Evidence map›Paper›PMID 34163592›Full record

ArticleChemical science2020

Ultrasensitive small molecule fluorogenic probe for human heparanase.

Jun Liu, Kelton A Schleyer, Tyrel L Bryan, Changjian Xie, Gustavo Seabra, Yongmei Xu, Arjun Kafle, Chao Cui, Ying Wang, Kunlun Yin and 7 more

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. A Coumarin-Porphyrin FRET Break-Apart Probe for Heme Oxygenase-1.Journal of the American Chemical Society · 2021
    Article
  8. 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

17 authors at 3 institutions in 1 country.

Jun LiuDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Kelton A SchleyerDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Tyrel L BryanDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Changjian XieDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Gustavo SeabraDepartment of Medicinal Chemistry, College of Pharmacy, University of Florida Gainesville FL 32610 USA linacui@cop.ufl.edu.
Yongmei XuDivision of Chemical Biology and Medicinal Chemistry, Eshelman School of Pharmacy, University of North Carolina Chapel Hill NC 27599 USA.
Arjun KafleDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Chao CuiDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Ying WangDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Kunlun YinDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Benjamin FetrowDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Paul K P HendersonDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Peter Z FatlandDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.
Jian LiuDivision of Chemical Biology and Medicinal Chemistry, Eshelman School of Pharmacy, University of North Carolina Chapel Hill NC 27599 USA.
Chenglong LiDepartment of Medicinal Chemistry, College of Pharmacy, University of Florida Gainesville FL 32610 USA linacui@cop.ufl.edu.
Hua GuoDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.ORCID https://orcid.org/0000-0001-9901-053X
Lina CuiDepartment of Chemistry and Chemical Biology, University of New Mexico Albuquerque NM 87131 USA.ORCID https://orcid.org/0000-0002-8149-5206
University of New Mexico · USUniversity of North Carolina at Chapel Hill · USUniversity of Florida · US

Funding

Probing the role of heparanase via in situ labelingR35GM124963 · NIGMS · UNIVERSITY OF NEW MEXICO · PI CUI, LINA · 2017 to 2021
$1.9M
Acquisition of a Q Exactive HF Hybrid Quadrupole-OrbitrapS10OD021758 · OD · UNIVERSITY OF FLORIDA · PI BASSO, KARI B · 2017 to 2017
$600k
NIGMS NIH HHS R35 GM124963NIH HHS S10 OD021758
6 · The paper itself

Abstract

Heparanase (HPA) is a critical enzyme involved in the remodeling of the extracellular matrix (ECM), and its elevated expression has been linked with diseases such as various types of cancer and inflammation. The detection of heparanase enzymatic activity holds tremendous value in the study of the cellular microenvironment, and search of molecular therapeutics targeting heparanase, however, no structurally defined probes are available for the detection of heparanase activity. Here we present the development of the first ultrasensitive fluorogenic small-molecule probe for heparanase enzymatic activity

Identifiers

PMID34163592
PMCPMC8178809
OpenAlexW3094278139

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.