KK, Blout ER. Conformational changes in aspartate trancarbamylase. I. Studies of ligand binding and of subunit interactions by circular dichroism spectroscopy. The Journal of Biological Chemistry. 247: 6482-90. PMID 4561937 |
0.164 |
|
| 1962 |
Bloom SM, Fasman GD, de Loze C, Blout ER. The Effect of Amino Acid Composition on the Conformations of Synthetic Polypeptides, Polymers and Copolymers of L-Methionine S-Methyl-L-cysteine and L-Valine Journal of the American Chemical Society. 84: 458-463. DOI: 10.1021/Ja00862A027 |
0.161 |
|
| 1971 |
Doyle BB, Traub W, Lorenzi GP, Blout ER. Conformational investigations on the polypeptide and oligopeptides with the repeating sequence L-alanyl-L-prolylglycine. Biochemistry. 10: 3052-60. PMID 5126923 |
0.159 |
|
| 1967 |
Morita K, Simons ER, Blout ER. Polypeptides. 53. Water-soluble copolypeptides of L-glutamic acid, L-lysine, and L-alanine. Biopolymers. 5: 259-71. PMID 6040032 DOI: 10.1002/Bip.1967.360050304 |
0.157 |
|
| 1967 |
Morita K, Simons ER, Blout ER. Polypeptides. 53. Water-soluble copolypeptides of L-glutamic acid, L-lysine, and L-alanine. Biopolymers. 5: 259-71. PMID 6040032 DOI: 10.1002/Bip.1967.360050304 |
0.157 |
|
| 1956 |
Blout ER, Idelson M. POLYPEPTIDES. VI. POLY-α-L-GLUTAMIC ACID: PREPARATION AND HELIX-COIL CONVERSIONS1 Journal of the American Chemical Society. 78: 497-498. DOI: 10.1021/JA01583A069 |
0.154 |
|
| 1961 |
Fasman GD, Idelson M, Blout ER. The Synthesis and Conformation of High Molecular Weight Poly-ε-carbobenzyloxy-L-lysine and Poly-L-lysine·HCl1,2 Journal of the American Chemical Society. 83: 709-712. DOI: 10.1021/ja01464a041 |
0.154 |
|
| 1980 |
Kosen PA, Creighton TE, Blout ER. Ultraviolet difference spectroscopy of intermediates trapped in unfolding and refolding of bovine pancreatic trypsin inhibitor. Biochemistry. 19: 4936-44. PMID 7426636 |
0.152 |
|
| 1960 |
Fasman GD, Blout ER. The Synthesis and the Conformation of Poly-L-serine and Poly-O-acetyl-L-serine1,2 Journal of the American Chemical Society. 82: 2262-2267. DOI: 10.1021/ja01494a041 |
0.152 |
|
| 1956 |
Blout ER, Asadourian A. Polypeptides. V. The Infrared Spectra of Polypeptides Derived from γ-Benzyl-L-glutamate Journal of the American Chemical Society. 78: 955-961. DOI: 10.1021/JA01586A022 |
0.151 |
|
| 1952 |
Blout ER, Linsley SG. Infrared Spectra and the Structure of Glycine and Leucine Peptides1 Journal of the American Chemical Society. 74: 1946-1951. DOI: 10.1021/JA01128A023 |
0.15 |
|
| 1955 |
BLOUT ER, LENORMANT H. Changes in the infrared spectra of solutions of deoxypentose nucleic acid in relation to its structure. Biochimica Et Biophysica Acta. 17: 325-31. PMID 13239687 |
0.149 |
|
| 1954 |
BLOUT ER, LENORMANT H. Changes in the infrared spectra of solutions of deoxypentose nucleic acid. Biochimica Et Biophysica Acta. 15: 303. PMID 13208704 |
0.138 |
|
| 1973 |
Griffin JH, Rosenbusch JP, Blout ER, Weber KK. Conformational changes in aspartate transcarbamylase. II. Circular dichroism evidence for the involvement of metal ions in allosteric interactions. The Journal of Biological Chemistry. 248: 5057-62. PMID 4577763 |
0.137 |
|
| 1959 |
Morgan RS, Blout ER. Infrared Spectra and the Structure of Polyriboadenylic Acid Journal of the American Chemical Society. 81: 4625-4629. DOI: 10.1021/JA01526A044 |
0.137 |
|
