Agard DA - Search Results

1

Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.

Noddings CM, Wang RY, Johnson JL, Agard DA. Noddings CM, et al. Among authors: agard da. Nature. 2022 Jan;601(7893):465-469. doi: 10.1038/s41586-021-04236-1. Epub 2021 Dec 22. Nature. 2022. PMID: 34937936 Free PMC article.

2

Microtubule nucleation by gamma-tubulin-containing rings in the centrosome.

Moritz M, Braunfeld MB, Sedat JW, Alberts B, Agard DA. Moritz M, et al. Among authors: agard da. Nature. 1995 Dec 7;378(6557):638-40. doi: 10.1038/378638a0. Nature. 1995. PMID: 8524401

3

Unfolded conformations of alpha-lytic protease are more stable than its native state.

Sohl JL, Jaswal SS, Agard DA. Sohl JL, et al. Among authors: agard da. Nature. 1998 Oct 22;395(6704):817-9. doi: 10.1038/27470. Nature. 1998. PMID: 9796818

4

Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism.

Shiau AK, Barstad D, Radek JT, Meyers MJ, Nettles KW, Katzenellenbogen BS, Katzenellenbogen JA, Agard DA, Greene GL. Shiau AK, et al. Among authors: agard da. Nat Struct Biol. 2002 May;9(5):359-64. doi: 10.1038/nsb787. Nat Struct Biol. 2002. PMID: 11953755

5

The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site.

Harris SF, Shiau AK, Agard DA. Harris SF, et al. Among authors: agard da. Structure. 2004 Jun;12(6):1087-97. doi: 10.1016/j.str.2004.03.020. Structure. 2004. PMID: 15274928 Free article.

6

Insights into microtubule nucleation from the crystal structure of human gamma-tubulin.

Aldaz H, Rice LM, Stearns T, Agard DA. Aldaz H, et al. Among authors: agard da. Nature. 2005 May 26;435(7041):523-7. doi: 10.1038/nature03586. Nature. 2005. PMID: 15917813

7

Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.

Shiau AK, Harris SF, Southworth DR, Agard DA. Shiau AK, et al. Among authors: agard da. Cell. 2006 Oct 20;127(2):329-40. doi: 10.1016/j.cell.2006.09.027. Cell. 2006. PMID: 17055434 Free article.

8

Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.

Krukenberg KA, Förster F, Rice LM, Sali A, Agard DA. Krukenberg KA, et al. Among authors: agard da. Structure. 2008 May;16(5):755-65. doi: 10.1016/j.str.2008.01.021. Structure. 2008. PMID: 18462680 Free PMC article.

9

Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle.

Southworth DR, Agard DA. Southworth DR, et al. Among authors: agard da. Mol Cell. 2008 Dec 5;32(5):631-40. doi: 10.1016/j.molcel.2008.10.024. Mol Cell. 2008. PMID: 19061638 Free PMC article.

10

pH-dependent conformational changes in bacterial Hsp90 reveal a Grp94-like conformation at pH 6 that is highly active in suppression of citrate synthase aggregation.

Krukenberg KA, Southworth DR, Street TO, Agard DA. Krukenberg KA, et al. Among authors: agard da. J Mol Biol. 2009 Jul 10;390(2):278-91. doi: 10.1016/j.jmb.2009.04.080. Epub 2009 May 7. J Mol Biol. 2009. PMID: 19427321 Free PMC article.

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