| Year |
Citation |
Score |
| 2023 |
Das SK, Kumar A, Hao F, Cutter DiPiazza AR, Fang H, Lee TH, Hayes JJ. Histone H3 Tail Modifications Alter Structure and Dynamics of the H1 C-Terminal Domain Within Nucleosomes. Journal of Molecular Biology. 435: 168242. PMID 37619707 DOI: 10.1016/j.jmb.2023.168242 |
0.444 |
|
| 2023 |
Das SK, Kumar A, Hao F, DiPiazza ARC, Lee TH, Hayes JJ. Histone H3 tail modifications regulate structure and dynamics of the H1 C-terminal domain within nucleosomes. Biorxiv : the Preprint Server For Biology. PMID 37214834 DOI: 10.1101/2023.05.11.540398 |
0.498 |
|
| 2023 |
Kumar A, Maurya P, Hayes JJ. Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease. International Journal of Molecular Sciences. 24. PMID 36674981 DOI: 10.3390/ijms24021463 |
0.455 |
|
| 2022 |
Bhat JA, Balliano AJ, Hayes JJ. Histone protein surface accessibility dictates direction of RSC-dependent nucleosome mobilization. Nucleic Acids Research. PMID 36161493 DOI: 10.1093/nar/gkac790 |
0.534 |
|
| 2022 |
Hao F, Mishra L, Jaya P, Jones R, Hayes JJ. Identification and analysis of six phosphorylation sites within the Xenopus laevis H1.0 C-terminal domain indicate distinct effects on nucleosome structure. Molecular & Cellular Proteomics : McP. 100250. PMID 35618225 DOI: 10.1016/j.mcpro.2022.100250 |
0.461 |
|
| 2022 |
Marr LT, Jaya P, Mishra LN, Hayes JJ. Whole-genome methods to define DNA and histone accessibility and long-range interactions in chromatin. Biochemical Society Transactions. 50: 199-212. PMID 35166326 DOI: 10.1042/BST20210959 |
0.399 |
|
| 2021 |
Poulet A, Mishra LN, Téletchéa S, Hayes JJ, Jacob Y, Thiriet C, Duc C. Identification and characterization of histones in evidence a phylogenetic vicinity of Mycetozoans to the animal kingdom. Nar Genomics and Bioinformatics. 3: lqab107. PMID 34805990 DOI: 10.1093/nargab/lqab107 |
0.458 |
|
| 2021 |
Hao F, Kale S, Dimitrov S, Hayes JJ. Unraveling linker histone interactions in nucleosomes. Current Opinion in Structural Biology. 71: 87-93. PMID 34246862 DOI: 10.1016/j.sbi.2021.06.001 |
0.458 |
|
| 2021 |
Marr LT, Ocampo J, Clark DJ, Hayes JJ. Global histone protein surface accessibility in yeast indicates a uniformly loosely packed genome with canonical nucleosomes. Epigenetics & Chromatin. 14: 5. PMID 33430969 DOI: 10.1186/s13072-020-00381-5 |
0.407 |
|
| 2020 |
Hao F, Murphy KJ, Kujirai T, Kamo N, Kato J, Koyama M, Okamato A, Hayashi G, Kurumizaka H, Hayes JJ. Acetylation-modulated communication between the H3 N-terminal tail domain and the intrinsically disordered H1 C-terminal domain. Nucleic Acids Research. PMID 33125082 DOI: 10.1093/nar/gkaa949 |
0.403 |
|
| 2019 |
Marr L, Clark DJ, Hayes JJ. A method for assessing histone surface accessibility genome-wide. Methods (San Diego, Calif.). PMID 31830524 DOI: 10.1016/J.Ymeth.2019.12.002 |
0.613 |
|
| 2018 |
Mishra LN, Hayes J. A nucleosome-free region locally abrogates histone H1-dependent restriction of linker DNA accessibility in chromatin. The Journal of Biological Chemistry. PMID 30373774 DOI: 10.1074/Jbc.Ra118.005721 |
0.667 |
|
| 2017 |
Gatchalian J, Wang X, Ikebe J, Cox KL, Tencer AH, Zhang Y, Burge NL, Di L, Gibson MD, Musselman CA, Poirier MG, Kono H, Hayes JJ, Kutateladze TG. Accessibility of the histone H3 tail in the nucleosome for binding of paired readers. Nature Communications. 8: 1489. PMID 29138400 DOI: 10.1038/S41467-017-01598-X |
0.647 |
|
| 2017 |
Tencer AH, Cox KL, Di L, Bridgers JB, Lyu J, Wang X, Sims JK, Weaver TM, Allen HF, Zhang Y, Gatchalian J, Darcy MA, Gibson MD, Ikebe J, Li W, ... ... Hayes JJ, et al. Covalent Modifications of Histone H3K9 Promote Binding of CHD3. Cell Reports. 21: 455-466. PMID 29020631 DOI: 10.1016/J.Celrep.2017.09.054 |
0.621 |
|
| 2017 |
Murphy KJ, Cutter AR, Fang H, Postnikov YV, Bustin M, Hayes JJ. HMGN1 and 2 remodel core and linker histone tail domains within chromatin. Nucleic Acids Research. 45: 9917-9930. PMID 28973435 DOI: 10.1093/Nar/Gkx579 |
