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Portland, OR, United States

Turner M.,University of California at Davis | Zhang Y.,University of California at Davis | Carlson H.L.,101 SW Sam Jackson Park Road | Stadler H.S.,101 SW Sam Jackson Park Road | And 2 more authors.
Biomolecular NMR Assignments | Year: 2015

The homeobox gene (Hoxd13) codes for a transcription factor protein that binds to AT-rich DNA sequences and controls expression of proteins that control embryonic morphogenesis. We report NMR chemical shift assignments of mouse Hoxd13 DNA binding domain bound to an 11-residue DNA duplex (BMRB No. 25133). © 2014, Springer Science+Business Media Dordrecht. Source

Boudko S.P.,101 SW Sam Jackson Park Road | Boudko S.P.,Oregon Health And Science University | Engel J.,University of Basel | Bachinger H.P.,101 SW Sam Jackson Park Road | Bachinger H.P.,Oregon Health And Science University
International Journal of Biochemistry and Cell Biology | Year: 2012

Collagens contain large numbers of Gly-Xaa-Yaa peptide repeats that form the characteristic triple helix, where the individual chains fold into a polyproline II helix and three of these helices form a right-handed triple helix. For the proper folding of the triple helix collagens contain trimerization domains. These domains ensure a single starting point for triple helix formation and are also responsible for the chain selection in heterotrimeric collagens. Trimerization domains are non-collagenous domains of very different structures. The size of trimerization domains varies from 35 residues in type IX collagen to around 250 residues for the fibrillar collagens. These domains are not only crucial for biological functions, but they are also attractive tools for generating recombinant collagen fragments of interest as well as for general use in protein engineering and biomaterial design. Here we review the current knowledge of the structure and function of these trimerization domains. © 2011 Elsevier Ltd. All rights reserved. Source

Perez W.D.,101 SW Sam Jackson Park Road | Perez W.D.,Oregon Health And Science University | Weller C.R.,Oregon State University | Shou S.,University of Chicago | And 2 more authors.
Developmental Dynamics | Year: 2010

The loss of HOXA13 function severely disrupts embryonic limb development. However, because embryos lacking HOXA13 die by mid-gestation, the defects present in the mutant limb could arise as a secondary consequence of failing embryonic health. In our analysis of the mutant Hoxa13GFP allele, we identified a surviving cohort of homozygous mutants exhibiting severe limb defects including: missing phalanx elements, fusions of the carpal/tarsal elements, and significant reductions in metacarpal/metatarsal length. Characterization of prochondrogenic genes in the affected carpal/tarsal regions revealed significant reduction in Gdf5 expression, whereas Bmp2 expression was significantly elevated. Analysis of Gdf5 mRNA localization also revealed diffuse expression in the carpal/tarsal anlagen, suggesting a role for HOXA13 in the organization of the cells necessary to delineate individual carpal/tarsal elements. Together these results identify Gdf5 as a potential target gene of HOXA13 target gene and confirm a specific role for HOXA13 during appendicular skeletal development. © 2009 Wiley-Liss, Inc. Source

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