| 1961 |
Blout E. Helical sense of polypeptides and proteins Tetrahedron. 13: 123-133. DOI: 10.1016/S0040-4020(01)92207-0 |
0.134 |
|
| 1968 |
Coleman DL, Blout ER. The optical activity of the disulfide bond in L-cystine and some derivatives of L-cystine. Journal of the American Chemical Society. 90: 2405-16. PMID 5642070 |
0.134 |
|
| 1968 |
Coleman DL, Blout ER. The optical activity of the disulfide bond in L-cystine and some derivatives of L-cystine. Journal of the American Chemical Society. 90: 2405-16. PMID 5642070 |
0.134 |
|
| 1970 |
Doyle BB, Traub W, Lorenzi GP, Brown FR, Blout ER. Synthesis and structural investigation of poly(L-alanyl-L-alanyl-glycine). Journal of Molecular Biology. 51: 47-59. PMID 5481279 DOI: 10.1016/0022-2836(70)90269-X |
0.132 |
|
| 1948 |
Blout ER, Fields M, Karplus R. Absorption Spectra. VI. The Infrared Spectra of Certain Compounds Containing Conjugated Double Bonds Journal of the American Chemical Society. 70: 194-198. DOI: 10.1021/JA01181A056 |
0.131 |
|
| 1976 |
Bauer CA, Thompson RC, Blout ER. The active centers of Streptomyces griseus protease 3, alpha-chymotrypsin, and elastase: enzyme-substrate interactions close to the scissile bond. Biochemistry. 15: 1296-9. PMID 814925 |
0.13 |
|
| 1962 |
BEYCHOK S, DE LOZE C, BLOUT ER. Helix contents of solutions of native and acid-denatured ferrihemoglobin and ferrimyoglobin. Journal of Molecular Biology. 4: 421-9. PMID 13868740 |
0.129 |
|
| 1972 |
Brown FR, Di Corato A, Lorenzi GP, Blout ER. Synthesis and structural studies of two collagen analogues: poly (L-prolyl-L-seryl-glycyl) and poly (L-prolyl-L-alanyl-glycyl). Journal of Molecular Biology. 63: 85-99. PMID 5016973 DOI: 10.1016/0022-2836(72)90523-2 |
0.129 |
|
| 1960 |
Karlson RH, Norland KS, Fasman GD, Blout ER. The Helical Sense of Poly-β-benzyl-L-aspartate. Synthesis and Rotatory Dispersion of Copolymers of β-Benzyl-L and D-Aspartate with γ-Benzyl-L-glutamate1 Journal of the American Chemical Society. 82: 2268-2275. DOI: 10.1021/ja01494a042 |
0.127 |
|
| 1968 |
Ramachandran GN, Doyle BB, Blout ER. Single-chain triple helical structure. Biopolymers. 6: 1771-5. PMID 5704347 DOI: 10.1002/bip.1968.360061213 |
0.127 |
|
| 1968 |
Ramachandran GN, Doyle BB, Blout ER. Single-chain triple helical structure. Biopolymers. 6: 1771-5. PMID 5704347 DOI: 10.1002/bip.1968.360061213 |
0.127 |
|
| 1966 |
Bloom SM, Dasgupta SK, Patel RP, Blout ER. The synthesis of glycyl-L-prolylglycyl and glycyl-L-prolyl-L-alanyl oligopeptides and sequential polypeptides Journal of the American Chemical Society. 88: 2035-2041. |
0.122 |
|
| 1957 |
Doty P, Wada A, Yang JT, Blout ER. Polypeptides. VIII. Molecular configurations of poly-L-glutamic acid in water-dioxane solution Journal of Polymer Science. 23: 851-861. DOI: 10.1002/Pol.1957.1202310429 |
0.122 |
|
| 1969 |
Simons ER, Schneider EG, Blout ER. Thermal effects on the circular dichroism spectra of ribonuclease A and of ribonuclease S-protein. The Journal of Biological Chemistry. 244: 4023-6. PMID 5800432 |
0.119 |
|
| 1971 |
Lorenzi GP, Doyle BB, Blout ER. Synthesis of polypeptides and oligopeptides with the repeating sequence L-alanyl-L-prolylglycine. Biochemistry. 10: 3046-51. PMID 5126922 |
0.118 |
|
| 1963 |
