Ferré-D'Amaré A - Search Results

1

X-ray crystallographic studies of eukaryotic transcription factors.

Burley SK, Clark KL, Ferré-D'Amaré A, Kim JL, Nikolov DB. Burley SK, et al. Cold Spring Harb Symp Quant Biol. 1993;58:123-32. doi: 10.1101/sqb.1993.058.01.016. Cold Spring Harb Symp Quant Biol. 1993. PMID: 7956022

2

Structure and function of the b/HLH/Z domain of USF.

Ferré-D'Amaré AR, Pognonec P, Roeder RG, Burley SK. Ferré-D'Amaré AR, et al. EMBO J. 1994 Jan 1;13(1):180-9. doi: 10.1002/j.1460-2075.1994.tb06247.x. EMBO J. 1994. PMID: 8306960 Free PMC article.

3

Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain.

Ferré-D'Amaré AR, Prendergast GC, Ziff EB, Burley SK. Ferré-D'Amaré AR, et al. Nature. 1993 May 6;363(6424):38-45. doi: 10.1038/363038a0. Nature. 1993. PMID: 8479534

4

Probing the solution structure of the DNA-binding protein Max by a combination of proteolysis and mass spectrometry.

Cohen SL, Ferré-D'Amaré AR, Burley SK, Chait BT. Cohen SL, et al. Protein Sci. 1995 Jun;4(6):1088-99. doi: 10.1002/pro.5560040607. Protein Sci. 1995. PMID: 7549873 Free PMC article.

5

Anti-cooperative biphasic equilibrium binding of transcription factor upstream stimulatory factor to its cognate DNA monitored by protein fluorescence changes.

Sha M, Ferré-D'Amaré AR, Burley SK, Goss DJ. Sha M, et al. J Biol Chem. 1995 Aug 18;270(33):19325-9. doi: 10.1074/jbc.270.33.19325. J Biol Chem. 1995. PMID: 7642609 Free article.

6

Use of dynamic light scattering to assess crystallizability of macromolecules and macromolecular assemblies.

Ferré-D'Amaré AR, Burley SK. Ferré-D'Amaré AR, et al. Structure. 1994 May 15;2(5):357-9. doi: 10.1016/s0969-2126(00)00037-x. Structure. 1994. PMID: 8081751 No abstract available.

7

Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 A resolution.

Párraga A, Bellsolell L, Ferré-D'Amaré AR, Burley SK. Párraga A, et al. Structure. 1998 May 15;6(5):661-72. doi: 10.1016/s0969-2126(98)00067-7. Structure. 1998. PMID: 9634703 Free article.

8

The semidominant Mi(b) mutation identifies a role for the HLH domain in DNA binding in addition to its role in protein dimerization.

Steingrímsson E, Nii A, Fisher DE, Ferré-D'Amaré AR, McCormick RJ, Russell LB, Burley SK, Ward JM, Jenkins NA, Copeland NG. Steingrímsson E, et al. EMBO J. 1996 Nov 15;15(22):6280-9. EMBO J. 1996. PMID: 8947051 Free PMC article.

9

Molecular basis of mouse microphthalmia (mi) mutations helps explain their developmental and phenotypic consequences.

Steingrímsson E, Moore KJ, Lamoreux ML, Ferré-D'Amaré AR, Burley SK, Zimring DC, Skow LC, Hodgkinson CA, Arnheiter H, Copeland NG, et al. Steingrímsson E, et al. Nat Genet. 1994 Nov;8(3):256-63. doi: 10.1038/ng1194-256. Nat Genet. 1994. PMID: 7874168

10

[10] Dynamic light scattering in evaluating crystallizability of macromolecules.

Ferré-D'Amaré AR, Burley SK. Ferré-D'Amaré AR, et al. Methods Enzymol. 1997;276:157-166. doi: 10.1016/S0076-6879(97)76056-7. Methods Enzymol. 1997. PMID: 27799091 No abstract available.

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