Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure

Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyc...

Celý popis

Uložené v:

Podrobná bibliografia
Vydané v:	Nature (London) Ročník 544; číslo 7651; s. 440 - 445
Hlavní autori:	Liu, Xiaoyu, Li, Meijing, Xia, Xian, Li, Xueming, Chen, Zhucheng
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	London Nature Publishing Group UK 27.04.2017 Nature Publishing Group
Predmet:	101/28 631/337/100/102 631/535/1258/1259 Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphatases - ultrastructure Amino Acid Sequence ATP Binding Sites Chromatin Chromatin Assembly and Disassembly Cryoelectron Microscopy Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism Enzymes Flexibility Histones - chemistry Histones - metabolism Humanities and Social Sciences Models, Molecular multidisciplinary Nucleosomes - chemistry Nucleosomes - metabolism Nucleosomes - ultrastructure Protein Binding Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - ultrastructure Science Transcription Factors - chemistry Transcription Factors - metabolism Transcription Factors - ultrastructure
ISSN:	0028-0836, 1476-4687, 1476-4687
On-line prístup:	Získať plný text
Tagy:	Pridať tag Žiadne tagy, Buďte prvý, kto otaguje tento záznam!

Abstract	Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyces cerevisiae bound to the nucleosome. The structure shows that the two core domains of Snf2 are realigned upon nucleosome binding, suggesting activation of the enzyme. The core domains contact each other through two induced Brace helices, which are crucial for coupling ATP hydrolysis to chromatin remodelling. Snf2 binds to the phosphate backbones of one DNA gyre of the nucleosome mainly through its helicase motifs within the major domain cleft, suggesting a conserved mechanism of substrate engagement across different remodellers. Snf2 contacts the second DNA gyre via a positively charged surface, providing a mechanism to anchor the remodeller at a fixed position of the nucleosome. Snf2 locally deforms nucleosomal DNA at the site of binding, priming the substrate for the remodelling reaction. Together, these findings provide mechanistic insights into chromatin remodelling. The cryo-electron microscopy structure of Saccharomyces cerevisiae Snf2 chromatin remodeller bound to a nucleosome and a proposed mechanism for DNA translocation by Snf2 are presented. Structure of a chromatin remodeller Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions in order to allow regulatory proteins access to DNA. Here, Zhucheng Chen and colleagues report the cryo-electron microscopy structure of the budding yeast Snf2 chromatin remodeller bound to a nucleosome and propose a mechanism for DNA translocation by Snf2. The remodeller interacts with the nucleosome mainly using helicase motifs and binds the phosphate backbones along the DNA minor groove. Most of the DNA-binding elements within Snf2 are conserved across other families of remodelling enzymes, indicating that this mode of nucleosome engagement is likely to be widespread.
AbstractList	Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyces cerevisiae bound to the nucleosome. The structure shows that the two core domains of Snf2 are realigned upon nucleosome binding, suggesting activation of the enzyme. The core domains contact each other through two induced Brace helices, which are crucial for coupling ATP hydrolysis to chromatin remodelling. Snf2 binds to the phosphate backbones of one DNA gyre of the nucleosome mainly through its helicase motifs within the major domain cleft, suggesting a conserved mechanism of substrate engagement across different remodellers. Snf2 contacts the second DNA gyre via a positively charged surface, providing a mechanism to anchor the remodeller at a fixed position of the nucleosome. Snf2 locally deforms nucleosomal DNA at the site of binding, priming the substrate for the remodelling reaction. Together, these findings provide mechanistic insights into chromatin remodelling. Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyces cerevisiae bound to the nucleosome. The structure shows that the two core domains of Snf2 are realigned upon nucleosome binding, suggesting activation of the enzyme. The core domains contact each other through two induced Brace helices, which are crucial for coupling ATP hydrolysis to chromatin remodelling. Snf2 binds to the phosphate backbones of one DNA gyre of the nucleosome mainly through its helicase motifs within the major domain cleft, suggesting a conserved mechanism of substrate engagement across different remodellers. Snf2 contacts the second DNA gyre via a positively charged surface, providing a mechanism to anchor the remodeller at a fixed position of the nucleosome. Snf2 locally deforms nucleosomal DNA at the site of binding, priming the substrate for the remodelling reaction. Together, these findings provide mechanistic insights into chromatin remodelling.Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyces cerevisiae bound to the nucleosome. The structure shows that the two core domains of Snf2 are realigned upon nucleosome binding, suggesting activation of the enzyme. The core domains contact each other through two induced Brace helices, which are crucial for coupling ATP hydrolysis to chromatin remodelling. Snf2 binds to the phosphate backbones of one DNA gyre of the nucleosome mainly through its helicase motifs within the major domain cleft, suggesting a conserved mechanism of substrate engagement across different remodellers. Snf2 contacts the second DNA gyre via a positively charged surface, providing a mechanism to anchor the remodeller at a fixed position of the nucleosome. Snf2 locally deforms nucleosomal DNA at the site of binding, priming the substrate for the remodelling reaction. Together, these findings provide mechanistic insights into chromatin remodelling. Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyces cerevisiae bound to the nucleosome. The structure shows that the two core domains of Snf2 are realigned upon nucleosome binding, suggesting activation of the enzyme. The core domains contact each other through two induced Brace helices, which are crucial for coupling ATP hydrolysis to chromatin remodelling. Snf2 binds to the phosphate backbones of one DNA gyre of the nucleosome mainly through its helicase motifs within the major domain cleft, suggesting a conserved mechanism of substrate engagement across different remodellers. Snf2 contacts the second DNA gyre via a positively charged surface, providing a mechanism to anchor the remodeller at a fixed position of the nucleosome. Snf2 locally deforms nucleosomal DNA at the site of binding, priming the substrate for the remodelling reaction. Together, these findings provide mechanistic insights into chromatin remodelling. The cryo-electron microscopy structure of Saccharomyces cerevisiae Snf2 chromatin remodeller bound to a nucleosome and a proposed mechanism for DNA translocation by Snf2 are presented. Structure of a chromatin remodeller Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions in order to allow regulatory proteins access to DNA. Here, Zhucheng Chen and colleagues report the cryo-electron microscopy structure of the budding yeast Snf2 chromatin remodeller bound to a nucleosome and propose a mechanism for DNA translocation by Snf2. The remodeller interacts with the nucleosome mainly using helicase motifs and binds the phosphate backbones along the DNA minor groove. Most of the DNA-binding elements within Snf2 are conserved across other families of remodelling enzymes, indicating that this mode of nucleosome engagement is likely to be widespread.
