Evidence map›Paper›PMID 34226627›Full record

ArticleCommunications biology2021

An in situ activity assay for lysyl oxidases.

Huilei Wang, Alan Poe, Lydia Pak, Kavitha Nandakumar, Sandeep Jandu, Jochen Steppan, Reik Löser, Lakshmi Santhanam

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. LOXL2 inhibition ameliorates pulmonary artery remodeling in pulmonary hypertension.American journal of physiology. Lung cellular and molecular physiology · 2024
    Article
  7. Article
  8. Sex differences and role of lysyl oxidase-like 2 in angiotensin II-induced hypertension in mice.American journal of physiology. Heart and circulatory physiology · 2024
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Huilei WangDepartment of Biomedical Engineering, Johns Hopkins University, Baltimore, MD, USA.
Alan PoeDepartment of Biomedical Engineering, Johns Hopkins University, Baltimore, MD, USA.
Lydia PakDepartment of Biomedical Engineering, Johns Hopkins University, Baltimore, MD, USA.
Kavitha NandakumarDepartment of Anesthesiology and Critical Care Medicine, Johns Hopkins University, Baltimore, MD, USA.
Sandeep JanduDepartment of Anesthesiology and Critical Care Medicine, Johns Hopkins University, Baltimore, MD, USA.
Jochen SteppanDepartment of Anesthesiology and Critical Care Medicine, Johns Hopkins University, Baltimore, MD, USA.ORCID http://orcid.org/0000-0001-9856-512X
Reik LöserInstitute of Radiopharmaceutical Cancer Research, Helmholtz-Zentrum Dresden-Rossendorf, Dresden, Germany.ORCID http://orcid.org/0000-0003-1531-7601
Lakshmi SanthanamDepartment of Biomedical Engineering, Johns Hopkins University, Baltimore, MD, USA. LSantha1@jh.edu.ORCID http://orcid.org/0000-0002-2097-9397
Johns Hopkins University · USHelmholtz-Zentrum Dresden-Rossendorf · DE

Funding

Lysyl Oxidase Like 2: A Novel Target in Aging Associated Vascular StiffeningR01HL148112 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI SANTHANAM, LAKSHMI · 2020 to 2023
$1.9M
The Therapeutic Role for LOLX2 in Pulmonary HypertensionK08HL145132 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI STEPPAN, JOCHEN · 2019 to 2023
$859k
NHLBI NIH HHS K08 HL145132NHLBI NIH HHS R01 HL148112
6 · The paper itself

Abstract

The lysyl oxidase family of enzymes (LOXs) catalyze oxidative deamination of lysine side chains on collagen and elastin to initialize cross-linking that is essential for the formation of the extracellular matrix (ECM). Elevated expression of LOXs is highly associated with diverse disease processes. To date, the inability to detect total LOX catalytic function in situ has limited the ability to fully elucidate the role of LOXs in pathobiological mechanisms. Using LOXL2 as a representative member of the LOX family, we developed an in situ activity assay by utilizing the strong reaction between hydrazide and aldehyde to label the LOX-catalyzed allysine (-CHO) residues with biotin-hydrazide. The biotinylated ECM proteins are then labeled via biotin-streptavidin interaction and detected by fluorescence microscopy. This assay detects the total LOX activity in situ for both overexpressed and endogenous LOXs in cells and tissue samples and can be used for studies of LOXs as therapeutic targets.

Indexed as

Amino Acid OxidoreductasesAnimalsAortaBiocatalysisBlotting, WesternCell LineEnzyme AssaysFluorometryHumansMaleMiceMice, Inbred C57BLMice, KnockoutProtein-Lysine 6-OxidaseRatsAmino Acid OxidoreductasesLoxl2 protein, mouseProtein-Lysine 6-Oxidase

Identifiers

PMID34226627
PMCPMC8257687
OpenAlexW3178709272

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.