521:
regarding the mechanism of histone modification. The first of the theories suggested that they may affect electrostatic interactions between the histone tails and DNA to "loosen" chromatin structure. Later it was proposed that combinations of these modifications may create binding epitopes with which to recruit other proteins. Recently, given that more modifications have been found in the structured regions of histones, it has been put forward that these modifications may affect histone-DNA and histone-histone interactions within the nucleosome core. Modifications (such as acetylation or phosphorylation) that lower the charge of the globular histone core are predicted to "loosen" core-DNA association; the strength of the effect depends on location of the modification within the core. Some modifications have been shown to be correlated with gene silencing; others seem to be correlated with gene activation. Common modifications include
666:
nucleosome through the transferring of the base pair, this means DNA twists can cause nucleosome sliding. Nucleosome crystal structures have shown that superhelix location 2 and 5 on the nucleosome are commonly found to be where DNA twist defects occur as these are common remodeler binding sites. There are a variety of chromatin remodelers but all share the existence of an ATPase motor which facilitates chromatin sliding on DNA through the binding and hydrolysis of ATP. ATPase has an open and closed state. When the ATPase motor is changing from open and closed states, the DNA duplex changes geometry and exhibits base pair tilting. The initiation of the twist defects via the ATPase motor causes tension to accumulate around the remodeler site. The tension is released when the sliding of DNA has been completed throughout the nucleosome via the spread of two twist defects (one on each strand) in opposite directions.
366:
Although nucleosomes tend to prefer some DNA sequences over others, they are capable of binding practically to any sequence, which is thought to be due to the flexibility in the formation of these water-mediated interactions. In addition, non-polar interactions are made between protein side-chains and the deoxyribose groups, and an arginine side-chain intercalates into the DNA minor groove at all 14 sites where it faces the octamer surface. The distribution and strength of DNA-binding sites about the octamer surface distorts the DNA within the nucleosome core. The DNA is non-uniformly bent and also contains twist defects. The twist of free B-form DNA in solution is 10.5 bp per turn. However, the overall twist of nucleosomal DNA is only 10.2 bp per turn, varying from a value of 9.4 to 10.9 bp per turn.
756:(CAF-1) complex, which consists of three subunits (p150, p60, and p48). Newly synthesized H3 and H4 are assembled by the replication coupling assembly factor (RCAF). RCAF contains the subunit Asf1, which binds to newly synthesized H3 and H4 proteins. The old H3 and H4 proteins retain their chemical modifications which contributes to the passing down of the epigenetic signature. The newly synthesized H3 and H4 proteins are gradually acetylated at different lysine residues as part of the chromatin maturation process. It is also thought that the old H3 and H4 proteins in the new nucleosomes recruit histone modifying enzymes that mark the new histones, contributing to epigenetic memory.
513:
606:. Remodeling enzymes have been shown to slide nucleosomes along DNA, disrupt histone-DNA contacts to the extent of destabilizing the H2A/H2B dimer and to generate negative superhelical torsion in DNA and chromatin. Recently, the Swr1 remodeling enzyme has been shown to introduce the variant histone H2A.Z into nucleosomes. At present, it is not clear if all of these represent distinct reactions or merely alternative outcomes of a common mechanism. What is shared between all, and indeed the hallmark of ATP-dependent chromatin remodeling, is that they all result in altered DNA accessibility.
20:
803:
297:
794:
785:
352:
an anti-parallel orientation, and, in the case of H3 and H4, two such dimers form a 4-helix bundle stabilised by extensive H3-H3' interaction. The H2A/H2B dimer binds onto the H3/H4 tetramer due to interactions between H4 and H2B, which include the formation of a hydrophobic cluster. The histone octamer is formed by a central H3/H4 tetramer sandwiched between two H2A/H2B dimers. Due to the highly basic charge of all four core histones, the histone octamer is stable only in the presence of DNA or very high salt concentrations.
728:
189:
477:
accessible. Indeed, this can be extended to the observation that introducing a DNA-binding sequence within the nucleosome increases the accessibility of adjacent regions of DNA when bound. This propensity for DNA within the nucleosome to "breathe" has important functional consequences for all DNA-binding proteins that operate in a chromatin environment. In particular, the dynamic breathing of nucleosomes plays an important role in restricting the advancement of
393:
678:
464:
alter chromatin structure, many of which do so via nucleosome sliding. In 2012, Beena Pillai's laboratory has demonstrated that nucleosome sliding is one of the possible mechanism for large scale tissue specific expression of genes. The work shows that the transcription start site for genes expressed in a particular tissue, are nucleosome depleted while, the same set of genes in other tissue where they are not expressed, are nucleosome bound.
695:. A reaction consisting of the histone octamers and a naked DNA template can be incubated together at a salt concentration of 2 M. By steadily decreasing the salt concentration, the DNA will equilibrate to a position where it is wrapped around the histone octamers, forming nucleosomes. In appropriate conditions, this reconstitution process allows for the nucleosome positioning affinity of a given sequence to be mapped experimentally.
289:
494:
Well-positioned nucleosomes form boundaries of NFR. These nucleosomes are called +1-nucleosome and β1-nucleosome and are located at canonical distances downstream and upstream, respectively, from transcription start site. +1-nucleosome and several downstream nucleosomes also tend to incorporate H2A.Z
454:
Work performed in the
Bradbury laboratory showed that nucleosomes reconstituted onto the 5S DNA positioning sequence were able to reposition themselves translationally onto adjacent sequences when incubated thermally. Later work showed that this repositioning did not require disruption of the histone
379:
tail of histone H4, on the other hand, has a region of highly basic amino acids (16β25), which, in the crystal structure, forms an interaction with the highly acidic surface region of a H2A-H2B dimer of another nucleosome, being potentially relevant for the higher-order structure of nucleosomes. This
360:
The nucleosome contains over 120 direct protein-DNA interactions and several hundred water-mediated ones. Direct protein - DNA interactions are not spread evenly about the octamer surface but rather located at discrete sites. These are due to the formation of two types of DNA binding sites within the
314:
Nucleosome core particles are observed when chromatin in interphase is treated to cause the chromatin to unfold partially. The resulting image, via an electron microscope, is "beads on a string". The string is the DNA, while each bead in the nucleosome is a core particle. The nucleosome core particle
772:
histone proteins are released and degraded; therefore, newly assembled H2A and H2B proteins are incorporated into new nucleosomes. H2A and H2B are assembled into dimers which are then loaded onto nucleosomes by the nucleosome assembly protein-1 (NAP-1) which also assists with nucleosome sliding. The
617:
have revealed that chromatin remodeling events and transcription-factor binding are cyclical and periodic in nature. While the consequences of this for the reaction mechanism of chromatin remodeling are not known, the dynamic nature of the system may allow it to respond faster to external stimuli. A
229:
critical to achieving the 1997 nucleosome crystal structure was developed by the Bunick group at Oak Ridge
National Laboratory in Tennessee. The structures of over 20 different nucleosome core particles have been solved to date, including those containing histone variants and histones from different
351:
The core histone proteins contains a characteristic structural motif termed the "histone fold", which consists of three alpha-helices (Ξ±1-3) separated by two loops (L1-2). In solution, the histones form H2A-H2B heterodimers and H3-H4 heterotetramers. Histones dimerise about their long Ξ±2 helices in
715:
which is stable against H2A/H2B dimer loss during nucleosome reconstitution. A second crosslink can be introduced between the H3 N-terminal histone tail and the nucleosome DNA ends via an incorporated convertible nucleotide. The DNA-histone octamer crosslink stabilizes the nucleosome core particle
476:
revealed that DNA within the nucleosome remains fully wrapped for only 250 ms before it is unwrapped for 10-50 ms and then rapidly rewrapped. This implies that DNA does not need to be actively dissociated from the nucleosome but that there is a significant fraction of time during which it is fully
374:
The histone tail extensions constitute up to 30% by mass of histones, but are not visible in the crystal structures of nucleosomes due to their high intrinsic flexibility, and have been thought to be largely unstructured. The N-terminal tails of histones H3 and H2B pass through a channel formed by
463:
binding sites act as nucleosome positioning anchors so that, when used to align various genomic signals, multiple flanking nucleosomes can be readily identified. Although nucleosomes are intrinsically mobile, eukaryotes have evolved a large family of ATP-dependent chromatin remodelling enzymes to
365:
between both side-chain basic and hydroxyl groups and main-chain amides with the DNA backbone phosphates form the bulk of interactions with the DNA. This is important, given that the ubiquitous distribution of nucleosomes along genomes requires it to be a non-sequence-specific DNA-binding factor.
656:
binding sites became more or less accessible, respectively. In general, only one or two nucleosomes were repositioned at the promoter to effect these transcriptional changes. However, even in chromosomal regions that were not associated with transcriptional changes, nucleosome repositioning was
326:
reveals its nucleosome structure. Because DNA portions of nucleosome core particles are less accessible for DNAse than linking sections, DNA gets digested into fragments of lengths equal to multiplicity of distance between nucleosomes (180, 360, 540 base pairs etc.). Hence a very characteristic
735:
Nucleosomes are the basic packing unit of genomic DNA built from histone proteins around which DNA is coiled. They serve as a scaffold for formation of higher order chromatin structure as well as for a layer of regulatory control of gene expression. Nucleosomes are quickly assembled onto newly
441:
Although the nucleosome is a very stable protein-DNA complex, it is not static and has been shown to undergo a number of different structural re-arrangements including nucleosome sliding and DNA site exposure. Depending on the context, nucleosomes can inhibit or facilitate transcription factor
665:
DNA twist defects are when the addition of one or a few base pairs from one DNA segment are transferred to the next segment resulting in a change of the DNA twist. This will not only change the twist of the DNA but it will also change the length. This twist defect eventually moves around the
520:
Since they were discovered in the mid-1960s, histone modifications have been predicted to affect transcription. The fact that most of the early post-translational modifications found were concentrated within the tail extensions that protrude from the nucleosome core lead to two main theories
152:, which can be up to about 80 bp long. Technically, a nucleosome is defined as the core particle plus one of these linker regions; however the word is often synonymous with the core particle. Genome-wide nucleosome positioning maps are now available for many model organisms and human cells.
657:
observed, suggesting that the covering and uncovering of transcriptional DNA does not necessarily produce a transcriptional event. After transcription, the rDNA region has to protected from any damage, it suggested HMGB proteins play a major role in protecting the nucleosome free region.
