C Romier
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Explore the profile of C Romier including associated specialties, affiliations and a list of published articles.
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Articles
16
Citations
442
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Recent Articles
1.
Wutz D, Gluhacevic D, Chakrabarti A, Schmidtkunz K, Robaa D, Erdmann F, et al.
Org Biomol Chem
. 2017 May;
15(22):4882-4896.
PMID: 28537315
Histone deacetylases (HDACs) play a crucial role in numerous biological processes and therefore are targeted in anticancer research and in the field of epigenetics. Dithienylethenes (DTEs) and fulgimides were functionalized...
2.
Gangloff Y, Pointud J, Thuault S, Carre L, Romier C, Muratoglu S, et al.
Mol Cell Biol
. 2001 Jul;
21(15):5109-21.
PMID: 11438666
The RNA polymerase II transcription factor TFIID comprises the TATA binding protein (TBP) and a set of TBP-associated factors (TAF(II)s). TFIID has been extensively characterized for yeast, Drosophila, and humans,...
3.
Gangloff Y, Romier C, Thuault S, Werten S, Davidson I
Trends Biochem Sci
. 2001 Apr;
26(4):250-7.
PMID: 11295558
Transcription factor TFIID is a multiprotein complex composed of the TATA binding protein and its associated factors, and is required for accurate and regulated initiation of transcription by RNA polymerase...
4.
Gangloff Y, Sanders S, Romier C, Kirschner D, Weil P, Tora L, et al.
Mol Cell Biol
. 2001 Mar;
21(5):1841-53.
PMID: 11238921
We show that the yeast TFIID (yTFIID) component yTAF(II)47 contains a histone fold domain (HFD) with homology to that previously described for hTAF(II)135. Complementation in vivo indicates that the yTAF(II)47...
5.
Fribourg S, Romier C, Werten S, Gangloff Y, Poterszman A, Moras D
J Mol Biol
. 2001 Mar;
306(2):363-73.
PMID: 11237605
Using the human basal transcription factors TFIID and TFIIH as examples, we show that pairwise coexpression of polypeptides in Escherichia coli can be used as a tool for the identification...
6.
Gangloff Y, Werten S, Romier C, Carre L, Poch O, Moras D, et al.
Mol Cell Biol
. 1999 Dec;
20(1):340-51.
PMID: 10594036
It has been previously proposed that the transcription complexes TFIID and SAGA comprise a histone octamer-like substructure formed from a heterotetramer of H4-like human hTAF(II)80 (or its Drosophila melanogaster dTAF(II)60...
7.
Davidson I, Romier C, Lavigne A, Birck C, Mengus G, Poch O, et al.
Cold Spring Harb Symp Quant Biol
. 1999 Jun;
63:233-41.
PMID: 10384287
The past few years have brought many new insights concerning the structure and function of TAFII proteins. In the future, further biochemical and structural studies will no doubt lead to...
8.
Lavigne A, Gangloff Y, Carre L, Mengus G, Birck C, Poch O, et al.
Mol Cell Biol
. 1999 Jun;
19(7):5050-60.
PMID: 10373554
Coexpression of the human TATA-binding protein (TBP)-associated factor 28 (hTAFII28) with the altered-specificity mutant TBP spm3 synergistically enhances transcriptional activation by the activation function 2 of the nuclear receptors (NRs)...
9.
Romier C, Dominguez R, Lahm A, Dahl O, Suck D
Proteins
. 1998 Sep;
32(4):414-24.
PMID: 9726413
The reaction mechanism of nuclease P1 from Penicillium citrinum has been investigated using single-stranded dithiophosphorylated di-, tetra-, and hexanucleotides as substrate analogs. The complexes crystallize in tetragonal and orthorhombic space...
10.
Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne A, et al.
Cell
. 1998 Aug;
94(2):239-49.
PMID: 9695952
Determination of the crystal structure of the human TBP-associated factor (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel histone-like pair in the TFIID complex. The histone folds in hTAF(II)28...