0.686 |
|
| 2017 |
Bednar J, Garcia-Saez I, Boopathi R, Cutter AR, Papai G, Reymer A, Syed SH, Lone IN, Tonchev O, Crucifix C, Menoni H, Papin C, Skoufias DA, Kurumizaka H, Lavery R, ... ... Hayes JJ, et al. Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1. Molecular Cell. 66: 729. PMID 28575663 DOI: 10.1016/J.Molcel.2017.05.018 |
0.51 |
|
| 2017 |
Bednar J, Garcia-Saez I, Boopathi R, Cutter AR, Papai G, Reymer A, Syed SH, Lone IN, Tonchev O, Crucifix C, Menoni H, Papin C, Skoufias DA, Kurumizaka H, Lavery R, ... ... Hayes JJ, et al. Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1. Molecular Cell. 66: 384-397.e8. PMID 28475873 DOI: 10.1016/J.Molcel.2017.04.012 |
0.581 |
|
| 2017 |
Balliano A, Hao F, Njeri C, Balakrishnan L, Hayes JJ. HMGB1 Stimulates Activity of Polymerase β on Nucleosome Substrates. Biochemistry. PMID 28098985 DOI: 10.1021/Acs.Biochem.6B00569 |
0.516 |
|
| 2016 |
Cutter AR, Hayes JJ. Linker histones: Novel insights into structure-specific recognition of the nucleosome. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. PMID 28177778 DOI: 10.1139/Bcb-2016-0097 |
0.653 |
|
| 2016 |
Mishra LN, Pepenella S, Rogge R, Hansen JC, Hayes JJ. Acetylation Mimics Within a Single Nucleosome Alter Local DNA Accessibility In Compacted Nucleosome Arrays. Scientific Reports. 6: 34808. PMID 27708426 DOI: 10.1038/Srep34808 |
0.648 |
|
| 2016 |
Fang H, Wei S, Lee TH, Hayes JJ. Chromatin structure-dependent conformations of the H1 CTD. Nucleic Acids Research. PMID 27365050 DOI: 10.1093/Nar/Gkw586 |
0.576 |
|
| 2016 |
Black PJ, Miller AS, Hayes JJ. Radioresistance of GGG sequences to prompt strand break formation from direct-type radiation damage. Radiation and Environmental Biophysics. PMID 27349757 DOI: 10.1007/S00411-016-0660-7 |
0.366 |
|
| 2016 |
Yue H, Fang H, Wei S, Hayes JJ, Lee TH. Single Molecule Studies on the Linker Histone H1 Binding to DNA and the Nucleosome. Biochemistry. PMID 27010485 DOI: 10.1021/Acs.Biochem.5B01247 |
0.625 |
|
| 2015 |
Balliano AJ, Hayes JJ. Base excision repair in chromatin: Insights from reconstituted systems. Dna Repair. PMID 26411876 DOI: 10.1016/J.Dnarep.2015.09.009 |
0.526 |
|
| 2015 |
Cutter AR, Hayes JJ. A brief review of nucleosome structure. Febs Letters. PMID 25980611 DOI: 10.1016/J.Febslet.2015.05.016 |
0.648 |
|
| 2015 |
Shimbo T, Lavender C, Grimm SA, Doi MI, Henriques T, Cannady KR, Murphy KJ, Gilchrist DA, Burkholder A, Hayes JJ, Adelman K, Archer TK, Zaret KS, Wade PA. Abstract 2862: MBD3 regulates chromatin accessibility at active promoters Cancer Research. 75: 2862-2862. DOI: 10.1158/1538-7445.Am2015-2862 |
0.485 |
|
| 2014 |
Pepenella S, Murphy KJ, Hayes JJ. A distinct switch in interactions of the histone H4 tail domain upon salt-dependent folding of nucleosome arrays. The Journal of Biological Chemistry. 289: 27342-51. PMID 25122771 DOI: 10.1074/Jbc.M114.595140 |
0.582 |
|
| 2014 |
Pepenella S, Murphy KJ, Hayes JJ. Intra- and inter-nucleosome interactions of the core histone tail domains in higher-order chromatin structure. Chromosoma. 123: 3-13. PMID 23996014 DOI: 10.1007/S00412-013-0435-8 |
0.622 |
|
| 2013 |
Raghuram N, Strickfaden H, McDonald D, Williams K, Fang H, Mizzen C, Hayes JJ, Th'ng J, Hendzel MJ. Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin. The Journal of Cell Biology. 203: 57-71. PMID 24100296 DOI: 10.1083/Jcb.201305159 |
0.539 |
|
| 2013 |
Elliott GO, Murphy KJ, Hayes JJ, Thiriet C. Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4. Nucleic Acids Research. 41: 2228-38. PMID 23303778 DOI: 10.1093/Nar/Gks1451 |
0.567 |
|
| 2013 |
Hayes J. Linker Histone Structural Transitions Upon Binding to DNA, Mononucleosomes, and Oligonucleosomal Arrays Biophysical Journal. 104. DOI: 10.1016/J.Bpj.2012.11.056 |
0.584 |
|
| 2012 |
Liu N, Hayes JJ. Preparation of nucleosomes containing a specific H2A-H2A cross-link forming a DNA-constraining loop structure. Methods in Molecular Biology (Clifton, N.J.). 833: 351-71. PMID 22183604 DOI: 10.1007/978-1-61779-477-3_21 |
