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Targeted Inactivation of Dipeptidyl Peptidase 9 Enzymatic Activity Causes Mouse Neonate Lethality
TLDR
The first gene knock-in mouse with a serine to alanine point mutation at the DPP9 active site (S729A) is made, suggesting that DPP 9 enzymatic activity is essential for early neonatal survival in mice.
The conserved N-terminal helix of acylpeptide hydrolase from archaeon Aeropyrum pernix K1 is important for its hyperthermophilic activity.
TLDR
The results suggest that the N-terminal helix is likely to play an important role for stabilizing all other enzymes in this family of enzymes, including acylpeptide hydrolases from hyperthermophilic archaeon Aeropyrum pernix K1.
Dipeptidyl peptidase 9 subcellular localization and a role in cell adhesion involving focal adhesion kinase and paxillin.
TLDR
It is shown that while some DPP9 is associated with mitochondria, the strongest co-localization was with microtubules, and mechanistic insights into the regulatory role of D PP9 in cell movement are provided, and may thus implicate DPP 9 in tissue and tumor growth and metastasis.
A Novel Purification Procedure for Active Recombinant Human DPP4 and the Inability of DPP4 to Bind SARS-CoV-2
TLDR
A procedure for high purity high yield soluble human DPP4 was achieved and used to show that, unlike MERS, SARS-CoV-2 does not bind human D PP4.
A rare variant in human fibroblast activation protein associated with ER stress, loss of enzymatic function and loss of cell surface localisation.
TLDR
Data on the first loss of function human FAP gene variant indicates that although the protein is vulnerable to an amino acid substitution in the β-propeller domain, inactive, unfolded FAP can be tolerated by cells.
Advances in Understanding the Expression and Function of Dipeptidyl Peptidase 8 and 9
DPP8 and DPP9 are recently identified members of the dipeptidyl peptidase IV (DPPIV) enzyme family, which is characterized by the rare ability to cleave a post-proline bond two residues from the
Regulation of dipeptidyl peptidase 8 and 9 expression in activated lymphocytes and injured liver.
TLDR
These expression patterns point to biological roles for DPP8 and DPP9 in lymphocyte activation and apoptosis and in hepatocytes during liver disease pathogenesis.
Chapter 5:Targeting Dipeptidyl Peptidase-4 (DPP-4) and Fibroblast Activation Protein (FAP) for Diabetes and Cancer Therapy
TLDR
An overall understanding of DPP-4 and FAP structure–function relationships, distribution, and enzymatic and extra-enzymatic biological roles provides an insight into their therapeutic usefulness as disease targets.
A Novel Purification Procedure for Active Recombinant Human DPP4 and the Inability of DPP4 to Bind SARS-CoV-2
Proteases catalyse irreversible posttranslational modifications that often alter a biological function of the substrate. The protease dipeptidyl peptidase 4 (DPP4) is a pharmacological target in type
A Novel Purification Procedure for Active Recombinant Human DPP4 and the Inability of DPP4 to Bind SARS-CoV-2
TLDR
A procedure for high purity high yield soluble human DPP4 was achieved and used to show that, unlike MERS, SARS-CoV-2 does not bind human D PP4.
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