ArticleMatrix biology plus2019
Allysine modifications perturb tropoelastin structure and mobility on a local and global scale.
Article in Matrix biology plus, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Modification of extracellular matrix proteins by oxidants and electrophiles.Biochemical Society transactions · 2024Review
- Multiscale modelling of the extracellular matrix.Matrix biology plus · 2022Article
- Fuzzy binding model of molecular interactions between tropoelastin and integrin alphaVbeta3.Biophysical journal · 2021Article
- Elastin-like polypeptide modified silk fibroin porous scaffold promotes osteochondral repair.Bioactive materials · 2021Article
- Tropoelastin and Elastin Assembly.Frontiers in bioengineering and biotechnology · 2021Review
- Transglutaminase-Mediated Cross-Linking of Tropoelastin to Fibrillin Stabilises the Elastin Precursor Prior to Elastic Fibre Assembly.Journal of molecular biology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Elastin provides elastic tissues with resilience through stretch and recoil cycles, and is primarily made of its extensively cross-linked monomer, tropoelastin. Here, we leverage the recently published full atomistic model of tropoelastin to assess how allysine modifications, which are essential to cross-linking, contribute to the dynamics and structural changes that occur in tropoelastin in the context of elastin assembly. We used replica exchange molecular dynamics to generate structural ensembles of allysine containing tropoelastin. We conducted principal component analysis on these ensembles and found that the molecule departs from the canonical structural ensemble. Furthermore, we showed that, while the canonical scissors-twist movement was retained, new movements emerged that deviated from those of the wild type protein, providing evidence for the involvement of a variety of molecular motions in elastin assembly. Additionally, we highlighted secondary structural changes and linked these perturbations to the longevity of specific salt bridges. We propose a model where allysines in tropoelastin contribute to hierarchical elastin assembly through global and local perturbations to molecular structure and dynamics.
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Registered trials
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.