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Daniel L. Weeks
Researcher at University of Iowa
Publications - 66
Citations - 4557
Daniel L. Weeks is an academic researcher from University of Iowa. The author has contributed to research in topics: Xenopus & Oligonucleotide. The author has an hindex of 36, co-authored 65 publications receiving 4451 citations. Previous affiliations of Daniel L. Weeks include Purdue University & Academia Sinica.
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Journal ArticleDOI
A maternal mRNA localized to the vegetal hemisphere in xenopus eggs codes for a growth factor related to TGF-β
Daniel L. Weeks,Doug Melton +1 more
TL;DR: It is proposed that the formation of mesoderm during frog development is specified by the products of localized maternal mRNAs, including Vg1, a maternal mRNA localized to the vegetal hemisphere of frog eggs.
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Identification and Cloning of Localized Maternal RNAs From Xenopus Eggs
TL;DR: These studies show that some informational molecules, specifically RNAs, are localized in eggs and are inherited by particular blastomeres.
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Epithelial-mesenchymal transformation of embryonic cardiac endothelial cells is inhibited by a modified antisense oligodeoxynucleotide to transforming growth factor beta 3
TL;DR: Modified antisense oligodeoxynucleotides generated to nonconserved regions of TGF beta 1, -2, -3, and -4 to examine the possible roles of these members in this transformation demonstrate that a specific member of the TGF Beta family, TGFbeta 3, is essential for the epithelial-mesenchymal cell transformation.
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TGFβ2 and TGFβ3 Have Separate and Sequential Activities during Epithelial–Mesenchymal Cell Transformation in the Embryonic Heart
Angelique S. Boyer,Ingrid I. Ayerinskas,Eric B. Vincent,Lisa A. McKinney,Daniel L. Weeks,Raymond B. Runyan +5 more
TL;DR: TGFbeta2 and TGFbeta3 are sequentially and separately involved in the process of EMT, which mediates initial endothelial cell-cell separation while TGF beta3 is required for the cell morphological change that enables the migration of cells into the underlying ECM.
Journal ArticleDOI
RanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase.
Peter Askjaer,Angela Bachi,Matthias Wilm,F. Ralf Bischoff,Daniel L. Weeks,Vera M Ogniewski,Mutsuhito Ohno,Christof Niehrs,Jørgen Kjems,Iain W. Mattaj,Maarten Fornerod +10 more
TL;DR: Using a quantitativeCRM1-NES cargo binding assay, significant differences in affinity for CRM1 among natural NESs are demonstrated, suggesting that the steady-state nucleocytoplasmic distribution of shuttling proteins could be determined by the relative strengths of their NESs.