Year |
Citation |
Score |
2011 |
Hadjithomas M, Moudrianakis EN. Experimental evidence for the role of domain swapping in the evolution of the histone fold. Proceedings of the National Academy of Sciences of the United States of America. 108: 13462-7. PMID 21813758 DOI: 10.1073/Pnas.1108649108 |
0.69 |
|
2005 |
Dohm JA, Hsu MH, Hwu JR, Huang RC, Moudrianakis EN, Lattman EE, Gittis AG. Influence of ions, hydration, and the transcriptional inhibitor P4N on the conformations of the Sp1 binding site. Journal of Molecular Biology. 349: 731-44. PMID 15896803 DOI: 10.1016/J.Jmb.2005.04.001 |
0.553 |
|
2001 |
Karantza V, Freire E, Moudrianakis EN. Thermodynamic studies of the core histones: Stability of the octamer subunits is not altered by removal of their terminal Domains Biochemistry. 40: 13114-13123. PMID 11669650 DOI: 10.1021/Bi0110140 |
0.395 |
|
1999 |
Bal W, Karantza V, Moudrianakis EN, Kasprzak KS. Interaction of nickel(II) with histones: In vitro binding of nickel(II) to the core histone tetramer Archives of Biochemistry and Biophysics. 364: 161-166. PMID 10190970 DOI: 10.1006/Abbi.1999.1137 |
0.343 |
|
1997 |
Akhmanova A, Miedema K, Wang Y, van Bruggen M, Berden JH, Moudrianakis EN, Hennig W. The localization of histone H3.3 in germ line chromatin of Drosophila males as established with a histone H3.3-specific antiserum. Chromosoma. 106: 335-47. PMID 9362542 DOI: 10.1007/S004120050255 |
0.368 |
|
1997 |
Santisteban MS, Arents G, Moudrianakis EN, Smith MM. Histone octamer function in vivo: Mutations in the dimer-tetramer interfaces disrupt both gene activation and repression Embo Journal. 16: 2493-2506. PMID 9171362 DOI: 10.1093/Emboj/16.9.2493 |
0.356 |
|
1996 |
Pruss D, Bartholomew B, Persinger J, Hayes J, Arents G, Moudrianakis EN, Wolffe AP. An asymmetric model for the nucleosome: A binding site for linker histones inside the DNA gyres Science. 274: 614-617. PMID 8849453 DOI: 10.1126/Science.274.5287.614 |
0.425 |
|
1996 |
Karantza V, Freire E, Moudrianakis EN. Thermodynamic studies of the core histones: pH and ionic strength effects on the stability of the (H3-H4)/(H3-H4)2 system Biochemistry. 35: 2037-2046. PMID 8639689 DOI: 10.1021/Bi9518858 |
0.339 |
|
1995 |
Karantza V, Baxevanis AD, Freire E, Moudrianakis EN. Thermodynamic studies of the core histones: Ionic strength and pH dependence of H2A-H2B dimer stability Biochemistry. 34: 5988-5996. PMID 7727455 DOI: 10.1021/Bi00017A028 |
0.367 |
|
1995 |
Baxevanis AD, Arents G, Moudrianakis EN, Landsman D. A variety of DNA-binding and multimeric proteins contain the histone fold motif Nucleic Acids Research. 23: 2685-2691. PMID 7651829 DOI: 10.1093/Nar/23.14.2685 |
0.43 |
|
1995 |
Arents G, Moudrianakis EN. The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization Proceedings of the National Academy of Sciences of the United States of America. 92: 11170-11174. PMID 7479959 DOI: 10.1073/Pnas.92.24.11170 |
0.428 |
|
1994 |
Wang BC, Rose J, Arents G, Moudrianakis EN. The octameric histone core of the nucleosome: Structural issues resolved Journal of Molecular Biology. 236: 179-188. PMID 8107103 DOI: 10.1006/Jmbi.1994.1127 |
0.31 |
|
1993 |