503:
Eukaryotic genomes are ubiquitously associated into chromatin; however, cells must spatially and temporally regulate specific loci independently of bulk chromatin. In order to achieve the high level of control required to co-ordinate nuclear processes such as DNA replication, repair, and
504:
transcription, cells have developed a variety of means to locally and specifically modulate chromatin structure and function. This can involve covalent modification of histones, the incorporation of histone variants, and non-covalent remodelling by ATP-dependent remodeling enzymes.
159:
and its isoforms are involved in chromatin compaction and sit at the base of the nucleosome near the DNA entry and exit binding to the linker region of the DNA. Non-condensed nucleosomes without the linker histone resemble "beads on a string of DNA" under an
419:
A crystal structure of a tetranucleosome has been presented and used to build up a proposed structure of the 30 nm fiber as a two-start helix. There is still a certain amount of contention regarding this model, as it is incompatible with recent
569:
Although histones are remarkably conserved throughout evolution, several variant forms have been identified. This diversification of histone function is restricted to H2A and H3, with H2B and H4 being mostly invariant. H2A can be replaced by
217:
Pioneering structural studies in the 1980s by Aaron Klug's group provided the first evidence that an octamer of histone proteins wraps DNA around itself in about 1.7 turns of a left-handed superhelix. In 1997 the first near atomic resolution
442:
binding. Nucleosome positions are controlled by three major contributions: First, the intrinsic binding affinity of the histone octamer depends on the DNA sequence. Second, the nucleosome can be displaced or recruited by the competitive or
108:
Nucleosomes were first observed as particles in the electron microscope by Don and Ada Olins in 1974, and their existence and structure (as histone octamers surrounded by approximately 200 base pairs of DNA) were proposed by
489:
Promoters of active genes have nucleosome free regions (NFR). This allows for promoter DNA accessibility to various proteins, such as transcription factors. Nucleosome free region typically spans for 200 nucleotides in
424:
data. Beyond this, the structure of chromatin is poorly understood, but it is classically suggested that the 30 nm fiber is arranged into loops along a central protein scaffold to form transcriptionally active
652:). In addition, the removal of nucleosomes usually corresponded to transcriptional activation and the replacement of nucleosomes usually corresponded to transcriptional repression, presumably because
230:
species. The structure of the nucleosome core particle is remarkably conserved, and even a change of over 100 residues between frog and yeast histones results in electron density maps with an overall
618:
recent study indicates that nucleosome positions change significantly during mouse embryonic stem cell development, and these changes are related to binding of developmental transcription factors.
1627:
Harp JM, Palmer EL, York MH, Gewiess A, Davis M, Bunick GJ (October 1995). "Preparative separation of nucleosome core particles containing defined-sequence DNA in multiple translational phases".
926:
3382:
Albert I, Mavrich TN, Tomsho LP, Qi J, Zanton SJ, Schuster SC, Pugh BF (March 2007). "Translational and rotational settings of H2A.Z nucleosomes across the
Saccharomyces cerevisiae genome".
278:
642:
in nucleosome repositioning during a global transcriptional reprogramming event to elucidate the effects on nucleosome displacement during genome-wide transcriptional changes in yeast (
773:
nucleosomes are also spaced by ATP-dependent nucleosome-remodeling complexes containing enzymes such as Isw1 Ino80, and Chd1, and subsequently assembled into higher order structure.
2353:
Pennings S, Muyldermans S, Meersseman G, Wyns L (May 1989). "Formation, stability and core histone positioning of nucleosomes reassembled on bent and other nucleosome-derived DNA".
113:. The role of the nucleosome as a regulator of transcription was demonstrated by Lorch et al. in vitro in 1987 and by Han and Grunstein and Clark-Adams et al. in vivo in 1988.
4029:
Dyer PN, Edayathumangalam RS, White CL, Bao Y, Chakravarthy S, Muthurajan UM, Luger K (2004). "Reconstitution of nucleosome core particles from recombinant histones and DNA".
4560:
4154:
Ferentz AE, Verdine GL (1994). "The
Convertible Nucleoside Approach: Structural Engineering of Nucleic Acids by Disulfide Cross-Linking". In Eckstein F, Lilley DM (eds.).
4070:
Yenidunya A, Davey C, Clark D, Felsenfeld G, Allan J (April 1994). "Nucleosome positioning on chicken and human globin gene promoters in vitro. Novel mapping techniques".
3339:
Teif VB, Vainshtein Y, Caudron-Herger M, Mallm JP, Marth C, HΓΆfer T, Rippe K (November 2012). "Genome-wide nucleosome positioning during embryonic stem cell development".
274:(which varies from 10 - 80 bp in length depending on species and tissue type).The whole structure generates a cylinder of diameter 11 nm and a height of 5.5 nm.
101:. Nucleosome positions in the genome are not random, and it is important to know where each nucleosome is located because this determines the accessibility of the DNA to
2067:
Davey CA, Sargent DF, Luger K, Maeder AW, Richmond TJ (June 2002). "Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution".
472:
Work from the Widom laboratory has shown that nucleosomal DNA is in equilibrium between a wrapped and unwrapped state. Measurements of these rates using time-resolved
4271:
Tyler JK, Adams CR, Chen SR, Kobayashi R, Kamakaka RT, Kadonaga JT (December 1999). "The RCAF complex mediates chromatin assembly during DNA replication and repair".
171:
to package their genomic DNA, most likely to achieve an even higher packaging ratio. Histone equivalents and a simplified chromatin structure have also been found in
404:
into the cell nucleus is necessary, but it is not yet well understood. The current understanding is that repeating nucleosomes with intervening "linker" DNA form a
1108:
Lorch Y, LaPointe JW, Kornberg RD (April 1987). "Nucleosomes inhibit the initiation of transcription but allow chain elongation with the displacement of histones".
557:, since it is not encoded in the DNA but is still inherited to daughter cells. The maintenance of a repressed or activated status of a gene is often necessary for
5110:
400:
The organization of the DNA that is achieved by the nucleosome cannot fully explain the packaging of DNA observed in the cell nucleus. Further compaction of
634:. About 80% of the yeast genome appears to be covered by nucleosomes and the pattern of nucleosome positioning clearly relates to DNA regions that regulate
3002:
Whitehouse I, Flaus A, Cairns BR, White MF, Workman JL, Owen-Hughes T (August 1999). "Nucleosome mobilization catalysed by the yeast SWI/SNF complex".
1250:
Luger K, MΓ€der AW, Richmond RK, Sargent DF, Richmond TJ (September 1997). "Crystal structure of the nucleosome core particle at 2.8 A resolution".
51:. Each nucleosome is composed of a little less than two turns of DNA wrapped around a set of eight proteins called histones, which are known as a
4545:
691:
by either using purified native or recombinant histones. One standard technique of loading the DNA around the histones involves the use of salt
4611:
4584:
2441:"Proximity of H2A.Z containing nucleosome to the transcription start site influences gene expression levels in the mammalian liver and brain"
2194:
Schalch T, Duda S, Sargent DF, Richmond TJ (July 2005). "X-ray structure of a tetranucleosome and its implications for the chromatin fibre".
3533:
Lee W, Tillo D, Bray N, Morse RH, Davis RW, Hughes TR, Nislow C (October 2007). "A high-resolution atlas of nucleosome occupancy in yeast".
752:
from disassembled old nucleosomes are kept in the vicinity and randomly distributed on the newly synthesized DNA. They are assembled by the
361:
octamer; the Ξ±1Ξ±1 site, which uses the Ξ±1 helix from two adjacent histones, and the L1L2 site formed by the L1 and L2 loops. Salt links and
3482:
Whitehouse I, Rando OJ, Delrow J, Tsukiyama T (December 2007). "Chromatin remodelling at promoters suppresses antisense transcription".
4187:
Yamasu K, Senshu T (January 1990). "Conservative segregation of tetrameric units of H3 and H4 histones during nucleosome replication".
586:
in mammals are enriched in macroH2A. H3 can be replaced by H3.3 (which correlates with activate genes and regulatory elements) and in
5008:
4224:"The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication"
707:
crosslinks. Two different crosslinks can be introduced into the nucleosome core particle. A first one crosslinks the two copies of
5063:
5058:
899:
408:, described as "beads on a string", and have a packing ratio of about five to ten. A chain of nucleosomes can be arranged in a
5100:
4741:
4171:
1310:
909:
882:
3251:"Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter"
648:). The results suggested that nucleosomes that were localized to promoter regions are displaced in response to stress (like
5105:
1970:
Harp JM, Hanson BL, Timm DE, Bunick GJ (December 2000). "Asymmetries in the nucleosome core particle at 2.5 A resolution".
1754:
Harp JM, Hanson BL, Timm DE, Bunick GJ (December 2000). "Asymmetries in the nucleosome core particle at 2.5 A resolution".
1576:
Richmond TJ, Finch JT, Rushton B, Rhodes D, Klug A (1984). "Structure of the nucleosome core particle at 7 A resolution".
473:
4863:
2247:"EM measurements define the dimensions of the "30-nm" chromatin fiber: evidence for a compact, interdigitated structure"
1670:
Palmer EL, Gewiess A, Harp JM, York MH, Bunick GJ (October 1995). "Large-scale production of palindrome DNA fragments".
1434:"Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin"
1951:
603:
1039:
4604:
4046:
3627:"Dynamic remodeling of individual nucleosomes across a eukaryotic genome in response to transcriptional perturbation"
1806:
963:
446:
of other protein factors. Third, the nucleosome may be actively translocated by ATP-dependent remodeling complexes.
4880:
4566:
Dynamic
Remodeling of Individual Nucleosomes Across a Eukaryotic Genome in Response to Transcriptional Perturbation
1789:
Hanson BL, Alexander C, Harp JM, Bunick GJ (2004). "Preparation and crystallization of nucleosome core particle".
222:
of the nucleosome was solved by the
Richmond group, showing the most important details of the particle. The human
4570:
2306:"Predicting nucleosome positions on the DNA: combining intrinsic sequence preferences and remodeler activities"
703:
A recent advance in the production of nucleosome core particles with enhanced stability involves site-specific
2390:"The insulator binding protein CTCF positions 20 nucleosomes around its binding sites across the human genome"
638:, regions that are transcribed and regions that initiate DNA replication. Most recently, a new study examined
5143:
4726:
2491:
Li G, Levitus M, Bustamante C, Widom J (January 2005). "Rapid spontaneous accessibility of nucleosomal DNA".