Author	Liu, Xiaoyu Xia, Xian Li, Xueming Li, Meijing Chen, Zhucheng
Author_xml	– sequence: 1 givenname: Xiaoyu surname: Liu fullname: Liu, Xiaoyu organization: Ministry of Education Key Laboratory of Protein Science, Tsinghua University, School of Life Sciences, Tsinghua University, Tsinghua-Peking Joint Center for Life Sciences – sequence: 2 givenname: Meijing surname: Li fullname: Li, Meijing organization: Ministry of Education Key Laboratory of Protein Science, Tsinghua University, School of Life Sciences, Tsinghua University, Tsinghua-Peking Joint Center for Life Sciences – sequence: 3 givenname: Xian surname: Xia fullname: Xia, Xian organization: Ministry of Education Key Laboratory of Protein Science, Tsinghua University, School of Life Sciences, Tsinghua University – sequence: 4 givenname: Xueming surname: Li fullname: Li, Xueming email: lixueming@mail.tsinghua.edu.cn organization: Ministry of Education Key Laboratory of Protein Science, Tsinghua University, School of Life Sciences, Tsinghua University, Tsinghua-Peking Joint Center for Life Sciences – sequence: 5 givenname: Zhucheng surname: Chen fullname: Chen, Zhucheng email: Zhucheng_chen@tsinghua.edu.cn organization: Ministry of Education Key Laboratory of Protein Science, Tsinghua University, School of Life Sciences, Tsinghua University
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/28424519$$D View this record in MEDLINE/PubMed
BookMark	eNpt0U1LxDAQBuAgiruunrxLwYug1Xy0TXKUxS9Y8aCeSzaduF3aRJNU8N-bsgoiSw5J4JnhZeYA7VpnAaFjgi8JZuLKqjh4oBSzagdNScGrvKgE30VTjKnIsWDVBB2EsMYYl4QX-2hCRUGLksgpWjyCXinbhj5zJtMr73oVW5t56F0DXdfat_T-BNVBky2_sriC7NkamttBd-CC6yEL0Q96zHCI9ozqAhz93DP0envzMr_PF093D_PrRa6ZJDEnVJZK4bIUKeay4kVBlrLhlS41cMUqLiiTAIzLxoAhnKWvMaJU2DAstWQzdLbp--7dxwAh1n0bdEqrLLgh1ERIguV4Ej39R9du8DalGxWVDAtZJXXyo4ZlD0397tte-a_6d04JkA3Q3oXgwdS6jWlQzkav2q4muB53Uf_ZRao5_1fz23a7vtjokJR9A_8n6Bb-DZLmmXU
CODEN	NATUAS
CitedBy_id	crossref_primary_10_1016_j_jmb_2022_167581 crossref_primary_10_1016_j_sbi_2018_07_002 crossref_primary_10_1016_j_molcel_2025_04_020 crossref_primary_10_1038_s41594_025_01556_y crossref_primary_10_1091_mbc_E18_05_0331 crossref_primary_10_1038_s41467_024_46178_y crossref_primary_10_1038_s41467_021_24320_4 crossref_primary_10_1088_1674_1056_27_5_058703 crossref_primary_10_3390_microorganisms8071029 crossref_primary_10_1038_s41586_020_2087_1 crossref_primary_10_1074_jbc_M117_798397 crossref_primary_10_1038_s41586_018_0029_y crossref_primary_10_3390_ijms19103049 crossref_primary_10_1038_s41594_018_0023_y crossref_primary_10_1038_s41594_017_0007_3 crossref_primary_10_1016_j_sbi_2021_05_006 crossref_primary_10_1042_EBC20190074 crossref_primary_10_7554_eLife_33442 crossref_primary_10_1016_j_cell_2019_10_044 crossref_primary_10_1016_j_dnarep_2018_08_007 crossref_primary_10_1146_annurev_cancerbio_030617_050151 crossref_primary_10_1007_s13238_018_0524_9 crossref_primary_10_1016_j_sbi_2019_07_011 crossref_primary_10_1016_j_sbi_2019_09_002 crossref_primary_10_1016_j_cell_2019_11_024 crossref_primary_10_1016_j_tibs_2020_08_010 crossref_primary_10_1002_anie_201713158 crossref_primary_10_1016_j_csbj_2022_12_009 crossref_primary_10_1016_j_cell_2018_09_032 crossref_primary_10_1038_s41586_025_09100_0 crossref_primary_10_1016_j_molcel_2019_06_024 crossref_primary_10_3389_fcell_2020_560098 crossref_primary_10_1016_j_cell_2023_08_001 crossref_primary_10_1038_s41467_024_45237_8 crossref_primary_10_1021_jacs_4c14136 crossref_primary_10_1038_s41598_018_19875_0 crossref_primary_10_1016_j_molcel_2017_08_018 crossref_primary_10_7554_eLife_37774 crossref_primary_10_1016_j_cell_2020_09_051 crossref_primary_10_1016_j_seizure_2025_05_019 crossref_primary_10_1002_chem_202203961 crossref_primary_10_1016_j_jmb_2021_166929 crossref_primary_10_1093_nar_gkaa023 crossref_primary_10_1038_s41586_018_0135_x crossref_primary_10_1038_s41588_023_01451_6 crossref_primary_10_1038_s41594_018_0166_x crossref_primary_10_1016_j_bbrc_2020_03_169 crossref_primary_10_1038_s41467_018_06014_6 crossref_primary_10_1016_j_sbi_2018_11_006 crossref_primary_10_1038_s41467_020_19402_8 crossref_primary_10_1098_rsob_220066 crossref_primary_10_1007_s11010_019_03600_0 crossref_primary_10_3390_ijms22010076 crossref_primary_10_1016_j_sbi_2019_10_003 crossref_primary_10_1016_j_molcel_2021_08_010 crossref_primary_10_1126_science_aay0033 crossref_primary_10_1101_gad_348897_121 crossref_primary_10_1016_j_molcel_2017_10_017 crossref_primary_10_3390_ijms22115578 crossref_primary_10_7554_eLife_87672_3 crossref_primary_10_1007_s00294_020_01072_0 crossref_primary_10_1016_j_molcel_2020_09_024 crossref_primary_10_1093_lifemeta_loaf013 crossref_primary_10_1093_nar_gkz670 crossref_primary_10_1101_gad_326066_119 crossref_primary_10_7554_eLife_35720 crossref_primary_10_1080_21501203_2024_2425170 crossref_primary_10_1002_1873_3468_12973 crossref_primary_10_1007_s00428_020_02839_z crossref_primary_10_1038_s41594_019_0199_9 crossref_primary_10_1038_s41467_019_10247_4 crossref_primary_10_15252_embj_2020105907 crossref_primary_10_3389_freae_2023_1245832 crossref_primary_10_7554_eLife_46057 crossref_primary_10_1126_science_aat7716 crossref_primary_10_1002_pro_3535 crossref_primary_10_1038_s41477_024_01640_z crossref_primary_10_1074_jbc_RA119_009782 crossref_primary_10_21641_los_2025_22_1_262 crossref_primary_10_1038_s41467_022_35002_0 crossref_primary_10_1038_s41594_021_00719_x crossref_primary_10_1038_s41467_018_04503_2 crossref_primary_10_1038_s41467_021_27295_4 crossref_primary_10_1038_s41594_020_00528_8 crossref_primary_10_1002_bies_201900234 crossref_primary_10_1038_s41586_018_0021_6 crossref_primary_10_12688_f1000research_21933_1 crossref_primary_10_1016_j_jmb_2020_09_007 crossref_primary_10_1038_s41594_022_00779_7 crossref_primary_10_1038_s41594_023_00966_0 crossref_primary_10_1038_s41467_020_17457_1 crossref_primary_10_1016_j_dnarep_2021_103201 crossref_primary_10_1093_nar_gkaf734 crossref_primary_10_1126_science_abf8705 crossref_primary_10_1038_s41467_018_03677_z crossref_primary_10_1371_journal_pcbi_1006512 crossref_primary_10_1016_j_bpj_2017_12_008 crossref_primary_10_1038_nature24658 crossref_primary_10_1093_nar_gky206 crossref_primary_10_1038_s41467_020_17959_y crossref_primary_10_1093_pcp_pcaf075 crossref_primary_10_1038_s41467_024_49465_w crossref_primary_10_1038_nsmb_3415 crossref_primary_10_1038_s41594_017_0005_5 crossref_primary_10_1038_s41422_025_01103_w crossref_primary_10_1038_s41586_022_04658_5 crossref_primary_10_1038_s41594_018_0115_8 crossref_primary_10_1038_s41586_019_1029_2 crossref_primary_10_1016_j_sbi_2020_06_024 crossref_primary_10_1186_s13072_019_0264_y crossref_primary_10_1042_EBC20180059 crossref_primary_10_1007_s12013_023_01140_5 crossref_primary_10_1042_BST20180043 crossref_primary_10_1038_s41392_022_01251_0 crossref_primary_10_1016_j_sbi_2020_06_008 crossref_primary_10_1016_j_tibs_2019_09_002 crossref_primary_10_1038_s41467_019_12007_w crossref_primary_10_1146_annurev_biophys_082520_080201 crossref_primary_10_1186_s12967_025_07004_1 crossref_primary_10_1016_j_bbrc_2022_02_007 crossref_primary_10_7554_eLife_87672 crossref_primary_10_1038_s41594_023_01174_6 crossref_primary_10_1016_j_pbiomolbio_2017_12_006 crossref_primary_10_1042_BST20230070 crossref_primary_10_7554_eLife_34100 crossref_primary_10_1002_ange_201713158 crossref_primary_10_1088_1751_8121_aafea0 crossref_primary_10_26508_lsa_202201790 