Arents G, Moudrianakis EN. Topography of the histone octamer surface: Repeating structural motifs utilized in the docking of nucleosomal DNA Proceedings of the National Academy of Sciences of the United States of America. 90: 10489-10493. PMID 8248135 DOI: 10.1073/Pnas.90.22.10489 |
0.41 |
|
1992 |
Moehs CP, Baxevanis AD, Moudrianakis EN, Spiker S. Enhanced stability of histone octamers from plant nucleosomes: Role of H2A and H2B histones Biochemistry. 31: 10844-10851. PMID 1420197 DOI: 10.1021/Bi00159A027 |
0.388 |
|
1991 |
Arents G, Burlingame RW, Wang BIC, Love WE, Moudrianakis EN. The nucleosomal core histone octamer at 3.1 Å resolution: A tripartite protein assembly and a left-handed superhelix Proceedings of the National Academy of Sciences of the United States of America. 88: 10148-10152. PMID 1946434 DOI: 10.1073/Pnas.88.22.10148 |
0.395 |
|
1991 |
Baxevanis AD, Godfrey JE, Moudrianakis EN. Associative behavior of the histone (H3-H4)2 Tetramer: Dependence on ionic environment Biochemistry. 30: 8817-8823. PMID 1888742 DOI: 10.1021/Bi00100A013 |
0.322 |
|
1990 |
Baxevanis AD, Godfrey JE, Moudrianakis EN, Park K, Fasman GD. Effect of aggregation of histone octamers in high-salt solutions on circular dichroism spectra Biochemistry. 29: 973-976. PMID 2340288 DOI: 10.1021/Bi00456A019 |
0.349 |
|
1990 |
Godfrey JE, Baxevanis AD, Moudrianakis EN. Spectropolarimetric analysis of the core histone octamer and its subunits Biochemistry. 29: 965-972. PMID 2187535 DOI: 10.1021/Bi00456A018 |
0.392 |
|
1988 |
Elia MC, Moudrianakis EN. Regulation of H2a-specific proteolysis by the histone H3:H4 tetramer Journal of Biological Chemistry. 263: 9958-9964. PMID 3290217 |
0.325 |
|
1988 |
Eickbush TH, Godfrey JE, Elia MC, Moudrianakis EN. H2a-specific proteolysis as a unique probe in the analysis of the histone octamer. The Journal of Biological Chemistry. 263: 18972-8. PMID 3058692 |
0.309 |
|
1986 |
Feinstein DL, Moudrianakis EN. Thiol reactivity of histone H3 in soluble and DNA-associated histone complexes: evidence for allosteric and torsional regulation. Biochemistry. 25: 8409-18. PMID 3828286 DOI: 10.1021/Bi00374A013 |
0.425 |
|
1985 |
Moudrianakis EN, Love WE, Wang BC, Xuong NG, Burlingame RW. Crystallographic structure of the octamer histone core of the nucleosome. Science (New York, N.Y.). 229: 1110-2. PMID 17753284 DOI: 10.1126/Science.229.4718.1110 |
0.373 |
|
1985 |
Burlingame RW, Love WE, Wang BC, Hamlin R, Nguyen HX, Moudrianakis EN. Crystallographic structure of the octameric histone core of the nucleosome at a resolution of 3.3 Å Science. 228: 546-553. PMID 3983639 DOI: 10.1126/Science.3983639 |
0.386 |
|
1984 |
McCarthy MP, Steffen PK, Allewell NM, Benedict RC, Moudrianakis EN, Ackers GK. Effects of ionic strength and state of assembly on kinetics of hydrogen exchange of calf thymus histones. Biochemistry. 23: 2227-30. PMID 6733085 DOI: 10.1021/Bi00305A020 |
0.348 |
|
1984 |
Burlingame RW, Love WE, Moudrianakis EN. Crystals of the octameric histone core of the nucleosome Science. 223: 413-414. PMID 6691154 DOI: 10.1126/Science.6691154 |
0.309 |
|
1984 |
