ArticleProceedings of the National Academy of Sciences of the United States of America2012
Mass spectrometry study of a transferrin-based protein drug reveals the key role of protein aggregation for successful oral delivery.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. 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
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
6 citing papers in PubMed, 17 citations in OpenAlex.
- Natural Oral Absorption of Therapeutic Peptides: Mechanisms and Physiological Determinants.Pharmaceutics · 2026Review
- Characterization of Large Immune Complexes with Size Exclusion Chromatography and Native Mass Spectrometry Supplemented with Gas Phase Ion Chemistry.Analytical chemistry · 2024Article
- Identification of reduction-susceptible disulfide bonds in transferrin by differential alkylation using O(16)/O(18) labeled iodoacetic acid.Journal of the American Society for Mass Spectrometry · 2015Article
- An 18O-labeling assisted LC/MS method for assignment of aspartyl/isoaspartyl products from Asn deamidation and Asp isomerization in proteins.Analytical chemistry · 2013Article
- Emerging mass spectrometry-based approaches to probe protein-receptor interactions: focus on overcoming physiological barriers.Advanced drug delivery reviews · 2013Review
- Mass spectrometry-guided optimization and characterization of a biologically active transferrin-lysozyme model drug conjugate.Molecular pharmaceutics · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
A recently designed human growth hormone/transferrin fusion protein (GHT) remains one of the very few examples of a protein capable of eliciting measurable therapeutic response after oral administration. To better understand the underlying factors that resulted in this rare success of nonparenteral protein drug delivery, we analyzed proteolytic stability and receptor binding properties of this protein, the key factors in overcoming the primary barriers to successful oral delivery. Analysis of GHT by a combination of size exclusion chromatography and mass spectrometry revealed that a significant protein population exists in an oligomeric (GHTx) state in addition to the anticipated monomer (GHT1). These states of GHT were evaluated for their survivability in stomach-like conditions, as well as their ability to bind transferrin receptor (TfR). Our results reveal an exceptional stability of GHTx, as well as the preserved ability to bind TfR, a critical first step in crossing the epithelial-intestinal barrier through receptor-mediated transcytosis.
Indexed as
Identifiers
What 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.