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Items: 1 to 20 of 101

1.

Bi-functional cross-linking reagents efficiently capture protein-DNA complexes in Drosophila embryos.

Aoki T, Wolle D, Preger-Ben Noon E, Dai Q, Lai EC, Schedl P.

Fly (Austin). 2014;8(1):43-51. doi: 10.4161/fly.26805. Epub 2013 Dec 13.

2.
3.

ChIP bias as a function of cross-linking time.

Baranello L, Kouzine F, Sanford S, Levens D.

Chromosome Res. 2016 May;24(2):175-81. doi: 10.1007/s10577-015-9509-1. Epub 2015 Dec 21.

PMID:
26685864
4.

Analysis of chromatin structure by in vivo formaldehyde cross-linking.

Orlando V, Strutt H, Paro R.

Methods. 1997 Feb;11(2):205-14.

PMID:
8993033
5.

An in vivo crosslinking approach to isolate protein complexes from Drosophila embryos.

Gao M, McCluskey P, Loganathan SN, Arkov AL.

J Vis Exp. 2014 Apr 23;(86). doi: 10.3791/51387.

6.

Isolation of intracellular protein--DNA complexes using HaloCHIP, an antibody-free alternative to chromatin immunoprecipitation.

Daniels DL, Urh M.

Methods Mol Biol. 2013;977:111-24. doi: 10.1007/978-1-62703-284-1_9.

PMID:
23436357
7.

Successful co-immunoprecipitation of Oct4 and Nanog using cross-linking.

Zhang L, Rayner S, Katoku-Kikyo N, Romanova L, Kikyo N.

Biochem Biophys Res Commun. 2007 Sep 28;361(3):611-4. Epub 2007 Jul 25.

8.

Genome-wide localization of replication factors.

Lubelsky Y, MacAlpine HK, MacAlpine DM.

Methods. 2012 Jun;57(2):187-95. doi: 10.1016/j.ymeth.2012.03.022. Epub 2012 Mar 24.

PMID:
22465279
9.

Chromatin immunoprecipitation for determining the association of proteins with specific genomic sequences in vivo.

Aparicio O, Geisberg JV, Struhl K.

Curr Protoc Cell Biol. 2004 Sep;Chapter 17:Unit 17.7. doi: 10.1002/0471143030.cb1707s23. Review.

PMID:
18228445
10.

In vivo formaldehyde cross-linking: it is time for black box analysis.

Gavrilov A, Razin SV, Cavalli G.

Brief Funct Genomics. 2015 Mar;14(2):163-5. doi: 10.1093/bfgp/elu037. Epub 2014 Sep 19.

PMID:
25241225
11.

Fish'n ChIPs: chromatin immunoprecipitation in the zebrafish embryo.

Lindeman LC, Vogt-Kielland LT, Aleström P, Collas P.

Methods Mol Biol. 2009;567:75-86. doi: 10.1007/978-1-60327-414-2_5. Review.

PMID:
19588086
12.

Chromatin immunoprecipitation for determining the association of proteins with specific genomic sequences in vivo.

Aparicio O, Geisberg JV, Sekinger E, Yang A, Moqtaderi Z, Struhl K.

Curr Protoc Mol Biol. 2005 Feb;Chapter 21:Unit 21.3. doi: 10.1002/0471142727.mb2103s69.

PMID:
18265358
13.

Finding Downstream Target DNAs for Chromatin Proteins by X-CHIP in Drosophila.

Nègre N, Cavalli G.

Mapping Protein/DNA Interactions by Cross-Linking [Internet]. Paris: Institut national de la santé et de la recherche médicale; 2001.

14.

Utility of formaldehyde cross-linking and mass spectrometry in the study of protein-protein interactions.

Sutherland BW, Toews J, Kast J.

J Mass Spectrom. 2008 Jun;43(6):699-715. doi: 10.1002/jms.1415.

PMID:
18438963
15.
16.

Fixated on fixation: using ChIP to interrogate the dynamics of chromatin interactions.

Keren L, Segal E.

Genome Biol. 2013 Nov 21;14(11):138. doi: 10.1186/gb4139.

18.

Elba, a novel developmentally regulated chromatin boundary factor is a hetero-tripartite DNA binding complex.

Aoki T, Sarkeshik A, Yates J, Schedl P.

Elife. 2012 Dec 13;1:e00171. doi: 10.7554/eLife.00171.

19.

Chromatin composition is changed by poly(ADP-ribosyl)ation during chromatin immunoprecipitation.

Beneke S, Meyer K, Holtz A, Hüttner K, Bürkle A.

PLoS One. 2012;7(3):e32914. doi: 10.1371/journal.pone.0032914. Epub 2012 Mar 30.

20.

Chromatin immunoprecipitation in adult zebrafish red cells.

Trompouki E, Bowman TV, Dibiase A, Zhou Y, Zon LI.

Methods Cell Biol. 2011;104:341-52. doi: 10.1016/B978-0-12-374814-0.00019-7.

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