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Amir Rattner
Researcher at Johns Hopkins University School of Medicine
Publications - 48
Citations - 7353
Amir Rattner is an academic researcher from Johns Hopkins University School of Medicine. The author has contributed to research in topics: Wnt signaling pathway & Retina. The author has an hindex of 31, co-authored 46 publications receiving 6701 citations. Previous affiliations of Amir Rattner include Howard Hughes Medical Institute & Johns Hopkins University.
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A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is mutated in recessive Stargardt macular dystrophy
Rando Allikmets,Nanda A. Singh,Hui Sun,Noah F. Shroyer,Amy Hutchinson,Abirami Chidambaram,Bernard Gerrard,Lisa Baird,Dora Stauffer,Andy Peiffer,Amir Rattner,Philip M. Smallwood,Yixin Li,Kent L. Anderson,Richard A. Lewis,Jeremy Nathans,Mark Leppert,Michael Dean,James R. Lupski +18 more
TL;DR: Mutational analysis of ABCR in STGD families revealed a total of 19 different mutations including homozygous mutations in two families with consanguineous parentage, indicating that ABCR is the causal gene of STGD/FFM.
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A new secreted protein that binds to Wnt proteins and inhibits their activites
Jen Chih Hsieh,Laurent Kodjabachian,Martha L. Rebbert,Amir Rattner,Philip M. Smallwood,Cindy Harryman Samos,Roel Nusse,Igor B. Dawid,Jeremy Nathans +8 more
TL;DR: Wnt-inhibitory factor-1 (WIF-1) is described, a secreted protein that binds to Wnt proteins and inhibits their activities, and results indicate that WNT proteins interact with structurally diverse extracellular inhibitors to fine-tune the spatial and temporal patterns of Wnt activity.
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A family of secreted proteins contains homology to the cysteine-rich ligand-binding domain of frizzled receptors
Amir Rattner,Jen Chih Hsieh,Philip M. Smallwood,Debra J. Gilbert,N. G. Copeland,Nancy A. Jenkins,Jeremy Nathans +6 more
TL;DR: Observations suggest that sFRPs may function in vivo to modulate Wnt signaling, or, alternatively, as novel ligands for as yet unidentified receptors.
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Insights into Wnt binding and signalling from the structures of two Frizzled cysteine-rich domains
Charles E. Dann,Jen Chih Hsieh,Amir Rattner,Divya Sharma,Jeremy Nathans,Jeremy Nathans,Daniel J. Leahy +6 more
TL;DR: A previously unknown protein fold is shown, and the design and interpretation of CRD mutations that identify a Wnt-binding site are shown, which provides a framework for studies of homologous CRDs in proteins including muscle-specific kinase and Smoothened, a component of the Hedgehog signalling pathway.
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Biochemical characterization of Wnt-frizzled interactions using a soluble, biologically active vertebrate Wnt protein.
TL;DR: The production in Drosophila S2 cells of biologically active Xenopus Wnt8 (XWnt8) is reported, with results that demonstrate the use of these proteins for studying the interactions between soluble XWnt 8 and various Frizzled proteins, membrane anchored or secreted CRDs, and a set of insertion mutants in the CRD of DrosophileFrizzled 2.