Results 41 to 50 of about 103,544 (298)
The HtrA family of serine proteases [PDF]
Molecular Microbiology, 1997 HtrA, also known as DegP and probably identical to the Do protease, is a heat shock‐induced serine protease that is active in the periplasm of Escherichia coli. Homologues of HtrA have been described in a wide range of bacteria and in eukaryotes. Its chief role is to degrade misfolded proteins in the periplasm.
M J, Pallen, B W, Wren
openaire +2 more sources
Streptococcus pneumoniae serine protease HtrA, but not SFP or PrtA, is a major virulence factor in pneumonia. [PDF]
PLoS 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
Frontiers 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
Family C1 cysteine proteases: Biological diversity or redundancy? [PDF]
, 2003 Recent progress in the identification and partial characterization of novel genes encoding cysteine proteases of the papain family has considerably increased our knowledge of this family of enzymes.
M\ue9nard, Robert +3 more
core +1 more source
Ecotin-like serine peptidase inhibitor ISP1 of Leishmania major plays a role in flagellar pocket dynamics and promastigote differentiation [PDF]
, 2012 Leishmania ISPs are ecotin-like natural peptide inhibitors of trypsin-family serine peptidases, enzymes that are absent from the Leishmania genome. This led to the proposal that ISPs inhibit host serine peptidases and we have recently shown that ISP2 ...
Petr Volf +28 more
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Serpin functions in host-pathogen interactions [PDF]
PeerJ, 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
Serine Proteases of Parasitic Helminths
The Korean Journal of Parasitology, 2015 Serine proteases form one of the most important families of enzymes and perform significant functions in a broad range of biological processes, such as intra- and extracellular protein metabolism, digestion, blood coagulation, regulation of development, and fertilization.
Yang, Yong +6 more
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Characteristics of intracellular peptidase and proteinase activities from the mycelium of a cord-forming wood decay fungus Serpula lacrymans [PDF]
, 2001 Serpula lacrymans is a basidiomycete cord-forming wood decay fungus which reallocates nitrogen within an extensive perennial mycelial system in response to spatial discontinuities in external nutrient supply.
Burton, Kerry S. +2 more
core +1 more source
Serine proteases, serine protease inhibitors, and protease-activated receptors: Roles in synaptic function and behavior [PDF]
Brain Research, 2011 Serine proteases, serine protease inhibitors, and protease-activated receptors have been intensively investigated in the periphery and their roles in a wide range of processes-coagulation, inflammation, and digestion, for example-have been well characterized (see Coughlin, 2000; Macfarlane et al., 2001; Molinari et al., 2003; Wang et al., 2008; Di Cera,
Antoine G, Almonte, J David, Sweatt
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FEBS Letters, EarlyView.The Ile181Asn variant of human UDP‐xylose synthase (hUXS1), associated with a short‐stature genetic syndrome, has previously been reported as inactive. Our findings demonstrate that Ile181Asn‐hUXS1 retains catalytic activity similar to the wild‐type but exhibits reduced stability, a looser oligomeric state, and an increased tendency to precipitate ...
Tuo Li +2 more
wiley +1 more source