(PDF) The F-Box Protein AhSLF-S2 Physically Interacts With

The F-Box Protein AhSLF-S2 Physically Interacts With S-RNases That May Be Inhibited by the Ubiquitin/26s Proteasome Pathway of Protein Degradation During Compatible Pollination in Antirrhinum

Plant Cell - United States

doi 10.1105/tpc.017673

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February 18, 2004

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American Society of Plant Biologists (ASPB)

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The F-Box Protein AhSLF-S2 Physically Interacts With S-RNases That May Be Inhibited by the Ubiquitin/26s Proteasome Pathway of Protein Degradation During Compatible Pollination in Antirrhinum

Plant Cell - United States

doi 10.1105/tpc.017673

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

The Ubiquitin Ligase F-Box/G-Domain Protein 1 Promotes the Degradation of the Disease-Linked Protein torsinA Through the Ubiquitin–proteasome Pathway and Macroautophagy

The Cdc48 Unfoldase Prepares Well-Folded Protein Substrates for Degradation by the 26S Proteasome

Direct Observation of Protein Translocation by the 26S Proteasome

26S Proteasome, S2 State

The Proteasome Subunit Rpn8 Interacts With the Small Nucleolar RNA Protein (snoRNP) Assembly Protein Pih1 and Mediates Its Ubiquitin-Independent Degradation inSaccharomyces Cerevisiae

The Degradation of Apolipoprotein B100 Is Mediated by the Ubiquitin-Proteasome Pathway and Involves Heat Shock Protein 70

Elevated Expression of ISG15 in Tumor Cells Interferes With the Ubiquitin/26s Proteasome Pathway

Inhibition ofPCSK9Transcription by Berberine Involves Down-Regulation of Hepatic HNF1α Protein Expression Through the Ubiquitin-Proteasome Degradation Pathway

Degradation of the G Protein-Coupled Receptor Kinase 2 by the Proteasome Pathway