ArticleJournal of pharmaceutical sciences2005
Lipid binding region (2303-2332) is involved in aggregation of recombinant human FVIII (rFVIII).
Article in Journal of pharmaceutical sciences, 2005. 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
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
15 citing papers in PubMed, 23 citations in OpenAlex.
- Tolerogenic form of Factor VIII to prevent inhibitor development in the treatment of Hemophilia A.Journal of thrombosis and haemostasis : JTH · 2021Article
- Rational design of a nanoparticle platform for oral prophylactic immunotherapy to prevent immunogenicity of therapeutic proteins.Scientific reports · 2021Article
- How Full-Length FVIII Benefits from Its Heterogeneity - Insights into the Role of the B-Domain.Pharmaceutical research · 2019Article
- Intravenous administration of Factor VIII-O-Phospho-L-Serine (OPLS) complex reduces immunogenicity and preserves pharmacokinetics of the therapeutic protein.European journal of pharmaceutical sciences : official journal of the European Federation for Pharmaceutical Sciences · 2015Article
- Native-like aggregates of factor VIII are immunogenic in von Willebrand factor deficient and hemophilia a mice.Journal of pharmaceutical sciences · 2012Article
- Phosphatidylserine reduces immune response against human recombinant Factor VIII in Hemophilia A mice by regulation of dendritic cell function.Clinical immunology (Orlando, Fla.) · 2011Article
- Phosphatidylinositol containing lipidic particles reduces immunogenicity and catabolism of factor VIII in hemophilia a mice.The AAPS journal · 2010Article
- Delivery of therapeutic proteins.Journal of pharmaceutical sciences · 2010Review
- Role of glycosylation in conformational stability, activity, macromolecular interaction and immunogenicity of recombinant human factor VIII.The AAPS journal · 2009Article
- Phosphatidylserine containing liposomes reduce immunogenicity of recombinant human factor VIII (rFVIII) in a murine model of hemophilia A.Journal of pharmaceutical sciences · 2008Article
- Development and characterization of lipidic cochleate containing recombinant factor VIII.Biochimica et biophysica acta · 2007Article
- O-phospho-L-serine, multi-functional excipient for B domain deleted recombinant factor VIII.The AAPS journal · 2007Article
- Interaction of dicaproyl phosphatidylserine with recombinant factor VIII and its impact on immunogenicity.The AAPS journal · 2006Article
- Influence of aggregation on immunogenicity of recombinant human Factor VIII in hemophilia A mice.Journal of pharmaceutical sciences · 2006Article
- Aggregation kinetics of recombinant human FVIII (rFVIII).Journal of pharmaceutical sciences · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Factor VIII (FVIII) is a multi-domain protein that is important in the clotting cascade. Its deficiency causes Hemophilia A, a bleeding disorder. The unfolding of protein domains can lead to physical instability such as aggregation, and hinder their use in replacement therapy. It has been shown that the aggregation of rFVIIII is initiated by small fluctuations in the protein's tertiary structure (Grillo et al., 2001, Biochemistry 40:586-595). We have investigated the domain(s) involved in the initiation of aggregation using circular dichroism (CD), size exclusion chromatography (SEC), fluorescence anisotropy, domain specific antibody binding, and clotting activity studies. The studies indicated that aggregation may be initiated as a result of conformational change in the C2 domain encompassing the lipid-binding region (2303-2332). The presence of O-phospho-L-Serine (OPLS), which binds to the lipid-binding region of FVIII, prevented aggregation of the protein.
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.