1892:"Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions"
4565:
412:, a compacted structure with a packing ratio of ~50 and whose formation is dependent on the presence of the
4597:
3676:
Murugesapillai D, McCauley MJ, Huo R, Nelson Holte MH, Stepanyants A, Maher LJ, et al. (August 2014).
2853:
Cosgrove MS, Boeke JD, Wolberger C (November 2004). "Regulated nucleosome mobility and the histone code".
512:
753:
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Studies in 2007 have catalogued nucleosome positions in yeast and shown that nucleosomes are depleted in
340:
281:
5133:
4540:
4490:"Replication-Coupled Nucleosome Assembly and Positioning by ATP-Dependent Chromatin-Remodeling Enzymes"
231:
4873:
4324:"Modifications of H3 and H4 during chromatin replication, nucleosome assembly, and histone exchange"
3300:"Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling"
2745:"Acetylation and Methylation of Histones and Their Possible Role in the Regulation of RNA Synthesis"
1151:
Han M, Grunstein M (December 1988). "Nucleosome loss activates yeast downstream promoters in vivo".
82:
is further compacted by being folded into a series of more complex structures, eventually forming a
4927:
4711:
644:
635:
558:
4575:
3931:"Chromatin remodelers couple inchworm motion with twist-defect formation to slide nucleosomal DNA"
716:
against DNA dissociation at very low particle concentrations and at elevated salt concentrations.
3678:"DNA bridging and looping by HMO1 provides a mechanism for stabilizing nucleosome-free chromatin"
2102:
Segal E, Fondufe-Mittendorf Y, Chen L, ThΓ₯strΓΆm A, Field Y, Moore IK, et al. (August 2006).
2898:"Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly"
2159:
Zheng C, Hayes JJ (April 2003). "Structures and interactions of the core histone tail domains".
4833:
4806:
4400:"Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding"
1707:"X-ray diffraction analysis of crystals containing twofold symmetric nucleosome core particles"
284:. Digested chromatin is in the first lane; the second contains DNA standard to compare lengths.
3990:"In vitro reconstitution and analysis of mononucleosomes containing defined DNAs and proteins"
1481:
Clarke HJ (1992). "Nuclear and chromatin composition of mammalian gametes and early embryos".
4868:
4766:
631:
94:
3194:"ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex"
5138:
5088:
5013:
4998:
4828:
4776:
4751:
4691:
4280:
3942:
3491:
3391:
3205:
3143:
Havas K, Flaus A, Phelan M, Kingston R, Wade PA, Lilley DM, Owen-Hughes T (December 2000).
3011:
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1846:
1718:
1585:
1540:
1388:
1259:
1074:
996:
653:
226:
4200:
3894:
2696:"Understanding nucleosome dynamics and their links to gene expression and DNA replication"
1328:"NucPosDB: a database of nucleosome positioning in vivo and nucleosomics of cell-free DNA"
47:
and resembles thread wrapped around a spool. The nucleosome is the fundamental subunit of
8:
4756:
820:) - different views showing details of histone folding and organization. Histones
443:
421:
332:
161:
4284:
3946:
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3395:
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3015:
2962:
2815:
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2651:
2594:
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Chakravarthy S, Park YJ, Chodaparambil J, Edayathumangalam RS, Luger K (February 2005).
1722:
1589:
1544:
1392:
1377:"Position and orientation of the globular domain of linker histone H5 on the nucleosome"
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1078:
1000:
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4131:
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3775:
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3677:
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3577:
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3415:
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3231:
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3035:
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2897:
2878:
2835:
2720:
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2611:
2578:
2559:
2516:
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2440:
2416:
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2227:
2136:
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1872:
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1609:
1458:
1433:
1414:
1352:
1327:
1283:
1176:
1133:
1020:
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955:
627:
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interaction is thought to occur under physiological conditions also, and suggests that
102:
4322:
Benson LJ, Gu Y, Yakovleva T, Tong K, Barrows C, Strack CL, et al. (April 2006).
4240:
4223:
4038:
3316:
3299:
3267:
3250:
3161:
3144:
3111:
3094:
Bruno M, Flaus A, Stockdale C, Rencurel C, Ferreira H, Owen-Hughes T (December 2003).
3071:
3054:
2802:
Strahl BD, Allis CD (January 2000). "The language of covalent histone modifications".
2779:
2744:
2439:
Bargaje R, Alam MP, Patowary A, Sarkar M, Ali T, Gupta S, et al. (October 2012).
2080:
1916:
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4204:
4167:
4136:
4087:
4052:
4042:
4011:
3970:
3908:
3856:
3807:
3756:
3727:"Single-molecule studies of high-mobility group B architectural DNA bending proteins"
3707:
3658:
3607:
3550:
3507:
3456:
3407:
3356:
3321:
3272:
3223:
3166:
3145:"Generation of superhelical torsion by ATP-dependent chromatin remodeling activities"
3125:
3076:
3027:
2984:
2927:
2870:
2827:
2784:
2725:
2665:
2616:
2551:
2508:
2470:
2421:
2370:
2366:
2335:
2286:
2219:
2176:
2141:
2084:
2049:
2041:
1987:
1947:
1921:
1864:
1812:
1802:
1771:
1736:
1687:
1644:
1601:
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1498:
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1418:
1406:
1357:
1306:
1275:
1217:
1168:
1164:
1125:
1121:
1090:
1065:
Kornberg RD (May 1974). "Chromatin structure: a repeating unit of histones and DNA".
1012:
959:
905:
878:
812:
478:
302:
219:
19:
4363:
Louters L, Chalkley R (June 1985). "Exchange of histones H1, H2A, and H2B in vivo".
4257:
3562:
3368:
2896:
Ye J, Ai X, Eugeni EE, Zhang L, Carpenter LR, Jelinek MA, et al. (April 2005).
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296:
4907:
4786:
4554:
4509:
4501:
4460:
4452:
4411:
4372:
4335:
4288:
4235:
4196:
4159:
4126:
4118:
4079:
4034:
4001:
3960:
3950:
3898:
3890:
3846:
3838:
3797:
3787:
3746:
3738:
3697:
3689:
3648:
3638:
3597:
3589:
3542:
3519:
3499:
3468:
3446:
3419:
3399:
3348:
3311:
3262:
3235:
3213:
3178:
3156:
3115:
3107:
3066:
3039:
3019:
2974:
2966:
2917:
2909:
2862:
2839:
2819:
2774:
2764:
2715:
2707:
2655:
2606:
2598:
2543:
2500:
2460:
2452:
2411:
2401:
2362:
2325:
2317:
2276:
2266:
2231:
2211:
2168:
2131:
2123:
2076:
2033:
1979:
1911:
1903:
1854:
1794:
1763:
1726:
1705:
Harp JM, Uberbacher EC, Roberson AE, Palmer EL, Gewiess A, Bunick GJ (March 1996).
1679:
1636:
1613:
1593:
1548:
1490:
1453:
1445:
1396:
1347:
1339:
1287:
1267:
1207:
1160:
1117:
1082:
1047:
1004:
951:
375:
the minor grooves of the two DNA strands, protruding from the DNA every 20 bp. The
362:
3284:
3249:
MΓ©tivier R, Penot G, HΓΌbner MR, Reid G, Brand H, Kos M, Gannon F (December 2003).
1859:
1834:
1040:"Milestone 9, (1973-1974) The nucleosome hypothesis: An alternative string theory"
4900:
4721:
4669:
4571:
Nucleosome positioning data and tools online (annotated list, constantly updated)
4505:
3955:
3643:
3096:"Histone H2A/H2B dimer exchange by ATP-dependent chromatin remodeling activities"
2913:
2579:"Nucleosomal fluctuations govern the transcription dynamics of RNA polymerase II"
2406:
1375:
Zhou YB, Gerchman SE, Ramakrishnan V, Travers A, Muyldermans S (September 1998).
1086:
1008:
712:
692:
546:
430:
251:
52:
4163:
2947:"Charge state of the globular histone core controls stability of the nucleosome"
2634:
Yuan GC, Liu YJ, Dion MF, Slack MD, Wu LF, Altschuler SJ, Rando OJ (July 2005).
455:
octamer but was consistent with nucleosomes being able to "slide" along the DNA
223:
43:. The structure of a nucleosome consists of a segment of DNA wound around eight
4791:
4715:
3842:
3451:
3434:
2749:
Proceedings of the
National Academy of Sciences of the United States of America
2251:
Proceedings of the
National Academy of Sciences of the United States of America
1907:
1343:
727:
583:
530:
208:
core histones, and DNA. The view is from the top through the superhelical axis.
188:
110:
4122:
3742:
2970:
1983:
1767:
1731:
1706:
898:
Alberts B (2002). "Chromosomal DNA and Its
Packaging in the Chromatin Fiber".
175:, suggesting that eukaryotes are not the only organisms that use nucleosomes.
55:. Each histone octamer is composed of two copies each of the histone proteins
5127:
4771:
3776:"A twist defect mechanism for ATP-dependent translocation of nucleosomal DNA"
2045:
1832:
1640:
871:
328:
4589:
3218:
2660:
2635:
2602:
2271:
4746:
4620:
4523:
4474:
4425:
4416:
4399:
4349:
4340:
4323:
4300:
4140:
4083:
4056:
4006:
3989:
3974:
3912:
3860:
3811:
3760:
3711:
3662:
3611:
3554:
3511:
3460:
3411:
3360:
3325:
3276:
3227:
3170:
3129:
3080:
3031:
2988:
2931:
2874:
2831:
2788:
2729:
2669:
2620:
2555:
2512:
2474:
2425:
2339:
2290:
2223:
2180:
2145:
2088:
1991:
1925:
1868:
1816:
1775:
1740:
1683:
1562:
1361:
1194:
Clark-Adams CD, Norris D, Osley MA, Fassler JS, Winston F (February 1988).
335:
of that DNA. Such digestion can occur also under natural conditions during
75:
4384:
4249:
4208:
4091:
4015:
2769:
2534:
Li G, Widom J (August 2004). "Nucleosomes facilitate their own invasion".
2374:
2053:
1691:
1648:
1605:
1502:
1410:
1279:
1221:
1172:
1129:
1094:
1016:
987:
Olins AL, Olins DE (January 1974). "Spheroid chromatin units (v bodies)".
