Results 1 to 10 of about 805,984 (229)
Extended plasma half-life of albumin-binding domain fused human IgA upon pH-dependent albumin engagement of human FcRn in vitro and in vivo [PDF]
Albumin has a serum half-life of 3 weeks in humans. This feature can be used to improve the pharmacokinetics of shorter-lived biologics. For instance, an albumin-binding domain (ABD) can be used to recruit albumin.
Simone Mester +7 more
doaj +7 more sources
Extended half-life recombinant FVIII products (EHL-rFVIIIs) have been engineered to improve the pharmacokinetic profile of FVIII, enabling better hemostatic protection with a reduced number of injections in persons with hemophilia. Previous studies showed several discrepancies in FVIII activity (FVIII:C) measurements for EHL-rFVIIIs comparing one-stage
Lancellotti, Stefano +4 more
openaire +3 more sources
A novel in vitro assay to predict neonatal Fc receptor-mediated human IgG half-life [PDF]
Immunoglobulin G (IgG) has an unusually long serum half-life in comparison to proteins of a similar size. It is well-known that this phenomenon is due to IgG's ability to bind the neonatal Fc receptor (FcRn) in a pH-dependent manner. FcRn binding properties can vary among IgGs, resulting in altered in vivo half-lives, and therefore it would be ...
Souders, Colby A +5 more
openaire +3 more sources
QSPR modelling ofin vitrodegradation half-life of acyl glucuronides
Acyl glucuronidation is an important Phase II biotransformation, which is an efficient detoxification mechanism for the metabolism of carboxylic acid group-containing drugs. However, the reactivity of acyl glucuronide (AG) metabolites associated with short half-lives may be an indication of idiosyncratic drug toxicity.The degradation half-lives of AGs ...
Gulcin Tugcu, Hande Sipahi
openaire +3 more sources
Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant. [PDF]
Polysome-associated c-myc mRNA is degraded relatively rapidly in cells and in an in vitro mRNA decay system containing extracts from cultured mammalian cells. Using this system, a competition/screening assay was devised to search for factors that bind to specific regions of polysome-associated c-myc mRNA and thereby alter its half-life.
P L, Bernstein +3 more
openaire +3 more sources
Excess proteolytic activity of matrix metalloproteinases (MMPs) contributes to the development of arthritis, cardiovascular diseases and cancer progression, implicating these enzymes as therapeutic targets. While many small molecule inhibitors of MMPs have been developed, clinical uses have been limited, in part by toxicity and off-target effects ...
Jyotica Batra +6 more
openaire +5 more sources
The increasing number of multidrug-resistant bacteria intensifies the need to develop new antimicrobial agents. Endolysins are bacteriophage-derived enzymes that degrade the bacterial cell wall and hold promise as a new class of highly specific and ...
Johan Seijsing +6 more
doaj +2 more sources
Fusion of a short peptide that binds immunoglobulin G to a recombinant protein substantially increases its plasma half-life in mice. [PDF]
We explore a strategy to substantially increase the half-life of recombinant proteins by genetic fusion to FcIII, a 13-mer IgG-Fc domain binding peptide (IgGBP) originally identified by DeLano and co-workers at Genentech [DeLano WL, et al. (2000) Science
Jonathan T Sockolosky +2 more
doaj +2 more sources
Alectinib, also known as Alecensa®, is prescribed for the therapeutic treatment of individuals diagnosed with metastatic non-small cell lung cancer (NSCLC) who have a specific genetic mutation referred to as anaplastic lymphoma kinase (ALK) positivity ...
Mohamed W. Attwa +3 more
doaj +1 more source
Selpercatinib (SLP; brand name Retevmo®) is a selective and potent RE arranged during transfection (RET) inhibitor. On 21 September 2022, the FDA granted regular approval to SLP (Retevmo, Eli Lilly, and Company).
Mohamed W. Attwa +4 more
doaj +1 more source

