Ubiquitin and ubiquitin-like proteins as multifunctional signals

By R. Welchman, C. Gordon, R. Mayer. Nature reviews. Molecular cell biology, 2005

871 citations recorded by the source corpus.

Subfields: Epidemiology, Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/23d967e974a5121ff3f15089688c48f9763d2dc0

How researchers see this paper

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In Epidemiology

1. Ivan Dikic
2. Y. Ohsumi
3. V. Kirkin
4. H. Nakatogawa
5. David G. McEwan
6. Yoshinobu Ichimura
7. I. Novak
8. D. Klionsky

In Molecular Biology

1. Ivan Dikic
2. V. Kirkin
3. Jian Lei
4. Rolf Hilgenfeld
5. Y. Ohsumi
6. Y. Kusov
7. Beth Levine
8. N. Mizushima

In Oncology

1. Jian Lei
2. Rolf Hilgenfeld
3. Ivan Dikic
4. Y. Ohsumi
5. Y. Kusov

Citations in the corpus

• Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein (2017, background): “Ubiquitination and deubiquitination cannot only regulate the immune response but also the cell-cycle, DNA damage repair, cellular growth etc. (Welchman et al., 2005), and these processes will involve a large number of host proteins.”
• Genes and growth performance in crustacean species : a review of relevant genomic studies in crustaceans and other taxa (2013, background): “Ubiquitins are normally ligated to other proteins in the cell as a monomer or polymer to regulate their activity and/or entry into proteasomal and other degradation pathways (Welchman et al. 2005).”
• A role for ubiquitin in selective autophagy. (2009, background): “Classically, conjugation with K48-linked polyUb chains allows recognition of the proteolytic substrate by UBD-containing proteasomal receptors, whereas the K63-linked chains have been associated with nonproteolytic functions of Ub (Welchman et al., 2005).”
• A genomic and functional inventory of deubiquitinating enzymes. (2005, neutral): “Protein ubiquitination comes in many different flavors that serve distinct functions (Welchman et al., 2005).”
• Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion. (2007, background): “It is generally believed that ubiquitin and other ubiquitin-like proteins serve as posttranslational modifiers that regulate the degradation, interactions, localization, and functions of their target proteins (Welchman et al., 2005).”