Norland KS, Fasman GD, Katchalski E, Blout ER. Some optical properties of poly-1-benzyl-L-histidine and poly-L-histidine Biopolymers. 1: 277-294. DOI: 10.1002/bip.360010307 |
0.117 |
|
| 1976 |
Bauer CA, Thompson RC, Blout ER. The active centers of Streptomyces griseus protease 3 and alpha-chymotrypsin: enzyme-substrate interactions remote from the scissile bond. Biochemistry. 15: 1291-5. PMID 814924 |
0.117 |
|
| 1950 |
Blout ER, Fields M. Absorption Spectra. VIII. The Infrared Spectra of Some Purines and Pyrimidines1,2 Journal of the American Chemical Society. 72: 479-484. DOI: 10.1021/JA01157A125 |
0.115 |
|
| 1963 |
Adler AJ, Fasman GD, Blout ER. Base-catalyzed Formation of Cyclic Compounds from Poly-β-benzyl-L-aspartate and Poly-γ-benzyl-L-glutamate Journal of the American Chemical Society. 85: 90-97. DOI: 10.1021/Ja00884A019 |
0.114 |
|
| 1958 |
Blout ER, Idelson M. Compositional Effects on the Configuration of Water-soluble Polypeptide Copolymers of L-Glutamic Acid and L-Lysine1 Journal of the American Chemical Society. 80: 4909-4913. DOI: 10.1021/JA01551A036 |
0.114 |
|
| 1958 |
Idelson M, Blout ER. High Molecular Weight Poly-α,L-glutamic Acid: Preparation and Optical Rotation Changes1 Journal of the American Chemical Society. 80: 4631-4634. DOI: 10.1021/JA01550A056 |
0.111 |
|
| 1959 |
Bird GR, Blout ER. The Infrared Streaming Dichroism of Some Synthetic Polypeptides1 Journal of the American Chemical Society. 81: 2499-2503. DOI: 10.1021/JA01519A052 |
0.111 |
|
| 1956 |
Blout ER, Karlson RH. Polypeptides. III. The Synthesis of High Molecular Weight Poly-γ-benzyl-L-glutamates1 Journal of the American Chemical Society. 78: 941-946. DOI: 10.1021/JA01586A020 |
0.108 |
|
| 2010 |
Blout ER, Fields M. On the Infrared Spectra of Nucleic Acids and Certain of Their Components. Science (New York, N.Y.). 107: 252. PMID 17814727 DOI: 10.1126/SCIENCE.107.2775.252 |
0.107 |
|
| 1953 |
BLOUT ER, LENORMANT H. Infrared spectroscopy of biologic materials in aqueous solutions. Journal of the Optical Society of America. 43: 1093-5. PMID 13109612 |
0.107 |
|
| 1957 |
BLOUT ER, LENORMANT H. Reversible configurational changes in poly-L-lysine hydrochloride induced by water. Nature. 179: 960-3. PMID 13430748 |
0.103 |
|
| 1954 |
BLOUT ER, ASADOURIAN A. The ultraviolet absorption spectra of desoxypentose nucleic acid. Biochimica Et Biophysica Acta. 13: 161-70. PMID 13140310 |
0.103 |
|
| 1958 |
Idelson M, Blout E. Additions and Corrections: Polypeptides. XVIII. A Kinetic Study of the Polymerization of Amino Acid N-Carboxyanhydrides Initiated by Strong Bases. Journal of the American Chemical Society. 80: 6701-6701. DOI: 10.1021/JA01557A639 |
0.102 |
|
| 1948 |
Blout ER, Fields M. Absorption Spectra. V. The Ultraviolet and Visible Spectra of Certain Polyene Aldehydes and Polyene Azines1 Journal of the American Chemical Society. 70: 189-193. DOI: 10.1021/JA01181A055 |
0.102 |
|
| 1963 |
Fasman GD, Blout ER. High molecular weight poly-L-proline: Synthesis and physical-chemical studies Biopolymers. 1: 3-14. DOI: 10.1002/bip.360010103 |
0.1 |
|
| 1946 |
Blout ER, Eager VW, Silverman DC. Absorption Spectra. III. Cyclic β-Diketones Journal of the American Chemical Society. 68: 566-571. DOI: 10.1021/JA01208A009 |
0.1 |
|
| 1956 |
Blout ER, Idelson M. POLYPEPTIDES. IX. THE KINETICS OF STRONG-BASE INITIATED POLYMERIZATIONS OF AMINO ACID-N-CARBOXYANHYDRIDES Journal of the American Chemical Society. 78: 3857-3858. DOI: 10.1021/JA01596A083 |
