Evidence map›Paper›PMID 35981509›Full record

ArticleBiochemistry2022

Cathepsin B Dipeptidyl Carboxypeptidase and Endopeptidase Activities Demonstrated across a Broad pH Range.

Michael C Yoon, Vivian Hook, Anthony J O'Donoghue

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.0field-weighted citation impact, top 7% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Targeting Lysosomes for Enhanced Anti-Cancer Therapeutics and Immune Response.International journal of biological sciences · 2026
    Review
  6. Article
  7. The mycotoxin Beauvericin is an uncompetitive inhibitor of Cathepsin B.Protein science : a publication of the Protein Society · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
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  17. Article
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

3 authors at 1 institution in 1 country.

Michael C YoonSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, California 92093, United States.ORCID 0000-0002-2900-5257
Vivian HookSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, California 92093, United States.ORCID 0000-0001-6461-7024
Anthony J O'DonoghueSkaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, La Jolla, California 92093, United States.
University of California San Diego · US

Funding

Development of Molecular Probe Inhibitors of Pathogenic, Cytosolic Cathespin B in Traumatic Brain Injury and Alzheimers Disease NeurodegenerationR01NS109075 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HOOK, VIVIAN Y. H · 2019 to 2023
$3.7M
Training Program in Marine BiotechnologyT32GM067550 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GERWICK, WILLIAM HENRY · 2004 to 2019
$2.0M
Tumor-specific drug activation by pericellular proteasesR21CA256460 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI O'DONOGHUE, ANTHONY JOHN, OWEN, SHAWN C · 2022 to 2023
$409k
NCI NIH HHS R21 CA256460NIGMS NIH HHS T32 GM067550NINDS NIH HHS R01 NS109075
6 · The paper itself

Abstract

Cathepsin B is a lysosomal protease that participates in protein degradation. However, cathepsin B is also active under neutral pH conditions of the cytosol, nuclei, and extracellular locations. The dipeptidyl carboxypeptidase (DPCP) activity of cathepsin B, assayed with the Abz-GIVR↓AK(Dnp)-OH substrate, has been reported to display an acidic pH optimum. In contrast, the endopeptidase activity, monitored with Z-RR-↓AMC, has a neutral pH optimum. These observations raise the question of whether other substrates can demonstrate cathepsin B DPCP activity at neutral pH and endopeptidase activity at acidic pH. To address this question, global cleavage profiling of cathepsin B with a diverse peptide library was conducted under acidic and neutral pH conditions. Results revealed that cathepsin B has (1) major DPCP activity and modest endopeptidase activity under both acidic and neutral pH conditions and (2) distinct pH-dependent amino acid preferences adjacent to cleavage sites for both DPCP and endopeptidase activities. The pH-dependent cleavage preferences were utilized to design a new Abz-G

Indexed as

Cathepsin BCathepsinsEndopeptidasesHydrogen-Ion ConcentrationHydrolysisProteolysisSubstrate SpecificityCathepsin BCathepsinsdipeptidyl carboxypeptidaseEndopeptidases

Identifiers

PMID35981509
PMCPMC9454093
OpenAlexW4293797655

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.