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pmid:34765964

Comprehensive quantitative characterization of the human term amnion proteome.

Eva Avilla-Royo · Katharina Gegenschatz-Schmid · Jonas Grossmann · Tobias Kockmann · Roland Zimmermann · Jess Gerrit Snedeker · Nicole Ochsenbein-Kölble · Martin Ehrbar

Matrix biology plus · 2021 doi:10.1016/j.mbplus.2021.100084

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complete

Experiment

complete

Data

partial

Analysis

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Execution

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title
Comprehensive quantitative characterization of the human term amnion proteome.
doi
10.1016/j.mbplus.2021.100084
pmid
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[0]
Eva Avilla-Royo
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Katharina Gegenschatz-Schmid
[2]
Jonas Grossmann
[3]
Tobias Kockmann
[4]
Roland Zimmermann
[5]
Jess Gerrit Snedeker
[6]
Nicole Ochsenbein-Kölble
[7]
Martin Ehrbar
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Matrix biology plus
year
2021
abstract
The loss of fetal membrane (FM) integrity and function at an early time point during pregnancy can have devastating consequences for the fetus and the newborn. However, biomaterials for preventive sealing and healing of FMs are currently non-existing, which can be partly attributed to the current fragmentary knowledge of FM biology. Despite recent advances in proteomics analysis, a robust and comprehensive description of the amnion proteome is currently lacking. Here, by an optimized protein sample preparation and offline fractionation before liquid chromatography coupled to mass spectrometry (LC-MS) analysis, we present a characterization of the healthy human term amnion proteome, which covers more than 40% of the previously reported transcripts in similar RNA sequencing datasets and, with more than 5000 identifications, greatly outnumbers previous reports. Together, beyond providing a basis for the study of compromised and preterm ruptured FMs, this comprehensive human amnion proteome is a stepping-stone for the development of novel healing-inducing biomaterials. The proteomic dataset has been deposited in the ProteomeXchange Consortium with the identifier PXD019410.
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Here, by an optimized protein sample preparation and offline fractionation before liquid chromatography coupled to mass spectrometry (LC-MS) analysis, we present a characterization of the healthy human term amnion proteome, which covers more than 40% of the previously reported transcripts in similar RNA sequencing datasets and, with more than 5000 identifications, greatly outnumbers previous reports.
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Here, by an optimized protein sample preparation and offline fractionation before liquid chromatography coupled to mass spectrometry (LC-MS) analysis, we present a characterization of the healthy human term amnion proteome, which covers more than 40% of the previously reported transcripts in similar RNA sequencing datasets and, with more than 5000 identifications, greatly outnumbers previous reports.
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Here, by an optimized protein sample preparation and offline fractionation before liquid chromatography coupled to mass spectrometry (LC-MS) analysis, we present a characterization of the healthy human term amnion proteome, which covers more than 40% of the previously reported transcripts in similar RNA sequencing datasets and, with more than 5000 identifications, greatly outnumbers previous reports.
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Here, by an optimized protein sample preparation and offline fractionation before liquid chromatography coupled to mass spectrometry (LC-MS) analysis, we present a characterization of the healthy human term amnion proteome, which covers more than 40% of the previously reported transcripts in similar RNA sequencing datasets and, with more than 5000 identifications, greatly outnumbers previous reports.
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