0.1 |
|
| 1969 |
Lorenzi GP, Blout ER, Kivirikko KI, Prockop DJ. Oligopeptides with the sequences ala-pro-gly and gly-pro-gly as substrates or inhibitors for protocollagen proline hydroxylase. The Journal of Biological Chemistry. 244: 2755-60. PMID 5769999 |
0.1 |
|
| 1969 |
Lorenzi GP, Blout ER, Kivirikko KI, Prockop DJ. Oligopeptides with the sequences ala-pro-gly and gly-pro-gly as substrates or inhibitors for protocollagen proline hydroxylase. The Journal of Biological Chemistry. 244: 2755-60. PMID 5769999 |
0.1 |
|
| 1958 |
Lenormant H, Baudras A, Blout ER. Reversible Configurational Changes in Sodium Poly-α,L-glutamate Induced by Water1 Journal of the American Chemical Society. 80: 6191-6195. DOI: 10.1021/JA01556A011 |
0.099 |
|
| 1945 |
Blout ER, Gofstein RM. The Absorption Spectra of Certain Aldazines Journal of the American Chemical Society. 67: 13-17. DOI: 10.1021/JA01217A005 |
0.097 |
|
| 1946 |
Blout ER, Eager VW, Gofstein RM. Absorption Spectra. IV. Ketazines1 Journal of the American Chemical Society. 68: 1983-1986. DOI: 10.1021/JA01214A032 |
0.097 |
|
| 1961 |
Blout ER, De Loze C, Asadourian A. The Deuterium Exchange of Water-soluble Polypeptides and Proteins as Measured by Infrared Spectroscopy Journal of the American Chemical Society. 83: 1895-1900. DOI: 10.1021/JA01469A028 |
0.097 |
|
| 1968 |
Simons ER, Blout ER. Circular dichroism of ribonuclease A, ribonuclease S, and some fragments. The Journal of Biological Chemistry. 243: 218-21. PMID 5635944 |
0.093 |
|
| 1957 |
Idelson M, Blout ER. Polypeptides. XV.1Infrared Spectroscopy and the Kinetics of the Synthesis of Polypeptides: Primary Amine Initiated Reactions Journal of the American Chemical Society. 79: 3948-3955. DOI: 10.1021/JA01572A002 |
0.091 |
|
| 1957 |
BLOUT ER. Aqueous solution infrared spectroscopy of biochemical polymers. Annals of the New York Academy of Sciences. 69: 84-93. PMID 13478993 |
0.089 |
|
| 1954 |
Doty P, Holtzer AM, Bradbury JH, Blout ER. POLYPEPTIDES. II. THE CONFIGURATION OF POLYMERS OF γ-BENZYL-L-GLUTAMATE IN SOLUTION1 Journal of the American Chemical Society. 76: 4493-4494. DOI: 10.1021/Ja01646A079 |
0.088 |
|
| 1957 |
Blout ER, Doty P, Yang JT. Polypeptides. XII. The Optical Rotation and Configurational Stability of α-Helices1 Journal of the American Chemical Society. 79: 749-750. DOI: 10.1021/Ja01560A068 |
0.088 |
|
| 1961 |
Stryer L, Blout ER. Optical rotatory dispersion of dyes bound to macromolecules. Cationic dyes: Polyglutamic acid complexes Journal of the American Chemical Society. 83: 1411-1418. DOI: 10.1021/Ja01467A036 |
0.083 |
|
| 1949 |
Blout ER, Mellors RC. Infrared Spectra of Tissues. Science (New York, N.Y.). 110: 137-8. PMID 17816857 DOI: 10.1126/science.110.2849.137 |
0.081 |
|
| 1964 |
BLOUT ER. EXTRINSIC AND INTRINSIC COTTON EFFECTS IN POLYPEPTIDES AND PROTEINS. Biopolymers Symposia. 13: 397-408. PMID 14210464 |
0.081 |
|
| 1964 |
BLOUT ER. EXTRINSIC AND INTRINSIC COTTON EFFECTS IN POLYPEPTIDES AND PROTEINS. Biopolymers Symposia. 13: 397-408. PMID 14210464 |
0.081 |
|
| 1945 |
Blout ER, Eager VW. Absorption Spectra. II. Some Aldehyde Condensation Products of Methyl Pyridines Journal of the American Chemical Society. 67: 1315-1319. DOI: 10.1021/JA01224A033 |
