<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Hsieh, J C</style></author><author><style face="normal" font="default" size="100%">Kodjabachian, L</style></author><author><style face="normal" font="default" size="100%">Rebbert, M L</style></author><author><style face="normal" font="default" size="100%">Rattner, A</style></author><author><style face="normal" font="default" size="100%">Smallwood, P M</style></author><author><style face="normal" font="default" size="100%">Samos, C H</style></author><author><style face="normal" font="default" size="100%">Nusse, R</style></author><author><style face="normal" font="default" size="100%">Dawid, I B</style></author><author><style face="normal" font="default" size="100%">Nathans, J</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">A new secreted protein that binds to Wnt proteins and inhibits their activities.</style></title><secondary-title><style face="normal" font="default" size="100%">Nature</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Apr</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">6726</style></number><pub-location><style face="normal" font="default" size="100%">Department of Molecular Biology and Genetics, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.</style></pub-location><volume><style face="normal" font="default" size="100%">398</style></volume><pages><style face="normal" font="default" size="100%">431–436</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The Wnt proteins constitute a large family of extracellular signalling molecules that are found throughout the animal kingdom and are important for a wide variety of normal and pathological developmental processes. Here we describe Wnt-inhibitory factor-1 (WIF-1), a secreted protein that binds to Wnt proteins and inhibits their activities. WIF-1 is present in fish, amphibia and mammals, and is expressed during Xenopus and zebrafish development in a complex pattern that includes paraxial presomitic mesoderm, notochord, branchial arches and neural crest derivatives. We use Xenopus embryos to show that WIF-1 overexpression affects somitogenesis (the generation of trunk mesoderm segments), in agreement with its normal expression in paraxial mesoderm. In vitro, WIF-1 binds to Drosophila Wingless and Xenopus Wnt8 produced by Drosophila S2 cells. Together with earlier results obtained with the secreted Frizzled-related proteins, our results indicate that Wnt proteins interact with structurally diverse extracellular inhibitors, presumably to fine-tune the spatial and temporal patterns of Wnt activity.</style></abstract></record></records></xml>