288:
277:
4965:
4960:
4823:
4801:
4796:
4664:
4551:
4441:"ATP-dependent chromatin remodeling shapes the DNA replication landscape"
4107:"Site-Specific Disulfide Crosslinked Nucleosomes with Enhanced Stability"
3693:
2456:
2321:
1467:
1449:
769:
765:
708:
621:
538:
526:
522:
426:
381:
259:
255:
242:
The nucleosome core particle (shown in the figure) consists of about 146
137:
133:
90:
60:
56:
4376:
3792:
3625:
Shivaswamy S, Bhinge A, Zhao Y, Jones S, Hirst M, Iyer VR (March 2008).
3593:
3503:
3403:
2711:
2215:
2127:
1553:
1528:
1212:
1195:
4985:
4975:
4970:
4955:
4895:
4885:
4761:
4735:
4676:
4624:
4398:
Park YJ, Chodaparambil JV, Bao Y, McBryant SJ, Luger K (January 2005).
2037:
849:
749:
745:
677:
649:
587:
554:
413:
392:
376:
271:
267:
263:
168:
156:
149:
145:
141:
83:
68:
64:
40:
4456:
3725:
Murugesapillai D, McCauley MJ, Maher LJ, Williams MC (February 2017).
3352:
2636:"Genome-scale identification of nucleosome positions in S. cerevisiae"
2388:
Fu Y, Sinha M, Peterson CL, Weng Z (July 2008). Van
Steensel B (ed.).
2172:
1946:(fourth ed.). New York - Basingstoke: W. H. Freeman and Company.
816:
306:
4937:
4681:
4659:
4640:
3675:
2577:
Hodges C, Bintu L, Lubkowska L, Kashlev M, Bustamante C (July 2009).
2021:
1597:
704:
401:
336:
323:
247:
243:
167:
In contrast to most eukaryotic cells, mature sperm cells largely use
125:
117:
79:
48:
24:
3193:
2866:
2689:
2687:
2547:
2504:
1494:
1237:
In different crystals, values of 146 and 147 basepairs were observed
1051:
192:
The crystal structure of the nucleosome core particle consisting of
4923:
4707:
4292:
3724:
3546:
2101:
687:
542:
98:
3192:
Mizuguchi G, Shen X, Landry J, Wu WH, Sen S, Wu C (January 2004).
3053:
Kassabov SR, Zhang B, Persinger J, Bartholomew B (February 2003).
3023:
2823:
1401:
1376:
1326:
Shtumpf M, Piroeva KV, Agrawal SP, Jacob DR, Teif VB (June 2022).
1271:
925:
lberts B, Johnson A, Lewis J, Raff M, Roberts K, Walter P (2002).
698:
270:. Adjacent nucleosomes are joined by a stretch of free DNA termed
5093:
4947:
4858:
4853:
3338:
3052:
2684:
2352:
384:
of the H4 tail distorts the higher-order structure of chromatin.
172:
129:
44:
3576:
Eaton ML, Galani K, Kang S, Bell SP, MacAlpine DM (April 2010).
5003:
4890:
4654:
4650:
4645:
4221:
1835:"Structure and dynamic properties of nucleosome core particles"
1374:
579:
550:
534:
3773:
3578:"Conserved nucleosome positioning defines replication origins"
3481:
5068:
5053:
5048:
5043:
5038:
5033:
5028:
5023:
5018:
4993:
4931:
4069:
2022:"Electrophoretic DNA analysis for the detection of apoptosis"
1972:
Acta Crystallographica. Section D, Biological Crystallography
1756:
Acta Crystallographica. Section D, Biological Crystallography
1711:
Acta Crystallographica. Section D, Biological Crystallography
1196:"Changes in histone gene dosage alter transcription in yeast"
1193:
591:
346:
319:
4397:
4222:
Kaufman PD, Kobayashi R, Kessler N, Stillman B (June 1995).
4028:
3774:
Winger J, Nodelman IM, Levendosky RF, Bowman GD (May 2018).
1704:
602:
A number of distinct reactions are associated with the term
3093:
2576:
575:
571:
507:
460:
116:
The nucleosome core particle consists of approximately 146
3001:
2244:
2193:
1575:
1325:
132:
octamer, consisting of 2 copies each of the core histones
3929:
Brandani GB, Takada S (November 2018). Onufriev A (ed.).
3624:
3298:
Nagaich AK, Walker DA, Wolford R, Hager GL (April 2004).
3297:
2438:
2245:
Robinson PJ, Fairall L, Huynh VA, Rhodes D (April 2006).
1788:
1249:
429:. Further compaction leads to transcriptionally inactive
121:
86:. Each human cell contains about 30 million nucleosomes.
74:
DNA must be compacted into nucleosomes to fit within the
36:
4033:. Methods in Enzymology. Vol. 375. pp. 23β44.
3142:
2490:
1793:. Methods in Enzymology. Vol. 375. pp. 44β62.
1305:(5th ed.). New York: Garland Science. p. 211.
944:
Encyclopedia of Bioinformatics and Computational Biology
928:
Chromosomal DNA and Its Packaging in the Chromatin Fiber
904:(4th ed.). New York: Garland Science. p. 207.
5111:
International System for Human Cytogenetic Nomenclature
4270:
3248:
2066:
942:
Teif VB, Clarkson CT (2019). "Nucleosome Positioning".
810:
The crystal structure of the nucleosome core particle (
516:
Histone tails and their function in chromatin formation
300:
The crystal structure of the nucleosome core particle (
2852:
924:
622:
Dynamic nucleosome remodelling across the Yeast genome
597:
4438:
4321:
3381:
3191:
3055:"SWI/SNF unwraps, slides, and rewraps the nucleosome"
2742:
1669:
1626:
1107:
237:
1969:
1753:
16:
Basic structural unit of DNA packaging in eukaryotes
4104:
3575:
2945:Fenley AT, Adams DA, Onufriev AV (September 2010).
2944:
2387:
553:. The information stored in this way is considered
339:("cell suicide" or programmed cell death), because
254:, consisting of 2 copies each of the core histones
4031:Chromatin and Chromatin Remodeling Enzymes, Part A
2020:Allen, Paul D.; Newland, Adrian C. (1 June 1998).
1791:Chromatin and Chromatin Remodeling Enzymes, Part A
1526:
870:
498:
4581:HistoneDB 2.0 - Database of histones and variants
4105:Frouws TD, Barth PD, Richmond TJ (January 2018).
3532:
1245:
1243:
574:(which leads to reduced nucleosome stability) or
183:
78:. In addition to nucleosome wrapping, eukaryotic
5125:
2633:
4487:
4362:
2895:
2486:
2484:
1828:
1826:
1522:
1520:
1518:
1516:
1514:
1512:
1431:
711:via an introduced cysteine (N38C) resulting in
699:Disulfide crosslinked nucleosome core particles
669:
148:. Core particles are connected by stretches of
4439:Vincent JA, Kwong TJ, Tsukiyama T (May 2008).
4153:
3928:
3876:
3827:"Uncovering a New Step in Sliding Nucleosomes"
3432:
2743:Allfrey VG, Faulkner R, Mirsky AE (May 1964).
1889:
1294:
1240:
719:
4619:
4605:
1890:White CL, Suto RK, Luger K (September 2001).
891:
868:
736:synthesized DNA behind the replication fork.
355:
4186:
3618:
3569:
3526:
3475:
3435:"The role of chromatin during transcription"
3426:
3375:
3291:
3242:
3185:
3136:
3087:
3046:
2995:
2938:
2889:
2846:
2795:
2736:
2527:
2481:
2432:
2381:
2238:
2152:
2060:
2019:
1883:
1823:
1782:
1747:
1698:
1509:
1150:
941:
3433:Li B, Carey M, Workman JL (February 2007).
2801:
2346:
2104:"A genomic code for nucleosome positioning"
1937:
1935:
1663:
1569:
1474:
1432:Thoma F, Koller T, Klug A (November 1979).
4612:
4598:
2158:
2009:(2nd ed.). New York: Garland Science.
986:
347:Protein interactions within the nucleosome
4513:
4464:
4445:Nature Structural & Molecular Biology
4415:
4339:
4239:
4130:
4005:
3964:
3954:
3902:
3850:
3801:
3791:
3750:
3701:
3652:
3642:
3601:
3450:
3341:Nature Structural & Molecular Biology
3315:
3266:
3217:
3160:
3119:
3070:
2978:
2921:
2855:Nature Structural & Molecular Biology
2778:
2768:
2719:
2659:
2610:
2536:Nature Structural & Molecular Biology
2493:Nature Structural & Molecular Biology
2464:
2415:
2405:
2329:
2303:
2280:
2270:
2135:
1965:
1963:
1915:
1858:
1730:
1552:
1527:Felsenfeld G, Groudine M (January 2003).
1457:
1400:
1351:
1233:
1231:
1211:
578:(which is associated with DNA repair and
484:
387:
315:is composed of DNA and histone proteins.
3987:
1932:
1064:
1037:
726:
676:
511:
508:Histone post-translational modifications
459:. In 2008, it was further revealed that
391:
295:
287:
276:
187:
18:
4546:Nucleosomes on the Richmond Lab website
2693:
2533:
2004:
1300:
897:
862:
369:
5126:
3824:
2700:Nature Reviews. Molecular Cell Biology
1960:
1941:
1480:
1228:
918:
764:In contrast to old H3 and H4, the old
396:The current chromatin compaction model
5101:List of organisms by chromosome count
4593:
4201:10.1093/oxfordjournals.jbchem.a122999
3924:
3922:
3895:10.1146/annurev-biophys-082520-080201
3872:
3870:
449:
93:inherited information in the form of
4488:Yadav T, Whitehouse I (April 2016).
3879:"Biophysics of Chromatin Remodeling"
877:. San Francisco: Benjamin Cummings.
660:
613:and, more astonishingly, remodeling
467:
4404:The Journal of Biological Chemistry
4328:The Journal of Biological Chemistry
4156:Nucleic Acids and Molecular Biology
3877:Nodelman IM, Bowman GD (May 2021).
2304:Teif VB, Rippe K (September 2009).
609:Studies looking at gene activation
598:ATP-dependent nucleosome remodeling
564:
246:of DNA wrapped in 1.67 left-handed
13:
3919:
3867:
2694:Lai WK, Pugh BF (September 2017).
1044:Nature Milestones: Gene Expression
956:10.1016/B978-0-12-809633-8.20242-2
604:ATP-dependent chromatin remodeling
238:The nucleosome core particle (NCP)
14:
5155:
4534:
481:during transcription elongation.
