CD16a Glycoform Affinity Measurements via Mass Spectrometry

111.4 KB of Excel data describes a targeted mass spectrometry method for studying Fcγ receptor glycosylation. Carlos H. Pavan developed a parallel reaction monitoring (PRM) method to assess high-affinity glycoforms of CD16a at site N162. The data, available via ProteomeXchange identifier PXD071784, was applied to models of monocyte differentiation and primary human cells.

Use Cases

• Analyze changes in CD16a glycosylation based on the described PRM mass spectrometry method
• Compare high-mannose glycoform proportions based on the affinity measurements for site N162
• Study monocyte differentiation models based on the application of the method to primary cells
• Adapt the analytical strategy for clinical studies based on the description of its suitability for immunotherapy research

Strengths

• 111.4 KB file size indicates a focused dataset with specific measurements
• Data is linked to a public ProteomeXchange repository with identifier PXD071784
• Method is described as targeted and site-specific for N-glycosylation

Limitations

• Row count is unknown, which may limit suitability assessment
• Column-level documentation is absent; field semantics must be inferred after download
• The dataset's 111.4 KB size suggests a limited scope of observations

Provenance

Source

figshare

Collection Method

Targeted nanoliquid chromatography tandem mass spectrometry parallel reaction monitoring (PRM)

Freshness

Last updated 2026-04-24 04:06:35; freshness should be verified