0.619 |
|
| 2012 |
Schlick T, Hayes J, Grigoryev S. Toward convergence of experimental studies and theoretical modeling of the chromatin fiber. The Journal of Biological Chemistry. 287: 5183-91. PMID 22157002 DOI: 10.1074/Jbc.R111.305763 |
0.486 |
|
| 2012 |
Fang H, Clark DJ, Hayes JJ. DNA and nucleosomes direct distinct folding of a linker histone H1 C-terminal domain. Nucleic Acids Research. 40: 1475-84. PMID 22021384 DOI: 10.1093/Nar/Gkr866 |
0.549 |
|
| 2011 |
Yang Z, Hayes JJ. The divalent cations Ca2+ and Mg2+ play specific roles in stabilizing histone-DNA interactions within nucleosomes that are partially redundant with the core histone tail domains. Biochemistry. 50: 9973-81. PMID 22007636 DOI: 10.1021/Bi201377X |
0.621 |
|
| 2011 |
Almouzni G, Hayes JJ. International symposium on the physicochemical field for genetic activities. Awaji Island, Japan, January 24–26, 2011. Nucleus (Austin, Tex.). 2: 253-7. PMID 21941116 DOI: 10.4161/Nucl.2.4.16785 |
0.535 |
|
| 2011 |
Liu N, Peterson CL, Hayes JJ. SWI/SNF- and RSC-catalyzed nucleosome mobilization requires internal DNA loop translocation within nucleosomes Molecular and Cellular Biology. 31: 4165-4175. PMID 21859889 DOI: 10.1128/Mcb.05605-11 |
0.636 |
|
| 2011 |
Meyer S, Becker NB, Syed SH, Goutte-Gattat D, Shukla MS, Hayes JJ, Angelov D, Bednar J, Dimitrov S, Everaers R. From crystal and NMR structures, footprints and cryo-electron-micrographs to large and soft structures: nanoscale modeling of the nucleosomal stem. Nucleic Acids Research. 39: 9139-54. PMID 21835779 DOI: 10.1093/Nar/Gkr573 |
0.509 |
|
| 2011 |
Caterino TL, Fang H, Hayes JJ. Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain. Molecular and Cellular Biology. 31: 2341-8. PMID 21464206 DOI: 10.1128/Mcb.05145-11 |
0.615 |
|
| 2011 |
Jagannathan I, Pepenella S, Hayes JJ. Activity of FEN1 endonuclease on nucleosome substrates is dependent upon DNA sequence but not flap orientation. The Journal of Biological Chemistry. 286: 17521-9. PMID 21454907 DOI: 10.1074/Jbc.M111.229658 |
0.555 |
|
| 2011 |
Caterino TL, Hayes JJ. Structure of the H1 C-terminal domain and function in chromatin condensation. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 89: 35-44. PMID 21326361 DOI: 10.1139/O10-024 |
0.47 |
|
| 2011 |
Liu N, Balliano A, Hayes JJ. Mechanism(s) of SWI/SNF-induced nucleosome mobilization. Chembiochem : a European Journal of Chemical Biology. 12: 196-204. PMID 21243709 DOI: 10.1002/Cbic.201000455 |
0.593 |
|
| 2011 |
Shukla MS, Syed SH, Goutte-Gattat D, Richard JL, Montel F, Hamiche A, Travers A, Faivre-Moskalenko C, Bednar J, Hayes JJ, Angelov D, Dimitrov S. The docking domain of histone H2A is required for H1 binding and RSC-mediated nucleosome remodeling. Nucleic Acids Research. 39: 2559-70. PMID 21131284 DOI: 10.1093/Nar/Gkq1174 |
0.575 |
|
| 2011 |
Hayes J. Jonathan Widom 1955-2011 Nature Structural & Molecular Biology. 18: 965-966. DOI: 10.1038/Nsmb.2132 |
0.473 |
|
| 2010 |
Liu N, Hayes JJ. When push comes to shove: SWI/SNF uses a nucleosome to get rid of a nucleosome. Molecular Cell. 38: 484-6. PMID 20513424 DOI: 10.1016/J.Molcel.2010.05.005 |
0.458 |
|
| 2010 |
Syed SH, Goutte-Gattat D, Becker N, Meyer S, Shukla MS, Hayes JJ, Everaers R, Angelov D, Bednar J, Dimitrov S. Single-base resolution mapping of H1-nucleosome interactions and 3D organization of the nucleosome. Proceedings of the National Academy of Sciences of the United States of America. 107: 9620-5. PMID 20457934 DOI: 10.1073/Pnas.1000309107 |
0.647 |
|
| 2010 |
Cole HA, Tabor-Godwin JM, Hayes JJ. Uracil DNA glycosylase activity on nucleosomal DNA depends on rotational orientation of targets. The Journal of Biological Chemistry. 285: 2876-85. PMID 19933279 DOI: 10.1074/Jbc.M109.073544 |
0.654 |
|
| 2009 |
