Evidence map›Paper›PMID 19352404›Full record

ReviewNature reviews. Molecular cell biology2009

Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways.

Brenda A Schulman, J Wade Harper

Abstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 511 papers.

0numbers the graph read from it
0cells of the map it votes in
511citing 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

511 citing papers in PubMed.

  1. Evolving CRBN ligands enhance the drug-like properties of protein degraders.Journal of enzyme inhibition and medicinal chemistry · 2026
    Review
  2. Review
  3. Article
  4. The ubiquitin-activating enzyme inhibitor TAK-243 activates store-operated CaBiochimica et biophysica acta. Molecular cell research · 2026
    Article
  5. Article
  6. Article
  7. Article
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  9. Article
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  12. Cell autonomous inflammation in VEXAS is mediated by cGAS-STING.bioRxiv : the preprint server for biology · 2026
    Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Molecular insights for the tumor suppressor role of SPOP in prostate cancer.Biochimica et biophysica acta. Reviews on cancer · 2026
    Review
  19. Review
  20. Article

451 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

2 authors.

Brenda A SchulmanHoward Hughes Medical Institute, Department of Structural Biology, St Jude Children's Research Hospital, Memphis, Tennessee 38105, USA. brenda.schulman@stjude.org
J Wade Harper

Funding

Ubiquitin Mediated Proteolysis and Cell Cycle ControlR01AG011085 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI JEFFREY W HARPER · 1993 to 2026
$10.9M
SYSTEMATIC ANALYSIS OF THE DUB PROTEOMER01GM054137 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HARPER, JEFFREY W · 1996 to 2012
$4.1M
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
Structures/mechanisms in a noncanonical ubiquitin-like protein transfer cascadeR01GM077053 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2006 to 2014
$1.8M
Structure and Mechanism of the Parkin Ubiquitin LigaseR03AG022633 · NIA · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI SCHULMAN, BRENDA A · 2003 to 2003
$75k
Howard Hughes Medical InstituteNIA NIH HHS R01 AG011085NIA NIH HHS R03 AG022633NIGMS NIH HHS R01 GM054137NIGMS NIH HHS R01 GM069530NIGMS NIH HHS R01 GM070565NIGMS NIH HHS R01 GM077053
6 · The paper itself

Abstract

Attachment of ubiquitin or ubiquitin-like proteins (known as UBLs) to their targets through multienzyme cascades is a central mechanism to modulate protein functions. This process is initiated by a family of mechanistically and structurally related E1 (or activating) enzymes. These activate UBLs through carboxy-terminal adenylation and thiol transfer, and coordinate the use of UBLs in specific downstream pathways by charging cognate E2 (or conjugating) enzymes, which then interact with the downstream ubiquitylation machinery to coordinate the modification of the target. A broad understanding of how E1 enzymes activate UBLs and how they selectively coordinate UBLs with downstream function has come from enzymatic, structural and genetic studies.

Indexed as

AnimalsHumansSignal TransductionUbiquitinUbiquitin-Activating EnzymesUbiquitinationUbiquitinsUbiquitinUbiquitin-Activating EnzymesUbiquitins

Identifiers

PMID19352404
PMCPMC2712597

What OpenQuestion holds

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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.