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Cleavage preference distinguishes the two-component NS2B-NS3 serine proteinases of Dengue and West Nile viruses.
TLDR
The authors' objectives were to define the substrate recognition pattern of the NS2B-NS3 protease of West Nile and Dengue virises and to represent a valuable biochemical resource and a solid foundation to support the design of selective substrates and synthetic inhibitors of flaviviral proteinases. Expand
Switching the Substrate Specificity of the Two-Component NS2B-NS3 Flavivirus Proteinase by Structure-Based Mutagenesis
TLDR
This work is the first instance of engineering a viral proteinase with switched cleavage preferences and should provide valuable data for the design of optimized substrates and substrate-based selective inhibitors of flaviviral proteinases. Expand
New Details of HCV NS3/4A Proteinase Functionality Revealed by a High-Throughput Cleavage Assay
TLDR
The analysis revealed that mutations do not interfere with polyprotein processing in over 5,000 HCV isolates indicating a pivotal role of NS3/4A proteolysis in the virus life cycle. Expand
High-Throughput Multiplexed Peptide-Centric Profiling Illustrates Both Substrate Cleavage Redundancy and Specificity in the MMP Family.
TLDR
This study employed a high-throughput multiplexed peptide-centric profiling technology involving the cleavage of 18,583 peptides by 18 proteinases from the main sub-groups of the MMP family, resulting in a roadmap for the subsequent MMP structural-functional studies and efficient substrate and inhibitor design. Expand
Electron microscopy of beef heart mitochondrial F1‐ATPase
TLDR
The quaternary structure of isolated and membrane‐bound F1‐ATPase (submitochondrial particles) has been studied by electron microscopy and showed that the frontal view of the molecule can be approximately characterized by mirror plane symmetry. Expand
The nucleotide binding site of F1‐ATPase which carries out uni‐site catalysis is one of the alternating active sites of the enzyme
TLDR
It follows from the results obtained that the modification of just one of the F1‐ATPase catalytic sites is sufficient to complete the inhibition of ATPase activity. Expand
The non-catalytic nucleotide-binding site of mitochondrial ATPase is localised on the alpha-subunit(s) of factor F1.
TLDR
The results obtained testify to the fact that the non-catalytic site of mitochondrial ATP ase located on the alpha-subunit(s) of factor F1 may participate in the mechanism of ATP hydrolysis by membrane-bound ATPase. Expand
A Multiplexed Protein Kinase Assay
TLDR
A novel protein kinase assay designed for high‐throughput detection of one or many kinases in a complex mixture is reported and it is demonstrated that enzyme mixtures can be screened for activity and selectivity of inhibition. Expand
Efficient transfer of information from hexitol nucleic acids to RNA during nonenzymatic oligomerization.
TLDR
It is found that HNAs support efficient information transfer in nonensymatic template-directed reactions and appear to be superior to the corresponding DNA heterosequences in facilitating synthesis of complementary oligonucleotides from nucleoside-5'-phosphoro-2-methyl imidazolides. Expand
High-Resolution Analysis and Functional Mapping of Cleavage Sites and Substrate Proteins of Furin in the Human Proteome
TLDR
An approach for proteinase target identification that combines an in silico discovery pipeline with highly multiplexed proteinase activity assays is devised and suggests an important role of furin in development, including axonal guidance, cardiogenesis, and maintenance of stem cell pluripotency. Expand
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