Proteomics

Dataset Information

0

APEX-Gal1 Labeled C2C12 Myoblasts


ABSTRACT: Myogenic differentiation is influenced by interactions at the cell surface involving the glycan binding protein galectin-1. Using a proximity labeling galectin-1 construct, we biotinylated and enriched galectin-1 interactors in mouse myoblasts, and analyzed them by LC/MS/MS to determine relevant galectin-1 interactors.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Skeletal Muscle Myoblast, Cell Culture

SUBMITTER: Zak Vilen  

LAB HEAD: Mia L. Huang

PROVIDER: PXD026718 | Pride | 2021-07-05

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
MS221021_MH_ZV_B2_046.msf Msf
MS221021_MH_ZV_B2_046.raw Raw
MS221027_MH_ZV_B2_052.msf Msf
MS221027_MH_ZV_B2_052.raw Raw
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Publications

Proximity Tagging Identifies the Glycan-Mediated Glycoprotein Interactors of Galectin-1 in Muscle Stem Cells.

Vilen Zak Z   Joeh Eugene E   Critcher Meg M   Parker Christopher G CG   Huang Mia L ML  

ACS chemical biology 20210628 10


Myogenic differentiation, the irreversible developmental process where precursor myoblast muscle stem cells become contractile myotubes, is heavily regulated by glycosylation and glycan-protein interactions at the cell surface and the extracellular matrix. The glycan-binding protein galectin-1 has been found to be a potent activator of myogenic differentiation. While it is being explored as a potential therapeutic for muscle repair, a precise understanding of its glycoprotein interactors is lack  ...[more]

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