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For: Bailey L, Ivanov R, Wallace J, Polyak S. Artifactual detection of biotin on histones by streptavidin. Analytical Biochemistry 2008;373:71-7. [DOI: 10.1016/j.ab.2007.09.003] [Cited by in Crossref: 41] [Cited by in F6Publishing: 37] [Article Influence: 2.9] [Reference Citation Analysis]
Number Citing Articles
1 Pendini NR, Bailey LM, Booker GW, Wilce MC, Wallace JC, Polyak SW. Microbial biotin protein ligases aid in understanding holocarboxylase synthetase deficiency. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2008;1784:973-82. [DOI: 10.1016/j.bbapap.2008.03.011] [Cited by in Crossref: 25] [Cited by in F6Publishing: 23] [Article Influence: 1.8] [Reference Citation Analysis]
2 Bao B, Pestinger V, Hassan YI, Borgstahl GE, Kolar C, Zempleni J. Holocarboxylase synthetase is a chromatin protein and interacts directly with histone H3 to mediate biotinylation of K9 and K18. J Nutr Biochem 2011;22:470-5. [PMID: 20688500 DOI: 10.1016/j.jnutbio.2010.04.001] [Cited by in Crossref: 32] [Cited by in F6Publishing: 26] [Article Influence: 2.7] [Reference Citation Analysis]
3 Fernandez-mejia C, Lazo-de-la-vega-monroy M. Biological Effects of Pharmacological Concentrations of Biotin. J Evid Based Complementary Altern Med 2011;16:40-8. [DOI: 10.1177/1533210110392947] [Cited by in Crossref: 16] [Cited by in F6Publishing: 8] [Article Influence: 1.5] [Reference Citation Analysis]
4 Gravel RA. Holocarboxylase synthetase: a multitalented protein with roles in biotin transfer, gene regulation and chromatin dynamics. Mol Genet Metab 2014;111:305-6. [PMID: 24361214 DOI: 10.1016/j.ymgme.2013.11.010] [Cited by in Crossref: 2] [Article Influence: 0.2] [Reference Citation Analysis]
5 Healy S, Heightman TD, Hohmann L, Schriemer D, Gravel RA. Nonenzymatic biotinylation of histone H2A. Protein Sci 2009;18:314-28. [PMID: 19160459 DOI: 10.1002/pro.37] [Cited by in Crossref: 24] [Cited by in F6Publishing: 20] [Article Influence: 1.8] [Reference Citation Analysis]
6 Hassan YI, Zempleni J. A novel, enigmatic histone modification: biotinylation of histones by holocarboxylase synthetase: Nutrition Reviews©, Vol. 66, No. 12. Nutrition Reviews 2008;66:721-5. [DOI: 10.1111/j.1753-4887.2008.00127.x] [Cited by in Crossref: 30] [Cited by in F6Publishing: 25] [Article Influence: 2.1] [Reference Citation Analysis]
7 Zempleni J, Liu D, Camara DT, Cordonier EL. Novel roles of holocarboxylase synthetase in gene regulation and intermediary metabolism. Nutr Rev 2014;72:369-76. [PMID: 24684412 DOI: 10.1111/nure.12103] [Cited by in Crossref: 6] [Cited by in F6Publishing: 5] [Article Influence: 0.8] [Reference Citation Analysis]
8 Bao B, Wijeratne SS, Rodriguez-Melendez R, Zempleni J. Human holocarboxylase synthetase with a start site at methionine-58 is the predominant nuclear variant of this protein and has catalytic activity. Biochem Biophys Res Commun 2011;412:115-20. [PMID: 21802411 DOI: 10.1016/j.bbrc.2011.07.055] [Cited by in Crossref: 11] [Cited by in F6Publishing: 9] [Article Influence: 1.0] [Reference Citation Analysis]
9 Sakabe K, Wang Z, Hart GW. Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc Natl Acad Sci U S A 2010;107:19915-20. [PMID: 21045127 DOI: 10.1073/pnas.1009023107] [Cited by in Crossref: 251] [Cited by in F6Publishing: 235] [Article Influence: 20.9] [Reference Citation Analysis]
10 Esaki S, Malkaram SA, Zempleni J. Effects of single-nucleotide polymorphisms in the human holocarboxylase synthetase gene on enzyme catalysis. Eur J Hum Genet 2012;20:428-33. [PMID: 22027809 DOI: 10.1038/ejhg.2011.198] [Cited by in Crossref: 8] [Cited by in F6Publishing: 9] [Article Influence: 0.7] [Reference Citation Analysis]
