Ubiquitin-binding domains — from structures to functions

By Ivan Dikic, Soichi Wakatsuki, K. Walters. Nature reviews. Molecular cell biology, 2009

878 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/bf418123750812870716bca3b200fcc7b4d7bccb

How researchers see this paper

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

In Molecular Biology

1. D. Komander
2. M. Rapé
3. Tony Pawson
4. Ivan Dikic
5. Y. L. Deribe
6. Shuai Jiang
7. Jian Lei
8. Yu Xue

In Oncology

1. D. Komander
2. M. Rapé
3. Tony Pawson
4. Jian Lei
5. Rolf Hilgenfeld
6. Ivan Dikic
7. Y. Ye
8. Y. Kusov

Citations in the corpus

• The ubiquitin code. (2012, background): “Proteins with multiple UBDs exploit this property by introducing a defined spacer between the UBDs, as seen in proteins that containtandemrepeatsofubiquitin-interacting helix with a hydrophobic binding site for the Ile44 patch of ubiquitin (84).”
• GPS-SUMO: a tool for the prediction of sumoylation sites and SUMO-interaction motifs (2014, background): “Compared to diverse ubiquitin-binding domains (UBDs) that commonly interact the -sheet around Ile44 of ubiquitin (23,24), Song et al.”
• Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein (2017, background): “This hydrophobic patch of Ub is commonly used to interact with Ub-binding proteins (Dikic et al., 2009).”
• Building ubiquitin chains: E2 enzymes at work (2009, background): “Substrates modified with ubiquitin are recognized in cells by a cohort of proteins containing ubiquitin-binding motifs such as the ubiquitin-interacting motif (UIM) and ubiquitin-associated (UBA) domains”
• 53BP1 is a reader of the DNA damage-induced H2A Lys15 ubiquitin mark (2013, neutral): “Class switching to IgG1 was assayed in 53BP1 murine primary B cells complemented with 53BP1 (1-1711) and mutants thereof by retroviral delivery.”
• Post-translational modifications in signal integration (2010, background): “Ubiquitin is recognized by various ubiquitin-binding domains (UBDs), depending primarily on the type of linkage used to create the chai”
• Interpreting thelanguage of histone and DNA modifications (2014, background): “This is one of the few examples of how ubiquitination on a histone may be driving recruitment of a chromatin modifier, and further, underscores the more general potential for how histone monoubiquitination may serve as a binding platform, as is found for monoubiquitinated proteins in cell signaling ”
• Structured states of disordered proteins from genomic sequences (2016, neutral): “None of the contacts that we predict are long range, agreeing with the NMR structures of PSMD4 bound to di-ubiquitin (PDB: 2kde (Zhang et al., 2009)) (Dikic et al., 2009).”