Evidence map›Paper›PMID 34944490›Full record

ArticleBiomolecules2021

Oligomeric States and Hydrodynamic Properties of Lysyl Oxidase-Like 2.

Alex A Meier, Hee-Jung Moon, Ronald Toth, Ewa Folta-Stogniew, Krzysztof Kuczera, C Russell Middaugh, Minae Mure

Abstract read
In one paragraph

Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
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

5 citing papers in PubMed.

  1. LOXL2 in Cancer: A Two-Decade Perspective.International journal of molecular sciences · 2023
    Review
  2. Insight into the Spatial Arrangement of the Lysine Tyrosylquinone and CuInternational journal of molecular sciences · 2022
    Article
  3. Article
  4. Mass Spectrometry-Based Disulfide Mapping of Lysyl Oxidase-like 2.International journal of molecular sciences · 2022
    Article
  5. Review
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

7 authors.

Alex A MeierDepartment of Chemistry, University of Kansas, Lawrence, KS 66045, USA.
Hee-Jung MoonDepartment of Chemistry, University of Kansas, Lawrence, KS 66045, USA.
Ronald TothDepartment of Pharmaceutical Chemistry, School of Pharmacy, University of Kansas, Lawrence, KS 66047, USA.
Ewa Folta-StogniewW.M. Keck Biotechnology Resource Laboratory, Department of Molecular Biophysics and Biochemistry, Yale School of Medicine, New Haven, CT 06511, USA.
Krzysztof KuczeraDepartment of Chemistry, University of Kansas, Lawrence, KS 66045, USA.ORCID 0000-0003-2358-1349
C Russell MiddaughDepartment of Pharmaceutical Chemistry, School of Pharmacy, University of Kansas, Lawrence, KS 66047, USA.
Minae MureDepartment of Chemistry, University of Kansas, Lawrence, KS 66045, USA.

Funding

Transgenic & Gene-Targeting Shared ResourceP30CA168524 · NCI · UNIVERSITY OF KANSAS MEDICAL CENTER · PI NICOLE L NOLLEN · 2012 to 2026
$40.1M
Protein Structure Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2014 to 2018
$5.6M
PHARMACEUTICAL ASPECTS OF BIOTECHNOLOGY TRAININGT32GM008359 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI SIAHAAN, TERUNA J., VOLKIN, DAVID · 1989 to 2018
$5.0M
Understanding the roles of PTM's in modulating molecular functions of lysyl oxidase-like 2 in breast cancer cellsR01GM113101 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI MURE, MINAE · 2014 to 2017
$1.1M
National Institute of Health 1S10RR023748 01National Institute of Health R01GM113101NCI NIH HHS P30 CA168524NIGMS NIH HHS P30 GM110761NIGMS NIH HHS R01 GM113101NIGMS NIH HHS T32 GM008359NIGMS NIH HHS T32-GM008359University of Kansas GM110761University of Kansas Cancer Center P30CA168524
6 · The paper itself

Abstract

Lysyl oxidase-like 2 (LOXL2) has emerged as a promising therapeutic target against metastatic/invasive tumors and organ and tissue fibrosis. LOXL2 catalyzes the oxidative deamination of lysine and hydroxylysine residues in extracellular matrix (ECM) proteins to promote crosslinking of these proteins, and thereby plays a major role in ECM remodeling. LOXL2 secretes as 100-kDa full-length protein (fl-LOXL2) and then undergoes proteolytic cleavage of the first two scavenger receptor cysteine-rich (SRCR) domains to yield 60-kDa protein (Δ1-2SRCR-LOXL2). This processing does not affect the amine oxidase activity of LOXL2 in vitro. However, the physiological importance of this cleavage still remains elusive. In this study, we focused on characterization of biophysical properties of fl- and Δ1-2SRCR-LOXL2s (e.g., oligomeric states, molecular weights, and hydrodynamic radii in solution) to gain insight into the structural role of the first two SRCR domains. Our study reveals that fl-LOXL2 exists predominantly as monomer but also dimer to the lesser extent when its concentration is <~1 mM. The hydrodynamic radius (

Indexed as

Amino Acid OxidoreductasesCell LineCrystallography, X-RayHumansHydrodynamicsModels, MolecularProtein DomainsProtein MultimerizationProtein Structure, TertiaryProteolysisAmino Acid OxidoreductasesLOXL2 protein, humananalytical ultracentrifugationextracellular matrixhydrodynamic radiusisoelectric pointslysyl oxidase-like 2scavenger receptor cysteine-rich

Identifiers

PMID34944490
PMCPMC8699698

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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.