11 Mock DM. Biotin: From Nutrition to Therapeutics. J Nutr 2017;147:1487-92. [PMID: 28701385 DOI: 10.3945/jn.116.238956] [Cited by in Crossref: 33] [Cited by in F6Publishing: 27] [Article Influence: 6.6] [Reference Citation Analysis]
12 Li Y, Hassan YI, Moriyama H, Zempleni J. Holocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events. J Nutr Biochem 2013;24:1446-52. [PMID: 23337344 DOI: 10.1016/j.jnutbio.2012.12.003] [Cited by in Crossref: 15] [Cited by in F6Publishing: 12] [Article Influence: 1.7] [Reference Citation Analysis]
13 Cavalieri V. The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape. Genes (Basel) 2021;12:1596. [PMID: 34680990 DOI: 10.3390/genes12101596] [Cited by in Crossref: 1] [Article Influence: 1.0] [Reference Citation Analysis]
14 Salazar-Anzures T, Pastén-Hidalgo K, Sicilia-Argumedo G, Riverón-Negrete L, Hernández-Vázquez AJ, Fernanadez-Mejia C. Dietary biotin supplementation increases proliferation pathways in mice testes without affecting serum follicle-stimulating hormone levels and stem cell factor expression. Toxicol Appl Pharmacol 2021;433:115774. [PMID: 34699867 DOI: 10.1016/j.taap.2021.115774] [Reference Citation Analysis]
15 Zee BM, Young NL, Garcia BA. Quantitative proteomic approaches to studying histone modifications. Curr Chem Genomics 2011;5:106-14. [PMID: 21966350 DOI: 10.2174/1875397301005010106] [Cited by in Crossref: 15] [Cited by in F6Publishing: 12] [Article Influence: 1.4] [Reference Citation Analysis]
16 Singh MP, Wijeratne SS, Zempleni J. Biotinylation of lysine 16 in histone H4 contributes toward nucleosome condensation. Arch Biochem Biophys 2013;529:105-11. [PMID: 23219734 DOI: 10.1016/j.abb.2012.11.005] [Cited by in Crossref: 15] [Cited by in F6Publishing: 12] [Article Influence: 1.5] [Reference Citation Analysis]
17 Zempleni J, Li Y, Xue J, Cordonier EL. The role of holocarboxylase synthetase in genome stability is mediated partly by epigenomic synergies between methylation and biotinylation events. Epigenetics 2011;6:892-4. [PMID: 21555910 DOI: 10.4161/epi.6.7.15544] [Cited by in Crossref: 6] [Cited by in F6Publishing: 4] [Article Influence: 0.5] [Reference Citation Analysis]
18 Pestinger V, Wijeratne SS, Rodriguez-Melendez R, Zempleni J. Novel histone biotinylation marks are enriched in repeat regions and participate in repression of transcriptionally competent genes. J Nutr Biochem 2011;22:328-33. [PMID: 20691578 DOI: 10.1016/j.jnutbio.2010.02.011] [Cited by in Crossref: 39] [Cited by in F6Publishing: 37] [Article Influence: 3.3] [Reference Citation Analysis]
19 Zempleni J, Teixeira DC, Kuroishi T, Cordonier EL, Baier S. Biotin requirements for DNA damage prevention. Mutat Res 2012;733:58-60. [PMID: 21871906 DOI: 10.1016/j.mrfmmm.2011.08.001] [Cited by in Crossref: 19] [Cited by in F6Publishing: 13] [Article Influence: 1.7] [Reference Citation Analysis]
20 Abrams ST, Su D, Sahraoui Y, Lin Z, Cheng Z, Nesbitt K, Alhamdi Y, Harrasser M, Du M, Foley J, Lillicrap D, Wang G, Toh CH. Assembly of alternative prothrombinase by extracellular histones initiate and disseminate intravascular coagulation. Blood. 2020. [PMID: 32722805 DOI: 10.1182/blood.2019002973] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 3.0] [Reference Citation Analysis]
21 Romagnolo DF, Zempleni J, Selmin OI. Nuclear receptors and epigenetic regulation: opportunities for nutritional targeting and disease prevention. Adv Nutr 2014;5:373-85. [PMID: 25022987 DOI: 10.3945/an.114.005868] [Cited by in Crossref: 23] [Cited by in F6Publishing: 18] [Article Influence: 2.9] [Reference Citation Analysis]