crossref_primary_10_1016_j_sbi_2019_11_013 crossref_primary_10_1016_j_bbagrm_2022_194851 crossref_primary_10_1126_science_aaz9761 crossref_primary_10_7554_eLife_71420 crossref_primary_10_1107_S2053230X24004655 crossref_primary_10_1016_j_chemosphere_2019_03_096 crossref_primary_10_3390_biology9070146 crossref_primary_10_1016_j_sbi_2019_05_017 crossref_primary_10_1038_s44318_025_00407_2 crossref_primary_10_1016_j_bpc_2020_106436 crossref_primary_10_1016_j_jmb_2021_166876 crossref_primary_10_1073_pnas_1818163116 crossref_primary_10_1016_j_jbc_2021_101145 crossref_primary_10_1038_s41467_020_20538_w crossref_primary_10_1042_BST20210773 crossref_primary_10_1074_jbc_RA120_013196 crossref_primary_10_1016_j_cell_2024_09_007 crossref_primary_10_1038_s41564_019_0524_4 crossref_primary_10_1038_s41467_019_09657_1 crossref_primary_10_7554_eLife_54449 crossref_primary_10_1016_j_pharmthera_2019_107406 crossref_primary_10_1038_s42003_017_0002_6 crossref_primary_10_1038_nature24046 crossref_primary_10_1091_mbc_E23_05_0197 crossref_primary_10_7554_eLife_56178 crossref_primary_10_1111_mmi_14272 crossref_primary_10_1038_s41598_017_17284_3 crossref_primary_10_1126_science_adu5654 crossref_primary_10_1038_s41580_023_00683_y crossref_primary_10_3389_fmolb_2022_1070489 crossref_primary_10_1016_j_sbi_2019_03_010 crossref_primary_10_1093_nar_gky158 crossref_primary_10_1126_science_adf4197 crossref_primary_10_1038_s41467_023_40386_8 crossref_primary_10_1038_nrm_2017_26 crossref_primary_10_1038_s41467_020_15183_2
Cites_doi	10.1016/j.sbi.2010.11.006 10.1016/S0076-6879(10)81005-5 10.1128/MCB.00693-08 10.1038/nsmb.1403 10.1016/j.jsb.2015.09.003 10.1146/annurev.biochem.71.110601.135400 10.1016/j.cell.2013.08.016 10.1038/nature08621 10.7554/eLife.10051 10.1107/S0907444912001308 10.1038/ncomms8108 10.1038/38444 10.1016/j.molcel.2005.02.024 10.1038/nsmb.3259 10.1038/nsmb.2457 10.1038/nsmb1071 10.1128/MCB.25.14.5880-5892.2005 10.1038/nrm1945 10.1038/nature09947 10.1093/nar/gks007 10.1016/j.molcel.2016.03.032 10.1038/nsmb973 10.1016/S1047-8477(03)00069-8 10.1146/annurev.biochem.77.062706.153223 10.1016/j.cell.2013.07.011 10.7554/eLife.11182 10.1073/pnas.0913380107 10.1007/978-1-60761-842-3_9 10.1002/jcc.20084 10.1006/jmbi.1997.1494 10.1038/nature11625 10.1038/nmeth.2115 10.1038/nmeth.2472 10.1016/j.str.2004.12.008 10.1038/nsmb.2648 10.1016/j.molcel.2010.08.012 10.1016/j.cell.2013.08.018 10.1038/nature09321 10.1016/j.jmb.2007.02.062 10.1038/nature20590 10.1016/j.cell.2005.03.026 10.1006/jsbi.1996.0030 10.1016/j.str.2015.06.026 10.1016/j.sbi.2011.10.002
ContentType	Journal Article
Copyright	Macmillan Publishers Limited, part of Springer Nature. All rights reserved. 2017 Copyright Nature Publishing Group Apr 27, 2017
Copyright_xml	– notice: Macmillan Publishers Limited, part of Springer Nature. All rights reserved. 2017 – notice: Copyright Nature Publishing Group Apr 27, 2017
DBID	AAYXX CITATION CGR CUY CVF ECM EIF NPM 3V. 7QG 7QL 7QP 7QR 7RV 7SN 7SS 7ST 7T5 7TG 7TK 7TM 7TO 7U9 7X2 7X7 7XB 88A 88E 88G 88I 8AF 8AO 8C1 8FD 8FE 8FG 8FH 8FI 8FJ 8FK 8G5 ABJCF ABUWG AEUYN AFKRA ARAPS ATCPS AZQEC BBNVY BEC BENPR BGLVJ BHPHI BKSAR C1K CCPQU D1I DWQXO FR3 FYUFA GHDGH GNUQQ GUQSH H94 HCIFZ K9. KB. KB0 KL. L6V LK8 M0K M0S M1P M2M M2O M2P M7N M7P M7S MBDVC NAPCQ P5Z P62 P64 PATMY PCBAR PDBOC PHGZM PHGZT PJZUB PKEHL PPXIY PQEST PQGLB PQQKQ PQUKI PRINS PSYQQ PTHSS PYCSY Q9U R05 RC3 S0X SOI 7X8
DOI	10.1038/nature22036
DatabaseName	CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed ProQuest Central (Corporate) Animal Behavior Abstracts Bacteriology Abstracts (Microbiology B) Calcium & Calcified Tissue Abstracts Chemoreception Abstracts Nursing & Allied Health Database Ecology Abstracts Entomology Abstracts (Full archive) Environment Abstracts Immunology Abstracts Meteorological & Geoastrophysical Abstracts Neurosciences Abstracts Nucleic Acids Abstracts Oncogenes and Growth Factors Abstracts Virology and AIDS Abstracts Agricultural Science Collection Health & Medical Collection ProQuest Central (purchase pre-March 2016) Biology Database (Alumni Edition) Medical Database (Alumni Edition) Psychology Database (Alumni) Science Database (Alumni Edition) STEM Database ProQuest Pharma Collection Public Health Database Technology Research Database ProQuest SciTech Collection ProQuest Technology Collection ProQuest Natural Science Collection Hospital Premium Collection Hospital Premium Collection (Alumni Edition) ProQuest Central (Alumni) (purchase pre-March 2016) ProQuest Research Library Materials Science & Engineering Collection (ProQuest) ProQuest Central (Alumni) ProQuest One Sustainability ProQuest Central UK/Ireland Advanced Technologies & Aerospace Collection (ProQuest) Agricultural & Environmental Science Collection ProQuest Central Essentials - QC Biological Science Collection (ProQuest) eLibrary ProQuest Central Technology collection Natural Science Collection (ProQuest) Earth, Atmospheric & Aquatic Science Collection Environmental Sciences and Pollution Management ProQuest One Community College ProQuest Materials Science Collection ProQuest Central Engineering Research Database Health Research Premium Collection Health Research Premium Collection (Alumni) ProQuest Central Student Research Library Prep AIDS and Cancer Research Abstracts SciTech Premium Collection (ProQuest) ProQuest Health & Medical Complete (Alumni) Materials Science Database Nursing & Allied Health Database (Alumni Edition) Meteorological & Geoastrophysical Abstracts - Academic ProQuest Engineering Collection Biological Sciences Agriculture Science Database Health & Medical Collection (Alumni) Medical Database Psychology Database Research Library Science Database (ProQuest) Algology Mycology and Protozoology Abstracts (Microbiology C) Biological Science Database Engineering Database Research Library (Corporate) Nursing & Allied Health Premium Advanced Technologies & Aerospace Database (ProQuest) ProQuest Advanced Technologies & Aerospace Collection Biotechnology and BioEngineering Abstracts Environmental Science Database Earth, Atmospheric & Aquatic Science Database Materials Science Collection ProQuest Central Premium ProQuest One Academic ProQuest Health & Medical Research Collection ProQuest One Academic Middle East (New) ProQuest One Health & Nursing ProQuest One Academic Eastern Edition (DO NOT USE) ProQuest One Applied & Life Sciences ProQuest One Academic (retired) ProQuest One Academic UKI Edition ProQuest Central China One Psychology Engineering Collection (ProQuest) Environmental Science Collection ProQuest Central Basic University of Michigan Genetics Abstracts SIRS Editorial Environment Abstracts MEDLINE - Academic