0.081 |
|
| 1962 |
Kulkarni RK, Blout ER. Water-Soluble Helical Polypeptides Journal of the American Chemical Society. 84: 3971-3972. DOI: 10.1021/JA00879A040 |
0.081 |
|
| 1958 |
Blout E, Karlson R. Additions and Corrections: Poly-β-benzyl Aspartates: Optical Rotation and the Sense of the Helix. Journal of the American Chemical Society. 80: 6701-6701. DOI: 10.1021/JA01557A636 |
0.079 |
|
| 1986 |
Durkin JT, Andersen OS, Blout ER, Heitz F, Koeppe RE, Trudelle Y. Structural information from functional measurements: single-channel studies on gramicidin analogues. Biophysical Journal. 49: 118-21. PMID 19431612 DOI: 10.1016/S0006-3495(86)83618-9 |
0.079 |
|
| 1986 |
Durkin JT, Andersen OS, Blout ER, Heitz F, Koeppe RE, Trudelle Y. Structural information from functional measurements: single-channel studies on gramicidin analogues. Biophysical Journal. 49: 118-21. PMID 19431612 DOI: 10.1016/S0006-3495(86)83618-9 |
0.079 |
|
| 1958 |
Idelson M, Blout ER. Polypeptides. XVIII.1A Kinetic Study of the Polymerization of Amino Acid N-Carboxyanhydrides Initiated by Strong Bases Journal of the American Chemical Society. 80: 2387-2393. DOI: 10.1021/JA01543A012 |
0.079 |
|
| 1964 |
SHECHTER E, BLOUT ER. AN ANALYSIS OF THE OPTICAL ROTATORY DISPERSION OF POLYPEPTIDES AND PROTEINS. II. Proceedings of the National Academy of Sciences of the United States of America. 51: 794-800. PMID 14172993 |
0.078 |
|
| 1950 |
UZMAN LL, BLOUT ER. Infra-red spectra of films of native and denatured pepsin. Nature. 166: 862-3. PMID 14785648 |
0.078 |
|
| 1958 |
Blout ER, Karlson RH. POLY-β-BENZYL ASPARTATES: OPTICAL ROTATION AND THE SENSE OF THE HELIX1 Journal of the American Chemical Society. 80: 1259-1260. DOI: 10.1021/JA01538A058 |
0.078 |
|
| 1972 |
Brown FR, Hopfinger AJ, Blout ER. The collagen-like triple helix to random-chain transition: experiment and theory. Journal of Molecular Biology. 63: 101-15. PMID 5016967 DOI: 10.1016/0022-2836(72)90524-4 |
0.075 |
|
| 1964 |
SHECHTER E, BLOUT ER. AN ANALYSIS OF THE OPTICAL ROTATORY DISPERSION OF POLYPEPTIDES AND PROTEINS. Proceedings of the National Academy of Sciences of the United States of America. 51: 695-702. PMID 14166777 |
0.074 |
|
| 1950 |
BLOUT ER, DOTY PM. Protein and nucleic acid conference. Science (New York, N.Y.). 112: 639-43. PMID 14787490 DOI: 10.1126/Science.112.2918.639 |
0.071 |
|
| 1966 |
Carver JP, Shechter E, Blout ER. Analysis of the optical rotatory dispersion of polypeptides and proteins. IV. A digital computer analysis for the region 190-600 mμ Journal of the American Chemical Society. 88: 2550-2561. |
0.071 |
|
| 1966 |
Carver JP, Shechter E, Blout ER. Analysis of the optical rotatory dispersion of polypeptides and proteins. V. A comparison of methods Journal of the American Chemical Society. 88: 2562-2573. |
0.069 |
|
| 1958 |
Bird GR, Parrish M, Blout ER. Apparatus for the observation of infrared streaming dichroism of polymer solutions Review of Scientific Instruments. 29: 305-309. DOI: 10.1063/1.1716182 |
0.069 |
|
| 1962 |
Blout ER, Schmier I, Simmons NS. New Cotton Effects in Polypeptides and Proteins Journal of the American Chemical Society. 84: 3193-3194. DOI: 10.1021/JA00875A038 |
0.066 |
|
| 1963 |
Fasman GD, Blout ER. Copolymers ofL-proline and sarcosine: Synthesis and physical-chemical studies Biopolymers. 1: 99-109. DOI: 10.1002/bip.360010202 |
