Evidence map›Paper›PMID 23201271›Full record

ArticleStructure (London, England : 1993)2013

Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes.

Julie K Monda, Daniel C Scott, Darcie J Miller, John Lydeard, David King, J Wade Harper, Eric J Bennett, Brenda A Schulman

Open access · bronzeAbstract 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 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
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

76 citing papers in PubMed, 126 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Fine mapping and prediction of a candidate gene for wrinkled rind in melon (Cucumis melo L.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025
    Article
  7. Article
  8. Review
  9. InPathogens (Basel, Switzerland) · 2025
    Article
  10. Review
  11. Article
  12. Article
  13. Methylation profiles at birth linked to early childhood obesity.Journal of developmental origins of health and disease · 2024
    Article
  14. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  15. Methylation profiles at birth linked to early childhood obesity.medRxiv : the preprint server for health sciences · 2024
    Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Article

16 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Julie K MondaDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA; Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
Daniel C ScottDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA; Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA; Howard Hughes Medical Institute, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
Darcie J MillerDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
John LydeardDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
David KingHHMI Mass Spectrometry Laboratory, University of California, Berkeley, CA 94720, USA.
J Wade HarperDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.
Eric J BennettDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115, USA; Division of Biological Sciences, University of California San Diego, La Jolla, CA 92093, USA.
Brenda A SchulmanDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA; Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA; Howard Hughes Medical Institute, St. Jude Children's Research Hospital, Memphis, TN 38105, USA. Electronic address: brenda.schulman@stjude.org.
Harvard University · USSt. Jude Children's Research Hospital · USUniversity of California, Berkeley · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
Ubiquitin-like Protein Transfer CascadesR01GM069530 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2003 to 2013
$3.4M
SYSTEMATIC ANALYSIS OF PROTEOLYSIS PATHWAYS FOR CULLIN TARGETSR01GM070565 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HARPER, JEFFREY W · 2005 to 2012
$2.6M
Howard Hughes Medical InstituteNCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301NIGMS NIH HHS R01 GM069530NIGMS NIH HHS R01GM069530NIGMS NIH HHS R01 GM070565NIGMS NIH HHS R01GM070565
6 · The paper itself

Abstract

Little is known about molecular recognition of acetylated N termini, despite prevalence of this modification among eukaryotic cytosolic proteins. We report that the family of human DCN-like (DCNL) co-E3s, which promote ligation of the ubiquitin-like protein NEDD8 to cullin targets, recognizes acetylated N termini of the E2 enzymes UBC12 and UBE2F. Systematic biochemical and biophysical analyses reveal 40- and 10-fold variations in affinities among different DCNL-cullin and DCNL-E2 complexes, contributing to varying efficiencies of different NEDD8 ligation cascades. Structures of DCNL2 and DCNL3 complexes with N-terminally acetylated peptides from UBC12 and UBE2F illuminate a common mechanism by which DCNL proteins recognize N-terminally acetylated E2s and how selectivity for interactions dependent on N-acetyl-methionine are established through side chains recognizing distal residues. Distinct preferences of UBC12 and UBE2F peptides for inhibiting different DCNLs, including the oncogenic DCNL1 protein, suggest it may be possible to develop small molecules blocking specific N-acetyl-methionine-dependent protein interactions.

Indexed as

AcetylationAmino Acid SequenceAnimalsCell Cycle ProteinsCrystallography, X-RayHumansHydrophobic and Hydrophilic InteractionsIntracellular Signaling Peptides and ProteinsKineticsMiceModels, MolecularMolecular Sequence DataNEDD8 ProteinNIH 3T3 CellsPeptide FragmentsProtein BindingCell Cycle ProteinsDCUN1D1 protein, humanDCUN1D3 protein, humanIntracellular Signaling Peptides and ProteinsNEDD8 ProteinNEDD8 protein, humanPeptide FragmentsProteinsProto-Oncogene ProteinsUBE2F protein, humanUbiquitin-Conjugating EnzymesUbiquitins

Identifiers

PMID23201271
PMCPMC3786212
OpenAlexW2066787685

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.