Benedict RC, Moudrianakis EN, Ackers GK. Interactions of the nucleosomal core histones: A calorimetric study of octamer assembly Biochemistry. 23: 1214-1218. DOI: 10.1021/Bi00301A029 |
0.361 |
|
1983 |
Hatch CL, Bonner WM, Moudrianakis EN. Differential accessibility of the amino and carboxy termini of histone H2A in the nucleosome and its histone subunits. Biochemistry. 22: 3016-23. PMID 6871182 DOI: 10.1021/Bi00281A035 |
0.389 |
|
1983 |
Hatch CL, Bonner WM, Moudrianakis EN. Minor histone 2A variants and ubiquinated forms in the native H2A:H2B dimer. Science (New York, N.Y.). 221: 468-70. PMID 6306766 DOI: 10.1126/Science.6306766 |
0.375 |
|
1982 |
Lattman E, Burlingame R, Hatch C, Moudrianakis EN. Crystallization of the tetramer of histones H3 and H4. Science (New York, N.Y.). 216: 1016-8. PMID 7079748 DOI: 10.1126/Science.7079748 |
0.325 |
|
1982 |
Watson DK, Moudrianakis EN. Histone-dependent reconstitution and nucleosomal localization of a nonhistone chromosomal protein: The H2A-specific protease Biochemistry. 21: 248-256. PMID 7041960 DOI: 10.1021/Bi00531A008 |
0.44 |
|
1980 |
Godfrey JE, Eickbush TH, Moudrianakis EN. Reversible association of calf thymus histones to form the symmetrical octamer (H2AH2BH3H4)2: a case of a mixed-associating system. Biochemistry. 19: 1339-46. PMID 7387992 DOI: 10.1021/Bi00548A012 |
0.324 |
|
1979 |
Kurth PD, Bustin M, Moudrianakis EN. Concanavalin A binds to puffs in polytene chromosomes [29] Nature. 279: 448-450. DOI: 10.1038/279448A0 |
0.309 |
|
1978 |
Eickbush TH, Moudrianakis EN. The histone core complex: an octamer assembled by two sets of protein-protein interactions. Biochemistry. 17: 4955-64. PMID 718868 DOI: 10.1021/Bi00616A016 |
0.418 |
|
1978 |
Kurth PD, Moudrianakis EN, Bustin M. Histone localization in polytene chromosomes by immunofluorescence Journal of Cell Biology. 78: 910-918. PMID 359571 DOI: 10.1083/Jcb.78.3.910 |
0.334 |
|
1978 |
Eickbush TH, Moudrianakis EN. The compaction of DNA helices into either continuous supercoils or folded-fiber rods and toroids. Cell. 13: 295-306. PMID 203402 DOI: 10.1016/0092-8674(78)90198-8 |
0.329 |
|
1977 |
Eickbush TH, Moudrianakis EN. A mechanism for the entrapment of DNA at an air-water interface. Biophysical Journal. 18: 275-88. PMID 890027 DOI: 10.1016/S0006-3495(77)85613-0 |
0.31 |
|
1977 |
Tiefert MA, Roy H, Moudrianakis EN. Binding of adenine nucleotides and pyrophosphate by the purified coupling factor of photophosphorylation Biochemistry. 16: 2396-2404. PMID 193559 DOI: 10.1021/Bi00630A014 |
0.312 |
|
1977 |
Tiefert MA, Roy H, Moudrianakis EN. Conversion of bound adenine nucleotides by the purified coupling factor of photophosphorylation Biochemistry. 16: 2404-2409. PMID 16644 DOI: 10.1021/Bi00630A015 |
0.31 |
|
1976 |
Adolfsen R, Moudrianakis EN. Binding of adenine nucleotides to the purified 13S coupling factor of bacterial oxidative phosphorylation Archives of Biochemistry and Biophysics. 172: 425-433. PMID 1259416 DOI: 10.1016/0003-9861(76)90094-1 |
0.323 |
|
1976 |
Eickbush TH, Watson DK, Moudrianakis EN. A chromatin-bound proteolytic activity with unique specificity for histone H2A. Cell. 9: 785-92. PMID 13934 DOI: 10.1016/0092-8674(76)90141-0 |
0.446 |
|
1976 |