292:Scheme of nucleosome organization
89:Nucleosomes are thought to carry
801:
792:
783:
35:is the basic structural unit of
4722:Macrochromosome/Microchromosome
4481:
4432:
4391:
4356:
4315:
4264:
4215:
4180:
4158:. Vol. 8. pp. 14β40.
4147:
4098:
4063:
4022:
3981:
3818:
3767:
3718:
3669:
3332:
2627:
2570:
2297:
2187:
2095:
2013:
1998:
1620:
1425:
1368:
1319:
1187:
499:Modulating nucleosome structure
3831:Trends in Biochemical Sciences
1529:"Controlling the double helix"
1144:
1101:
1058:
1031:
980:
935:
759:
681:Diagram of nucleosome assembly
582:differentiation), whereas the
184:Structure of the core particle
1:
4541:MBInfo - What are nucleosomes
4241:10.1016/S0092-8674(05)80015-7
4039:10.1016/s0076-6879(03)75002-2
3988:Hayes JJ, Lee KM (May 1997).
3317:10.1016/S1097-2765(04)00178-9
3268:10.1016/S0092-8674(03)00934-6
3162:10.1016/S0092-8674(00)00215-4
3112:10.1016/S1097-2765(03)00499-4
3072:10.1016/S1097-2765(03)00039-X
2081:10.1016/S0022-2836(02)00386-8
1860:10.1016/j.febslet.2004.11.030
1799:10.1016/s0076-6879(03)75003-4
1483:Biochemistry and Cell Biology
1303:Molecular Biology of the Cell
901:Molecular biology of the cell
855:
685:Nucleosomes can be assembled
4506:10.1016/J.CELREP.2016.03.059
4111:Journal of Molecular Biology
4072:Journal of Molecular Biology
3956:10.1371/journal.pcbi.1006512
3644:10.1371/journal.pbio.0060065
2914:10.1016/j.molcel.2005.02.031
2407:10.1371/journal.pgen.1000138
2367:10.1016/0022-2836(89)90449-X
2355:Journal of Molecular Biology
2069:Journal of Molecular Biology
1165:10.1016/0092-8674(88)90258-9
1122:10.1016/0092-8674(87)90561-7
1087:10.1126/science.184.4139.868
1038:McDonald D (December 2005).
1009:10.1126/science.183.4122.330
869:Reece J, Campbell N (2006).
739:
731:Steps in nucleosome assembly
178:
124:wrapped in 1.67 left-handed
7:
4164:10.1007/978-3-642-78666-2_2
3883:Annual Review of Biophysics
1438:The Journal of Cell Biology
843:
754:chromatin assembly factor 1
436:
329:pattern similar to a ladder
212:
10:
5160:
4762:Dinoflagellate chromosomes
3935:PLOS Computational Biology
3843:10.1016/j.tibs.2019.05.001
3452:10.1016/j.cell.2007.01.015
1344:10.1007/s00412-021-00766-9
776:
356:Histone - DNA interactions
232:root mean square deviation
5106:List of sequenced genomes
5081:
4984:
4946:
4916:
4874:Chromosomal translocation
4844:
4747:A chromosome/B chromosome
4738:(or accessory chromosome)
4700:
4631:
4576:Histone protein structure
4123:10.1016/j.jmb.2017.10.029
3825:Bowman GD (August 2019).
3743:10.1007/s12551-016-0236-4
2971:10.1016/j.bpj.2010.06.046
1984:10.1107/S0907444900011847
1768:10.1107/s0907444900011847
1732:10.1107/S0907444995009139
4928:Telomere-binding protein
4742:Supernumerary chromosome
1908:10.1093/emboj/20.18.5207
1641:10.1002/elps.11501601305
645:Saccharomyces cerevisiae
559:cellular differentiation
155:Linker histones such as
4189:Journal of Biochemistry
3582:Genes & Development
3219:10.1126/science.1090701
2661:10.1126/science.1112178
2603:10.1126/science.1172926
2272:10.1073/pnas.0601212103
2026:Molecular Biotechnology
1672:Analytical Biochemistry
1200:Genes & Development
343:typically is its role.
282:Apoptotic DNA laddering
4864:Structural alterations
4417:10.1074/jbc.M411347200
4341:10.1074/jbc.M512956200
4084:10.1006/jmbi.1994.1243
4007:10.1006/meth.1997.0441
3682:Nucleic Acids Research
2445:Nucleic Acids Research
2310:Nucleic Acids Research
2007:Essential Cell Biology
1684:10.1006/abio.1995.1509
732:
682:
632:origins of replication
584:inactive X chromosomes
517:
485:Nucleosome free region
397:
388:Higher order structure
341:autodestruction of DNA
311:
293:
285:
209:
95:covalent modifications
28:
4881:Numerical alterations
4869:Chromosomal inversion
4767:Homologous chromosome
4561:Nucleosome at the PDB
2770:10.1073/pnas.51.5.786
730:
680:
515:
395:
299:
291:
280:
191:
22:
5144:Nuclear organization
5089:Extrachromosomal DNA
4777:Satellite chromosome
4752:Lampbrush chromosome
4692:Nuclear organization
1978:(Pt 12): 1513β1534.
1762:(Pt 12): 1513β1534.
1450:10.1083/jcb.83.2.403
720:Nucleosome assembly
670:Nucleosome assembly
654:transcription factor
370:Histone tail domains
4782:Centromere position
4757:Polytene chromosome
4727:Circular chromosome
4377:10.1021/bi00334a002
4285:1999Natur.402..555T
3947:2018PLSCB..14E6512B
3793:10.7554/eLife.34100
3731:Biophysical Reviews
3594:10.1101/gad.1913210
3504:10.1038/nature06391
3496:2007Natur.450.1031W
3490:(7172): 1031β1035.
3404:10.1038/nature05632
3396:2007Natur.446..572A
3210:2004Sci...303..343M
3016:1999Natur.400..784W
2963:2010BpJ....99.1577F
2951:Biophysical Journal
2816:2000Natur.403...41S
2761:1964PNAS...51..786A
2712:10.1038/nrm.2017.47
2652:2005Sci...309..626Y
2595:2009Sci...325..626H
2263:2006PNAS..103.6506R
2216:10.1038/nature03686
2208:2005Natur.436..138S
2128:10.1038/nature04979
2120:2006Natur.442..772S
1851:2005FEBSL.579..895C
1723:1996AcCrD..52..283H
1590:1984Natur.311..532R
1554:10.1038/nature01411
1545:2003Natur.421..448F
1444:(2 Pt 1): 403β427.
1393:1998Natur.395..402Z
1264:1997Natur.389..251L
1213:10.1101/gad.2.2.150
1079:1974Sci...184..868K
1001:1974Sci...183..330O
444:cooperative binding
422:electron microscopy
333:gel electrophoresis
162:electron microscope
103:regulatory proteins
3694:10.1093/nar/gku635
2457:10.1093/nar/gks665
2322:10.1093/nar/gkp610
2038:10.1007/BF02915798
2005:Alberts B (2009).
1489:(10β11): 856β866.
1301:Alberts B (2007).
931:. Garland Science.
733:
683:
590:H3 is replaced by
518:
450:Nucleosome sliding
398:
331:is visible during
312:
294:
286:
248:superhelical turns
210:
126:superhelical turns
29:
5134:Molecular biology
5119:
5118:
5077:
5076:
4814:Centromere number
4731:Linear chromosome
4457:10.1038/nsmb.1419
4371:(13): 3080β3085.
4334:(14): 9287β9296.
4279:(6761): 555β560.
4173:978-3-642-78668-6
3688:(14): 8996β9004.
3541:(10): 1235β1244.
3390:(7135): 572β576.
3353:10.1038/nsmb.2419
3347:(11): 1185β1192.
3204:(5656): 343β348.
3010:(6746): 784β787.
2861:(11): 1037β1043.
2646:(5734): 626β630.
2589:(5940): 626β628.
2451:(18): 8965β8978.
2316:(17): 5641β5655.
2257:(17): 6506β6511.
2202:(7047): 138β141.
2173:10.1002/bip.10303
2114:(7104): 772β778.
1942:Stryer L (1995).
1902:(18): 5207β5218.
1717:(Pt 2): 283β288.
1635:(10): 1861β1864.
1539:(6921): 448β453.
1387:(6700): 402β405.
1312:978-0-8153-4106-2
1258:(6648): 251β260.
1073:(4139): 868β871.
995:(4122): 330β332.
911:978-0-8153-4072-0
884:978-0-8053-6624-2
661:DNA Twist Defects
495:histone variant.
479:RNA polymerase II
468:DNA site exposure
220:crystal structure
5151:
4944:
4943:
4908:Polyploidization
4736:Extra chromosome
4651:Genetic material
4614:
4607:
4600:
4591:
4590:
4528:
4527:
4517:
4485:
4479:
4478:
4468:
4436:
4430:
4429:
4419:
4410:(3): 1817β1825.
4395:
4389:
4388:
4360:
4354:
4353:
4343:
4319:
4313:
4312:
4268:
4262:
4261:
4243:
4234:(7): 1105β1114.
4219:
4213:
4212:
4184:
4178:
4177:
4151:
4145:
4144:
4134:
4102:
4096:
4095:
4067:
4061:
4060:
4026:
4020:
4019:
4009:
3985:
3979:
3978:
3968:
3958:
3941:(11): e1006512.
3926:
3917:
3916:
3906:
3874:
3865:
3864:
3854:
3822:
3816:
3815:
3805:
3795:
3771:
3765:
3764:
3754:
3722:
3716:
3715:
3705:
3673:
3667:
3666:
3656:
3646:
3622:
3616:
3615:
3605:
3573:
3567:
3566:
3530:
3524:
3523:
3479:
3473:
3472:
3454:
3430:
3424:
3423:
3379:
3373:
3372:
3336:
3330:
3329:
3319:
3295:
3289:
3288:
3270:
3246:
3240:
3239:
3221:
3189:
3183:
3182:
3164:
3155:(7): 1133β1142.
3140:
3134:
3133:
3123:
3106:(6): 1599β1606.
3091:
3085:
3084:
3074:
3050:
3044:
3043:
2999:
2993:
2992:
2982:
2957:(5): 1577β1585.
