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Database of Abstracts of Reviews of Effects (DARE): Quality-assessed Reviews [Internet].

York (UK): Centre for Reviews and Dissemination (UK); 1995-.

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GeneReviews® [Internet].

Adam MP, Feldman J, Mirzaa GM, et al., editors.

Seattle (WA): University of Washington, Seattle; 1993-2024.

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Healthcare Cost and Utilization Project (HCUP) Statistical Briefs [Internet].

Rockville (MD): Agency for Healthcare Research and Quality (US); 2006 Feb-.

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Endotext [Internet].

Feingold KR, Anawalt B, Blackman MR, et al., editors.

South Dartmouth (MA): MDText.com, Inc.; 2000-.

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PDQ Cancer Information Summaries [Internet].

Bethesda (MD): National Cancer Institute (US); 2002-.

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Statistical Brief (Medical Expenditure Panel Survey (US)) [Internet].

Rockville (MD): Agency for Healthcare Research and Quality (US); 2001-.

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Mother To Baby | Fact Sheets [Internet].

Brentwood (TN): Organization of Teratology Information Specialists (OTIS); 1994-.

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LiverTox: Clinical and Research Information on Drug-Induced Liver Injury [Internet].

Bethesda (MD): National Institute of Diabetes and Digestive and Kidney Diseases; 2012-.

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WormBook: The Online Review of C. elegans Biology [Internet].

Pasadena (CA): WormBook; 2005-2018.

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Citing Medicine: The NLM Style Guide for Authors, Editors, and Publishers [Internet]. 2nd edition.

Patrias K, author; Wendling D, editor.

Bethesda (MD): National Library of Medicine (US); 2007-.

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Madame Curie Bioscience Database [Internet].

Austin (TX): Landes Bioscience; 2000-2013.

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15th Report on Carcinogens [Internet].

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Research Triangle Park (NC): National Toxicology Program; 2021 Dec 21.

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Bethesda (MD): National Institute of Child Health and Human Development; 2006-.

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The Guide to Clinical Preventive Services 2014: Recommendations of the U.S. Preventive Services Task Force.

Rockville (MD): Agency for Healthcare Research and Quality (US); 2014 May.

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Therapeutics Letter.

Perry T, editor.

Vancouver (BC): Therapeutics Initiative; 1994-.

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Molecular Imaging and Contrast Agent Database (MICAD) [Internet].

Bethesda (MD): National Center for Biotechnology Information (US); 2004-2013.

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AHRQ Evidence Report Summaries.

Rockville (MD): Agency for Healthcare Research and Quality (US); 1998-2005.

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The CBHSQ Report.

Rockville (MD): Substance Abuse and Mental Health Services Administration (US); 2013-.

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StatPearls [Internet].

Treasure Island (FL): StatPearls Publishing; 2024 Jan-.

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Institute for Quality and Efficiency in Health Care: Executive Summaries [Internet].

Cologne, Germany: Institute for Quality and Efficiency in Health Care (IQWiG); 2005-.

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Figure 7

Sequence alignment of WIF domains. The full color version of this figure is available at the publisher's web site, www. eurekah.com.

Secreted Antagonists/Modulators of Wnt Signaling.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.
Figure 15

Stages of SOM adaptation. A planar (10 × 10) SOM was trained to map a two-dimensional data distribution (small black spots). The receptive fields of the final map are indicated by Voronoi tessellation in the lower left projection. A and B denote two “empty” neurons, i.e., there are no data points captured by these neurons. The simulation was performed using the SOM tutorial software written by H.S. Loos and B. Fritzke;¹¹³ Figures were adapted from the graphical www output.

Analysis of Chemical Space.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.
Figure 1

Comparison of the Hsp70 nucleotide exchange factor structures. Panels A-C depict the crystal structures of the complexes of GrpE-DnaK, BAG-Hsc70 and HspBP1-Hsp70, respectively.44^,55^,60 The peptide backbones are shown in ribbon representation with the nucleotide exchange factors in green and the ATPase subdomains IA, IB, IIA and IIB in brown, blue, yellow and grey, respectively. For better comparison, the Cα atoms of the ATPase domains were aligned. The HspBP1-Hsp70 structure in panel C contains an additional nucleotide shown in ball-and-stick representation. Augmentation with AMP-PNP was necessary for crystallization of HspBP1 with lobe II of the Hsp70 ATPase domain, but strongly inhibited HspBP1 binding to the full ATPase domain.44 Panel D illustrates the rotation of subdomain IIB observed between the crystal structures of the ATPase domain in complex with ADP and with BAG.58^,60 The ATPase domains were superimposed, and are shown in the same orientation as in panel B; the peptide backbone of subdomain IIB in the BAG-Hsc70 complex is highlighted in bright green, otherwise the same coloring scheme as in panel B was applied. The Figure was created using the programs Molscript and Raster3D.70^,71 A color version of this figure is available online at www. Eurekah.com.

Nucleotide Exchange Factors for Hsp70 Molecular Chaperones.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.
Figure 2

Structure-based amino acid alignment of coronins 3 (1C) and 7 with coronin 1 (1A). The line under a specific amino acid sequence indicated as ′pred′ shows the predicted secondary structure as obtained by PSIPRED (H – helical, E – extended/β-strand, C – coil).47 Residues in italics indicate that they provide a structural feature at this location, but appear elsewhere in the amino acid sequence. The residues of the extended coronin signature motif are highlighted by underscore. Arg30, the residue crucial for F-actin bundling in coronin 2 (1B) is marked with *. White on black highlights indicate residues involved in anchoring Trp379 (coronin 1) to the β propeller, white on grey highlights indicate residues involved in the interface around Tyr364 (coronin 1). Conservative mutations in these interfaces are highlighted in grey. The putative phosphorylation site Ser463 (coronin 3) is highlighted by vertical stripes. Shown in bold letters is the acidic motif conserved in all long coronins and similar to those found in Arp2/3-activating proteins of the SCAR/WASP family. The horizontally striped backgrounds indicate the sorting signal recognised by the µ subunit of clathrin assembly protein 1. The very C-terminal region of coronin 7b appears under the ‘coiled coil’ region simply for purposes of amino acid alignment. Residues 472-482 of coronin 7a might provide strand A of blade 1 of coronin 7a. A color version of this figure is available at www. Eurekah.com.

Coronin Structure and Implications.

Madame Curie Bioscience Database [Internet]. Austin (TX): Landes Bioscience; 2000-2013.