Chafin DR, Hayes JJ. Site-directed cleavage of DNA by protein-Fe(II) EDTA conjugates within model chromatin complexes. Methods in Molecular Biology (Clifton, N.J.). 543: 121-38. PMID 19378164 DOI: 10.1007/978-1-60327-015-1_10 |
0.527 |
|
| 2009 |
Jagannathan I, Hayes JJ. Hydroxyl radical footprinting of protein-DNA complexes. Methods in Molecular Biology (Clifton, N.J.). 543: 57-71. PMID 19378159 DOI: 10.1007/978-1-60327-015-1_5 |
0.478 |
|
| 2009 |
Thiriet C, Hayes JJ. Linker histone phosphorylation regulates global timing of replication origin firing. The Journal of Biological Chemistry. 284: 2823-2829. PMID 19015270 DOI: 10.1074/Jbc.M805617200 |
0.598 |
|
| 2009 |
Kan PY, Caterino TL, Hayes JJ. The H4 tail domain participates in intra- and internucleosome interactions with protein and DNA during folding and oligomerization of nucleosome arrays. Molecular and Cellular Biology. 29: 538-46. PMID 19001093 DOI: 10.1128/Mcb.01343-08 |
0.556 |
|
| 2008 |
Wang X, Hayes JJ. Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure. Molecular and Cellular Biology. 28: 227-36. PMID 17938198 DOI: 10.1128/Mcb.01245-07 |
0.541 |
|
| 2007 |
Caterino TL, Hayes JJ. Chromatin structure depends on what's in the nucleosome's pocket. Nature Structural & Molecular Biology. 14: 1056-8. PMID 17984968 DOI: 10.1038/Nsmb1107-1056 |
0.585 |
|
| 2007 |
Wang X, Hayes JJ. Site-specific binding affinities within the H2B tail domain indicate specific effects of lysine acetylation. The Journal of Biological Chemistry. 282: 32867-76. PMID 17711854 DOI: 10.1074/Jbc.M706035200 |
0.519 |
|
| 2007 |
Kan PY, Hayes JJ. Detection of interactions between nucleosome arrays mediated by specific core histone tail domains. Methods (San Diego, Calif.). 41: 278-85. PMID 17309837 DOI: 10.1016/J.Ymeth.2006.08.012 |
0.534 |
|
| 2007 |
Kan PY, Lu X, Hansen JC, Hayes JJ. The H3 tail domain participates in multiple interactions during folding and self-association of nucleosome arrays. Molecular and Cellular Biology. 27: 2084-91. PMID 17242202 DOI: 10.1128/Mcb.02181-06 |
0.525 |
|
| 2007 |
Yang Z, Zheng C, Hayes JJ. The core histone tail domains contribute to sequence-dependent nucleosome positioning. The Journal of Biological Chemistry. 282: 7930-8. PMID 17234628 DOI: 10.1074/Jbc.M610584200 |
0.659 |
|
| 2007 |
Hayes J, Kan P, Wang X, Lu X, Hansen J. Short and long range Inter-nucleosome interactions of the core histone tail domains The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A38-E |
0.501 |
|
| 2006 |
Wang X, Hayes JJ. Physical methods used to study core histone tail structures and interactions in solution. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 84: 578-88. PMID 16936830 DOI: 10.1139/o06-076 |
0.521 |
|
| 2006 |
Thiriet C, Hayes JJ. Histone dynamics during transcription: exchange of H2A/H2B dimers and H3/H4 tetramers during pol II elongation. Results and Problems in Cell Differentiation. 41: 77-90. PMID 16909891 DOI: 10.1007/400_009 |
0.586 |
|
| 2006 |
Jagannathan I, Cole HA, Hayes JJ. Base excision repair in nucleosome substrates. Chromosome Research : An International Journal On the Molecular, Supramolecular and Evolutionary Aspects of Chromosome Biology. 14: 27-37. PMID 16506094 DOI: 10.1007/S10577-005-1020-7 |
0.567 |
|
| 2005 |
Zheng C, Lu X, Hansen JC, Hayes JJ. Salt-dependent intra- and internucleosomal interactions of the H3 tail domain in a model oligonucleosomal array. The Journal of Biological Chemistry. 280: 33552-7. PMID 16079127 DOI: 10.1074/Jbc.M507241200 |
0.506 |
|
| 2005 |
Owen BA, Yang Z, Lai M, Gajec M, Gajek M, Badger JD, Hayes JJ, Edelmann W, Kucherlapati R, Wilson TM, McMurray CT. (CAG)(n)-hairpin DNA binds to Msh2-Msh3 and changes properties of mismatch recognition. Nature Structural & Molecular Biology. 12: 663-70. PMID 16025128 DOI: 10.1038/Nsmb965 |
0.514 |
|
| 2005 |
Thiriet C, Hayes JJ. Chromatin in need of a fix: phosphorylation of H2AX connects chromatin to DNA repair. Molecular Cell. 18: 617-22. PMID 15949437 DOI: 10.1016/J.Molcel.2005.05.008 |
0.65 |
|
| 2005 |
