The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
A Candidate X-linked Mental Retardation Gene Is a Component of a New Family of Histone Deacetylase-containing Complexes
Open accessAbstract
Eukaryotic genes are under the control of regulatory complexes acting through chromatin structure to control gene expression. Here we report the identification of a family of multiprotein corepressor complexes that function through modifying chromatin structure to keep genes silent. The polypeptide composition of these complexes has in common a core of two subunits, HDAC1,2 and BHC110, an FAD-binding protein. A candidate X-linked mental retardation gene and the transcription initiation factor II-I (TFII-I) are components of a novel member of this family of complexes. Other subunits of these complexes include polypeptides associated with cancer causing chromosomal translocations. These findings not only delineate a novel class of multiprotein complexes involved in transcriptional repression but also reveal an unanticipated role for TFII-I in transcriptional repression.
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
Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
Imai, S.-I., Armstrong, C. M., Kaeberlein, M., & Guarente, L. (2000) · Nature · doi:10.1038/35001622 · Cited by 3,510
A Mammalian Histone Deacetylase Related to the Yeast Transcriptional Regulator Rpd3p
Taunton, J., Hassig, C. A., & Schreiber, S. L. (1996) · Science · doi:10.1126/science.272.5260.408 · Cited by 1,829
Three proteins define a class of human histone deacetylases related to yeast Hda1p
Grozinger, C. M., Hassig, C. A., & Schreiber, S. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.9.4868 · Cited by 770
Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex
Tong, J. K., Hassig, C. A., Schnitzler, G. R., Kingston, R. E., & Schreiber, S. L. (1998) · Nature · doi:10.1038/27699 · Cited by 692
Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex
Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P., & Reinberg, D. (1997) · Cell · doi:10.1016/s0092-8674(00)80216-0 · Cited by 578
Humphrey, G. W., Wang, Y., Russanova, V. R., Hirai, T., Qin, J., Nakatani, Y., & Howard, B. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007372200 · Cited by 331
Cited by
Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
Shi, Y., Lan, F., Matson, C., Mulligan, P., Whetstine, J. R., Cole, P. A., Casero, R. A., & Shi, Y. (2004) · Cell · doi:10.1016/j.cell.2004.12.012 · Cited by 4,051
LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
Metzger, E., Wissmann, M., Yin, N., Müller, J. M., Schneider, R., Peters, A. H. F. M., Günther, T., Buettner, R., & Schüle, R. (2005) · Nature · doi:10.1038/nature04020 · Cited by 1,733
Shilatifard, A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142422 · Cited by 1,103
Regulation of histone methylation by demethylimination and demethylation
Klose, R. J., & Zhang, Y. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2143 · Cited by 887
Regulation of LSD1 Histone Demethylase Activity by Its Associated Factors
Shi, Y.-J., Matson, C., Lan, F., Iwase, S., Baba, T., & Shi, Y. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.08.027 · Cited by 886
Metadata
- Authors
- Hakimi, M.-A., Dong, Y., Lane, W. S., Speicher, D. W., & Shiekhattar, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-02
- Volume
- 278
- Issue
- 9
- Pages
- 7234-7239
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2077642616
- Cited by
- 221
- References
- 6
- FWCI
- 3.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: A Candidate X-linked Mental Retardation Gene Is a Component of a New Family of Histone Deacetylase-containing Complexes. https://app.cochat.ai/papers/10.1074/jbc.m208992200
- The paper
- Hakimi, M.-A., Dong, Y., Lane, W. S., Speicher, D. W., & Shiekhattar, R. (2003). A Candidate X-linked Mental Retardation Gene Is a Component of a New Family of Histone Deacetylase-containing Complexes. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m208992200
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.