0.066 |
|
| 1976 |
Bauer CA, Thompson RC, Blout ER. The active centers of Streptomyces griseus protease 3, α-chymotrypsin, and elastase: Enzyme-substrate interactions close to the scissile bond Biochemistry. 15: 1296-1299. |
0.065 |
|
| 1976 |
Bauer CA, Thompson RC, Blout ER. The active centers of Streptomyces griseus protease 3 and α-chymotrypsin: Enzyme-substrate interactions remote from the scissile bond Biochemistry. 15: 1291-1295. |
0.063 |
|
| 1947 |
Corley RS, Blout ER. The Reaction of β-Naphthol, β-Naphthylamine and Formaldehyde. II. 1-(2'-Naphthylaminomethyl)-2-naphthol and its Isomerization to 2'-Amino-2-hydroxy-1,1'-dinaphthylmethane Journal of the American Chemical Society. 69: 761-763. DOI: 10.1021/JA01196A008 |
0.062 |
|
| 1964 |
Cheung HT, Murthy TS, Blout ER. The synthesis of an octapeptide corresponding to a sequence around the "reactive serine" of chymotrypsin [6] Journal of the American Chemical Society. 86: 4200-4202. |
0.061 |
|
| 1959 |
Blout ER, Stryer L. ANOMALOUS OPTICAL ROTATORY DISPERSION OF DYE: POLYPEPTIDE COMPLEXES. Proceedings of the National Academy of Sciences of the United States of America. 45: 1591-3. PMID 16590549 |
0.058 |
|
| 1959 |
Blout ER, Stryer L. ANOMALOUS OPTICAL ROTATORY DISPERSION OF DYE: POLYPEPTIDE COMPLEXES. Proceedings of the National Academy of Sciences of the United States of America. 45: 1591-3. PMID 16590549 |
0.058 |
|
| 1967 |
Laufer DA, Blout ER. A new stepwise synthesis of an octapeptide corresponding to a sequence around the "reactive" serine of chymotrypsin. Journal of the American Chemical Society. 89: 1246-9. PMID 6041348 |
0.057 |
|
| 1948 |
Fields M, Blout ER. Polarographic Studies on Aliphatic Polyene Aldehydes Journal of the American Chemical Society. 70: 930-935. DOI: 10.1021/JA01183A013 |
0.057 |
|
| 1944 |
Blout ER, Silverman DC. The Catalytic Reduction of Nitrocinnamic Acids and Esters Journal of the American Chemical Society. 66: 1442-1443. DOI: 10.1021/JA01237A006 |
0.055 |
|
| 1951 |
BLOUT ER, BIRD GR. Infrared microspectroscopy. II. Journal of the Optical Society of America. 41: 547-51. PMID 14861716 |
0.051 |
|
| 1947 |
Corley RS, Blout ER. The Reaction of β-Naphthol, β-Naphthylamine and Formaldehyde. I. 2-Amino-2'-hydroxy-1,1'-dinaphthylmethane Journal of the American Chemical Society. 69: 755-760. DOI: 10.1021/JA01196A007 |
0.05 |
|
| 1960 |
Simmons NS, Blout ER. The Structure of Tobacco Mosaic Virus and Its Components: Ultraviolet Optical Rotatory Dispersion. Biophysical Journal. 1: 55-62. PMID 19431302 |
0.048 |
|
| 1960 |
Simmons NS, Blout ER. The Structure of Tobacco Mosaic Virus and Its Components: Ultraviolet Optical Rotatory Dispersion. Biophysical Journal. 1: 55-62. PMID 19431302 |
0.048 |
|
| 1964 |
SIMONS ER, BLOUT ER. THE EFFECT OF PROTEOLYTIC ENZYMES ON SYNTHETIC POLYPEPTIDES. Biochimica Et Biophysica Acta. 92: 197-9. PMID 14243781 |
0.046 |
|
| 1954 |
Blout ER, Karlson RH, Doty P, Hargitay B. POLYPEPTIDES. I. THE SYNTHESIS AND THE MOLECULAR WEIGHT OF HIGH MOLECULAR WEIGHT POLYGLUTAMIC ACIDS AND ESTERS1 Journal of the American Chemical Society. 76: 4492-4493. DOI: 10.1021/Ja01646A078 |
0.045 |
|
| 1960 |