22 Rios-Avila L, Pestinger V, Zempleni J. K16-biotinylated histone H4 is overrepresented in repeat regions and participates in the repression of transcriptionally competent genes in human Jurkat lymphoid cells. J Nutr Biochem 2012;23:1559-64. [PMID: 22192339 DOI: 10.1016/j.jnutbio.2011.10.009] [Cited by in Crossref: 9] [Cited by in F6Publishing: 9] [Article Influence: 0.8] [Reference Citation Analysis]
23 Reyes-Carmona S, Valadéz-Graham V, Aguilar-Fuentes J, Zurita M, León-Del-Río A. Trafficking and chromatin dynamics of holocarboxylase synthetase during development of Drosophila melanogaster. Mol Genet Metab 2011;103:240-8. [PMID: 21463962 DOI: 10.1016/j.ymgme.2011.03.005] [Cited by in Crossref: 3] [Article Influence: 0.3] [Reference Citation Analysis]
24 Xue J, Wijeratne SS, Zempleni J. Holocarboxylase synthetase synergizes with methyl CpG binding protein 2 and DNA methyltransferase 1 in the transcriptional repression of long-terminal repeats. Epigenetics 2013;8:504-11. [PMID: 23624957 DOI: 10.4161/epi.24449] [Cited by in Crossref: 20] [Cited by in F6Publishing: 16] [Article Influence: 2.2] [Reference Citation Analysis]
25 Hymbaugh SJ, Pecor LM, Tracy CM, Comstock LR. Protein Arginine Methyltransferase 1‐Dependent Labeling and Isolation of Histone H4 through N ‐Mustard Analogues of S ‐Adenosyl‐ l ‐methionine. ChemBioChem 2018;20:379-84. [DOI: 10.1002/cbic.201800477] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.3] [Reference Citation Analysis]
26 Chen X, Chou HH, Wurtele ES. Holocarboxylase synthetase 1 physically interacts with histone h3 in Arabidopsis. Scientifica (Cairo) 2013;2013:983501. [PMID: 24278788 DOI: 10.1155/2013/983501] [Cited by in Crossref: 2] [Cited by in F6Publishing: 2] [Article Influence: 0.2] [Reference Citation Analysis]
27 Alban C. Biotin (Vitamin B8) Synthesis in Plants. Biosynthesis of Vitamins in Plants Part B. Elsevier; 2011. pp. 39-66. [DOI: 10.1016/b978-0-12-385853-5.00005-2] [Cited by in Crossref: 8] [Article Influence: 0.7] [Reference Citation Analysis]
28 Eng WK, Giraud D, Schlegel VL, Wang D, Lee BH, Zempleni J. Identification and assessment of markers of biotin status in healthy adults. Br J Nutr 2013;110:321-9. [PMID: 23302490 DOI: 10.1017/S0007114512005065] [Cited by in Crossref: 20] [Cited by in F6Publishing: 9] [Article Influence: 2.2] [Reference Citation Analysis]
29 Bailey LM, Wallace JC, Polyak SW. Holocarboxylase synthetase: correlation of protein localisation with biological function. Arch Biochem Biophys 2010;496:45-52. [PMID: 20153287 DOI: 10.1016/j.abb.2010.01.015] [Cited by in Crossref: 19] [Cited by in F6Publishing: 15] [Article Influence: 1.6] [Reference Citation Analysis]
30 Kobza K, Sarath G, Zempleni J. Prokaryotic BirA ligase biotinylates K4, K9, K18 and K23 in histone H3. BMB Rep 2008;41:310-5. [PMID: 18452652 DOI: 10.5483/bmbrep.2008.41.4.310] [Cited by in Crossref: 36] [Cited by in F6Publishing: 31] [Article Influence: 2.6] [Reference Citation Analysis]
31 Satiaputra J, Eijkelkamp BA, McDevitt CA, Shearwin KE, Booker GW, Polyak SW. Biotin-mediated growth and gene expression in Staphylococcus aureus is highly responsive to environmental biotin. Appl Microbiol Biotechnol 2018;102:3793-803. [PMID: 29508030 DOI: 10.1007/s00253-018-8866-z] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 0.8] [Reference Citation Analysis]
