Evidence map›Paper›PMID 10954757›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Integration of the ubiquitin-proteasome pathway with a cytosolic oligopeptidase activity.

E W Wang, B M Kessler, A Borodovsky, B F Cravatt, M Bogyo, H L Ploegh, R Glas

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

28 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Proteases in MHC class I presentation and cross-presentation.Journal of immunology (Baltimore, Md. : 1950) · 2010
    Review
  11. Article
  12. Article
  13. Article
  14. Activation of cellular death programs associated with immunosenescence-like phenotype in TPPII knockout mice.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  15. Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  16. Molecular architecture and assembly mechanism of Drosophila tripeptidyl peptidase II.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  17. Review
  18. Review
  19. Article
  20. Review
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

7 authors at 2 institutions in 1 country.

E W WangDepartment of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
B M Kessler
A Borodovsky
B F Cravatt
M Bogyo
H L Ploegh
R Glas
Scripps Research Institute · USHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytosolic proteolysis is carried out predominantly by the proteasome. We show that a large oligopeptidase, tripeptidylpeptidase II (TPPII), can compensate for compromised proteasome activity. Overexpression of TPPII is sufficient to prevent accumulation of polyubiquitinated proteins and allows survival of EL-4 cells at otherwise lethal concentrations of the covalent proteasome inhibitor NLVS (NIP-leu-leu-leu-vinylsulfone). Elevated TPPII activity also partially restores peptide loading of MHC molecules. Purified proteasomes from adapted cells lack the chymotryptic-like activity, but still degrade longer peptide substrates via residual activity of their Z subunits. However, growth of adapted cells depends on induction of other proteolytic activities. Therefore, cytosolic oligopeptidases such as TPPII normalize rates of intracellular protein breakdown required for normal cellular function and viability.

Indexed as

Amino Acid SequenceAnimalsCaspasesCysteine EndopeptidasesCytosolHistocompatibility Antigens Class IKineticsLymphomaMiceMolecular Sequence DataMultienzyme ComplexesPeptide FragmentsPeptide HydrolasesProteasome Endopeptidase ComplexRecombinant ProteinsSubstrate SpecificityCaspasesCysteine EndopeptidasesHistocompatibility Antigens Class IMultienzyme ComplexesoligopeptidasePeptide FragmentsPeptide HydrolasesProteasome Endopeptidase ComplexRecombinant ProteinsTrypsinUbiquitins

Identifiers

PMID10954757
PMCPMC27648
OpenAlexW2097790679

What OpenQuestion holds

Textmetadata
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.