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| Home > Publications database > The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4 > print |
| 001 | 140870 | ||
| 005 | 20250730162626.0 | ||
| 024 | 7 | _ | |a pmid:22575888 |2 pmid |
| 024 | 7 | _ | |a pmc:PMC3437443 |2 pmc |
| 024 | 7 | _ | |a 10.1016/j.jmb.2012.04.031 |2 doi |
| 024 | 7 | _ | |a 1089-8638 |2 ISSN |
| 024 | 7 | _ | |a 0022-2836 |2 ISSN |
| 024 | 7 | _ | |a WOS:000308267700002 |2 WOS |
| 024 | 7 | _ | |a altmetric:732013 |2 altmetric |
| 024 | 7 | _ | |a openalex:W2060740961 |2 openalex |
| 037 | _ | _ | |a PHPPUBDB-24948 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Watson, A. A. |
| 110 | 1 | _ | |a DESY |b European Molecular Biology Laboratory |
| 245 | _ | _ | |a The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4 |
| 260 | _ | _ | |a Amsterdam [u.a.] |b Elsevier |c 2012 |
| 300 | _ | _ | |a 3-17 |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a article |2 DRIVER |
| 336 | 7 | _ | |a Journal Article |m journal |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 440 | _ | 0 | |a J. Mol. Biol. |v 422 |y 1-2 |x 0022-2836 |0 PERI:(DE-600)1355192-9 |
| 500 | _ | _ | |3 Converted on 2013-05-30 09:49 |
| 500 | _ | _ | |3 Converted on 2013-06-21 19:21 |
| 520 | _ | _ | |a The NuRD (nucleosome remodeling and deacetylase) complex serves as a crucial epigenetic regulator of cell differentiation, proliferation, and hematopoietic development by coupling the deacetylation and demethylation of histones, nucleosome mobilization, and the recruitment of transcription factors. The core nucleosome remodeling function of the mammalian NuRD complex is executed by the helicase-domain-containing ATPase CHD4 (Mi-2β) subunit, which also contains N-terminal plant homeodomain (PHD) and chromo domains. The mode of regulation of chromatin remodeling by CHD4 is not well understood, nor is the role of its PHD and chromo domains. Here, we use small-angle X-ray scattering, nucleosome binding ATPase and remodeling assays, limited proteolysis, cross-linking, and tandem mass spectrometry to propose a three-dimensional structural model describing the overall shape and domain interactions of CHD4 and discuss the relevance of these for regulating the remodeling of chromatin by the NuRD complex. |
| 536 | _ | _ | |0 G:(DE-H253)POF2-D1.2-20130405 |f POF II |x 0 |c POF2-54G13 |a DORIS Beamline D1.2 (POF2-54G13) |
| 588 | _ | _ | |a Dataset connected to Pubmed |
| 650 | _ | 2 | |2 MeSH |a Adenosine Triphosphatases: metabolism |
| 650 | _ | 2 | |2 MeSH |a Autoantigens: chemistry |
| 650 | _ | 2 | |2 MeSH |a Autoantigens: metabolism |
| 650 | _ | 2 | |2 MeSH |a Binding Sites |
| 650 | _ | 2 | |2 MeSH |a Chromatin: metabolism |
| 650 | _ | 2 | |2 MeSH |a Chromatin Assembly and Disassembly |
| 650 | _ | 2 | |2 MeSH |a Electrophoretic Mobility Shift Assay |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Mi-2 Nucleosome Remodeling and Deacetylase Complex: chemistry |
| 650 | _ | 2 | |2 MeSH |a Mi-2 Nucleosome Remodeling and Deacetylase Complex: metabolism |
| 650 | _ | 2 | |2 MeSH |a Models, Biological |
| 650 | _ | 2 | |2 MeSH |a Nucleosomes: metabolism |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 2 | |2 MeSH |a Proteolysis |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Autoantigens |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a CHD4 protein, human |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Chromatin |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Nucleosomes |
| 650 | _ | 7 | |0 EC 3.5.1.98 |2 NLM Chemicals |a Mi-2 Nucleosome Remodeling and Deacetylase Complex |
| 650 | _ | 7 | |0 EC 3.6.1.- |2 NLM Chemicals |a Adenosine Triphosphatases |
| 693 | _ | _ | |a DORIS III |f DORIS Beamline D1.2 |1 EXP:(DE-H253)DORISIII-20150101 |0 EXP:(DE-H253)D-D1.2-20150101 |6 EXP:(DE-H253)D-D1.2-20150101 |x 0 |
| 700 | 1 | _ | |a Mahajan, P. |
| 700 | 1 | _ | |a Mertens, H. D. |
| 700 | 1 | _ | |a Deery, M. J. |
| 700 | 1 | _ | |a Zhang, W. |
| 700 | 1 | _ | |a Pham, P. |
| 700 | 1 | _ | |a Du, X. |
| 700 | 1 | _ | |a Bartke, T. |
| 700 | 1 | _ | |a Edlich, C. |
| 700 | 1 | _ | |a Berridge, G. |
| 700 | 1 | _ | |a Chen, Y. |
| 700 | 1 | _ | |a Burgess-Brown, N. A. |
| 700 | 1 | _ | |a Kouzarides, T. |
| 700 | 1 | _ | |a Wiechens, N. |
| 700 | 1 | _ | |a Owen-Hughes, T. |
| 700 | 1 | _ | |a Svergun, D. I. |
| 700 | 1 | _ | |a Gileadi, O. |
| 700 | 1 | _ | |a Laue, E. D. |
| 773 | _ | _ | |0 PERI:(DE-600)1355192-9 |a 10.1016/j.jmb.2012.04.031 |g Vol. 422, p. 3-17 |p 3-17 |q 422<3-17 |t Journal of molecular biology |v 422 |x 0022-2836 |y 2012 |
| 856 | 4 | 0 | |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3437443/ |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3437443 |
| 909 | C | O | |o oai:bib-pubdb1.desy.de:140870 |p VDB |
| 910 | 1 | _ | |0 I:(DE-HGF)0 |a Externes Institut |k Extern |
| 913 | 1 | _ | |0 G:(DE-HGF)POF2-54G13 |1 G:(DE-HGF)POF2-540 |2 G:(DE-HGF)POF2-500 |9 G:(DE-H253)POF2-D1.2-20130405 |b Struktur der Materie |v DORIS III |x 0 |a DE-H253 |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF2 |l Forschung mit Photonen, Neutronen, Ionen |
| 914 | 1 | _ | |a (c) Elsevier. Code P. Bitte nach post referee recherchieren. |y 2012 |
| 915 | _ | _ | |a JCR/ISI refereed |0 StatID:(DE-HGF)0010 |
| 915 | _ | _ | |a Medline |0 StatID:(DE-HGF)0300 |2 StatID |
| 915 | _ | _ | |a No Author Disambiguation |0 StatID:(DE-HGF)1 |2 StatID |
| 920 | _ | 1 | |k EMBL |i European Molecular Biology Laboratory |
| 920 | 1 | _ | |0 I:(DE-H253)EMBL_-2012_-20130307 |k EMBL |l European Molecular Biology Laboratory |x 0 |
| 920 | _ | _ | |k 001 |
| 980 | _ | _ | |a PHPPUBDB |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a UNRESTRICTED |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a I:(DE-H253)EMBL_-2012_-20130307 |
| 980 | _ | _ | |a ConvertedRecord |
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