32 Singh D, Pannier AK, Zempleni J. Identification of holocarboxylase synthetase chromatin binding sites in human mammary cell lines using the DNA adenine methyltransferase identification technology. Anal Biochem 2011;413:55-9. [PMID: 21303649 DOI: 10.1016/j.ab.2011.02.001] [Cited by in Crossref: 9] [Cited by in F6Publishing: 8] [Article Influence: 0.8] [Reference Citation Analysis]
33 Bao B, Rodriguez-Melendez R, Zempleni J. Cytosine methylation in miR-153 gene promoters increases the expression of holocarboxylase synthetase, thereby increasing the abundance of histone H4 biotinylation marks in HEK-293 human kidney cells. J Nutr Biochem 2012;23:635-9. [PMID: 21764280 DOI: 10.1016/j.jnutbio.2011.03.007] [Cited by in Crossref: 9] [Cited by in F6Publishing: 7] [Article Influence: 0.8] [Reference Citation Analysis]
34 Yao W, Wu N, Lin Z, Chen J, Li S, Weng S, Zhang L, Liu A, Lin X. Fluorescent turn-off competitive immunoassay for biotin based on hydrothermally synthesized carbon dots. Microchim Acta 2017;184:907-14. [DOI: 10.1007/s00604-017-2078-6] [Cited by in Crossref: 7] [Cited by in F6Publishing: 4] [Article Influence: 1.4] [Reference Citation Analysis]
35 Healy S, Perez-Cadahia B, Jia D, McDonald MK, Davie JR, Gravel RA. Biotin is not a natural histone modification. Biochim Biophys Acta 2009;1789:719-33. [PMID: 19770080 DOI: 10.1016/j.bbagrm.2009.09.003] [Cited by in Crossref: 27] [Cited by in F6Publishing: 25] [Article Influence: 2.1] [Reference Citation Analysis]
36 Liu D, Zempleni J. Holocarboxylase synthetase interacts physically with nuclear receptor co-repressor, histone deacetylase 1 and a novel splicing variant of histone deacetylase 1 to repress repeats. Biochem J 2014;461:477-86. [PMID: 24840043 DOI: 10.1042/BJ20131208] [Cited by in Crossref: 8] [Cited by in F6Publishing: 2] [Article Influence: 1.0] [Reference Citation Analysis]
37 Qaddoori Y, Abrams ST, Mould P, Alhamdi Y, Christmas SE, Wang G, Toh CH. Extracellular Histones Inhibit Complement Activation through Interacting with Complement Component 4. J Immunol. 2018;200:4125-4133. [PMID: 29752310 DOI: 10.4049/jimmunol.1700779] [Cited by in Crossref: 12] [Cited by in F6Publishing: 11] [Article Influence: 3.0] [Reference Citation Analysis]
38 Zempleni J, Hassan YI, Wijeratne SS. Biotin and biotinidase deficiency. Expert Rev Endocrinol Metab. 2008;3:715-724. [PMID: 19727438 DOI: 10.1586/17446651.3.6.715] [Cited by in Crossref: 92] [Cited by in F6Publishing: 71] [Article Influence: 11.5] [Reference Citation Analysis]
39 Trujillo-Gonzalez I, Cervantes-Roldan R, Gonzalez-Noriega A, Michalak C, Reyes-Carmona S, Barrios-Garcia T, Meneses-Morales I, Leon-Del-Rio A. Holocarboxylase synthetase acts as a biotin-independent transcriptional repressor interacting with HDAC1, HDAC2 and HDAC7. Mol Genet Metab 2014;111:321-30. [PMID: 24239178 DOI: 10.1016/j.ymgme.2013.10.016] [Cited by in Crossref: 8] [Cited by in F6Publishing: 5] [Article Influence: 0.9] [Reference Citation Analysis]
40 Kuroishi T, Rios-Avila L, Pestinger V, Wijeratne SS, Zempleni J. Biotinylation is a natural, albeit rare, modification of human histones. Mol Genet Metab 2011;104:537-45. [PMID: 21930408 DOI: 10.1016/j.ymgme.2011.08.030] [Cited by in Crossref: 41] [Cited by in F6Publishing: 35] [Article Influence: 3.7] [Reference Citation Analysis]
41 Atak S, Langlhofer G, Schaefer N, Kessler D, Meiselbach H, Delto C, Schindelin H, Villmann C. Disturbances of Ligand Potency and Enhanced Degradation of the Human Glycine Receptor at Affected Positions G160 and T162 Originally Identified in Patients Suffering from Hyperekplexia. Front Mol Neurosci 2015;8:79. [PMID: 26733802 DOI: 10.3389/fnmol.2015.00079] [Cited by in Crossref: 6] [Cited by in F6Publishing: 8] [Article Influence: 0.9] [Reference Citation Analysis]