Katchalski E, Fasman G, Simons E, Blout E, Gurd F, Koltun W. Synthetic histidine-containing polypeptides as catalysts for the hydrolysis of p-nitrophenyl acetate Archives of Biochemistry and Biophysics. 88: 361-365. DOI: 10.1016/0003-9861(60)90251-4 |
0.045 |
|
| 1951 |
Blout E, Bird G, Grey D. Infra-red microspectroscopy Spectrochimica Acta. 4: 421-422. DOI: 10.1016/0371-1951(51)80053-5 |
0.043 |
|
| 1950 |
Blout ER, Bird GR, Grey DS. Infra-Red Microspectroscopy* Journal of the Optical Society of America. 40: 304. DOI: 10.1364/JOSA.40.000304 |
0.043 |
|
| 1968 |
Shechter E, Carver JP, Blout ER. Analyse des courbes de dispersion optique rotatoire des polypeptides et des protéines : Comparaison des méthodes Journal De Chimie Physique. 65: 118-124. DOI: 10.1051/JCP/1968650118 |
0.041 |
|
| 1961 |
BEYCHOK S, BLOUT ER. Optical rotatory dispersion of sperm whale ferrimyoglobin and horse ferrihemoglobin. Journal of Molecular Biology. 3: 769-77. PMID 13868739 |
0.041 |
|
| 1948 |
Cohen SG, Ostberg BE, Sparrow DB, Blout ER. Light-induced polymerization of some monomers containing allyl and methacrylate groups Journal of Polymer Science. 3: 264-282. DOI: 10.1002/Pol.1948.120030212 |
0.041 |
|
| 1973 |
Mosher DF, Blout ER. Heterogeneity of bovine fibrinogen and fibrin. The Journal of Biological Chemistry. 248: 6896-903. PMID 4745449 |
0.04 |
|
| 1972 |
Stenn KS, Blout ER. Mechanism of bovine prothrombin activation by an insoluble preparation of bovine factor X a (thrombokinase). Biochemistry. 11: 4502-15. PMID 4675875 |
0.04 |
|
| 1962 |
Blout ER, Lozé C, Asadourian A. Der Deuteriumaustausch von wasserlöslichen Polypeptiden und Proteinen, gemessen mittels Infrarot-Spektroskopie Kolloid-Zeitschrift & Zeitschrift FüR Polymere. 183: 88-88. DOI: 10.1007/BF02260588 |
0.038 |
|
| 1956 |
Bird GR, Blout ER. Infrared Flow Dichroism The Journal of Chemical Physics. 25: 798-799. DOI: 10.1063/1.1743082 |
0.036 |
|
| 1962 |
Zubay G, Wilkins M, Blout ER. An X-ray diffraction study of a complex of DNA and a synthetic polypeptide Journal of Molecular Biology. 4: 69-IN2. DOI: 10.1016/S0022-2836(62)80038-2 |
0.036 |
|
| 1948 |
Blout ER, Karplus R. The Infrared Spectrum of Polyvinyl Alcohol Journal of the American Chemical Society. 70: 862-864. DOI: 10.1021/JA01182A504 |
0.034 |
|
| 1953 |
LENORMANT H, BLOUT ER. Origin of the absorption band at 1,550 cm.-1 in proteins. Nature. 172: 770-1. PMID 13111185 |
0.034 |
|
| 1955 |
BLOUT ER, ABBATE MJ. Infrared microspectroscopy. IV. A double-beam infrared microspectrometer. Journal of the Optical Society of America. 45: 1028-30. PMID 13272101 |
0.034 |
|
| 1955 |
BLOUT ER, ABBATE MJ. Infrared microspectroscopy. IV. A double-beam infrared microspectrometer. Journal of the Optical Society of America. 45: 1028-30. PMID 13272101 |
0.034 |
|
| 1969 |
Sigman DS, Torchia DA, Blout ER. Phenacyl bromides as chromophoric reagents for alpha-chymotrypsin. Biochemistry. 8: 4560-6. PMID 5353114 DOI: 10.1021/bi00839a049 |
0.033 |
|
| 1947 |
Blout ER, Corley RS. The Reaction of β-Naphthol, β-Naphthylamine and Formaldehyde. III. The Dibenzacridine Products Journal of the American Chemical Society. 69: 763-769. DOI: 10.1021/JA01196A009 |
0.029 |
|
| 1952 |
BIRD GR, BLOUT ER. Infrared microspectroscopy of biologic materials. Laboratory Investigation; a Journal of Technical Methods and Pathology. 1: 266-72. PMID 14939742 |
0.027 |
|
| 1946 |