2942:
2936:
2935:
2925:
2893:
2887:
2886:
2850:
2844:
2843:
2799:
2793:
2792:
2782:
2772:
2740:
2734:
2733:
2723:
2691:
2682:
2681:
2663:
2631:
2625:
2624:
2614:
2574:
2568:
2567:
2531:
2525:
2524:
2488:
2479:
2478:
2468:
2436:
2430:
2429:
2419:
2409:
2385:
2379:
2378:
2350:
2344:
2343:
2333:
2301:
2295:
2294:
2284:
2274:
2242:
2236:
2235:
2191:
2185:
2184:
2156:
2150:
2149:
2139:
2099:
2093:
2092:
2075:(5): 1097β1113.
2064:
2058:
2057:
2017:
2011:
2010:
2002:
1996:
1995:
1967:
1958:
1957:
1939:
1930:
1929:
1919:
1896:The EMBO Journal
1887:
1881:
1880:
1862:
1830:
1821:
1820:
1786:
1780:
1779:
1751:
1745:
1744:
1734:
1702:
1696:
1695:
1667:
1661:
1660:
1624:
1618:
1617:
1598:10.1038/311532a0
1573:
1567:
1566:
1556:
1524:
1507:
1506:
1478:
1472:
1471:
1461:
1429:
1423:
1422:
1404:
1372:
1366:
1365:
1355:
1323:
1317:
1316:
1298:
1292:
1291:
1247:
1238:
1235:
1226:
1225:
1215:
1191:
1185:
1184:
1159:(6): 1137β1145.
1148:
1142:
1141:
1105:
1099:
1098:
1062:
1056:
1055:
1035:
1029:
1028:
984:
978:
977:
939:
933:
932:
922:
916:
915:
895:
889:
888:
876:
866:
839:
835:
831:
827:
823:
819:
805:
796:
787:
565:Histone variants
410:30 nm fiber
363:hydrogen bonding
309:
207:
203:
199:
195:
45:histone proteins
5159:
5158:
5154:
5153:
5152:
5150:
5149:
5148:
5124:
5123:
5120:
5115:
5073:
4980:
4942:
4912:
4901:Paleopolyploidy
4846:
4840:
4696:
4670:Heterochromatin
4633:
4627:
4618:
4537:
4532:
4531:
4486:
4482:
4437:
4433:
4396:
4392:
4361:
4357:
4320:
4316:
4269:
4265:
4220:
4216:
4185:
4181:
4174:
4152:
4148:
4103:
4099:
4068:
4064:
4049:
4027:
4023:
3986:
3982:
3927:
3920:
3875:
3868:
3823:
3819:
3772:
3768:
3723:
3719:
3674:
3670:
3623:
3619:
3574:
3570:
3535:Nature Genetics
3531:
3527:
3480:
3476:
3431:
3427:
3380:
3376:
3337:
3333:
3296:
3292:
3247:
3243:
3190:
3186:
3141:
3137:
3092:
3088:
3051:
3047:
3000:
2996:
2943:
2939:
2894:
2890:
2867:10.1038/nsmb851
2851:
2847:
2810:(6765): 41β45.
2800:
2796:
2741:
2737:
2692:
2685:
2632:
2628:
2575:
2571:
2548:10.1038/nsmb801
2532:
2528:
2505:10.1038/nsmb869
2489:
2482:
2437:
2433:
2400:(7): e1000138.
2386:
2382:
2351:
2347:
2302:
2298:
2243:
2239:
2192:
2188:
2157:
2153:
2100:
2096:
2065:
2061:
2018:
2014:
2003:
1999:
1994:. PDB ID: 1EQZ.
1968:
1961:
1954:
1940:
1933:
1888:
1884:
1831:
1824:
1809:
1787:
1783:
1752:
1748:
1703:
1699:
1668:
1664:
1629:Electrophoresis
1625:
1621:
1584:(5986): 532β7.
1574:
1570:
1525:
1510:
1495:10.1139/o92-134
1479:
1475:
1430:
1426:
1373:
1369:
1324:
1320:
1313:
1299:
1295:
1248:
1241:
1236:
1229:
1192:
1188:
1149:
1145:
1106:
1102:
1063:
1059:
1052:10.1038/nrm1798
1036:
1032:
985:
981:
966:
940:
936:
923:
919:
912:
896:
892:
885:
867:
863:
858:
846:
837:
833:
829:
825:
821:
811:
806:
797:
788:
779:
762:
742:
725:
713:histone octamer
701:
675:
663:
640:dynamic changes
624:
600:
567:
547:phosphorylation
510:
501:
487:
470:
452:
439:
431:heterochromatin
390:
372:
358:
349:
301:
252:histone octamer
240:
227:palindromic DNA
224:alpha satellite
215:
205:
201:
197:
193:
186:
181:
53:histone octamer
23:Basic units of
17:
12:
11:
5:
5157:
5147:
5146:
5141:
5136:
5117:
5116:
5114:
5113:
5108:
5103:
5098:
5097:
5096:
5085:
5083:
5079:
5078:
5075:
5074:
5072:
5071:
5066:
5061:
5056:
5051:
5046:
5041:
5036:
5031:
5026:
5021:
5016:
5011:
5006:
5001:
4996:
4990:
4988:
4982:
4981:
4979:
4978:
4973:
4968:
4963:
4958:
4952:
4950:
4941:
4940:
4935:
4920:
4918:
4914:
4913:
4911:
4910:
4905:
4904:
4903:
4898:
4893:
4888:
4878:
4877:
4876:
4871:
4861:
4856:
4850:
4848:
4842:
4841:
4839:
4838:
4837:
4836:
4831:
4826:
4821:
4811:
4810:
4809:
4804:
4799:
4794:
4792:Submetacentric
4789:
4779:
4774:
4769:
4764:
4759:
4754:
4749:
4744:
4739:
4733:
4724:
4719:
4718:or heterosome)
4712:Sex chromosome
4704:
4702:
4698:
4697:
4695:
4694:
4689:
4684:
4679:
4674:
4673:
4672:
4667:
4657:
4648:
4643:
4637:
4635:
4629:
4628:
4617:
4616:
4609:
4602:
4594:
4588:
4587:
4578:
4573:
4568:
4563:
4558:
4548:
4543:
4536:
4535:External links
4533:
4530:
4529:
4500:(4): 715β723.
4480:
4451:(5): 477β484.
4431:
4390:
4355:
4314:
4293:10.1038/990147
4263:
4214:
4179:
4172:
4146:
4097:
4078:(4): 401β414.
4062:
4047:
4021:
3980:
3918:
3866:
3837:(8): 643β645.
3817:
3766:
3717:
3668:
3617:
3588:(8): 748β753.
3568:
3547:10.1038/ng2117
3525:
3474:
3445:(4): 707β719.
3425:
3374:
3331:
3310:(2): 163β174.
3304:Molecular Cell
3290:
3261:(6): 751β763.
3241:
3184:
3135:
3100:Molecular Cell
3086:
3065:(2): 391β403.
3059:Molecular Cell
3045:
2994:
2937:
2908:(1): 123β130.
2902:Molecular Cell
2888:
2845:
2794:
2755:(5): 786β794.
2735:
2706:(9): 548β562.
2683:
2626:
2569:
2542:(8): 763β769.
2526:
2480:
2431:
2380:
2361:(1): 183β192.
2345:
2296:
2237:
2186:
2167:(4): 539β546.
2151:
2094:
2059:
2032:(3): 247β251.
2012:
1997:
1959:
1953:978-0716720096
1952:
1931:
1882:
1845:(4): 895β898.
1822:
1807:
1781:
1746:
1697:
1678:(1): 109β114.
1662:
1619:
1568:
1508:
1473:
1424:
1367:
1338:(1β2): 19β28.
1318:
1311:
1293:
1239:
1227:
1206:(2): 150β159.
1186:
1143:
1116:(2): 203β210.
1100:
1057:
1030:
979:
964:
934:
917:
910:
890:
883:
860:
859:
857:
854:
853:
852:
845:
842:
840:are coloured.
808:
807:
800:
798:
791:
789:
782:
778:
775:
761:
758:
741:
738:
724:
718:
700:
697:
674:
668:
662:
659:
623:
620:
599:
596:
566:
563:
531:ubiquitination
509:
506:
500:
497:
486:
483:
469:
466:
451:
448:
438:
435:
389:
386:
371:
368:
357:
354:
348:
345:
239:
236:
234:of only 1.6Γ
.
