@article {1053,
	title = {The state of the filament},
	journal = {Embo Reports},
	volume = {6},
	number = {3},
	year = {2005},
	note = {ISI Document Delivery No.: 901QMTimes Cited: 22Cited Reference Count: 30},
	month = {Mar},
	pages = {220-226},
	type = {Review},
	abstract = {Movement is a defining characteristic of life. Macroscopic motion is driven by the dynamic interactions of myosin with actin filaments in muscle. Directed polymerization of actin behind the advancing membrane of a eukaryotic cell generates microscopic movement. Despite the fundamental importance of actin in these processes, the structure of the actin filament remains unknown. The Holmes model of the actin filament was published 15 years ago, and although it has been widely accepted, no high-resolution structural data have yet confirmed its veracity. Here, we review the implications of recently determined structures of F-actin-binding proteins for the structure of the actin filament and suggest a series of in silico tests for actin-filament models. We also review the significance of these structures for the arp2/3-mediated branched filament.},
	keywords = {actin filament, ACTIN-FILAMENT, ACTIVATION, ALDRICH-SYNDROME PROTEIN, arp2/3, ARP2/3 COMPLEX, BETA-ACTIN, CRYSTAL-STRUCTURE, DOMAIN, gelsolin, STRUCTURAL BASIS, STRUCTURE, WASp, WH2},
	isbn = {1469-221X},
	url = {<Go to ISI>://000227297000009},
	author = {Aguda, A. H. and Burtnick, L. D. and Robinson, R. C.}
}
@article {4696,
	title = {The highly conserved beta-hairpin of the paired DNA-binding domain is required for assembly of Pax-Ets ternary complexes},
	journal = {Molecular and Cellular Biology},
	volume = {19},
	number = {3},
	year = {1999},
	note = {ISI Document Delivery No.: 168MYTimes Cited: 37Cited Reference Count: 57},
	month = {Mar},
	pages = {2231-2241},
	type = {Article},
	abstract = {Pax family transcription factors bind DNA through the paired domain. This domain, which is comprised of two helix-turn-helix motifs and a beta-hairpin structure, is a target of mutations in congenital disorders of mice and humans. Previously, we showed that Pax-5 (B-cell-specific activator protein) recruits proteins of the Ets proto-oncogene family to bind a composite DNA site that is essential for efficient transcription of the early-B-cell-specific mb-1 promoter. Here, evidence is provided for specific interactions between Ets-1 and the amino-terminal subdomains of Pax proteins. By tethering deletion fragments of Pax-5 to a heterologous DNA-binding domain, we show that 73 amino acids (amino acids 12 to 84) of its amino-terminal subdomain can recruit the ETS domain of Ets-1 to bind the composite site. Furthermore, an amino acid (Gln22) within the highly conserved beta-hairpin motif of Pax-5 is essential for efficient recruitment of Ets-1. The ability to recruit Ets proteins to bind DNA is a shared property of Pax proteins, as demonstrated by cooperative DNA binding of Ets-1 with sequences derived from the paired domains of Pax-2 and Pax-3. The strict conservation of sequences required for recruitment of Ets proteins suggests that Pax-Ets interactions are important for regulating transcription in diverse tissues during cellular differentiation.},
	keywords = {B-CELL-DEVELOPMENT, BOX, GENE, HMG DOMAIN, MURINE ETS-1, POINT MUTATION, STRUCTURAL BASIS, TRANSCRIPTION FACTORS, V-ETS, WAARDENBURG-SYNDROME},
	isbn = {0270-7306},
	url = {<Go to ISI>://000078697900061},
	author = {Wheat, W. and Fitzsimmons, D. and Lennox, H. and Krautkramer, S. R. and Gentile, L. N. and McIntosh, L. P. and Hagman, J.}
}
