A High Throughput Screen to Identify Substrates for the Ubiquitin Ligase Rsp5 (Q57412344)

9

object named as

Cheryl Wolting

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author name string

Bart Kus

1

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Aaron Gajadhar

2

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Karen Stanger

3

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Rob Cho

4

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Warren Sun

5

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Nathalie Rouleau

6

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Tammy Lee

7

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Donovan Chan

8

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Roger Bosse

11

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Daniela Rotin

Journal of Biological Chemistry

12

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language of work or name

English

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publication date

13 June 2005

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published in

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volume

280

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issue

33

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page(s)

29470-29478

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1 reference

https://api.crossref.org/works/10.1074%2FJBC.M502197200

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A proteomics approach to understanding protein ubiquitination

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A hitchhiker's guide to the cullin ubiquitin ligases: SCF and its kin

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Ubiquitination and endocytosis of plasma membrane proteins: role of Nedd4/Rsp5p family of ubiquitin-protein ligases

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Solution structure of a Nedd4 WW domain-ENaC peptide complex

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Characterizing Class I WW domains defines key specificity determinants and generates mutant domains with novel specificities

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A map of WW domain family interactions

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NPl1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase

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The role of ubiquitin in down-regulation and intracellular sorting of membrane proteins: insights from yeast

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The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase

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Rsp5 ubiquitin-protein ligase mediates DNA damage-induced degradation of the large subunit of RNA polymerase II in Saccharomyces cerevisiae

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Defective regulation of the epithelial Na+ channel by Nedd4 in Liddle's syndrome.

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Domains of the Rsp5 ubiquitin-protein ligase required for receptor-mediated and fluid-phase endocytosis

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Functional domains of the Rsp5 ubiquitin-protein ligase.

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Yeast glycogen synthase kinase 3 is involved in protein degradation in cooperation with Bul1, Bul2, and Rsp5

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The mRNA nuclear export factor Hpr1 is regulated by Rsp5-mediated ubiquitylation

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A comprehensive two-hybrid analysis to explore the yeast protein interactome

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Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry

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Yeast RNA polymerase II at 5 A resolution

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von Hippel-Lindau protein binds hyperphosphorylated large subunit of RNA polymerase II through a proline hydroxylation motif and targets it for ubiquitination

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Identification of the RNA polymerase II subunit hsRPB7 as a novel target of the von Hippel-Lindau protein

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Rsp5 WW domains interact directly with the carboxyl-terminal domain of RNA polymerase II.

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Identification of a region within SEL1L protein required for tumour growth inhibition

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