Interdependence of kallikrein-related peptidases in proteolytic networks [PDF]
, 2010 Human kallikrein-related peptidases (KLKs) are 15 homologous serine proteases involved in several (patho)physiological processes, including cancer. Secreted as precursors, they are activated upon proteolytic release of a short propeptide. We searched for
Burkhart, Julia M. +27 more
core +1 more source
CLN6 deficiency causes selective changes in the lysosomal protein composition
PROTEOMICS, Volume 21, Issue 19, October 2021., 2021 Abstract Neuronal ceroid lipofuscinoses (NCLs) collectively account for the highest prevalence of inherited neurodegenerative diseases in childhood. This disease group is classified by the deposition of similar autofluorescence storage material in lysosomes that is accompanied by seizures, blindness and premature mortality in later disease stages ...
Andreas Tuermer +6 more
wiley +1 more source
The purification and characterisation of novel dipeptidyl peptidase IV-like activity from bovine serum [PDF]
, 2004 The discovery of a potentially novel proline-specific peptidase from bovine serum is presented which is capable of cleaving the dipeptidyl peptidase IV (DPIV) substrate Gly-Pro-MCA.
Buckley, Seamus J. +3 more
core +1 more source
Angiotensin‐converting enzyme open for business: structural insights into the subdomain dynamics
The FEBS Journal, Volume 288, Issue 7, Page 2238-2256, April 2021., 2021 Angiotensin‐1‐converting enzyme (ACE) has broad substrate specificity and physiological functions. The first open structure of ACE N‐domain (nACE) presented here shows similar domain opening as ACE2 (close ACE homologue) that allows substrates to bind, and suggests extended binding site for endopeptidase activity.
Gyles E. Cozier +3 more
wiley +1 more source
Peptidases affecting recombinant protein production by Streptomyces lividans [PDF]
, 2001 The influence of peptidases on human interleukin-3 (rhIL-3) production by a recombinant Streptomyces lividans strain was investigated. The bacterium produced several general peptidases and tripeptidyl peptidases compromising the authenticity of rhIL-3 ...
Soon-Il Yun +6 more
core +1 more source
, 2009 Many proteins undergo important post-translational proteolytic processing to remove targeting signals and activation peptides, and most proteins undergo proteolytic inactivation and catabolism.
Neil D. Rawlings, Alan J. Barrett
core +2 more sources
Solvent and thermal stability, and pH kinetics, of proline-specific dipeptidyl peptidase IV-like enzyme from bovine serum [PDF]
, 2007 Proline-specific dipeptidyl peptidase-like (DPP IV; EC 3.4.14.5) activity in bovine serum has attracted little attention despite its ready availability and the paucity of useful proline-cleaving enzymes.
Ruth, Deborah M. +4 more
core +1 more source
Natural, engineered and synthetic inhibitors of kallikrein-related peptidases [PDF]
, 2012 There is a rapidly growing appreciation of the important physiological roles played by kallikreins and kallikrein-related peptidases (KLKs). Recent studies have revealed that these enzymes control key events in processes as diverse as inflammation and ...
Joakim E. Swedberg +5 more
core +1 more source
The crude skin secretion of the pepper frog Leptodactylus labyrinthicus is rich in metallo and serine peptidases [PDF]
, 2014 Peptidases are ubiquitous enzymes involved in diverse biological processes. Fragments from bioactive peptides have been found in skin secretions from frogs, and their presence suggests processing by peptidases.
Mariana S Castro +15 more
core +1 more source
Seprase: An overview of an important matrix serine protease [PDF]
, 2008 Seprase or Fibroblast Activation Protein (FAP) is an integral membrane serine peptidase, which has been shown to have gelatinase activity. Seprase has a dual function in tumour progression.
O\u27Brien, Pamela +3 more
core +1 more source