Evidence map›Paper›PMID 35999181›Full record

ArticleAngewandte Chemie (International ed. in English)2022

Human Cyclophilin B Nuclease Activity Revealed via Nucleic Acid-Based Electrochemical Sensors.

Vincent Clark, Kelly Waters, Ben Orsburn, Namandjé N Bumpus, Nandini Kundu, Jonathan T Sczepanski, Partha Ray, Netzahualcóyotl Arroyo-Currás

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Biomaterials for biomarker imaging and detection.Journal of advanced research · 2026
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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.

Vincent ClarkChemistry-Biology Interface Program, Zanvyl Krieger School of Arts & Sciences, Johns Hopkins University, Baltimore, MD 21218, USA.
Kelly WatersDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Ben OrsburnDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Namandjé N BumpusDepartment of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Nandini KunduDepartment of Chemistry, Texas A&M University College Station, Texas, TX 77842, USA.
Jonathan T SczepanskiDepartment of Chemistry, Texas A&M University College Station, Texas, TX 77842, USA.
Partha RayDepartment of Surgery, Division of Surgical Oncology, Moores Cancer Center, Department of Medicine, Division of Infectious Diseases and Global Public Health, University of California San Diego Health, San Diego, CA 92093, USA.
Netzahualcóyotl Arroyo-CurrásChemistry-Biology Interface Program, Zanvyl Krieger School of Arts & Sciences, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0002-2740-6276
Johns Hopkins University · USTexas A&M University · USUC San Diego Health System · US

Funding

The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM080189 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2008 to 2022
$3.5M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM149382 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI STEVEN E ROKITA · 2023 to 2026
$1.4M
NIGMS NIH HHS T32 GM080189NIGMS NIH HHS T32 GM149382
6 · The paper itself

Abstract

Human cyclophilin B (CypB) is oversecreted by pancreatic cancer cells, making it a potential biomarker for early-stage disease diagnosis. Our group is motivated to develop aptamer-based assays to measure CypB levels in biofluids. However, human cyclophilins have been postulated to have collateral nuclease activity, which could impede the use of aptamers for CypB detection. To establish if CypB can hydrolyze electrode-bound nucleic acids, we used ultrasensitive electrochemical sensors to measure CypB's hydrolytic activity. Our sensors use ssDNA and dsDNA in the biologically predominant d-DNA form, and in the nuclease resistant l-DNA form. Challenging such sensors with CypB and control proteins, we unequivocally demonstrate that CypB can cleave nucleic acids. To our knowledge, this is the first study to use electrochemical biosensors to reveal the hydrolytic activity of a protein that is not known to be a nuclease. Future development of CypB bioassays will require the use of nuclease-resistant aptamer sequences.

Indexed as

Nucleic AcidsPancreatic NeoplasmsCyclophilinsDNAElectrochemical TechniquesEndonucleasesHumanscyclophilin BCyclophilinsDNAEndonucleasesNucleic AcidsAptamer-Based SensorsBiomarkerCyclophilin BNucleasePancreatic Cancer

Identifiers

PMID35999181
PMCPMC9633453
OpenAlexW4293032554

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.