A proteomics approach to understanding protein ubiquitination

By Junmin Peng, Daniel Schwartz, Joshua E. Elias, C. Thoreen, Dongmei Cheng, G. Marsischky, J. Roelofs, D. Finley, Steven P. Gygi. Nature Biotechnology, 2003

1,663 citations recorded by the source corpus.

Subfields: Cancer Research, Molecular Biology, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/5015d932f1428b60296de91f347b2144c9f46c2d

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cancer Research

In Molecular Biology

In Spectroscopy

Citations in the corpus

Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (2009, background): “Because proteins that are rapidly turned over are also typically present at low levels in cells, mass-spectrometry-based searches for ubiquitinated proteins and proteasome substrates have so far provided only incomplete surveys (28, 41, 42).”
A genomic and functional inventory of deubiquitinating enzymes. (2005, neutral): “More than a dozen different Ub and Ubl modifications have been described, and up to 20% of yeast proteins are conjugated to Ub under standard culture conditions (Peng et al., 2003; Welchman et al., 2005).”
Atypical ubiquitin chains: new molecular signals (2008, background): “…2005; Mukhopadhyay & riezman, 2007). in general, these modifications are controlled by a three-step reaction initialized by E1-mediated activation of ub, followed by conjugation to an E2 enzyme and finally substrate targeting by an E3 ub ligase (Hershko & ciechanover, 1998; pickart & Eddins, 2003).”
The ubiquitin code. (2012, background): “Alternatively, ubiquitylation can occur at endosomal membranes to control localization after internalization.”
Ubiquitin-binding domains (2005, background): “It is not known whether VHS, UEV, PAZ, GLUE or UBA domains bring about the ubiquitylation of the proteins in which they are contained, although some PAZ-, UBA- and UEV-domain-containing proteins are ubiquitylate”
Breaking the chains: structure and function of the deubiquitinases (2009, background): “All forms of chain linkage exist in eukaryotic cell”
Origin and Function of Ubiquitin-like Protein Conjugation (2009, background): “Ubiquitin modifies more than 1,000 different proteins in yeas”
Systematic and quantitative assessment of the ubiquitin modified proteome (2011, neutral): “Previous studies have focused on either the use of ubiquitin binding domains/antibodies or overexpression of epitope-tagged ubiquitin in an attempt to capture ubiquitylated proteins for identification by mass spectrometry (Danielsen et al., 2011; Matsumoto et al., 2005; Meierhofer et al., 2008; Peng”