214:
211:
185:
182:
180:
177:
111:Roger Kornberg
97:of their core
91:epigenetically
15:
9:
6:
4:
3:
2:
5156:
5145:
5142:
5140:
5137:
5135:
5132:
5131:
5129:
5122:
5112:
5109:
5107:
5104:
5102:
5099:
5095:
5092:
5091:
5090:
5087:
5086:
5084:
5080:
5070:
5067:
5065:
5062:
5060:
5057:
5055:
5052:
5050:
5047:
5045:
5042:
5040:
5037:
5035:
5032:
5030:
5027:
5025:
5022:
5020:
5017:
5015:
5012:
5010:
5007:
5005:
5002:
5000:
4997:
4995:
4992:
4991:
4989:
4987:
4983:
4977:
4974:
4972:
4969:
4967:
4964:
4962:
4959:
4957:
4954:
4953:
4951:
4949:
4945:
4939:
4936:
4933:
4929:
4925:
4922:
4921:
4919:
4915:
4909:
4906:
4902:
4899:
4897:
4894:
4892:
4889:
4887:
4884:
4883:
4882:
4879:
4875:
4872:
4870:
4867:
4866:
4865:
4862:
4860:
4857:
4855:
4852:
4851:
4849:
4847:and evolution
4843:
4835:
4832:
4830:
4827:
4825:
4822:
4820:
4817:
4816:
4815:
4812:
4808:
4805:
4803:
4800:
4798:
4795:
4793:
4790:
4788:
4785:
4784:
4783:
4780:
4778:
4775:
4773:
4772:Isochromosome
4770:
4768:
4765:
4763:
4760:
4758:
4755:
4753:
4750:
4748:
4745:
4743:
4740:
4737:
4734:
4732:
4728:
4725:
4723:
4720:
4717:
4713:
4709:
4706:
4705:
4703:
4699:
4693:
4690:
4688:
4685:
4683:
4680:
4678:
4675:
4671:
4668:
4666:
4663:
4662:
4661:
4658:
4656:
4652:
4649:
4647:
4644:
4642:
4639:
4638:
4636:
4630:
4626:
4622:
4615:
4610:
4608:
4603:
4601:
4596:
4595:
4592:
4586:
4582:
4579:
4577:
4574:
4572:
4569:
4567:
4564:
4562:
4559:
4557:
4556:
4553:
4549:
4547:
4544:
4542:
4539:
4538:
4525:
4521:
4516:
4511:
4507:
4503:
4499:
4495:
4491:
4484:
4476:
4472:
4467:
4462:
4458:
4454:
4450:
4446:
4442:
4435:
4427:
4423:
4418:
4413:
4409:
4405:
4401:
4394:
4386:
4382:
4378:
4374:
4370:
4366:
4359:
4351:
4347:
4342:
4337:
4333:
4329:
4325:
4318:
4310:
4306:
4302:
4298:
4294:
4290:
4286:
4282:
4278:
4274:
4267:
4259:
4255:
4251:
4247:
4242:
4237:
4233:
4229:
4225:
4218:
4210:
4206:
4202:
4198:
4194:
4190:
4183:
4175:
4169:
4165:
4161:
4157:
4150:
4142:
4138:
4133:
4128:
4124:
4120:
4116:
4112:
4108:
4101:
4093:
4089:
4085:
4081:
4077:
4073:
4066:
4058:
4054:
4050:
4048:9780121827793
4044:
4040:
4036:
4032:
4025:
4017:
4013:
4008:
4003:
3999:
3995:
3991:
3984:
3976:
3972:
3967:
3962:
3957:
3952:
3948:
3944:
3940:
3936:
3932:
3925:
3923:
3914:
3910:
3905:
3900:
3896:
3892:
3888:
3884:
3880:
3873:
3871:
3862:
3858:
3853:
3848:
3844:
3840:
3836:
3832:
3828:
3821:
3813:
3809:
3804:
3799:
3794:
3789:
3785:
3781:
3777:
3770:
3762:
3758:
3753:
3748:
3744:
3740:
3736:
3732:
3728:
3721:
3713:
3709:
3704:
3699:
3695:
3691:
3687:
3683:
3679:
3672:
3664:
3660:
3655:
3650:
3645:
3640:
3636:
3632:
3628:
3621:
3613:
3609:
3604:
3599:
3595:
3591:
3587:
3583:
3579:
3572:
3564:
3560:
3556:
3552:
3548:
3544:
3540:
3536:
3529:
3521:
3517:
3513:
3509:
3505:
3501:
3497:
3493:
3489:
3485:
3478:
3470:
3466:
3462:
3458:
3453:
3448:
3444:
3440:
3436:
3429:
3421:
3417:
3413:
3409:
3405:
3401:
3397:
3393:
3389:
3385:
3378:
3370:
3366:
3362:
3358:
3354:
3350:
3346:
3342:
3335:
3327:
3323:
3318:
3313:
3309:
3305:
3301:
3294:
3286:
3282:
3278:
3274:
3269:
3264:
3260:
3256:
3252:
3245:
3237:
3233:
3229:
3225:
3220:
3215:
3211:
3207:
3203:
3199:
3195:
3188:
3180:
3176:
3172:
3168:
3163:
3158:
3154:
3150:
3146:
3139:
3131:
3127:
3122:
3117:
3113:
3109:
3105:
3101:
3097:
3090:
3082:
3078:
3073:
3068:
3064:
3060:
3056:
3049:
3041:
3037:
3033:
3029:
3025:
3024:10.1038/23506
3021:
3017:
3013:
3009:
3005:
2998:
2990:
2986:
2981:
2976:
2972:
2968:
2964:
2960:
2956:
2952:
2948:
2941:
2933:
2929:
2924:
2919:
2915:
2911:
2907:
2903:
2899:
2892:
2884:
2880:
2876:
2872:
2868:
2864:
2860:
2856:
2849:
2841:
2837:
2833:
2829:
2825:
2824:10.1038/47412
2821:
2817:
2813:
2809:
2805:
2798:
2790:
2786:
2781:
2776:
2771:
2766:
2762:
2758:
2754:
2750:
2746:
2739:
2731:
2727:
2722:
2717:
2713:
2709:
2705:
2701:
2697:
2690:
2688:
2679:
2675:
2671:
2667:
2662:
2657:
2653:
2649:
2645:
2641:
2637:
2630:
2622:
2618:
2613:
2608:
2604:
2600:
2596:
2592:
2588:
2584:
2580:
2573:
2565:
2561:
2557:
2553:
2549:
2545:
2541:
2537:
2530:
2522:
2518:
2514:
2510:
2506:
2502:
2498:
2494:
2487:
2485:
2476:
2472:
2467:
2462:
2458:
2454:
2450:
2446:
2442:
2435:
2427:
2423:
2418:
2413:
2408:
2403:
2399:
2395:
2394:PLOS Genetics
2391:
2384:
2376:
2372:
2368:
2364:
2360:
2356:
2349:
2341:
2337:
2332:
2327:
2323:
2319:
2315:
2311:
2307:
2300:
2292:
2288:
2283:
2278:
2273:
2268:
2264:
2260:
2256:
2252:
2248:
2241:
2233:
2229:
2225:
2221:
2217:
2213:
2209:
2205:
2201:
2197:
2190:
2182:
2178:
2174:
2170:
2166:
2162:
2155:
2147:
2143:
2138:
2133:
2129:
2125:
2121:
2117:
2113:
2109:
2105:
2098:
2090:
2086:
2082:
2078:
2074:
2070:
2063:
2055:
2051:
2047:
2043:
2039:
2035:
2031:
2027:
2023:
2016:
2008:
2001:
1993:
1989:
1985:
1981:
1977:
1973:
1966:
1964:
1955:
1949:
1945:
1938:
1936:
1927:
1923:
1918:
1913:
1909:
1905:
1901:
1897:
1893:
1886:
1878:
1874:
1870:
1866:
1861:
1856:
1852:
1848:
1844:
1840:
1836:
1829:
1827:
1818:
1814:
1810:
1808:9780121827793
1804:
1800:
1796:
1792:
1785:
1777:
1773:
1769:
1765:
1761:
1757:
1750:
1742:
1738:
1733:
1728:
1724:
1720:
1716:
1712:
1708:
1701:
1693:
1689:
1685:
1681:
1677:
1673:
1666:
1658:
1654:
1650:
1646:
1642:
1638:
1634:
1630:
1623:
1615:
1611:
1607:
1603:
1599:
1595:
1591:
1587:
1583:
1579:
1572:
1564:
1560:
1555:
1550:
1546:
1542:
1538:
1534:
1530:
1523:
1521:
1519:
1517:
1515:
1513:
1504:
1500:
1496:
1492:
1488:
1484:
1477:
1469:
1465:
1460:
1455:
1451:
1447:
1443:
1439:
1435:
1428:
1420:
1416:
1412:
1408:
1403:
1402:10.1038/26521
1398:
1394:
1390:
1386:
1382:
1378:
1371:
1363:
1359:
1354:
1349:
1345:
1341:
1337:
1333:
1329:
1322:
1314:
1308:
1304:
1297:
1289:
1285:
1281:
1277:
1273:
1272:10.1038/38444
1269:
1265:
1261:
1257:
1253:
1246:
1244:
1234:
1232:
1223:
1219:
1214:
1209:
1205:
1201:
1197:
1190:
1182:
1178:
1174:
1170:
1166:
1162:
1158:
1154:
1147:
1139:
1135:
1131:
1127:
1123:
1119:
1115:
1111:
1104:
1096:
1092:
1088:
1084:
1080:
1076:
1072:
1068:
1061:
1053:
1049:
1045:
1041:
1034:
1026:
1022:
1018:
1014:
1010:
1006:
1002:
998:
994:
990:
983:
975:
971:
967:
965:9780128114322
961:
957:
953:
949:
945:
938:
930:
929:
921:
913:
907:
903:
902:
894:
886:
880:
875:
874:
865:
861:
851:
848:
847:
841:
818:
814:
804:
799:
795:
790:
786:
781:
780:
774:
771:
767:
757:
755:
751:
747:
737:
729:
723:
717:
714:
710:
706:
696:
694:
690:
689:
679:
673:
667:
658:
655:
651:
647:
646:
641:
637:
636:transcription
633:
629:
619:
616:
612:
607:
605:
595:
593:
589:
585:
581:
577:
573:
562:
560:
556:
552:
548:
544:
540:
536:
532:
528:
524:
514:
505:
496:
493:
492:S. cerevisiae
482:
480:
475:
465:
462:
458:
447:
445:
434:
432:
428:
423:
417:
415:
411:
407:
403:
394:
385:
383:
378:
367:
364:
353:
344:
342:
338:
334:
330:
325:
322:digestion of
321:
316:
308:
304:
298:
290:
283:
279:
275:
273:
269:
265:
261:
257:
253:
249:
245:
235:
233:
228:
225:
221:
190:
176:
174:
170:
165:
163:
158:
153:
151:
147:
143:
139:
135:
131:
127:
123:
119:
114:
112:
106:
104:
100:
96:
92:
87:
85:
81:
77:
72:
70:
66:
62:
58:
54:
50:
46:
42:
39:packaging in
38:
34:
26:
21:
5121:
4813:
4781:
4686:
4621:Cytogenetics
4550:
4497:
4494:Cell Reports
4493:
4483:
4448:
4444:
4434:
4407:
4403:
4393:
4368:
4365:Biochemistry
4364:
4358:
4331:
4327:
4317:
4276:
4272:
4266:
4231:
4227:
4217:
4195:(1): 15β20.
4192:
4188:
4182:
4155:
4149:
4117:(1): 45β57.
4114:
4110:
4100:
4075:
4071:
4065:
4030:
4024:
3997:
3993:
3983:
3938:
3934:
3889:(1): 73β93.
3886:
3882:
3834:
3830:
3820:
3783:
3779:
3769:
3737:(1): 17β40.
3734:
3730:
3720:
3685:
3681:
3671:
3634:
3631:PLOS Biology
3630:
3620:
3585:
3581:
3571:
3538:
3534:
3528:
3487:
3483:
3477:
3442:
3438:
3428:
3387:
3383:
3377:
3344:
3340:
3334:
3307:
3303:
3293:
3258:
3254:
3244:
3201:
3197:
3187:
3152:
3148:
3138:
3103:
3099:
3089:
3062:
3058:
3048:
3007:
3003:
2997:
2954:
2950:
2940:
2905:
2901:
2891:
2858:
2854:
2848:
2807:
2803:
2797:
2752:
2748:
2738:
2703:
2699:
2643:
2639:
2629:
2586:
2582:
2572:
2539:
2535:
2529:
2499:(1): 46β53.
