The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Do protein motifs read the histone code?: Review articles
Open accessAbstract
The existence of different patterns of chemical modifications (acetylation, methylation, phosphorylation, ubiquitination and ADP-ribosylation) of the histone tails led, some years ago, to the histone code hypothesis. According to this hypothesis, these modifications would provide binding sites for proteins that can change the chromatin state to either active or repressed. Interestingly, some protein domains present in histone-modifying enzymes are known to interact with these covalent marks in the histone tails. This was first shown for the bromodomain, which was found to interact selectively with acetylated lysines at the histone tails. More recently, it has been described that the chromodomain can be targeted to methylation marks in histone N-terminal domains. Finally, the interaction between the SANT domain and histones is also well documented. Overall, experimental evidence suggests that these domains could be involved in the recruitment of histone-modifying enzymes to discrete chromosomal locations, and/or in the regulation their enzymatic activity. Within this context, we review the distribution of bromodomains, chromodomains and SANT domains among chromatin-modifying enzymes and discuss how they can contribute to the translation of the histone code.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845 · cited 5×
“(62) Chromodomain and ATP-dependent remodelling enzymes Chromodomains are found in (1) members of the SNF2/ RAD54 helicase family (CHD3 in Arabidopsis thaliana, Drosophila and C. elegans),(63–65) (2) Mi-2 and human Mi-2b or CHD4,(66–68) (3) Mi-2a or CHD3,(68) and (4) CHD5.”
BackgroundInfluentialStructure and ligand of a histone acetyltransferase bromodomain
Dhalluin, C., Carlson, J. E., Zeng, L., He, C., Aggarwal, A. K., Zhou, M.-M., & Zhou, M.-M. (1999) · Nature · doi:10.1038/20974 · Cited by 1,732
Ahringer, J. (2000) · Trends in Genetics · doi:10.1016/s0168-9525(00)02066-7 · Cited by 388
Position effect variegation and chromatin proteins
Reute, G., & Spierer, P. (1992) · BioEssays · doi:10.1002/bies.950140907 · Cited by 309
Human HDAC7 Histone Deacetylase Activity Is Associated with HDAC3in Vivo
Fischle, W., Dequiedt, F., Fillion, M., Hendzel, M. J., Voelter, W., & Verdin, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104935200 · Cited by 232
Cited by
Functions of Site-Specific Histone Acetylation and Deacetylation
Shahbazian, M. D., & Grunstein, M. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.052705.162114 · Cited by 1,635
Nagy, Z., & Tora, L. (2007) · Oncogene · doi:10.1038/sj.onc.1210604 · Cited by 417
Myc-binding-site recognition in the human genome is determined by chromatin context
Guccione, E., Martinato, F., Finocchiaro, G., Luzi, L., Tizzoni, L., Dall' Olio, V., Zardo, G., Nervi, C., Bernard, L., & Amati, B. (2006) · Nature Cell Biology · doi:10.1038/ncb1434 · Cited by 366
Chromatin modifier enzymes, the histone code and cancer
Santos-Rosa, H., & Caldas, C. (2005) · European Journal of Cancer · doi:10.1016/j.ejca.2005.08.010 · Cited by 337
Molecular and phenotypic aspects of CHD7 mutation in CHARGE syndrome
Zentner, G. E., Layman, W. S., Martin, D. M., & Scacheri, P. C. (2010) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.33323 · Cited by 313
NAD+-dependent deacetylation of H4 lysine 16 by class III HDACs
Vaquero, A., Sternglanz, R., & Reinberg, D. (2007) · Oncogene · doi:10.1038/sj.onc.1210617 · Cited by 296
Epigenetic responses to environmental change and their evolutionary implications
Turner, B. M. (2009) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2009.0125 · Cited by 293
Epigenetic alterations in autoimmune rheumatic diseases
Ballestar, E. (2011) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2011.16 · Cited by 173
Digging deep into “dirty” drugs – modulation of the methylation machinery
Pleyer, L., & Greil, R. (2015) · Drug Metabolism Reviews · doi:10.3109/03602532.2014.995379 · Cited by 84
“This process is referred to as ‘‘histone coding’’ (de la Cruz et al., 2005).”
Metadata
- Authors
- de la Cruz, X., Lois, S., Sánchez-Molina, S., & Martínez-Balbás, M. A.
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 2005-01-21
- Volume
- 27
- Issue
- 2
- Pages
- 164-175
- ISSN
- 0265-9247 (ISSN-L)
- OpenAlex
- W2058607217
- Cited by
- 259
- References
- 6
- FWCI
- 2.18
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