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Agricultural Science Database ProQuest One Psychology Research Library Prep ProQuest Central Student Oncogenes and Growth Factors Abstracts ProQuest Advanced Technologies & Aerospace Collection ProQuest Central Essentials Nucleic Acids Abstracts elibrary ProQuest AP Science SciTech Premium Collection ProQuest Central China Environmental Sciences and Pollution Management ProQuest One Applied & Life Sciences ProQuest One Sustainability Health Research Premium Collection Meteorological & Geoastrophysical Abstracts Natural Science Collection Health & Medical Research Collection Biological Science Collection Chemoreception Abstracts ProQuest Central (New) ProQuest Medical Library (Alumni) Engineering Collection Advanced Technologies & Aerospace Collection Engineering Database Virology and AIDS Abstracts ProQuest Science Journals (Alumni Edition) ProQuest Biological Science Collection ProQuest One Academic Eastern Edition Earth, Atmospheric & Aquatic Science Database Agricultural Science Collection ProQuest Hospital Collection ProQuest Technology Collection Health Research Premium Collection (Alumni) Biological Science Database Ecology Abstracts Neurosciences Abstracts ProQuest Hospital Collection (Alumni) Biotechnology and BioEngineering Abstracts Environmental Science Collection Entomology Abstracts Nursing & Allied Health Premium ProQuest Health & Medical Complete ProQuest One Academic UKI Edition Environmental Science Database ProQuest Nursing & Allied Health Source (Alumni) Engineering Research Database ProQuest One Academic Calcium & Calcified Tissue Abstracts Meteorological & Geoastrophysical Abstracts - Academic ProQuest One Academic (New) University of Michigan Technology Collection Technology Research Database ProQuest One Academic Middle East (New) SIRS Editorial Materials Science Collection ProQuest Health & Medical Complete (Alumni) ProQuest Central (Alumni Edition) ProQuest One Community College ProQuest One Health & Nursing Research Library (Alumni Edition) ProQuest Natural Science Collection ProQuest Pharma Collection ProQuest Biology Journals (Alumni Edition) ProQuest Central Earth, Atmospheric & Aquatic Science Collection ProQuest Health & Medical Research Collection Genetics Abstracts ProQuest Engineering Collection Health and Medicine Complete (Alumni Edition) ProQuest Central Korea Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) Agricultural & Environmental Science Collection AIDS and Cancer Research Abstracts Materials Science Database ProQuest Research Library ProQuest Materials Science Collection ProQuest Public Health ProQuest Central Basic ProQuest Science Journals ProQuest Nursing & Allied Health Source ProQuest Psychology Journals (Alumni) ProQuest SciTech Collection Advanced Technologies & Aerospace Database ProQuest Medical Library ProQuest Psychology Journals Animal Behavior Abstracts Materials Science & Engineering Collection Immunology Abstracts Environment Abstracts ProQuest Central (Alumni) MEDLINE - Academic
DatabaseTitleList	MEDLINE Agricultural Science Database MEDLINE - Academic
Database_xml	– sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: PATMY name: Environmental Science Database url: http://search.proquest.com/environmentalscience sourceTypes: Aggregation Database
DeliveryMethod	fulltext_linktorsrc
Discipline	Sciences (General) Physics
EISSN	1476-4687
EndPage	445
ExternalDocumentID	4322080305 28424519 10_1038_nature22036
Genre	Research Support, Non-U.S. Gov't Journal Article
GroupedDBID	--- --Z -DZ -ET -~X .55 .CO .XZ 07C 0R~ 0WA 123 186 1OL 1VR 29M 2KS 2XV 39C 3V. 41X 53G 5RE 6TJ 70F 7RV 7X2 7X7 7XC 85S 88A 88E 88I 8AF 8AO 8C1 8CJ 8FE 8FG 8FH 8FI 8FJ 8G5 8R4 8R5 8WZ 97F 97L A6W A7Z AAEEF AAHBH AAHTB AAIKC AAKAB AAMNW AASDW AAYEP AAYZH AAZLF ABDQB ABFSI ABIVO ABJCF ABJNI ABLJU ABOCM ABPEJ ABPPZ ABUWG ABWJO ABZEH ACBEA ACBWK ACGFO ACGFS ACGOD ACIWK ACKOT ACMJI ACNCT ACPRK ACWUS ADBBV ADFRT ADUKH AENEX AEUYN AFFNX AFKRA AFLOW AFRAH AFSHS AGAYW AGHSJ AGHTU AGNAY AGSOS AHMBA AHSBF AIDAL AIDUJ ALFFA ALIPV ALMA_UNASSIGNED_HOLDINGS AMTXH ARAPS ARMCB ASPBG ATCPS ATWCN AVWKF AXYYD AZFZN AZQEC BBNVY BCU BEC BENPR BGLVJ BHPHI BIN BKEYQ BKKNO BKSAR BPHCQ BVXVI CCPQU CJ0 CS3 D1I D1J D1K DU5 DWQXO E.- E.L EAP EBS EE. EJD EMH EPS ESX EX3 EXGXG F5P FEDTE FQGFK FSGXE FYUFA GNUQQ GUQSH HCIFZ HG6 HMCUK HVGLF HZ~ I-F IAO ICQ IEA IEP IGS IH2 IHR INH INR IOF IPY ISR ITC K6- KB. KOO L6V L7B LK5 LK8 LSO M0K M0L M1P M2M M2O M2P M7P M7R M7S N9A NAPCQ NEJ NEPJS O9- OBC OES OHH OMK OVD P2P P62 PATMY PCBAR PDBOC PKN PQQKQ PROAC PSQYO PSYQQ PTHSS PYCSY Q2X R05 RND RNS RNT RNTTT RXW S0X SC5 SHXYY SIXXV SJFOW SJN SNYQT SOJ SV3 TAE TAOOD TBHMF TDRGL TEORI TN5 TSG TWZ U5U UIG UKHRP UKR UMD UQL VQA VVN WH7 WOW X7M XIH XKW XZL Y6R YAE YCJ YFH YIF YIN YNT YOC YQT YR2 YR5 YXB YZZ Z5M ZCA ZE2 ~02 ~7V ~88 ~KM AARCD AAYXX ABFSG ABUFD ACSTC ADXHL AETEA AFANA AFFHD AGSTI ALPWD ATHPR CITATION PHGZM PHGZT PJZUB PPXIY PQGLB TUS CGR CUY CVF ECM EIF NPM 7QG 7QL 7QP 7QR 7SN 7SS 7ST 7T5 7TG 7TK 7TM 7TO 7U9 7XB 8FD 8FK ADGHP C1K FR3 H94 K9. KL. M7N MBDVC P64 PKEHL PQEST PQUKI PRINS Q9U RC3 SOI 7X8
ID	FETCH-LOGICAL-c391t-1295aa0558687b67441b9d76c5ce7a3678239ee379dfef173239ff85a0f309c93
IEDL.DBID	P5Z
ISICitedReferencesCount	176
ISICitedReferencesURI	http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=000400051900035&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
ISSN	0028-0836 1476-4687
IngestDate	Sun Nov 09 09:30:56 EST 2025 Tue Oct 07 06:50:42 EDT 2025 Wed Feb 19 02:16:03 EST 2025 Sat Nov 29 02:12:21 EST 2025 Tue Nov 18 22:25:23 EST 2025 Fri Feb 21 02:38:42 EST 2025
IsPeerReviewed	true
IsScholarly	true
Issue	7651
Language	English
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c391t-1295aa0558687b67441b9d76c5ce7a3678239ee379dfef173239ff85a0f309c93
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
PMID	28424519
PQID	1892930896
PQPubID	40569
PageCount	6
ParticipantIDs	proquest_miscellaneous_1891090909 proquest_journals_1892930896 pubmed_primary_28424519 crossref_citationtrail_10_1038_nature22036 crossref_primary_10_1038_nature22036 springer_journals_10_1038_nature22036
PublicationCentury	2000
PublicationDate	2017-04-27
PublicationDateYYYYMMDD	2017-04-27
PublicationDate_xml	– month: 04 year: 2017 text: 2017-04-27 day: 27
PublicationDecade	2010
PublicationPlace	London
PublicationPlace_xml	– name: London – name: England
PublicationSubtitle	International weekly journal of science
PublicationTitle	Nature (London)
PublicationTitleAbbrev	Nature
PublicationTitleAlternate	Nature
PublicationYear	2017
Publisher	Nature Publishing Group UK Nature Publishing Group
Publisher_xml	– name: Nature Publishing Group UK – name: Nature Publishing Group
References	Lowary, Widom (CR17) 1998; 276 Makde, England, Yennawar, Tan (CR21) 2010; 467 Dürr, Körner, Müller, Hickmann, Hopfner (CR26) 2005; 121 Narlikar, Sundaramoorthy, Owen-Hughes (CR2) 2013; 154 Becker, Hörz (CR5) 2002; 71 Tan, Davey (CR31) 2011; 21 Racki (CR15) 2009; 462 Watanabe (CR11) 2015; 6 Nguyen (CR13) 2013; 154 Mueller-Planitz, Klinker, Becker (CR6) 2013; 20 Saha, Wittmeyer, Cairns (CR28) 2005; 12 Stark (CR34) 2010; 481 Saha, Wittmeyer, Cairns (CR4) 2006; 7 Fan, Trotter, Archer, Kingston (CR24) 2005; 17 Li (CR40) 2013; 10 Zofall, Persinger, Kassabov, Bartholomew (CR18) 2006; 13 Luger, Mäder, Richmond, Sargent, Richmond (CR3) 1997; 389 Yamada (CR14) 2011; 472 Clapier (CR22) 2016; 62 Leschziner, Lemon, Tjian, Nogales (CR16) 2005; 13 Harada (CR30) 2016; 5 Xia, Liu, Li, Fang, Chen (CR7) 2016; 23 Leschziner (CR10) 2011; 21 Dechassa (CR19) 2012; 40 Clapier, Cairns (CR25) 2012; 492 Mueller-Planitz, Klinker, Ludwigsen, Becker (CR32) 2013; 20 Szerlong (CR23) 2008; 15 Li, Zheng, Agard, Cheng (CR35) 2015; 192 Afonine (CR44) 2012; 68 Hauk, McKnight, Nodelman, Bowman (CR8) 2010; 39 Tosi (CR12) 2013; 154 Dechassa (CR20) 2008; 28 Ong, Richmond, Davey (CR33) 2007; 368 Ludtke (CR37) 2010; 673 Clapier, Cairns (CR1) 2009; 78 Smith, Peterson (CR27) 2005; 25 Mindell, Grigorieff (CR36) 2003; 142 Bharat, Russo, Löwe, Passmore, Scheres (CR38) 2015; 23 Scheres, Chen (CR41) 2012; 9 Bai, Rajendra, Yang, Shi, Scheres (CR42) 2015; 4 Yan, Wang, Tian, Xia, Chen (CR9) 2016; 540 Gu, Rice (CR29) 2010; 107 Pettersen (CR43) 2004; 25 Frank (CR39) 1996; 116 A Saha (BFnature22036_CR28) 2005; 12 X Xia (BFnature22036_CR7) 2016; 23 CR Clapier (BFnature22036_CR1) 2009; 78 CL Smith (BFnature22036_CR27) 2005; 25 X Li (BFnature22036_CR40) 2013; 10 VQ Nguyen (BFnature22036_CR13) 2013; 154 A Saha (BFnature22036_CR4) 2006; 7 L Yan (BFnature22036_CR9) 2016; 540 H Dürr (BFnature22036_CR26) 2005; 121 PB Becker (BFnature22036_CR5) 2002; 71 AE Leschziner (BFnature22036_CR10) 2011; 21 H Szerlong (BFnature22036_CR23) 2008; 15 SJ Ludtke (BFnature22036_CR37) 2010; 673 S Tan (BFnature22036_CR31) 2011; 21 J Frank (BFnature22036_CR39) 1996; 116 S Watanabe (BFnature22036_CR11) 2015; 6 A Tosi (BFnature22036_CR12) 2013; 154 JA Mindell (BFnature22036_CR36) 2003; 142 CR Clapier (BFnature22036_CR22) 2016; 62 X Li (BFnature22036_CR35) 2015; 192 K Yamada (BFnature22036_CR14) 2011; 472 F Mueller-Planitz (BFnature22036_CR32) 2013; 20 GJ Narlikar (BFnature22036_CR2) 2013; 154 K Luger (BFnature22036_CR3) 1997; 389 AE Leschziner (BFnature22036_CR16) 2005; 13 HY Fan (BFnature22036_CR24) 2005; 17 G Hauk (BFnature22036_CR8) 2010; 39 MS Ong (BFnature22036_CR33) 2007; 368 M Zofall (BFnature22036_CR18) 2006; 13 EF Pettersen (BFnature22036_CR43) 2004; 25 TA Bharat (BFnature22036_CR38) 2015; 23 F Mueller-Planitz (BFnature22036_CR6) 2013; 20 ML Dechassa (BFnature22036_CR19) 2012; 40 BT Harada (BFnature22036_CR30) 2016; 5 H Stark (BFnature22036_CR34) 2010; 481 SH Scheres (BFnature22036_CR41) 2012; 9 ML Dechassa (BFnature22036_CR20) 2008; 28 M Gu (BFnature22036_CR29) 2010; 107 CR Clapier (BFnature22036_CR25) 2012; 492 PV Afonine (BFnature22036_CR44) 2012; 68 LR Racki (BFnature22036_CR15) 2009; 462 PT Lowary (BFnature22036_CR17) 1998; 276 XC Bai (BFnature22036_CR42) 2015; 4 RD Makde (BFnature22036_CR21) 2010; 467 15780937 - Mol Cell. 2005 Mar 18;17(6):805-15 23202585 - Nat Struct Mol Biol. 2013 Jan;20(1):82-9 22298509 - Nucleic Acids Res. 2012 May;40(10):4412-21 23644547 - Nat Methods. 2013 Jun;10(6):584-90 21525927 - Nature. 2011 Apr 28;472(7344):448-53 12045097 - Annu Rev Biochem. 2002;71:247-73 20739938 - Nature. 2010 Sep 30;467(7315):562-6 12781660 - J Struct Biol. 2003 Jun;142(3):334-47 25964121 - Nat Commun. 2015 May 12;6:7108 18408732 - Nat Struct Mol Biol. 2008 May;15(5):469-76 22040801 - Curr Opin Struct Biol. 2011 Dec;21(6):709-18 27919072 - Nature. 2016 Dec 15;540(7633):466-469 24034246 - Cell. 2013 Sep 12;154(6):1220-31 16723979 - Nat Rev Mol Cell Biol. 2006 Jun;7(6):437-47 20887855 - Methods Enzymol. 2010;481:109-26 22842542 - Nat Methods. 2012 Sep;9(9):853-4 26623517 - Elife. 2015 Dec 01;4:null 24034245 - Cell. 2013 Sep 12;154(6):1207-19 27153540 - Mol Cell. 2016 May 5;62(3):453-61 15698570 - Structure. 2005 Feb;13(2):267-75 20033039 - Nature. 2009 Dec 24;462(7276):1016-21 20835797 - Methods Mol Biol. 2010;673:157-73 8742743 - J Struct Biol. 1996 Jan-Feb;116(1):190-9 15264254 - J Comput Chem. 2004 Oct;25(13):1605-12 16086025 - Nat Struct Mol Biol. 2005 Sep;12(9):747-55 19355820 - Annu Rev Biochem. 2009;78:273-304 21176878 - Curr Opin Struct Biol. 2011 Feb;21(1):128-36 26256537 - Structure. 2015 Sep 1;23(9):1743-53 20080715 - Proc Natl Acad Sci U S A. 2010 Jan 12;107(2):521-8 23143334 - Nature. 2012 Dec 13;492(7428):280-4 17379244 - J Mol Biol. 2007 May 11;368(4):1067-74 26370395 - J Struct Biol. 2015 Nov;192(2):174-8 24008565 - Nat Struct Mol Biol. 2013 Sep;20(9):1026-32 27399259 - Nat Struct Mol Biol. 2016 Aug;23(8):722-9 18644858 - Mol Cell Biol. 2008 Oct;28(19):6010-21 15988005 - Mol Cell Biol. 2005 Jul;25(14):5880-92 15882619 - Cell. 2005 May 6;121(3):363-73 9514715 - J Mol Biol. 1998 Feb 13;276(1):19-42 26895087 - Elife. 2016 Feb 19;5:null 20832723 - Mol Cell. 2010 Sep 10;39(5):711-23 22505256 - Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):352-67 23911317 - Cell. 2013 Aug 1;154(3):490-503 9305837 - Nature. 1997 Sep 18;389(6648):251-60 16518397 - Nat Struct Mol Biol. 2006 Apr;13(4):339-46
References_xml	– volume: 21 start-page: 128 year: 2011 end-page: 136 ident: CR31 article-title: Nucleosome structural studies publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2010.11.006 – volume: 481 start-page: 109 year: 2010 end-page: 126 ident: CR34 article-title: GraFix: stabilization of fragile macromolecular complexes for single particle cryo-EM publication-title: Methods Enzymol doi: 10.1016/S0076-6879(10)81005-5 – volume: 28 start-page: 6010 year: 2008 end-page: 6021 ident: CR20 article-title: Architecture of the SWI/SNF-nucleosome complex publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.00693-08 – volume: 15 start-page: 469 year: 2008 end-page: 476 ident: CR23 article-title: The HSA domain binds nuclear actin-related proteins to regulate chromatin-remodeling ATPases. publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb.1403 – volume: 192 start-page: 174 year: 2015 end-page: 178 ident: CR35 article-title: Asynchronous data acquisition and on-the-fly analysis of dose fractionated cryoEM images by UCSFImage publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.09.003 – volume: 71 start-page: 247 year: 2002 end-page: 273 ident: CR5 article-title: ATP-dependent nucleosome remodeling publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.71.110601.135400 – volume: 154 start-page: 1207 year: 2013 end-page: 1219 ident: CR12 article-title: Structure and subunit topology of the INO80 chromatin remodeler and its nucleosome complex publication-title: Cell doi: 10.1016/j.cell.2013.08.016 – volume: 462 start-page: 1016 year: 2009 end-page: 1021 ident: CR15 article-title: The chromatin remodeller ACF acts as a dimeric motor to space nucleosomes publication-title: Nature doi: 10.1038/nature08621 – volume: 5 start-page: 5 year: 2016 ident: CR30 article-title: Stepwise nucleosome translocation by RSC remodeling complexes. publication-title: eLife doi: 10.7554/eLife.10051 – volume: 68 start-page: 352 year: 2012 end-page: 367 ident: CR44 article-title: Towards automated crystallographic structure refinement with phenix.refine publication-title: Acta Crystallogr. D doi: 10.1107/S0907444912001308 – volume: 6 start-page: 7108 year: 2015 ident: CR11 article-title: Structural analyses of the chromatin remodelling enzymes INO80-C and SWR-C publication-title: Nature Commun doi: 10.1038/ncomms8108 – volume: 389 start-page: 251 year: 1997 end-page: 260 ident: CR3 article-title: Crystal structure of the nucleosome core particle at 2.8 Å resolution publication-title: Nature doi: 10.1038/38444 – volume: 17 start-page: 805 year: 2005 end-page: 815 ident: CR24 article-title: Swapping function of two chromatin remodeling complexes publication-title: Mol. Cell doi: 10.1016/j.molcel.2005.02.024 – volume: 23 start-page: 722 year: 2016 end-page: 729 ident: CR7 article-title: Structure of chromatin remodeler Swi2/Snf2 in the resting state publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb.3259 – volume: 20 start-page: 82 year: 2013 end-page: 89 ident: CR32 article-title: The ATPase domain of ISWI is an autonomous nucleosome remodeling machine publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb.2457 – volume: 13 start-page: 339 year: 2006 end-page: 346 ident: CR18 article-title: Chromatin remodeling by ISW2 and SWI/SNF requires DNA translocation inside the nucleosome. publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb1071 – volume: 25 start-page: 5880 year: 2005 end-page: 5892 ident: CR27 article-title: A conserved Swi2/Snf2 ATPase motif couples ATP hydrolysis to chromatin remodeling publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.25.14.5880-5892.2005 – volume: 7 start-page: 437 year: 2006 end-page: 447 ident: CR4 article-title: Chromatin remodelling: the industrial revolution of DNA around histones publication-title: Nature Rev. Mol. Cell Biol. doi: 10.1038/nrm1945 – volume: 472 start-page: 448 year: 2011 end-page: 453 ident: CR14 article-title: Structure and mechanism of the chromatin remodelling factor ISW1a publication-title: Nature doi: 10.1038/nature09947 – volume: 40 start-page: 4412 year: 2012 end-page: 4421 ident: CR19 article-title: Disparity in the DNA translocase domains of SWI/SNF and ISW2 publication-title: Nucleic Acids Res doi: 10.1093/nar/gks007 – volume: 62 start-page: 453 year: 2016 end-page: 461 ident: CR22 article-title: Regulation of DNA translocation efficiency within the chromatin remodeler RSC/Sth1 potentiates nucleosome sliding and ejection publication-title: Mol. Cell doi: 10.1016/j.molcel.2016.03.032 – volume: 12 start-page: 747 year: 2005 end-page: 755 ident: CR28 article-title: Chromatin remodeling through directional DNA translocation from an internal nucleosomal site. publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb973 – volume: 142 start-page: 334 year: 2003 end-page: 347 ident: CR36 article-title: Accurate determination of local defocus and specimen tilt in electron microscopy publication-title: J. Struct. Biol. doi: 10.1016/S1047-8477(03)00069-8 – volume: 78 start-page: 273 year: 2009 end-page: 304 ident: CR1 article-title: The biology of chromatin remodeling complexes publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.77.062706.153223 – volume: 154 start-page: 490 year: 2013 end-page: 503 ident: CR2 article-title: Mechanisms and functions of ATP-dependent chromatin-remodeling enzymes publication-title: Cell doi: 10.1016/j.cell.2013.07.011 – volume: 4 start-page: 4 year: 2015 ident: CR42 article-title: Sampling the conformational space of the catalytic subunit of human γ-secretase. publication-title: eLife doi: 10.7554/eLife.11182 – volume: 107 start-page: 521 year: 2010 end-page: 528 ident: CR29 article-title: Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0913380107 – volume: 673 start-page: 157 year: 2010 end-page: 173 ident: CR37 article-title: 3-D structures of macromolecules using single-particle analysis in EMAN publication-title: Methods Mol. Biol doi: 10.1007/978-1-60761-842-3_9 – volume: 25 start-page: 1605 year: 2004 end-page: 1612 ident: CR43 article-title: UCSF Chimera—a visualization system for exploratory research and analysis publication-title: J. Comput. Chem. doi: 10.1002/jcc.20084 – volume: 276 start-page: 19 year: 1998 end-page: 42 ident: CR17 article-title: New DNA sequence rules for high affinity binding to histone octamer and sequence-directed nucleosome positioning publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1997.1494 – volume: 492 start-page: 280 year: 2012 end-page: 284 ident: CR25 article-title: Regulation of ISWI involves inhibitory modules antagonized by nucleosomal epitopes publication-title: Nature doi: 10.1038/nature11625 – volume: 9 start-page: 853 year: 2012 end-page: 854 ident: CR41 article-title: Prevention of overfitting in cryo-EM structure determination publication-title: Nature Methods doi: 10.1038/nmeth.2115 – volume: 10 start-page: 584 year: 2013 end-page: 590 ident: CR40 article-title: Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM publication-title: Nature Methods doi: 10.1038/nmeth.2472 – volume: 13 start-page: 267 year: 2005 end-page: 275 ident: CR16 article-title: Structural studies of the human PBAF chromatin-remodeling complex publication-title: Structure doi: 10.1016/j.str.2004.12.008 – volume: 20 start-page: 1026 year: 2013 end-page: 1032 ident: CR6 article-title: Nucleosome sliding mechanisms: new twists in a looped history publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb.2648 – volume: 39 start-page: 711 year: 2010 end-page: 723 ident: CR8 article-title: The chromodomains of the Chd1 chromatin remodeler regulate DNA access to the ATPase motor publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.08.012 – volume: 154 start-page: 1220 year: 2013 end-page: 1231 ident: CR13 article-title: Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1 publication-title: Cell doi: 10.1016/j.cell.2013.08.018 – volume: 467 start-page: 562 year: 2010 end-page: 566 ident: CR21 article-title: Structure of RCC1 chromatin factor bound to the nucleosome core particle publication-title: Nature doi: 10.1038/nature09321 – volume: 368 start-page: 1067 year: 2007 end-page: 1074 ident: CR33 article-title: DNA stretching and extreme kinking in the nucleosome core publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.02.062 – volume: 540 start-page: 466 year: 2016 end-page: 469 ident: CR9 article-title: Structure and regulation of the chromatin remodeller ISWI publication-title: Nature doi: 10.1038/nature20590 – volume: 121 start-page: 363 year: 2005 end-page: 373 ident: CR26 article-title: X-ray structures of the SWI2/SNF2 ATPase core and its complex with DNA publication-title: Cell doi: 10.1016/j.cell.2005.03.026 – volume: 116 start-page: 190 year: 1996 end-page: 199 ident: CR39 article-title: SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields publication-title: J. Struct. Biol. doi: 10.1006/jsbi.1996.0030 – volume: 23 start-page: 1743 year: 2015 end-page: 1753 ident: CR38 article-title: Advances in single-particle electron cryomicroscopy structure determination applied to sub-tomogram averaging publication-title: Structure doi: 10.1016/j.str.2015.06.026 – volume: 21 start-page: 709 year: 2011 end-page: 718 ident: CR10 article-title: Electron microscopy studies of nucleosome remodelers publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2011.10.002 – volume: 78 start-page: 273 year: 2009 ident: BFnature22036_CR1 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.77.062706.153223 – volume: 25 start-page: 5880 year: 2005 ident: BFnature22036_CR27 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.25.14.5880-5892.2005 – volume: 25 start-page: 1605 year: 2004 ident: BFnature22036_CR43 publication-title: J. Comput. Chem. doi: 10.1002/jcc.20084 – volume: 462 start-page: 1016 year: 2009 ident: BFnature22036_CR15 publication-title: Nature doi: 10.1038/nature08621 – volume: 15 start-page: 469 year: 2008 ident: BFnature22036_CR23 publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb.1403 – volume: 389 start-page: 251 year: 1997 ident: BFnature22036_CR3 publication-title: Nature doi: 10.1038/38444 – volume: 7 start-page: 437 year: 2006 ident: BFnature22036_CR4 publication-title: Nature Rev. Mol. Cell Biol. doi: 10.1038/nrm1945 – volume: 68 start-page: 352 year: 2012 ident: BFnature22036_CR44 publication-title: Acta Crystallogr. D doi: 10.1107/S0907444912001308 – volume: 23 start-page: 722 year: 2016 ident: BFnature22036_CR7 publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb.3259 – volume: 20 start-page: 1026 year: 2013 ident: BFnature22036_CR6 publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb.2648 – volume: 107 start-page: 521 year: 2010 ident: BFnature22036_CR29 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0913380107 – volume: 9 start-page: 853 year: 2012 ident: BFnature22036_CR41 publication-title: Nature Methods doi: 10.1038/nmeth.2115 – volume: 17 start-page: 805 year: 2005 ident: BFnature22036_CR24 publication-title: Mol. Cell doi: 10.1016/j.molcel.2005.02.024 – volume: 481 start-page: 109 year: 2010 ident: BFnature22036_CR34 publication-title: Methods Enzymol doi: 10.1016/S0076-6879(10)81005-5 – volume: 276 start-page: 19 year: 1998 ident: BFnature22036_CR17 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1997.1494 – volume: 154 start-page: 490 year: 2013 ident: BFnature22036_CR2 publication-title: Cell doi: 10.1016/j.cell.2013.07.011 – volume: 40 start-page: 4412 year: 2012 ident: BFnature22036_CR19 publication-title: Nucleic Acids Res doi: 10.1093/nar/gks007 – volume: 540 start-page: 466 year: 2016 ident: BFnature22036_CR9 publication-title: Nature doi: 10.1038/nature20590 – volume: 673 start-page: 157 year: 2010 ident: BFnature22036_CR37 publication-title: Methods Mol. Biol doi: 10.1007/978-1-60761-842-3_9 – volume: 20 start-page: 82 year: 2013 ident: BFnature22036_CR32 publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb.2457 – volume: 192 start-page: 174 year: 2015 ident: BFnature22036_CR35 publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2015.09.003 – volume: 13 start-page: 339 year: 2006 ident: BFnature22036_CR18 publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb1071 – volume: 23 start-page: 1743 year: 2015 ident: BFnature22036_CR38 publication-title: Structure doi: 10.1016/j.str.2015.06.026 – volume: 13 start-page: 267 year: 2005 ident: BFnature22036_CR16 publication-title: Structure doi: 10.1016/j.str.2004.12.008 – volume: 121 start-page: 363 year: 2005 ident: BFnature22036_CR26 publication-title: Cell doi: 10.1016/j.cell.2005.03.026 – volume: 5 start-page: 5 year: 2016 ident: BFnature22036_CR30 publication-title: eLife doi: 10.7554/eLife.10051 – volume: 472 start-page: 448 year: 2011 ident: BFnature22036_CR14 publication-title: Nature doi: 10.1038/nature09947 – volume: 492 start-page: 280 year: 2012 ident: BFnature22036_CR25 publication-title: Nature doi: 10.1038/nature11625 – volume: 154 start-page: 1220 year: 2013 ident: BFnature22036_CR13 publication-title: Cell doi: 10.1016/j.cell.2013.08.018 – volume: 62 start-page: 453 year: 2016 ident: BFnature22036_CR22 publication-title: Mol. Cell doi: 10.1016/j.molcel.2016.03.032 – volume: 467 start-page: 562 year: 2010 ident: BFnature22036_CR21 publication-title: Nature doi: 10.1038/nature09321 – volume: 71 start-page: 247 year: 2002 ident: BFnature22036_CR5 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.71.110601.135400 – volume: 28 start-page: 6010 year: 2008 ident: BFnature22036_CR20 publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.00693-08 – volume: 10 start-page: 584 year: 2013 ident: BFnature22036_CR40 publication-title: Nature Methods doi: 10.1038/nmeth.2472 – volume: 12 start-page: 747 year: 2005 ident: BFnature22036_CR28 publication-title: Nature Struct. Mol. Biol doi: 10.1038/nsmb973 – volume: 21 start-page: 128 year: 2011 ident: BFnature22036_CR31 publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2010.11.006 – volume: 21 start-page: 709 year: 2011 ident: BFnature22036_CR10 publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2011.10.002 – volume: 6 start-page: 7108 year: 2015 ident: BFnature22036_CR11 publication-title: Nature Commun doi: 10.1038/ncomms8108 – volume: 116 start-page: 190 year: 1996 ident: BFnature22036_CR39 publication-title: J. Struct. Biol. doi: 10.1006/jsbi.1996.0030 – volume: 154 start-page: 1207 year: 2013 ident: BFnature22036_CR12 publication-title: Cell doi: 10.1016/j.cell.2013.08.016 – volume: 142 start-page: 334 year: 2003 ident: BFnature22036_CR36 publication-title: J. Struct. Biol. doi: 10.1016/S1047-8477(03)00069-8 – volume: 39 start-page: 711 year: 2010 ident: BFnature22036_CR8 publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.08.012 – volume: 4 start-page: 4 year: 2015 ident: BFnature22036_CR42 publication-title: eLife doi: 10.7554/eLife.11182 – volume: 368 start-page: 1067 year: 2007 ident: BFnature22036_CR33 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2007.02.062 – reference: 26895087 - Elife. 2016 Feb 19;5:null – reference: 22505256 - Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):352-67 – reference: 21176878 - Curr Opin Struct Biol. 2011 Feb;21(1):128-36 – reference: 16086025 - Nat Struct Mol Biol. 2005 Sep;12(9):747-55 – reference: 27399259 - Nat Struct Mol Biol. 2016 Aug;23(8):722-9 – reference: 18408732 - Nat Struct Mol Biol. 2008 May;15(5):469-76 – reference: 16723979 - Nat Rev Mol Cell Biol. 2006 Jun;7(6):437-47 – reference: 23143334 - Nature. 2012 Dec 13;492(7428):280-4 – reference: 26623517 - Elife. 2015 Dec 01;4:null – reference: 26256537 - Structure. 2015 Sep 1;23(9):1743-53 – reference: 12045097 - Annu Rev Biochem. 2002;71:247-73 – reference: 21525927 - Nature. 2011 Apr 28;472(7344):448-53 – reference: 27919072 - Nature. 2016 Dec 15;540(7633):466-469 – reference: 20832723 - Mol Cell. 2010 Sep 10;39(5):711-23 – reference: 20080715 - Proc Natl Acad Sci U S A. 2010 Jan 12;107(2):521-8 – reference: 23911317 - Cell. 2013 Aug 1;154(3):490-503 – reference: 17379244 - J Mol Biol. 2007 May 11;368(4):1067-74 – reference: 24034246 - Cell. 2013 Sep 12;154(6):1220-31 – reference: 16518397 - Nat Struct Mol Biol. 2006 Apr;13(4):339-46 – reference: 25964121 - Nat Commun. 2015 May 12;6:7108 – reference: 15264254 - J Comput Chem. 2004 Oct;25(13):1605-12 – reference: 8742743 - J Struct Biol. 1996 Jan-Feb;116(1):190-9 – reference: 26370395 - J Struct Biol. 2015 Nov;192(2):174-8 – reference: 15698570 - Structure. 2005 Feb;13(2):267-75 – reference: 20739938 - Nature. 2010 Sep 30;467(7315):562-6 – reference: 27153540 - Mol Cell. 2016 May 5;62(3):453-61 – reference: 24034245 - Cell. 2013 Sep 12;154(6):1207-19 – reference: 19355820 - Annu Rev Biochem. 2009;78:273-304 – reference: 15882619 - Cell. 2005 May 6;121(3):363-73 – reference: 23644547 - Nat Methods. 2013 Jun;10(6):584-90 – reference: 15780937 - Mol Cell. 2005 Mar 18;17(6):805-15 – reference: 22040801 - Curr Opin Struct Biol. 2011 Dec;21(6):709-18 – reference: 12781660 - J Struct Biol. 2003 Jun;142(3):334-47 – reference: 20033039 - Nature. 2009 Dec 24;462(7276):1016-21 – reference: 24008565 - Nat Struct Mol Biol. 2013 Sep;20(9):1026-32 – reference: 15988005 - Mol Cell Biol. 2005 Jul;25(14):5880-92 – reference: 9514715 - J Mol Biol. 1998 Feb 13;276(1):19-42 – reference: 20887855 - Methods Enzymol. 2010;481:109-26 – reference: 9305837 - Nature. 1997 Sep 18;389(6648):251-60 – reference: 18644858 - Mol Cell Biol. 2008 Oct;28(19):6010-21 – reference: 22298509 - Nucleic Acids Res. 2012 May;40(10):4412-21 – reference: 23202585 - Nat Struct Mol Biol. 2013 Jan;20(1):82-9 – reference: 22842542 - Nat Methods. 2012 Sep;9(9):853-4 – reference: 20835797 - Methods Mol Biol. 2010;673:157-73
SSID	ssj0005174
Score	2.5978768
Snippet	Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to...
