The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
Open accessOverview
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
Hagemeier, C., Bannister, A. J., Cook, A., & Kouzarides, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.4.1580 · Cited by 303
Cited by
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679
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
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
The coregulator exchange in transcriptional functions of nuclear receptors
Glass, C. K., & Rosenfeld, M. G. (2000) · Genes & Development · doi:10.1101/gad.14.2.121 · Cited by 2,233
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
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
Self-citationThe silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases
Landry, J., Sutton, A., Tafrov, S. T., Heller, R. C., Stebbins, J., Pillus, L., & Sternglanz, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.110148297 · Cited by 970
Histones: annotating chromatin
Campos, E. I., & Reinberg, D. (2009) · Annual Review of Genetics · doi:10.1146/annurev.genet.032608.103928 · Cited by 852
Sauve, A. A., Wolberger, C., Schramm, V. L., & Boeke, J. D. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133500 · Cited by 763
Histone acetylation and deacetylation in yeast
Kurdistani, S. K., & Grunstein, M. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1075 · Cited by 677
Self-citationThe epigenetic regulation of mammalian telomeres
Blasco, M. A. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2047 · Cited by 600
Transcriptional coactivator complexes.
Näär, A. M., Lemon, B. D., & Tjian, R. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.475 · Cited by 571
Acetylation of p53 inhibits its ubiquitination by Mdm2
Li, M., Luo, J., Brooks, C. L., & Gu, W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200578200 · Cited by 503
Telomeric and extra-telomeric roles for telomerase and the telomere-binding proteins
Martínez, P., & Blasco, M. A. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3025 · Cited by 468
O'Hagan, H. M., Mohammad, H. P., & Baylin, S. B. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000155 · Cited by 386
Nielsen, A. L., Ortiz, J. A., You, J., Oulad‐Abdelghani, M., Khechumian, R., Gansmuller, A., Chambon, P., & Losson, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.22.6385 · Cited by 361
Evidence That Spt6p Controls Chromatin Structure by a Direct Interaction with Histones
Bortvin, A., & Winston, F. (1996) · Science · doi:10.1126/science.272.5267.1473 · Cited by 354
Spreading of silent chromatin: inaction at a distance
Talbert, P. B., & Henikoff, S. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1920 · Cited by 300
A Role of Poly (ADP-Ribose) Polymerase in NF- B Transcriptional Activation
Hassa, P. O., & Hottiger, M. O. (1999) · Biological Chemistry · doi:10.1515/bc.1999.118 · Cited by 296
Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277
A soybean cDNA encoding a chromatin-binding peptide inhibits mitosis of mammalian cells.
Galvez, A. F., & de Lumen, B. O. (1999) · Nature Biotechnology · doi:10.1038/8676 · Cited by 174
Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160
Role of shelterin in cancer and aging
Martínez, P., & Blasco, M. A. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00596.x · Cited by 136
Epigenetic inheritance: uncontested
Zhu, B., & Reinberg, D. (2011) · Cell Research · doi:10.1038/cr.2011.26 · Cited by 100
An, W., Palhan, V. B., Karymov, M. A., Leuba, S. H., & Roeder, R. G. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00497-5 · Cited by 100
Verhage, R. A., Van Gool, A. J., Groot, N. D., Hoeijmakers, J. H. J., Putte, P. V. D., & Brouwer, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.2.496 · Cited by 98
Hiramatsu, R., Akagi, K., Matsuoka, M., Sakumi, K., Nakamura, H., Kingsbury, L., David, C., Hardy, R. R., Yamamura, K.-I., & Sakano, H. (1995) · Cell · doi:10.1016/0092-8674(95)90138-8 · Cited by 45
Leiva-Peláez, O., Gutiérrez-Escobedo, G., López-Fuentes, E., Cruz-Mora, J., De Las Peñas, A., & Castaño, I. (2018) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2018.05.005 · Cited by 10
Metadata
- Authors
- Hecht, A., Laroche, T., Strahl-Bolsinger, S., Gasser, S. M., & Grunstein, M.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-02
- Volume
- 80
- Issue
- 4
- Pages
- 583-592
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1995111407
- Cited by
- 780
- References
- 1
- FWCI
- 22.74
- 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.
