Article in mAbs, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it
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.
2 · The registry
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.
Maria Calderon VacaDepartment of Chemical, Environmental and Materials Engineering, University of Miami, Miami, FL, USA.
Matthew MatusewiczDepartment of Chemical Engineering, Manhattan University, Riverdale, NY, USA.
Connor SmithDepartment of Chemical Engineering, Manhattan University, Riverdale, NY, USA.
Joshin GeorgeDepartment of Chemical Engineering, Manhattan University, Riverdale, NY, USA.
Collin TaylorDepartment of Chemical, Environmental and Materials Engineering, University of Miami, Miami, FL, USA.
Michael S MarlowBiotherapeutics Discovery Department, Boehringer Ingelheim Pharmaceuticals Inc., Ridgefield, CT, USA.ORCID 0000-0002-9335-7652
Samiul AminDepartment of Chemical, Environmental and Materials Engineering, University of Miami, Miami, FL, USA.ORCID 0000-0002-3469-7358
Funding
No grant is acknowledged in the PubMed record.
6 · The paper itself
Abstract
High-concentration monoclonal antibody (mAb) formulations are frequently constrained by elevated viscosity and colloidal instability, stemming from enhanced intermolecular interactions under crowded conditions. In this study, we delineate the thermodynamic and rheological consequences of modulating protein-protein interactions through excipient-mediated and temperature-dependent mechanisms. Using an orthogonal analytical framework comprising diffusion interaction parameter (
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.
Temperature and excipient mediated modulation of monoclonal antibody interactions revealed by · full record | OpenQuestion