Blout ER, Ostberg BE. Polymerization of allyl methacrylate by means of ultraviolet radiation Journal of Polymer Science. 1: 230-231. DOI: 10.1002/POL.1946.120010311 |
0.027 |
|
| 1959 |
Blout ER, DesRoches ME. The Preparation of High Molecular Weight Polypeptides1 Journal of the American Chemical Society. 81: 370-372. DOI: 10.1021/JA01511A024 |
0.026 |
|
| 1953 |
BLOUT ER. Infrared microspectroscopy instrumentation and some instrumentation and some biological applications. Transactions of the New York Academy of Sciences. 15: 280-1. PMID 13090282 DOI: 10.1111/J.2164-0947.1953.TB00359.X |
0.026 |
|
| 1965 |
Latt S, Cheung H, Blout E. Additions and Corrections - Energy Transfer. A System with Relatively Fixed Donor-Acceptor Separation. Journal of the American Chemical Society. 87: 5810-5810. DOI: 10.1021/ja00952a612 |
0.025 |
|
| 1950 |
Blout ER, Corley RS, Snow PL. Infra-Red Transmitting Filters II The Region 1 to 6μ*† Journal of the Optical Society of America. 40: 415. DOI: 10.1364/JOSA.40.000415 |
0.025 |
|
| 1967 |
Sigman DS, Blout ER. Alkylation of chymotrypsin by alpha-bromo-4-nitroacetophenone, a charge-transfer acceptor. Journal of the American Chemical Society. 89: 1747-8. PMID 6039298 |
0.025 |
|
| 1953 |
BLOUT ER. Ultraviolet microscopy and ultraviolet microspectroscopy. Advances in Biological and Medical Physics. 3: 285-336. PMID 13030389 |
0.023 |
|
| 1962 |
Stryer L, Blout ER. Dispersion der optischen Drehung von an Makromolekülen gebundenen Farbstoffen. Kationische Farbstoffe: Polyglutaminsäure-Komplexe Kolloid-Zeitschrift & Zeitschrift FüR Polymere. 183: 93-93. DOI: 10.1007/BF02260610 |
0.023 |
|
| 1965 |
LATT SA, CHEUNG HT, BLOUT ER. ENERGY TRANSFER. A SYSTEM WITH RELATIVELY FIXED DONOR-ACCEPTOR SEPARATION. Journal of the American Chemical Society. 87: 995-1003. PMID 14284634 |
0.021 |
|
| 1955 |
Lenormant H, Blout ER. Technique des spectres infra-rouges en présence d’eau Il Nuovo Cimento. 2: 788-792. DOI: 10.1007/BF02822825 |
0.02 |
|
| 1952 |
Blout ER, Parrish M, Bird GR, Abbate MJ. Infrared Microspectroscopy III A Capillary Cell for Liquids*† Journal of the Optical Society of America. 42: 966. DOI: 10.1364/JOSA.42.000966 |
0.02 |
|
| 1954 |
Chubb LW, Grey DS, Blout ER, Land EH. Properties of Polarizers for Filters and Viewers for 3-D Motion Pictures Journal of the Society of Motion Picture and Television Engineers. 62: 120-124. DOI: 10.5594/J01726 |
0.019 |
|
| 1946 |
Clarke JT, Blout ER. Nature of the carbonyl groups in polyvinyl alcohol Journal of Polymer Science. 1: 419-428. DOI: 10.1002/POL.1946.120010509 |
0.018 |
|
| 1971 |
Visser L, Sigman DS, Blout ER. Elastase. I. A new inhibitor, 1-bromo-4(2,4-dinitrophenyl)-butan-2-one. Biochemistry. 10: 735-42. PMID 5549192 |
0.014 |
|
| 2010 |
BLOUT ER, AMON WF. Near infra-red transmitting filters. Journal of the Optical Society of America. 36: 460-4. PMID 20995603 DOI: 10.1364/JOSA.36.000460 |
0.011 |
|
| 1978 |
Blout ER, Grant DM, Jardetsky O, Phillips WD, Porter KR. Instrumentation funding Science. 202: 381. |
0.01 |
|
| 1949 |
Land EH, Blout ER, Grey DS, Flower MS, Husek H, Jones RC, Matz CH, Merrill DP. A Color Translating Ultraviolet Microscope. Science (New York, N.Y.). 109: 371-4. PMID 17749591 DOI: 10.1126/science.109.2833.371 |
0.01 |
|
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