Thiriet C, Hayes JJ. Replication-independent core histone dynamics at transcriptionally active loci in vivo. Genes & Development. 19: 677-82. PMID 15769942 DOI: 10.1101/Gad.1265205 |
0.503 |
|
| 2005 |
Yang Z, Zheng C, Thiriet C, Hayes JJ. The core histone N-terminal tail domains negatively regulate binding of transcription factor IIIA to a nucleosome containing a 5S RNA gene via a novel mechanism. Molecular and Cellular Biology. 25: 241-9. PMID 15601846 DOI: 10.1128/Mcb.25.1.241-249.2005 |
0.601 |
|
| 2005 |
Owen BAL, Yang Z, Lai M, Gajek M, Badger JD, Hayes JJ, Edelmann W, Kucherlapati R, Wilson TM, McMurray CT. Correction: Corrigendum: (CAG)n-hairpin DNA binds to Msh2–Msh3 and changes properties of mismatch recognition Nature Structural & Molecular Biology. 12: 824-824. DOI: 10.1038/Nsmb0905-824A |
0.342 |
|
| 2004 |
Yang Z, Hayes JJ. Large scale preparation of nucleosomes containing site-specifically chemically modified histones lacking the core histone tail domains. Methods (San Diego, Calif.). 33: 25-32. PMID 15039084 DOI: 10.1016/J.Ymeth.2003.10.017 |
0.58 |
|
| 2004 |
Hayes JJ. In vitro analysis of chromatin structure in model systems. Methods (San Diego, Calif.). 33: 1-2. PMID 15039080 DOI: 10.1016/J.Ymeth.2003.10.014 |
0.363 |
|
| 2004 |
Zheng C, Hayes JJ. Probing core histone tail-DNA interactions in a model dinucleosome system. Methods in Enzymology. 375: 179-93. PMID 14870667 DOI: 10.1016/S0076-6879(03)75012-5 |
0.623 |
|
| 2004 |
Vitolo JM, Yang Z, Basavappa R, Hayes JJ. Structural features of transcription factor IIIA bound to a nucleosome in solution. Molecular and Cellular Biology. 24: 697-707. PMID 14701742 DOI: 10.1128/Mcb.24.2.697-707.2004 |
0.675 |
|
| 2003 |
Yang Z, Hayes JJ. Xenopus transcription factor IIIA and the 5S nucleosome: development of a useful in vitro system. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 81: 177-84. PMID 12897852 DOI: 10.1139/O03-043 |
0.615 |
|
| 2003 |
Aoyagi S, Wade PA, Hayes JJ. Nucleosome sliding induced by the xMi-2 complex does not occur exclusively via a simple twist-diffusion mechanism. The Journal of Biological Chemistry. 278: 30562-8. PMID 12767978 DOI: 10.1074/Jbc.M304148200 |
0.6 |
|
| 2003 |
Zheng C, Hayes JJ. Intra- and inter-nucleosomal protein-DNA interactions of the core histone tail domains in a model system. The Journal of Biological Chemistry. 278: 24217-24. PMID 12697747 DOI: 10.1074/Jbc.M302817200 |
0.659 |
|
| 2003 |
Zheng C, Hayes JJ. Structures and interactions of the core histone tail domains. Biopolymers. 68: 539-46. PMID 12666178 DOI: 10.1002/Bip.10303 |
0.582 |
|
| 2002 |
Ye J, Yang Z, Hayes JJ, Eickbush TH. R2 retrotransposition on assembled nucleosomes depends on the translational position of the target site. The Embo Journal. 21: 6853-64. PMID 12486006 DOI: 10.1093/Emboj/Cdf665 |
0.449 |
|
| 2002 |
Huggins CF, Chafin DR, Aoyagi S, Henricksen LA, Bambara RA, Hayes JJ. Flap endonuclease 1 efficiently cleaves base excision repair and DNA replication intermediates assembled into nucleosomes. Molecular Cell. 10: 1201-11. PMID 12453426 DOI: 10.1016/S1097-2765(02)00736-0 |
0.592 |
|
| 2002 |
Aoyagi S, Hayes JJ. hSWI/SNF-catalyzed nucleosome sliding does not occur solely via a twist-diffusion mechanism. Molecular and Cellular Biology. 22: 7484-90. PMID 12370295 DOI: 10.1128/Mcb.22.21.7484-7490.2002 |
0.599 |
|
| 2002 |
Aoyagi S, Narlikar G, Zheng C, Sif S, Kingston RE, Hayes JJ. Nucleosome remodeling by the human SWI/SNF complex requires transient global disruption of histone-DNA interactions. Molecular and Cellular Biology. 22: 3653-62. PMID 11997502 DOI: 10.1128/Mcb.22.11.3653-3662.2002 |
0.63 |
|
| 2002 |
Ura K, Hayes JJ. Nucleotide excision repair and chromatin remodeling. European Journal of Biochemistry. 269: 2288-93. PMID 11985610 DOI: 10.1046/J.1432-1033.2002.02888.X |
0.582 |
|
| 2002 |
Hayes JJ. Changing chromatin from the inside. Nature Structural Biology. 9: 161-3. PMID 11875512 DOI: 10.1038/Nsb0302-161 |