SourceID	proquest pubmed crossref springer
SourceType	Aggregation Database Index Database Enrichment Source Publisher
StartPage	440
SubjectTerms	101/28 631/337/100/102 631/535/1258/1259 Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphatases - ultrastructure Amino Acid Sequence ATP Binding Sites Chromatin Chromatin Assembly and Disassembly Cryoelectron Microscopy Deoxyribonucleic acid DNA DNA - chemistry DNA - metabolism Enzymes Flexibility Histones - chemistry Histones - metabolism Humanities and Social Sciences Models, Molecular multidisciplinary Nucleosomes - chemistry Nucleosomes - metabolism Nucleosomes - ultrastructure Protein Binding Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - ultrastructure Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - ultrastructure Science Transcription Factors - chemistry Transcription Factors - metabolism Transcription Factors - ultrastructure
Title	Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure
URI	https://link.springer.com/article/10.1038/nature22036 https://www.ncbi.nlm.nih.gov/pubmed/28424519 https://www.proquest.com/docview/1892930896 https://www.proquest.com/docview/1891090909
Volume	544
WOSCitedRecordID	wos000400051900035&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVAQT databaseName: Nature customDbUrl: eissn: 1476-4687 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: RNT dateStart: 19970101 isFulltext: true titleUrlDefault: https://www.nature.com providerName: Nature Publishing – providerCode: PRVPQU databaseName: Advanced Technologies & Aerospace Database (ProQuest) customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: P5Z dateStart: 19880107 isFulltext: true titleUrlDefault: https://search.proquest.com/hightechjournals providerName: ProQuest – providerCode: PRVPQU databaseName: Agriculture Science Database customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: M0K dateStart: 19880107 isFulltext: true titleUrlDefault: https://search.proquest.com/agriculturejournals providerName: ProQuest – providerCode: PRVPQU databaseName: Biological Science Database customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: M7P dateStart: 19880107 isFulltext: true titleUrlDefault: http://search.proquest.com/biologicalscijournals providerName: ProQuest – providerCode: PRVPQU databaseName: Earth, Atmospheric & Aquatic Science Database customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: PCBAR dateStart: 19880107 isFulltext: true titleUrlDefault: https://search.proquest.com/eaasdb providerName: ProQuest – providerCode: PRVPQU databaseName: Engineering Database customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: M7S dateStart: 19880107 isFulltext: true titleUrlDefault: http://search.proquest.com providerName: ProQuest – providerCode: PRVPQU databaseName: Environmental Science Database customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: PATMY dateStart: 19880107 isFulltext: true titleUrlDefault: http://search.proquest.com/environmentalscience providerName: ProQuest – providerCode: PRVPQU databaseName: Health & Medical Collection customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: 7X7 dateStart: 19880107 isFulltext: true titleUrlDefault: https://search.proquest.com/healthcomplete providerName: ProQuest – providerCode: PRVPQU databaseName: Materials Science Database customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: KB. dateStart: 19880107 isFulltext: true titleUrlDefault: http://search.proquest.com/materialsscijournals providerName: ProQuest – providerCode: PRVPQU databaseName: Nursing & allied health premium. customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: 7RV dateStart: 19880107 isFulltext: true titleUrlDefault: https://search.proquest.com/nahs providerName: ProQuest – providerCode: PRVPQU databaseName: ProQuest Central customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: BENPR dateStart: 19880107 isFulltext: true titleUrlDefault: https://www.proquest.com/central providerName: ProQuest – providerCode: PRVPQU databaseName: Proquest Research Library customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: M2O dateStart: 19880107 isFulltext: true titleUrlDefault: https://search.proquest.com/pqrl providerName: ProQuest – providerCode: PRVPQU databaseName: Psychology Collection customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: M2M dateStart: 19880107 isFulltext: true titleUrlDefault: https://www.proquest.com/psychology providerName: ProQuest – providerCode: PRVPQU databaseName: Public Health Database customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: 8C1 dateStart: 19880107 isFulltext: true titleUrlDefault: https://search.proquest.com/publichealth providerName: ProQuest – providerCode: PRVPQU databaseName: Science Database customDbUrl: eissn: 1476-4687 dateEnd: 20241207 omitProxy: false ssIdentifier: ssj0005174 issn: 0028-0836 databaseCode: M2P dateStart: 19880107 isFulltext: true titleUrlDefault: https://search.proquest.com/sciencejournals providerName: ProQuest
link	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3_a9QwFH-4TcFf1M1v1XlEmKBCXJpcm-Qn2caGsN15bFNOfyltmuDAtfM6Bf9789LcbXriL1L4QGnahr68vA99yecBbElV87zKS2qsLulQWEe1EiW1fKgcc04IF9T1j-R4rKZTPYk_3Lq4rHI-J4aJum4N_iPfTpUP5IIpnb-9-EaxahRmV2MJjRVYQ5UEdMxJ9vlqiccfKsxxfx4TaruXzeSYhvs9Ii3RzKUUaYg8B3f_t8_34E7knGSnHyTrcMM2G3ArrP003QasR__uyMsoQv3qPhyNLO4JPuvOSeuI-TJrkdo2ZGZD7RzcxE5Q_cnHl5pUP4nnkeSkcZw2KJDcdu25Jb02rf8AD-DDwf7p3jsaKy9QI3R6ST0JyMqSZZnKlaxy6TlTpWuZm8xYWQof4LjQ1gqpa2ddKoU_dU5lJXOCaaPFQ1ht2sY-BsKFS7GmjPFEa-iyrCp9sMytp3lC14y5BF7Pv35hoiw5Vsf4WoT0uFDFNVMlsLVofNGrcfy92ebcHkV0ya64MkYCzxeXvTNhhqRsbPs9tMGFqv5I4FFv_sV7fBznqMWTwIv5eLj28OVOPPl3J57CbY4MgQ0pl5uw6i1in8FN8-PyrJsNYEUef0ScyoDKo9pLB7C2uz-eHPuzw903HkfsEJGPAr4POEGUPZ4Mgkf4-yY7p6NPvwBIkwix
linkProvider	ProQuest
linkToHtml	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V3dT9RAEJ8Q1MiLCH5VUNcEEjXZsLd77e4-GGNUAuG4mIjJvZV2uxtJoMUravin-BuZ6ceBnvGNB9Onppt2uzM782tn5jcAG9oUMsmTjDtvMz5UPnBrVMa9HJogQlAqNOz6Iz0em8nEfl6Ai74WhtIqe5vYGOqicvSPfGtg0JErYWzy7vQ7p65RFF3tW2i0arHnz3_hJ1v9dvcjyndTyu1PBx92eNdVgDtlB2ccHVycZSKOTWJ0nmjEA7ktdOJi53Wm0HhLZb1X2hbBh4FWeBqCiTMRlLCOyJfQ5N9CO64phUxP9FVKyR-sz109oFBmq6XplBT2-90DzsHauZBs4-m2l_-3NboP9zpMzd63m2AFFny5Cnea3FZXr8JKZ79q9qoj2X79AEb7nmqej-oTVgXmvk0rgu4lm_qmNxAV6TNit0L_WbD8nCFOZl_KIHlJBNBVXZ141nLv4oI_hK838n6PYLGsSv8EmFRhQD1zHALJYYjjPEMwkHiEscoWQoQI3vTSTl1Hu07dP47TJvyvTHpNNSLYmA0-bdlG_j5svZd_2pmcOr0SfgQvZ5fRWFAEKCt99aMZQ4m4eETwuFW32XMQp0jiGopgs9e_azefn8TTf0_iBdzdOdgfpaPd8d4aLElCQ2LIpV6HRZSOfwa33c-zo3r6vNlDDA5vWiEvAXkQVgs
linkToPdf	http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMw1V1Lb9QwEB5V5SEuQMsrUMBIrQRI1nrtTWwfEEKUFVWX1UqAVHFJE8dWK7VJ2RRQ_xq_jpk8toVF3HpAOUWx8rA_z3zOjL8B2NSmkEmeZNx5m_GR8oFbozLu5cgEEYJSoVHXn-jp1Ozt2dkK_Oz3wlBaZW8TG0NdVI7-kQ-GBh25EsYmg9ClRcy2x69PvnKqIEWR1r6cRguRXX_2A5dv9audbRzrLSnH7z69fc-7CgPcKTs85ejs4iwTcWwSo_NEIzfIbaETFzuvM4WGXCrrvdK2CD4MtcLTEEyciaCEdSTEhOb_isY1Ji38ZvGX8_SSPxSgu72BQplBK9kpKQT4uzdcorhL4dnG641v_c_9dRtudlybvWknxxqs-HIdrjU5r65eh7XOrtXseSe-_eIOTD542gt9WB-zKjB3MK-I0pds7puaQbR5n5HqFfrVguVnDPkz-1gGyUsShq7q6tizVpMXO_8ufL6U77sHq2VV-gfApApDqqXjkGCOQhznGZKExCO9VbYQIkTwsh_51HVy7FQV5Cht0gKUSS_AJILNReOTVoXk7802eiyknSmq03MgRPBscRmNCEWGstJX35o2lKCLRwT3W-gtnoP8RZIGUQRbPRYv3Hz5JR7--yWewnXEYTrZme4-ghuSSJIYcak3YBUHxz-Gq-776WE9f9JMJwb7l43HX44oXv4
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Mechanism+of+chromatin+remodelling+revealed+by+the+Snf2-nucleosome+structure&rft.jtitle=Nature+%28London%29&rft.au=Liu%2C+Xiaoyu&rft.au=Li%2C+Meijing&rft.au=Xia%2C+Xian&rft.au=Li%2C+Xueming&rft.date=2017-04-27&rft.issn=1476-4687&rft.eissn=1476-4687&rft.volume=544&rft.issue=7651&rft.spage=440&rft_id=info:doi/10.1038%2Fnature22036&rft.externalDBID=NO_FULL_TEXT
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0028-0836&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0028-0836&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0028-0836&client=summon