l‐Asparaginase (a hydrolase converting l‐asparagine to l‐aspartic acid) was the first
enzyme to be used in clinical practice as an anticancer agent after its approval in 1978 as a …

L-asparaginases (EC 3.5. 1.1) are a family of enzymes that catalyze the hydrolysis of L-
asparagine to L-aspartic acid and ammonia. These proteins with different biochemical …

l-Asparaginase (EC 3.5. 1.1) was first used as a component of combination drug therapies to
treat acute lymphoblastic leukemia (ALL), a cancer of the blood and bone marrow, almost 50 …

NMR-assisted crystallography—the integrated application of solid-state NMR, X-ray
crystallography, and first-principles computational chemistry—holds significant promise for …

l-Asparaginases have remained an intriguing research topic since their discovery∼ 120
years ago, especially after their introduction in the 1960s as very efficient antileukemic …

The Protein Data Bank (PDB) includes a carefully curated treasury of experimentally derived
structural data on biological macromolecules and their various complexes. Such information …

Covalent attachment of therapeutic proteins to polyethylene glycol (PEG) is widely used for
the improvement of its pharmacokinetic and pharmacological properties, as well as the …

Multispecific biologics are an emerging class of drugs, in which antibodies and/or proteins
designed to bind pharmacological targets are covalently linked or expressed as fusion …

L-Asparaginases, divided into three structural Classes, catalyze the hydrolysis of L-
asparagine to L-aspartic acid and ammonia. The members of Class 3, ReAIV and ReAV …

The heterogeneous composition of vaccine formulations and the relatively low concentration
make the characterization of the protein antigens extremely challenging. Aluminum …