0.547 |
|
| 2002 |
Hayes JJ, Hansen JC. New insights into unwrapping DNA from the nucleosome from a single-molecule optical tweezers method Proceedings of the National Academy of Sciences of the United States of America. 99: 1752-1754. PMID 11854477 DOI: 10.1073/Pnas.062034799 |
0.595 |
|
| 2001 |
Thiriet C, Hayes JJ. A novel labeling technique reveals a function for histone H2A/H2B dimer tail domains in chromatin assembly in vivo Genes & Development. 15: 2048-2053. PMID 11511536 DOI: 10.1101/Gad.910201 |
0.567 |
|
| 2001 |
Angelov D, Vitolo JM, Mutskov V, Dimitrov S, Hayes JJ. Preferential interaction of the core histone tail domains with linker DNA Proceedings of the National Academy of Sciences of the United States of America. 98: 6599-6604. PMID 11381129 DOI: 10.1073/Pnas.121171498 |
0.666 |
|
| 2001 |
Chafin DR, Hayes JJ. Site-directed cleavage of DNA by linker histone-Fe(II) EDTA conjugates. Methods of Molecular Biology. 148: 275-290. PMID 11357591 DOI: 10.1385/1-59259-208-2:275 |
0.501 |
|
| 2001 |
Hayes JJ, Hansen JC. Nucleosomes and the chromatin fiber Current Opinion in Genetics and Development. 11: 124-129. PMID 11250133 DOI: 10.1016/S0959-437X(00)00168-4 |
0.499 |
|
| 2000 |
Chafin DR, Vitolo JM, Henricksen LA, Bambara RA, Hayes JJ. Human DNA ligase I efficiently seals nicks in nucleosomes. The Embo Journal. 19: 5492-501. PMID 11032816 DOI: 10.1093/Emboj/19.20.5492 |
0.626 |
|
| 2000 |
Fernández De Henestrosa AR, Ogi T, Aoyagi S, Chafin D, Hayes JJ, Ohmori H, Woodgate R. Identification of additional genes belonging to the LexA regulon in Escherichia coli. Molecular Microbiology. 35: 1560-72. PMID 10760155 DOI: 10.1046/J.1365-2958.2000.01826.X |
0.335 |
|
| 2000 |
Widlund HR, Vitolo JM, Thiriet C, Hayes JJ. DNA sequence-dependent contributions of core histone tails to nucleosome stability: Differential effects of acetylation and proteolytic tail removal Biochemistry. 39: 3835-3841. PMID 10736184 DOI: 10.1021/Bi991957L |
0.639 |
|
| 2000 |
Vitolo JM, Thiriet C, Hayes JJ. The H3-H4 N-terminal tail domains are the primary mediators of transcription factor IIIA access to 5S DNA within a nucleosome. Molecular and Cellular Biology. 20: 2167-2175. PMID 10688663 DOI: 10.1128/Mcb.20.6.2167-2175.2000 |
0.709 |
|
| 1999 |
Vitolo JM, Thiriet C, Hayes JJ. DNase I and Hydroxyl Radical Characterization of Chromatin Complexes Current Protocols in Molecular Biology. 48. PMID 18265196 DOI: 10.1002/0471142727.Mb2104S48 |
0.624 |
|
| 1999 |
Chafin DR, Lee K, Hayes JJ. Site-Directed Chemical Probing of Histone-DNA Interactions Methods of Molecular Biology. 119: 27-43. PMID 10804502 DOI: 10.1385/1-59259-681-9:27 |
0.59 |
|
| 1999 |
Lee KM, Sif S, Kingston RE, Hayes JJ. hSWI/SNF disrupts interactions between the H2A N-terminal tail and nucleosomal DNA. Biochemistry. 38: 8423-9. PMID 10387088 DOI: 10.1021/Bi990090O |
0.644 |
|
| 1999 |
Lee K, Chafin DR, Hayes JJ. Targeted cross-linking and DNA cleavage within model chromatin complexes. Methods in Enzymology. 304: 231-251. PMID 10372363 DOI: 10.1016/S0076-6879(99)04014-8 |
0.596 |
|
| 1999 |
Thiriet C, Hayes JJ. Chromatin remodeling by cell cycle stage-specific extracts from Physarum polycephalum. European Journal of Cell Biology. 78: 214-220. PMID 10219572 DOI: 10.1016/S0171-9335(99)80101-0 |
0.431 |
|
| 1999 |
Thiriet C, Hayes JJ. Histone Proteinsin Vivo:Cell-Cycle-Dependent Physiological Effects of Exogenous Linker Histones Incorporated intoPhysarum polycephalum☆ Methods. 17: 140-150. PMID 10075892 DOI: 10.1006/Meth.1998.0725 |
0.518 |
|
| 1999 |
Wolffe AP, Hayes JJ. Chromatin disruption and modification Nucleic Acids Research. 27: 711-720. PMID 9889264 DOI: 10.1093/Nar/27.3.711 |
0.7 |
|
| 1998 |
Thiriet C, Hayes JJ. Functionally Relevant Histone-DNA Interactions Extend Beyond the Classically Defined Nucleosome Core Region Journal of Biological Chemistry. 273: 21352-21358. PMID 9694896 DOI: 10.1074/Jbc.273.33.21352 |
