ArticleAnalytical and bioanalytical chemistry2026
Strategies for in-depth and simultaneous analysis of N- and O-glycoproteome of platelets uncovering sex-specific signatures of human platelets.
Article in Analytical and bioanalytical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Platelets are pivotal circulating effector cells central to diverse physiological and pathological processes, with many of their essential functions-such as activation, adhesion, and signal transduction-being modulated by protein glycosylation. However, the inherent microheterogeneity and low ionization efficiency of glycopeptides continue to pose substantial technical barriers to achieving large-scale and precise analysis at the intact glycopeptide level, thereby limiting the in-depth exploration of platelet glycoproteome. In this study, we first evaluated three enzymatic digestion strategies-trypsin alone, Lys-C/trypsin combination, and Glu-C/trypsin combination, followed by optimization of mass spectrometry parameters for stepped-collision-energy high-energy collisional dissociation (sceHCD), ultimately establishing an efficient glycoproteomic workflow tailored to human peripheral blood platelets. Application of this workflow to platelets from healthy volunteers led to the successful identification and quantitation of 4696 intact N-glycopeptides mapping to 299 glycoproteins and 534 glycosites involving 447 distinct glycans. Extension to the O-glycoproteome further confirmed workflow generalizability, successfully identifying 2807 O-glycopeptides, 548 O-glycosites, and 340 O-glycoproteins. Exploratory functional analysis indicated that males were enriched with glycoproteins associated with coagulation and complement regulation, whereas for females pathways related to cell adhesion and viral infection response were enriched. These sex‑dimorphic glycoprotein signatures provide insights into sex‑related differences in platelet physiology.
Indexed as
Identifiers
41917452What OpenQuestion holds
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.