Evidence map›Paper›PMID 25785540›Full record

ArticleJournal of the American Chemical Society2015

Design of a highly selective quenched activity-based probe and its application in dual color imaging studies of cathepsin S activity localization.

Kristina Oresic Bender, Leslie Ofori, Wouter A van der Linden, Elliot D Mock, Gopal K Datta, Somenath Chowdhury, Hao Li, Ehud Segal, Mateo Sanchez Lopez, Jonathan A Ellman and 3 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.0field-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

42 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Redirecting the Peptide Cleavage Causes Protease Inactivation.Angewandte Chemie (International ed. in English) · 2025
    Article
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  8. Review
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  10. Review
  11. Article
  12. Enzyme-Activatable Chemokine Conjugates for In Vivo Targeting of Tumor-Associated Macrophages.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  13. Cathepsin S Evokes PARCancers · 2021
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

13 authors at 3 institutions in 2 countries.

Kristina Oresic Bender
Leslie Ofori
Wouter A van der Linden
Elliot D Mock
Gopal K Datta∥Department of Chemistry, University of California-Berkeley, Berkeley, California 94720, United States.
Somenath Chowdhury∥Department of Chemistry, University of California-Berkeley, Berkeley, California 94720, United States.
Hao Li
Ehud Segal
Mateo Sanchez Lopez
Jonathan A Ellman∥Department of Chemistry, University of California-Berkeley, Berkeley, California 94720, United States.
Carl G Figdor⊥Department of Tumor Immunology, Radboud University Medical Center, Radboud Institute for Molecular Life Sciences, 6500 HB Nijmegen, The Netherlands.
Matthew Bogyo
Martijn Verdoes⊥Department of Tumor Immunology, Radboud University Medical Center, Radboud Institute for Molecular Life Sciences, 6500 HB Nijmegen, The Netherlands.
University of California, Berkeley · USRadboud Institute for Molecular Life Sciences · NLRadboud University Medical Center · NL

Funding

TOTAL SYNTHESIS OF THIOSTREPTONR01AI055475 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI NICOLAOU, K. C. · 2002 to 2014
$7.0M
Substrate Activity Screening: A New Approach to Inhibitor DiscoveryR01GM054051 · NIGMS · YALE UNIVERSITY · PI ELLMAN, JONATHAN A · 1997 to 2016
$5.2M
Small Molecule Imaging of Protease ActivityR01EB005011 · NIBIB · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2005 to 2013
$3.0M
Cathepsin S-targeted probes for optical and PET imaging of lung fibrosisR01HL116307 · NHLBI · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2012 to 2014
$1.3M
European Research Council 269019NHLBI NIH HHS R01 HL116307NIAID NIH HHS AI055475NIBIB NIH HHS 3R01EB005011-06S1NIBIB NIH HHS R01 EB005011NIGMS NIH HHS R01 GM054051
6 · The paper itself

Abstract

The cysteine cathepsins are a group of 11 proteases whose function was originally believed to be the degradation of endocytosed material with a high degree of redundancy. However, it has become clear that these enzymes are also important regulators of both health and disease. Thus, selective tools that can discriminate between members of this highly related class of enzymes will be critical to further delineate the unique biological functions of individual cathepsins. Here we present the design and synthesis of a near-infrared quenched activity-based probe (qABP) that selectively targets cathepsin S which is highly expressed in immune cells. Importantly, this high degree of selectivity is retained both in vitro and in vivo. In combination with a new green-fluorescent pan-reactive cysteine cathepsin qABP we performed dual color labeling studies in bone marrow-derived immune cells and identified vesicles containing exclusively cathepsin S activity. This observation demonstrates the value of our complementary cathepsin probes and provides evidence for the existence of specific localization of cathepsin S activity in dendritic cells.

Indexed as

Drug DesignInfrared RaysAnimalsCathepsinsColorDendritic CellsFluorescent DyesHumansMammary Neoplasms, ExperimentalMiceOptical ImagingRAW 264.7 CellsSubstrate Specificitycathepsin SCathepsinsFluorescent Dyes

Identifiers

PMID25785540
PMCPMC4747655
OpenAlexW1990590874

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.