0.644 |
|
| 1998 |
Lee K, Hayes JJ. Linker DNA and H1-dependent reorganization of histone-DNA interactions within the nucleosome. Biochemistry. 37: 8622-8628. PMID 9628723 DOI: 10.1021/Bi980499Y |
0.682 |
|
| 1998 |
Ehmann A, Chafin D, Lee K, Hayes JJ. (1,4,7-trimethyl-1,4,7-triazacyclononane)iron (III)-mediated cleavage of DNA: detection of selected protein-DNA interactions Nucleic Acids Research. 26: 2086-2091. PMID 9547264 DOI: 10.1093/Nar/26.9.2086 |
0.547 |
|
| 1997 |
Lee K, Hayes JJ. The N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core Proceedings of the National Academy of Sciences of the United States of America. 94: 8959-8964. PMID 9256417 DOI: 10.1073/Pnas.94.17.8959 |
0.648 |
|
| 1997 |
Thiriet C, Hayes JJ. Antisera directed against anti-histone H4 antibodies recognize linker histones. Novel immunological probes to detect histone interactions. Journal of Biological Chemistry. 272: 18740-18745. PMID 9228046 DOI: 10.1074/Jbc.272.30.18740 |
0.492 |
|
| 1997 |
Hayes JJ, Lee KM. In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins Methods: a Companion to Methods in Enzymology. 12: 2-9. PMID 9169189 DOI: 10.1006/Meth.1997.0441 |
0.552 |
|
| 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 |
0.777 |
|
| 1996 |
Hayes JJ, Kaplan R, Ura K, Pruss D, Wolffe A. A Putative DNA Binding Surface in the Globular Domain of a Linker Histone Is Not Essential for Specific Binding to the Nucleosome Journal of Biological Chemistry. 271: 25817-25822. PMID 8824211 DOI: 10.1074/Jbc.271.42.25817 |
0.734 |
|
| 1996 |
Hayes JJ. Site-Directed Cleavage of DNA by a Linker Histone−Fe(II) EDTA Conjugate: Localization of a Globular Domain Binding Site within a Nucleosome† Biochemistry. 35: 11931-11937. PMID 8810896 DOI: 10.1021/Bi961590+ |
0.595 |
|
| 1995 |
Hayes JJ. Chemical probes of DNA structure in chromatin Chemistry & Biology. 2: 127-135. PMID 9383414 DOI: 10.1016/1074-5521(95)90066-7 |
0.579 |
|
| 1995 |
Pruss D, Hayes JJ, Wolffe AP. Nucleosomal anatomy – where are the histones? Bioessays. 17: 161-170. PMID 7748166 DOI: 10.1002/Bies.950170211 |
0.693 |
|
| 1995 |
Ura K, Hayes JJ, Wolffe AP. A positive role for nucleosome mobility in the transcriptional activity of chromatin templates: restriction by linker histones. The Embo Journal. 14: 3752-3765. DOI: 10.1002/J.1460-2075.1995.Tb00045.X |
0.73 |
|
| 1994 |
Bauer WR, Hayes JJ, White JH, Wolffe AP. Nucleosome structural changes due to acetylation. Journal of Molecular Biology. 236: 685-90. PMID 8114086 DOI: 10.1006/Jmbi.1994.1180 |
0.74 |
|
| 1994 |
Alfonso PJ, Crippa MP, Hayes JJ, Bustin M. The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits. Journal of Molecular Biology. 236: 189-98. PMID 8107104 DOI: 10.1006/Jmbi.1994.1128 |
0.639 |
|
| 1994 |
Hayes JJ, Pruss D, Wolffe AP. Contacts of the globular domain of histone H5 and core histones with DNA in a "chromatosome" Proceedings of the National Academy of Sciences of the United States of America. 91: 7817-7821. PMID 8052665 DOI: 10.1073/Pnas.91.16.7817 |
0.759 |
|
| 1994 |
Ura K, Wolffe AP, Hayes JJ. Core histone acetylation does not block linker histone binding to a nucleosome including a Xenopus borealis 5 S rRNA gene. Journal of Biological Chemistry. 269: 27171-27174. DOI: 10.1016/s0021-9258(18)46963-3 |
0.671 |
|
| 1994 |
Alfonso PJ, Crippa MP, Hayes JJ, Bustin M. Erratum: The footprint of chromosomal proteins HMG-14 and HMG-17 on chromatin subunits (Journal of Molecular Biology (1994) 236 (189-198)) Journal of Molecular Biology. 239. DOI: 10.1006/Jmbi.1994.1385 |
0.352 |
|
| 1993 |
Lee DY, Hayes JJ, Pruss D, Wolffe AP. A positive role for histone acetylation in transcription factor access to nucleosomal DNA Cell. 72: 73-84. PMID 8422685 DOI: 10.1016/0092-8674(93)90051-Q |
0.783 |
|
| 1993 |
Bashkin J, Hayes JJ, Tullius TD, Wolffe AP. Structure of DNA in a nucleosome core at high salt concentration and at high temperature Biochemistry. 32: 1895-1898. PMID 8383529 DOI: 10.1021/Bi00059A002 |