2496:
2492:
2448:
2444:
2434:
2397:
2393:
2383:
2358:
2354:
2348:
2313:
2309:
2299:
2254:
2250:
2240:
2199:
2195:
2189:
2164:
2160:
2154:
2111:
2107:
2097:
2072:
2068:
2062:
2029:
2025:
2015:
2006:
2000:
1975:
1971:
1944:Biochemistry
1943:
1899:
1895:
1885:
1842:
1839:FEBS Letters
1838:
1790:
1784:
1759:
1755:
1749:
1714:
1710:
1700:
1675:
1671:
1665:
1632:
1628:
1622:
1581:
1577:
1571:
1536:
1532:
1486:
1482:
1476:
1441:
1437:
1427:
1384:
1380:
1370:
1335:
1331:
1321:
1302:
1296:
1255:
1251:
1203:
1199:
1189:
1156:
1152:
1146:
1113:
1109:
1103:
1070:
1066:
1060:
1043:
1033:
992:
988:
982:
947:
943:
937:
927:
920:
900:
893:
872:
864:
809:
763:
743:
734:
721:
702:
686:
684:
671:
664:
643:
639:
630:regions and
625:
614:
610:
608:
601:
568:
519:
502:
491:
488:
471:
456:
453:
440:
418:
409:
405:
399:
373:
359:
350:
317:
313:
241:
216:
166:
154:
115:
107:
88:
76:cell nucleus
73:
32:
30:
5139:Epigenetics
4834:Polycentric
4824:Monocentric
4807:Holocentric
4802:Acrocentric
4797:Telocentric
4787:Metacentric
4665:Euchromatin
4625:chromosomes
4555:Nucleosomes
4552:Proteopedia
2161:Biopolymers
950:: 308β317.
760:H2A and H2B
588:centromeres
539:methylation
527:methylation
523:acetylation
427:euchromatin
406:10-nm-fiber
382:acetylation
250:around the
5128:Categories
4986:Centromere
4917:Structures
4896:Polyploidy
4886:Aneuploidy
4687:Nucleosome
4677:Chromosome
4000:(1): 2β9.
3786:: e34100.
3637:(3): e65.
1332:Chromosoma
856:References
850:Chromomere
650:heat shock
555:epigenetic
414:H1 histone
377:N-terminal
272:linker DNA
169:protamines
150:linker DNA
118:base pairs
84:chromosome
41:eukaryotes
33:nucleosome
4938:Protamine
4845:Processes
4829:Dicentric
4682:Chromatid
4660:Chromatin
4641:Karyotype
4309:205097512
2046:1559-0305
1419:204997317
744:Histones
740:H3 and H4
705:disulfide
402:chromatin
337:apoptosis
324:chromatin
244:base pair
179:Structure
128:around a
80:chromatin
49:chromatin
27:structure
25:chromatin
5082:See also
4924:Telomere
4891:Euploidy
4819:Acentric
4716:allosome
4708:Autosome
4634:concepts
4524:27149855
4475:18408730
4426:15516689
4350:16464854
4301:10591219
4258:13502921
4141:29113904
4057:14870657
3975:30395604
3913:33395550
3861:31171402
3812:29809147
3761:28303166
3712:25063301
3663:18351804
3612:20351051
3563:12816925
3555:17873876
3512:18075583
3461:17320508
3412:17392789
3369:34509771
3361:23085715
3326:15099516
3277:14675539
3228:14645854
3171:11163188
3130:14690611
3081:12620227
3032:10466730
2989:20816070
2932:15808514
2883:34704745
2875:15523479
2832:10638745
2789:14172992
2730:28537572
2678:43625066
2670:15961632
2621:19644123
2564:11299024
2556:15258568
2521:14540078
2513:15580276
2475:22821566
2426:18654629
2340:19625488
2291:16617109
2224:16001076
2181:12666178
2146:16862119
2089:12079350
1992:11092917
1926:11566884
1877:41706403
1869:15680970
1817:14870658
1776:11092917
1741:15299701
1657:20178479
1563:12540921
1362:35061087
1181:41520634
1138:21270171
1025:83480762
974:43929234
844:See also
722:in vivo
693:dialysis
688:in vitro
672:in vitro
628:promoter
615:in vitro
543:arginine
437:Dynamics
318:Partial
310:)
213:Overview
120:(bp) of
99:histones
5094:Plasmid
4948:Histone
4859:Meiosis
4854:Mitosis
4515:5063657
4466:2678716
4385:4027229
4281:Bibcode
4250:7600578
4209:2332416
4132:5757783
4092:8151701
4016:9169189
3994:Methods
3966:6237416
3943:Bibcode
3904:8428145
3852:7092708
3803:6031429
3752:5331113
3703:4132745
3654:2267817
3603:2854390
3520:4305576
3492:Bibcode
3469:1773333
3420:4416890
3392:Bibcode
3236:9881829
3206:Bibcode
3198:Science
3179:7911590
3121:3428624
3040:2841873
3012:Bibcode
2980:2931741
2959:Bibcode
2923:2855496
2840:4418993
2812:Bibcode
2757:Bibcode
2721:5831138
2648:Bibcode
2640:Science
2612:2775800
2591:Bibcode
2583:Science
2466:3467062
2417:2453330
2375:2738923
2331:2761276
2282:1436021
2259:Bibcode
2232:4387396
2204:Bibcode
2137:2623244
2116:Bibcode
2054:9718585
1847:Bibcode
1719:Bibcode
1692:8678288
1649:8586054
1614:4355982
1606:6482966
1586:Bibcode
1541:Bibcode
1503:1297351
1459:2111545
1411:9759733
1389:Bibcode
1353:8776978
1288:4328827
1280:9305837
1260:Bibcode
1222:2834270
1173:2849508
1130:3568125
1095:4825889
1075:Bibcode
1067:Science
1017:4128918
997:Bibcode
989:Science
873:Biology
777:Gallery
611:in vivo
173:Archaea
130:histone
4655:Genome
4646:Ploidy
4522:
4512:
4473:
4463:
4424:
4383:
4348:
4307:
4299:
4273:Nature
4256:
4248:
4207:
4170:
4139:
4129:
4090:
4055:
4045:
4014:
3973:
3963:
3911:
3901:
3859:
3849:
3810:
3800:
3759:
3749:
3710:
3700:
3661:
3651:
3610:
3600:
3561:
3553:
3518:
3510:
3484:Nature
3467:
3459:
3418:
3410:
3384:Nature
3367:
3359:
3324:
3285:145525
3283:
3275:
3234:
3226:
3177:
3169:
3128:
3118:
3079:
3038:
3030:
3004:Nature
2987:
2977:
2930:
2920:
2881:
2873:
2838:
2830:
2804:Nature
2787:
2780:300163
2777:
2728:
2718:
2676:
2668:
2619:
2609:
2562:
2554:
2519:
2511:
2473:
2463:
2424:
2414:
2373:
2338:
2328:
2289:
2279:
2230:
2222:
2196:Nature
2179:
2144:
2134:
2108:Nature
2087:
2052:
2044:
1990:
1950:
1924:
1917:125637
1914:
1875:
1867:
1815:
1805:
1774:
1739:
1690:
1655:
1647:
1612:
1604:
1578:Nature
1561:
1533:Nature
1501:
1468:387806
1466:
1456:
1417:
1409:
1381:Nature
1360:
1350:
1309:
1286:
1278:
1252:Nature
1220:
1179:
1171:
1136:
1128:
1093:
1023:
1015:
972:
962:
908:
881:
580:T cell
551:serine
545:; and
535:lysine
457:in cis
266:, and
144:, and
67:, and
4932:TINF2
4701:Types
4632:Basic
4305:S2CID
4254:S2CID
3780:eLife
3559:S2CID
3516:S2CID
3465:S2CID
3416:S2CID
3365:S2CID
3281:S2CID
3232:S2CID
3175:S2CID
3036:S2CID
2879:S2CID
2836:S2CID
2674:S2CID
2560:S2CID
2517:S2CID
2228:S2CID
1873:S2CID
1653:S2CID
1610:S2CID
1415:S2CID
1284:S2CID
1177:S2CID
1134:S2CID
1021:S2CID
970:S2CID
592:CENPA
529:, or
320:DNAse
4714:(or
4585:NCBI
4520:PMID
4471:PMID
4422:PMID
4381:PMID
4346:PMID
4297:PMID
4246:PMID
4228:Cell
4205:PMID
4168:ISBN
4137:PMID
4088:PMID
4053:PMID
4043:ISBN
4012:PMID
3971:PMID
3909:PMID
3857:PMID
3808:PMID
3757:PMID
3708:PMID
3659:PMID
3608:PMID
3551:PMID
3508:PMID
3457:PMID
3439:Cell
3408:PMID
3357:PMID
3322:PMID
3273:PMID
3255:Cell
3224:PMID
3167:PMID
3149:Cell
3126:PMID
3077:PMID
3028:PMID
2985:PMID
2928:PMID
2871:PMID
2828:PMID
2785:PMID
2726:PMID
2666:PMID
2617:PMID
2552:PMID
2509:PMID
2471:PMID
2422:PMID
2371:PMID
2336:PMID
2287:PMID
2220:PMID
2177:PMID
2142:PMID
2085:PMID
2050:PMID
2042:ISSN
1988:PMID
1948:ISBN
1922:PMID
1865:PMID
1813:PMID
1803:ISBN
1772:PMID
1737:PMID
1688:PMID
1645:PMID
1602:PMID
1559:PMID
1499:PMID
1464:PMID
1407:PMID
1358:PMID
1307:ISBN
1276:PMID
1218:PMID
1169:PMID
1153:Cell
1126:PMID
1110:Cell
1091:PMID
1013:PMID
960:ISBN
906:ISBN
879:ISBN
836:and
817:1EQZ
768:and
748:and
576:H2AX
572:H2AZ
474:FRET
461:CTCF
307:1EQZ
204:and
198:H2B
194:H2A
4966:H2B
4961:H2A
4583:at
4510:PMC
4502:doi
4461:PMC
4453:doi
4412:doi
4408:280
4373:doi
4336:doi
4332:281
4289:doi
4277:402
4236:doi
4197:doi
4193:107
4160:doi
4127:PMC
4119:doi
4115:430
4080:doi
4076:237
4035:doi
4002:doi
3961:PMC
3951:doi
3899:PMC
3891:doi
3847:PMC
3839:doi
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