(Q27641468)

1

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Cary D Gardner

2

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Robin P Wharton

3

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Aneel K Aggarwal

Comparison of ARM and HEAT protein repeats

4

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publication date

June 2003

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published in

Molecular Cell

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volume

11

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page(s)

1537-48

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issue

6

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cites work

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Poly(A)-independent regulation of maternal hunchback translation in the Drosophila embryo

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Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp

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Structure of importin-beta bound to the IBB domain of importin-alpha

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Overlapping but distinct RNA elements control repression and activation of nanos translation

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Translational regulation in development.

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The Nanos gradient in Drosophila embryos is generated by translational regulation.

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Smaug, a novel RNA-binding protein that operates a translational switch in Drosophila

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Themes in RNA-protein recognition.

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Control of translation initiation in animals.

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Crystallization and characterization of Smaug: a novel RNA-binding motif.

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Topological characteristics of helical repeat proteins

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The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs

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Crystal structure of E.coli RuvA with bound DNA Holliday junction at 6 A resolution

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression

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Translational regulation of maternal mRNAs

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A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery

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RNA-protein complexes

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Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons

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SAM as a protein interaction domain involved in developmental regulation

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A three-hybrid system to detect RNA-protein interactions in vivo

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smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo

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Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro

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Drosophila Brain Tumor is a translational repressor

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The crystal structure of an Eph receptor SAM domain reveals a mechanism for modular dimerization

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Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase

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Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses

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Automated MAD and MIR structure solution

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Oligomeric structure of the human EphB2 receptor SAM domain

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Genetic characterization of a mammalian protein-protein interaction domain by using a yeast reverse two-hybrid system

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Induced fit in RNA-protein recognition

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Translational control of growth factor and proto-oncogene expression

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