(PDF) Identification of a Novel E2F3 Product Suggests a

Identification of a Novel E2F3 Product Suggests a Mechanism for Determining Specificity of Repression by Rb Proteins

Molecular and Cellular Biology - United States

doi 10.1128/.20.10.3626-3632.2000

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January 1, 2000

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American Society for Microbiology

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Identification of a Novel E2F3 Product Suggests a Mechanism for Determining Specificity of Repression by Rb Proteins

Molecular and Cellular Biology - United States

doi 10.1128/.20.10.3626-3632.2000

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

A Combinatorial Mechanism for Determining the Specificity of E2F Activation and Repression

Identification of Genes Required for Glucan Exopolysaccharide Production in Lactobacillus Johnsonii Suggests a Novel Mechanism of Biosynthesis

Identification of Novel Glycogen Synthase Kinase-3β Substrate-Interacting Residues Suggests a Common Mechanism for Substrate Recognition

The 1.85 Å Structure of an 8r-Lipoxygenase Suggests a General Model for Lipoxygenase Product Specificity

Structure of Schmallenberg Orthobunyavirus Nucleoprotein Suggests a Novel Mechanism of Genome Encapsidation

Repression of the Arf Tumor Suppressor by E2F3 Is Required for Normal Cell Cycle Kinetics

TXR1-mediated Thrombospondin Repression: A Novel Mechanism of Resistance to Taxanes?

Transcriptional Repression by the Rb-Related Protein P107.

Specificity for the Hairy/Enhancer of Split Basic Helix-Loop-Helix (bHLH) Proteins Maps Outside the bHLH Domain and Suggests Two Separable Modes of Transcriptional Repression.