Evidence map›Paper›PMID 23823328›Full record

ArticleStructure (London, England : 1993)2013

Unique structural, dynamical, and functional properties of k11-linked polyubiquitin chains.

Carlos A Castañeda, Tanuja R Kashyap, Mark A Nakasone, Susan Krueger, David Fushman

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed.

  1. AmideBiomolecular NMR assignments · 2026
    Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Ubiquitination in the ERAD Process.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Review
  11. Article
  12. Unanchored Ubiquitin Chains, Revisited.Frontiers in cell and developmental biology · 2020
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. A Highly Efficient Synthesis of Polyubiquitin Chains.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2018
    Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Carlos A CastañedaDepartment of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, MD 20742, USA.
Tanuja R Kashyap
Mark A Nakasone
Susan Krueger
David Fushman

Funding

Solution structure and dynamics of polyubiquitin chainsR01GM065334 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI DAVID FUSHMAN · 2002 to 2026
$6.2M
Recognition of non-ubiquitin signals at the proteasomeR01GM095755 · NIGMS · UNIV OF MARYLAND, COLLEGE PARK · PI FUSHMAN, DAVID · 2011 to 2014
$1.4M
NIGMS NIH HHS GM065334NIGMS NIH HHS GM095755NIGMS NIH HHS R01 GM065334NIGMS NIH HHS R01 GM095755
6 · The paper itself

Abstract

K11-linked polyubiquitin chains play important signaling and regulatory roles in both degradative and nonproteolytic pathways in eukaryotes. To understand the structural basis of how these chains are recognized and distinguished from other polyubiquitins, we determined solution structures of K11-linked diubiquitin (K11-Ub2) in the absence and presence of salt. These structures reveal that K11-Ub2 adopts conformations distinct from those of K48-linked or K63-linked chains. Importantly, our solution NMR and SANS data are inconsistent with published crystal structures of K11-Ub2. We found that increasing salt concentration compacts K11-Ub2 and strengthens interactions between the two Ub units. Binding studies indicate that K11-Ub2 interacts with ubiquitin-receptor proteins from both proteasomal and nonproteasomal pathways but with intermediate affinity and different binding modes than either K48-linked or K63-linked diubiquitin. Our data support the hypothesis that polyubiquitin chains of different linkages possess unique conformational and dynamical properties, allowing them to be recognized differently by downstream receptor proteins.

Indexed as

HumansLigandsLysineModels, MolecularNeutron DiffractionNuclear Magnetic Resonance, BiomolecularPolyubiquitinProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryScattering, Small AngleSodium ChlorideSolutionsStructural Homology, ProteinLigandsLysinePolyubiquitinSodium ChlorideSolutions

Identifiers

PMID23823328
PMCPMC3802530

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.