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For: Hassan YI, Moriyama H, Olsen LJ, Bi X, Zempleni J. N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition. Mol Genet Metab 2009;96:183-8. [PMID: 19157941 DOI: 10.1016/j.ymgme.2008.12.006] [Cited by in Crossref: 20] [Cited by in F6Publishing: 19] [Article Influence: 1.5] [Reference Citation Analysis]
Number Citing Articles
1 Zempleni J, Wijeratne SSK, Kuroishi T. Biotin. In: Erdman JW, Macdonald IA, Zeisel SH, editors. Present Knowledge in Nutrition. Oxford: Wiley-Blackwell; 2012. pp. 359-74. [DOI: 10.1002/9781119946045.ch23] [Cited by in Crossref: 12] [Cited by in F6Publishing: 1] [Article Influence: 1.2] [Reference Citation Analysis]
2 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]
3 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]
4 Lee CK, Cheong C, Jeon YH. Substrate recognition characteristics of human holocarboxylase synthetase for biotin ligation. Biochem Biophys Res Commun 2010;391:455-60. [PMID: 19914215 DOI: 10.1016/j.bbrc.2009.11.079] [Reference Citation Analysis]
5 Sternicki LM, Wegener KL, Bruning JB, Booker GW, Polyak SW. Mechanisms Governing Precise Protein Biotinylation. Trends in Biochemical Sciences 2017;42:383-94. [DOI: 10.1016/j.tibs.2017.02.001] [Cited by in Crossref: 13] [Cited by in F6Publishing: 12] [Article Influence: 2.6] [Reference Citation Analysis]
6 Zempleni J, Chew YC, Bao B, Pestinger V, Wijeratne SS. Repression of transposable elements by histone biotinylation. J Nutr 2009;139:2389-92. [PMID: 19812216 DOI: 10.3945/jn.109.111856] [Cited by in Crossref: 18] [Cited by in F6Publishing: 17] [Article Influence: 1.4] [Reference Citation Analysis]
7 Pendini NR, Yap MY, Traore DA, Polyak SW, Cowieson NP, Abell A, Booker GW, Wallace JC, Wilce JA, Wilce MC. Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: an antibiotic target. Protein Sci 2013;22:762-73. [PMID: 23559560 DOI: 10.1002/pro.2262] [Cited by in Crossref: 27] [Cited by in F6Publishing: 26] [Article Influence: 3.0] [Reference Citation Analysis]
8 Hassan YI, Moriyama H, Zempleni J. The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation. Arch Biochem Biophys 2010;495:35-41. [PMID: 20026029 DOI: 10.1016/j.abb.2009.12.017] [Cited by in Crossref: 5] [Cited by in F6Publishing: 4] [Article Influence: 0.4] [Reference Citation Analysis]
9 Sittiwong W, Cordonier EL, Zempleni J, Dussault PH. β-Keto and β-hydroxyphosphonate analogs of biotin-5'-AMP are inhibitors of holocarboxylase synthetase. Bioorg Med Chem Lett 2014;24:5568-71. [PMID: 25466176 DOI: 10.1016/j.bmcl.2014.11.010] [Cited by in Crossref: 8] [Cited by in F6Publishing: 8] [Article Influence: 1.0] [Reference Citation Analysis]
10 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]
11 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]
12 Wongkittichote P, Ah Mew N, Chapman KA. Propionyl-CoA carboxylase - A review. Mol Genet Metab 2017;122:145-52. [PMID: 29033250 DOI: 10.1016/j.ymgme.2017.10.002] [Cited by in Crossref: 65] [Cited by in F6Publishing: 61] [Article Influence: 13.0] [Reference Citation Analysis]
13 Sternicki LM, Nguyen S, Pacholarz KJ, Barran P, Pendini NR, Booker GW, Huet Y, Baltz R, Wegener KL, Pukala TL, Polyak SW. Biochemical characterisation of class III biotin protein ligases from Botrytis cinerea and Zymoseptoria tritici. Arch Biochem Biophys 2020;691:108509. [PMID: 32717225 DOI: 10.1016/j.abb.2020.108509] [Reference Citation Analysis]
14 Cordonier EL, Adjam R, Teixeira DC, Onur S, Zbasnik R, Read PE, Döring F, Schlegel VL, Zempleni J. Resveratrol compounds inhibit human holocarboxylase synthetase and cause a lean phenotype in Drosophila melanogaster. J Nutr Biochem 2015;26:1379-84. [PMID: 26303405 DOI: 10.1016/j.jnutbio.2015.07.004] [Cited by in Crossref: 2] [Cited by in F6Publishing: 1] [Article Influence: 0.3] [Reference Citation Analysis]
15 Mayende L, Swift RD, Bailey LM, Soares da Costa TP, Wallace JC, Booker GW, Polyak SW. A novel molecular mechanism to explain biotin-unresponsive holocarboxylase synthetase deficiency. J Mol Med 2012;90:81-8. [DOI: 10.1007/s00109-011-0811-x] [Cited by in Crossref: 24] [Cited by in F6Publishing: 21] [Article Influence: 2.2] [Reference Citation Analysis]
16 Lee CK, Cheong C, Jeon YH. The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein. FEBS Lett 2010;584:675-80. [PMID: 20085763 DOI: 10.1016/j.febslet.2009.12.059] [Cited by in Crossref: 6] [Cited by in F6Publishing: 6] [Article Influence: 0.5] [Reference Citation Analysis]
17 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]
18 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]
19 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]
20 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]
21 Liu Y, Chen Z, Dong H, Ding Y, He R, Kang L, Li D, Shen M, Jin Y, Zhang Y, Song J, Tian Y, Cao Y, Liang D, Yang Y. Analysis of the relationship between phenotypes and genotypes in 60 Chinese patients with propionic acidemia: a fourteen-year experience at a tertiary hospital. Orphanet J Rare Dis 2022;17:135. [PMID: 35331292 DOI: 10.1186/s13023-022-02271-3] [Reference Citation Analysis]