Molecular discrimination of structurally equivalent Lys 63‐linked and linear polyubiquitin chains

By D. Komander, Francisca E. Reyes-Turcu, Julien D. F. Licchesi, P. Odenwaelder, K. Wilkinson, D. Barford. EMBO Reports, 2009

625 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/0f4d2dbd1e8717e8bd770c51456495dff65810c6

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. S. Urbé
4. M. J. Clague
5. Ivan Dikic
6. V. Dixit
7. Soichi Wakatsuki
8. Wenyi Wei

In Oncology

1. D. Komander
2. M. Rapé
3. Heiko Blaser
4. D. Brenner
5. Ivan Dikic
6. T. Mak

Citations in the corpus

• Ubiquitin-binding domains — from structures to functions (2009, background): “Lys63-linked and linear diubiquitins adopt similar extended conformations, with no contact between the two ubiquitin moietie”
• Regulation of tumour necrosis factor signalling: live or let die (2015, background): “CYLD associates with complex I via TRAF2 and removes both K63-and M1-linked polyubiquitin chains from target proteins 32,57,68,70 .”
• Signaling in innate immunity and inflammation. (2012, background): “CYLD cleaves both linear and K63-linked polyubiquitin efficiently in vitro (Komander et al. 2009), but mice lacking CYLD do not develop the multi-organ inflammation seen in A20-deficient mice, perhaps because CYLD normally is phosphorylated and inactivated by IKK (Reiley et al.”
• Breaking the chains: structure and function of the deubiquitinases (2009, background): “negatively charged transition state (stage (2) and (5)) is stabilized by the oxy-anion”
• The ubiquitin code. (2012, background): “In all cases, assigning a function to a ubiquitin modifi-cation requires a combination of these experimental approaches. code.”
• The role of ubiquitination in tumorigenesis and targeted drug discovery (2020, background): “Engineered deubiquitination synthesis reveals that the OTU specifically removes the K29 linkage Ub chain from the substrate,(111) and the JAMM, such as AMSH, AMSH-LP, BRCC36 and POH1, are often specific for the Ub chain for K63 linkage ubiquitination.(112,113) CYLD is more likely to act on linear ub”
• Molecular Basis of NF-κB Signaling (2013, background): “the TAB NZF are organized to optimize simultaneous binding to adjacent ubiquitin moieties in a configuration specific to Lys63-linked ubiquitin chains (56).”