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Items: 1 to 20 of 318


Regulation of replication fork progression through histone supply and demand.

Groth A, Corpet A, Cook AJ, Roche D, Bartek J, Lukas J, Almouzni G.

Science. 2007 Dec 21;318(5858):1928-31.


Replication stress interferes with histone recycling and predeposition marking of new histones.

Jasencakova Z, Scharf AN, Ask K, Corpet A, Imhof A, Almouzni G, Groth A.

Mol Cell. 2010 Mar 12;37(5):736-43. doi: 10.1016/j.molcel.2010.01.033.


Roles of histone chaperone CIA/Asf1 in nascent DNA elongation during nucleosome replication.

Ishikawa K, Ohsumi T, Tada S, Natsume R, Kundu LR, Nozaki N, Senda T, Enomoto T, Horikoshi M, Seki M.

Genes Cells. 2011 Oct;16(10):1050-62. doi: 10.1111/j.1365-2443.2011.01549.x. Epub 2011 Sep 7.


In vivo study of the nucleosome assembly functions of ASF1 histone chaperones in human cells.

Galvani A, Courbeyrette R, Agez M, Ochsenbein F, Mann C, Thuret JY.

Mol Cell Biol. 2008 Jun;28(11):3672-85. doi: 10.1128/MCB.00510-07. Epub 2008 Mar 31.


The histone chaperone Asf1 at the crossroads of chromatin and DNA checkpoint pathways.

Mousson F, Ochsenbein F, Mann C.

Chromosoma. 2007 Apr;116(2):79-93. Epub 2006 Dec 19. Review.


Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4.

Natsume R, Eitoku M, Akai Y, Sano N, Horikoshi M, Senda T.

Nature. 2007 Mar 15;446(7133):338-41. Epub 2007 Feb 11.


The histone chaperone anti-silencing function 1 stimulates the acetylation of newly synthesized histone H3 in S-phase.

Adkins MW, Carson JJ, English CM, Ramey CJ, Tyler JK.

J Biol Chem. 2007 Jan 12;282(2):1334-40. Epub 2006 Nov 15.


Acetylation of lysine 56 of histone H3 catalyzed by RTT109 and regulated by ASF1 is required for replisome integrity.

Han J, Zhou H, Li Z, Xu RM, Zhang Z.

J Biol Chem. 2007 Sep 28;282(39):28587-96. Epub 2007 Aug 9.


Structural insight into how the human helicase subunit MCM2 may act as a histone chaperone together with ASF1 at the replication fork.

Richet N, Liu D, Legrand P, Velours C, Corpet A, Gaubert A, Bakail M, Moal-Raisin G, Guerois R, Compper C, Besle A, Guichard B, Almouzni G, Ochsenbein F.

Nucleic Acids Res. 2015 Feb 18;43(3):1905-17. doi: 10.1093/nar/gkv021. Epub 2015 Jan 23.


The histone chaperone Asf1 is dispensable for direct de novo histone deposition in Xenopus egg extracts.

Ray-Gallet D, Quivy JP, Silljé HW, Nigg EA, Almouzni G.

Chromosoma. 2007 Oct;116(5):487-96. Epub 2007 Jun 19.


Asf1, a loveseat for a histone couple.

Bao Y, Shen X.

Cell. 2006 Nov 3;127(3):458-60.


Histone chaperones: 30 years from isolation to elucidation of the mechanisms of nucleosome assembly and disassembly.

Eitoku M, Sato L, Senda T, Horikoshi M.

Cell Mol Life Sci. 2008 Feb;65(3):414-44. Review.


Potential role of the histone chaperone, CAF-1, in transcription.

Kim HJ, Seol JH, Cho EJ.

BMB Rep. 2009 Apr 30;42(4):227-31.


Human Asf1 regulates the flow of S phase histones during replicational stress.

Groth A, Ray-Gallet D, Quivy JP, Lukas J, Bartek J, Almouzni G.

Mol Cell. 2005 Jan 21;17(2):301-11.


The tango of histone marks and chaperones at replication fork.

Falbo KB, Shen X.

Mol Cell. 2010 Mar 12;37(5):595-6. doi: 10.1016/j.molcel.2010.02.019.


Global replication-independent histone H4 exchange in budding yeast.

Linger J, Tyler JK.

Eukaryot Cell. 2006 Oct;5(10):1780-7. Epub 2006 Aug 25.


Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus.

Malay AD, Umehara T, Matsubara-Malay K, Padmanabhan B, Yokoyama S.

J Biol Chem. 2008 May 16;283(20):14022-31. doi: 10.1074/jbc.M800594200. Epub 2008 Mar 11.


Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing.

Sharp JA, Fouts ET, Krawitz DC, Kaufman PD.

Curr Biol. 2001 Apr 3;11(7):463-73.


Tousled-like kinases phosphorylate Asf1 to promote histone supply during DNA replication.

Klimovskaia IM, Young C, Strømme CB, Menard P, Jasencakova Z, Mejlvang J, Ask K, Ploug M, Nielsen ML, Jensen ON, Groth A.

Nat Commun. 2014 Mar 6;5:3394. doi: 10.1038/ncomms4394.

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