Adolfsen R, Moudrianakis EN. Molecular polymorphism and mechanisms of activation and deactivation of the hydrolytic function of the coupling factor of oxidative phosphorylation Biochemistry. 15: 4163-4170. PMID 9131 DOI: 10.1021/Bi00664A005 |
0.317 |
|
1975 |
Rubin RL, Moudrianakis EN. The F3-F2a1 complex as a unit in the self-assembly of nucleoproteins Biochemistry. 14: 1718-1726. PMID 1125196 DOI: 10.1021/Bi00679A026 |
0.385 |
|
1974 |
Angerer LM, Georghiou S, Moudrianakis EN. Studies on the structure of deoxyribonucleoproteins. Spectroscopic characterization of the ethidium bromide binding sites Biochemistry. 13: 1075-1082. PMID 4856024 DOI: 10.1021/Bi00703A003 |
0.633 |
|
1972 |
Angerer LM, Moudrianakis EN. Interaction of ethidium bromide with whole and selectively deproteinized deoxynucleoproteins from calf thymus Journal of Molecular Biology. 63. PMID 5062675 DOI: 10.1016/0022-2836(72)90444-5 |
0.347 |
|
1972 |
Rubin RL, Moudrianakis EN. Co-operative binding of histones to DNA Journal of Molecular Biology. 67. PMID 4558098 DOI: 10.1016/0022-2836(72)90456-1 |
0.418 |
|
1972 |
Adolfsen R, Moudrianakis EN. An exchange enzyme-catalyzing incorporation of inorganic phosphate into adenosine diphosphate in Alcaligenes faecalis Archives of Biochemistry and Biophysics. 148: 185-195. PMID 4333687 DOI: 10.1016/0003-9861(72)90130-0 |
0.32 |
|
1971 |
Roy H, Moudrianakis EN. Interactions between ADP and the coupling factor of photophosphorylation Proceedings of the National Academy of Sciences of the United States of America. 68: 464-468. PMID 5277102 DOI: 10.1073/Pnas.68.2.464 |
0.303 |
|
1971 |
Adolfsen R, Moudrianakis EN. Purification and properties of two soluble coupling factors of oxidative phosphorylation from alcaligenes faecalis Biochemistry. 10: 2247-2253. PMID 4255956 DOI: 10.1021/Bi00788A010 |
0.312 |
|
1967 |
Gal-Or L, Mellema JE, Moudrianakis EN, Beer M. Electron microscopic study of base sequence in nucleic acids. VII. Cytosine-specific addition of acyl hydrazides Biochemistry. 6: 1909-1915. PMID 6049434 DOI: 10.1021/Bi00859A006 |
0.582 |
|
1967 |
Howell SH, Moudrianakis EN. Hill Reaction site in chloroplast membranes: Non-participation of the quantasome particle in photoreduction Journal of Molecular Biology. 27. |
0.466 |
|
1965 |
MOUDRIANAKIS EN, BEER M. BASE SEQUENCE DETERMINATION IN NUCLEIC ACIDS WITH THE ELECTRON Proceedings of the National Academy of Sciences of the United States Of. 53: 564-571. PMID 14338235 DOI: 10.1073/Pnas.53.3.564 |
0.561 |
|
1965 |
MOUDRIANAKIS EN, BEER M. DETERMINATION OF BASE SEQUENCE IN NUCLEIC ACIDS WITH THE ELECTRON Biochimica Et Biophysica Acta. 95: 23-39. PMID 14289031 DOI: 10.1016/0005-2787(65)90207-8 |
0.575 |
|
1964 |
Moudrianakis EN, Beer M. A selective reagent for the study of base sequence in nucleic acids [18] Nature. 204: 685-686. PMID 14236291 DOI: 10.1038/204685A0 |
0.56 |
|
1962 |
Beer M, Moudrianakis EN. Determination of base sequence in nucleic acids with the electron microscope: visibility of a marker. Proceedings of the National Academy of Sciences of the United States of America. 48: 409-416. PMID 13866528 DOI: 10.1073/Pnas.48.3.409 |
0.56 |
|
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