ReviewCurrent pharmaceutical design2015
Characterizing Protein Structure, Dynamics and Conformation in Lyophilized Solids.
Review in Current pharmaceutical design, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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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
15 citing papers in PubMed.
- Optimization of Sugar-Derivatives Mixtures for Stabilizing Polyclonal Immunoglobulin G in Spray-Dried Inhalable Powders During Processing and Long-Term Storage.Pharmaceutics · 2026Article
- Understanding dry proteins and their protection with solid-state hydrogen-deuterium exchange.Protein science : a publication of the Protein Society · 2025Review
- Proteomic Characterization of Human Placenta: Insights into Potential Therapeutic Applications for Osteoarthritis.AAPS PharmSciTech · 2024Article
- Properties of a tardigrade desiccation-tolerance protein aerogel.Biophysical journal · 2023Article
- Protection by desiccation-tolerance proteins probed at the residue level.Protein science : a publication of the Protein Society · 2022Article
- Water's Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR.Biochemistry · 2021Article
- Pharmaceutical protein solids: Drying technology, solid-state characterization and stability.Advanced drug delivery reviews · 2021Review
- Surface-Enhanced Raman Scattering (SERS) Spectroscopy for Sensing and Characterization of Exosomes in Cancer Diagnosis.Cancers · 2021Review
- Analytical Techniques for Structural Characterization of Proteins in Solid Pharmaceutical Forms: An Overview.Pharmaceutics · 2021Review
- Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR.Biochemistry · 2021Article
- Comparison of the specificity of rheumatoid factor detected by latex fixation with that of regulatory rheumatoid factor.Journal of clinical laboratory analysis · 2020Article
- Solid Lipid Microparticles for Oral Delivery of Catalase: Focus on the Protein Structural Integrity and Gastric Protection.Molecular pharmaceutics · 2020Article
- Ge on Si waveguide mid-infrared absorption spectroscopy of proteins and their aggregates.Biomedical optics express · 2020Article
- Observation of high-temperature macromolecular confinement in lyophilised protein formulations using terahertz spectroscopy.International journal of pharmaceutics: X · 2019Article
- Terahertz Spectroscopy: An Investigation of the Structural Dynamics of Freeze-Dried Poly Lactic-co-glycolic Acid Microspheres.Pharmaceutics · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The long-term stability of protein therapeutics in the solid-state depends on the preservation of native structure during lyophilization and in the lyophilized powder. Proteins can reversibly or irreversibly unfold upon lyophilization, acquiring conformations susceptible to degradation during storage. Therefore, characterizing proteins in the dried state is crucial for the design of safe and efficacious formulations. This review summarizes the basic principles and applications of the analytical techniques that are commonly used to characterize protein structure, dynamics and conformation in lyophilized solids. The review also discusses the applications of recently developed mass spectrometry based methods (solid-state hydrogen deuterium exchange mass spectrometry (ssHDX-MS) and solid-state photolytic labeling mass spectrometry (ssPL-MS)) and their ability to study proteins in the solid-state at high resolution.
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Registered trials
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