0.697 |
|
| 1993 |
Hayes JJ, Wolffe AP. Preferential and asymmetric interaction of linker histones with 5S DNA in the nucleosome Proceedings of the National Academy of Sciences of the United States of America. 90: 6415-6419. PMID 8341648 DOI: 10.1073/Pnas.90.14.6415 |
0.783 |
|
| 1993 |
Wolffe AP, Almouzni G, Ura K, Pruss D, Hayes JJ. Transcription Factor Access to DNA in the Nucleosome Cold Spring Harbor Symposia On Quantitative Biology. 58: 225-235. PMID 7956033 DOI: 10.1101/Sqb.1993.058.01.027 |
0.759 |
|
| 1992 |
Hayes JJ, Wolffe AP. Histones H2A/H2B inhibit the interaction of transcription factor IIIA with the Xenopus borealis somatic 5S RNA gene in a nucleosome Proceedings of the National Academy of Sciences of the United States of America. 89: 1229-1233. PMID 1741376 DOI: 10.1073/Pnas.89.4.1229 |
0.751 |
|
| 1992 |
Hayes JJ, Wolffe AP. Experimental determination of DNA helical repeats Trends in Biochemical Sciences. 17: 250-250. PMID 1502726 DOI: 10.1016/0968-0004(92)90403-V |
0.654 |
|
| 1992 |
Hayes JJ, Tullius TD. Structure of the TFIIIA-5 S DNA complex Journal of Molecular Biology. 227: 407-417. PMID 1404361 DOI: 10.1016/0022-2836(92)90897-S |
0.492 |
|
| 1992 |
Hayes JJ, Wolffe AP. The interaction of transcription factors with nucleosomal DNA. Bioessays. 14: 597-603. PMID 1365915 DOI: 10.1002/Bies.950140905 |
0.744 |
|
| 1992 |
Hayes JJ, Clemens KR. Locations of contacts between individual zinc fingers of Xenopus laevis transcription factor IIIA and the internal control region of a 5S RNA gene. Biochemistry. 31: 11600-11605. PMID 1332765 DOI: 10.1021/Bi00161A045 |
0.51 |
|
| 1991 |
Hayes JJ, Scovell WM. cis-Diamminedichloroplatinum (II) modified chromatin and nucleosomal core particle probed with DNase I. Biochimica Et Biophysica Acta. 1088: 413-8. PMID 2015304 DOI: 10.1016/0167-4781(91)90134-8 |
0.562 |
|
| 1991 |
Hayes J, Scovell WM. cis-diamminedichloroplatinum (II) modified chromatin and nucleosomal core particle. Biochimica Et Biophysica Acta. 1089: 377-85. PMID 1859841 DOI: 10.1016/0167-4781(91)90179-P |
0.518 |
|
| 1991 |
Dixon WJ, Hayes JJ, Levin JR, Weidner MF, Dombroski BA, Tullius TD. Hydroxyl radical footprinting. Methods in Enzymology. 208: 380-413. PMID 1664026 DOI: 10.1016/0076-6879(91)08021-9 |
0.495 |
|
| 1991 |
Hayes JJ, Bashkin J, Tullius TD, Wolffe AP. The histone core exerts a dominant constraint on the structure of DNA in a nucleosome. Biochemistry. 30: 8434-40. PMID 1653013 DOI: 10.1021/Bi00098A022 |
0.718 |
|
| 1991 |
Hayes JJ, Clark DJ, Wolffe AP. Histone contributions to the structure of DNA in the nucleosome. Proceedings of the National Academy of Sciences of the United States of America. 88: 6829-33. PMID 1650485 DOI: 10.1073/Pnas.88.15.6829 |
0.745 |
|
| 1990 |
Hayes JJ, Kam L, Tullius TD. Footprinting protein-DNA complexes with γ-rays Methods in Enzymology. 186: 545-549. PMID 2172714 DOI: 10.1016/0076-6879(90)86148-O |
0.433 |
|
| 1990 |
Hayes JJ, Tullius TD, Wolffe AP. The structure of DNA in a nucleosome Proceedings of the National Academy of Sciences of the United States of America. 87: 7405-7409. PMID 2170977 DOI: 10.1073/Pnas.87.19.7405 |
0.721 |
|
| 1990 |
Churchill MEA, Hayes JJ, Tullius TD. Detection of drug binding to DNA by hydroxyl radical footprinting. Relationship of distamycin binding sites to DNA structure and positioned nucleosomes on 5S RNA genes of Xenopus Biochemistry. 29: 6043-6050. PMID 1696501 DOI: 10.1021/Bi00477A023 |
0.451 |
|
| 1989 |
Hayes JJ, Tullius TD. The missing nucleoside experiment: A new technique to study recognition of DNA by protein Biochemistry. 28: 9521-9527. PMID 2611245 DOI: 10.1021/Bi00450A041 |
0.477 |
|
| 1989 |
Hayes J, Tullius TD, Wolffe AP. A Protein-Protein Interaction Is Essential for Stable Complex Formation on a 5 S RNA Gene Journal of Biological Chemistry. 264: 6009-6012. DOI: 10.1016/s0021-9258(18)83302-6 |
0.446 |
|
| Show low-probability matches. |