Results 31 to 40 of about 183,910 (327)

T-SP1: a novel serine protease-like protein predominantly expressed in testis [PDF]

open access: yes, 2008
Here, we describe a novel member in the group of membrane-anchored chymotrypsin (S1)-like serine proteases, namely testis serine protease 1 (T-SP1), as it is principally expressed in testis tissue.
Geissler, Claudia   +6 more
core   +1 more source

Host and bacterial proteases influence biofilm formation and virulence in a murine model of enterococcal catheter-associated urinary tract infection [PDF]

open access: yes, 2017
Urinary tract infections: targeting enzymes might help Identifying bacterial and host enzymes that support biofilm formation may help prevent urinary tract infections caused by catheters.
Caparon, Michael G   +5 more
core   +3 more sources

Serine Proteases of Malaria Parasite Plasmodium falciparum: Potential as Antimalarial Drug Targets

open access: yesInterdisciplinary Perspectives on Infectious Diseases, 2014
Malaria is a major global parasitic disease and a cause of enormous mortality and morbidity. Widespread drug resistance against currently available antimalarials warrants the identification of novel drug targets and development of new drugs.
Asrar Alam
doaj   +1 more source

Leucoagaricus gongylophorus uses leaf-cutting ants to vector proteolytic enzymes towards new plant substrate [PDF]

open access: yes, 2014
The mutualism between leaf-cutting ants and their fungal symbionts revolves around processing and inoculation of fresh leaf pulp in underground fungus gardens, mediated by ant fecal fluid deposited on the newly added plant substrate.
Boomsma, Jacobus Jan   +5 more
core   +1 more source

Cross genome comparisons of serine proteases in Arabidopsis and rice

open access: yesBMC Genomics, 2006
Background Serine proteases are one of the largest groups of proteolytic enzymes found across all kingdoms of life and are associated with several essential physiological pathways.
Sowdhamini R, Tripathi Lokesh P
doaj   +1 more source

Streptococcus pneumoniae serine protease HtrA, but not SFP or PrtA, is a major virulence factor in pneumonia. [PDF]

open access: yesPLoS ONE, 2013
Streptococcus (S.) pneumoniae is a common causative pathogen in pneumonia. Serine protease orthologs expressed by a variety of bacteria have been found of importance for virulence. Previous studies have identified two serine proteases in S.
Sacha F de Stoppelaar   +6 more
doaj   +1 more source

Differential in vitro and in vivo effect of barley cysteine and serine protease inhibitors on phytopathogenic microorganisms [PDF]

open access: yes, 2011
Protease inhibitors from plants have been involved in defence mechanisms against pests and pathogens. Phytocystatins and trypsin/α-amylase inhibitors are two of the best characterized protease inhibitor families in plants.
Cambra Marin, Ines   +5 more
core   +2 more sources

Serpin functions in host-pathogen interactions [PDF]

open access: yesPeerJ, 2018
Serpins are a broadly distributed superfamily of protease inhibitors that are present in all kingdoms of life. The acronym, serpin, is derived from their function as potent serine proteases inhibitors.
Jialing Bao   +5 more
doaj   +2 more sources

Serpin–4 Facilitates Baculovirus Infection by Inhibiting Melanization in Asian Corn Borer, Ostrinia furnacalis (Guenée)

open access: yesFrontiers in Immunology, 2022
Phenoloxidase (PO)–catalyzed melanization is a vital immune response in insects for defense against pathogen infection. This process is mediated by clip domain serine proteases and regulated by members of the serpin superfamily. We here revealed that the
Jiayue Ji   +6 more
doaj   +1 more source

Interdependence of kallikrein-related peptidases in proteolytic networks [PDF]

open access: yes, 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
Debela   +21 more
core   +1 more source

Home - About - Disclaimer - Privacy