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ADAM9 + H2O
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54% cleavage
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aggrecan + H2O
aggrecan fragments
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the HtrA1-specific cleavage site is VQTV3562357TWPD within the interglobular domain of aggrecan
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alpha-tubulin + H2O
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alpha2-macroglobulin + H2O
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55% cleavage
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beta-tubulin + H2O
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biglycan + H2O
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substrate of isoforms HTRA1 and HTRA3
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bone morphogenetic protein + H2O
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substrate of isoform HTRA1
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chloride intracellular channel protein 1 + H2O
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51% cleavage
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clusterin + H2O
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50% cleavage
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decorin + H2O
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substrate of isoforms HTRA1 and HTRA3
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decorin + H2O
decorin peptide fragments
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the small leucine-rich proteoglycan is highly expressed in bone and regulates type I collagen fibril assembly
generation of fragments ranging from 150 to 75 kDa
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E-cadherin + H2O
85 kDa N-terminal fragment + 40 kDa C-terminal fragment
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selective substrate
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E-cadherin + H2O
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Faa1p + H2O
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direct interaction of Faa1p with the Omi/HtrA protease orthologue Ynm3p alters lipid homeostasis, Ynm3p modulates fatty acid metabolism and gene regulation through negative regulation of ACSL activity, overview
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fascin + H2O
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40% cleavage
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fibromodulin + H2O
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90% cleavage
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fibronectin + H2O
fibronectin peptide fragments
filamentous haemagglutinin precursor + H2O
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DegP contributes to degrading the filamentous haemagglutinin precursor when it is blocked intracellularly
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FkpA + H2O
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periplasmic peptidyl-prolyl cistrans isomerase, chaperone
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gamma-tubulin + H2O
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HCLS1-associated X1 + H2O
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substrate of isoform HTRA2
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insulin beta-chain + H2O
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insulin growth factor-binding protein 5 + H2O
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substrate of isoform HTRA1
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LamB + H2O
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DegP functions as a geniune chaperone
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MalE + H2O
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periplasmic maltose-binding protein
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matrix Gla protein + H2O
processed matrix Gla protein + 12 kDa peptide
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the protein substrate is present in cartilage, bone, and arteries
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OmpA + H2O
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outer membrane porin protein
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OmpC + H2O
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outer membrane porin protein
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OmpF + H2O
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outer membrane porin protein
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OmpW + H2O
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outer membrane porin protein
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OmpX + H2O
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outer membrane porin protein
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outer membrane protein + H2O
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outer membrane protein A + H2O
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in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone
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outer membrane protein C + H2O
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in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone
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outer membrane protein F + H2O
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in contrast to misfolded model substrates, which are degraded within a few min, the co-purified outer-membrane proteins are stable. Even in the presence of externally applied proteases, the bound outer-membrane proteins are almost entirely resistant to proteolytic degradation. DegP functions as a geniune chaperone
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reaction centre protein D1 + H2O
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reaction centre protein D2 + H2O
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talin-1 + H2O
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21% cleavage
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transforming growth factor-beta + H2O
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substrate of isoform HTRA1
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tuberous sclerosis complex 2 protein + H2O
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specific substrate for HtrA1 which is cleaved both in vitro and in vivo
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Vitronectin + H2O
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54% cleavage
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additional information
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Fibronectin + H2O
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selective substrate
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Fibronectin + H2O
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substrate of isoform HTRA1
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fibronectin + H2O
fibronectin peptide fragments
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HtrA is involved in cartilage catabolism
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fibronectin + H2O
fibronectin peptide fragments
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a major noncollagenous component of mineralized bone matrix
generation of fragments ranging from 200 to 150 kDa
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Protein + H2O
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reaction centre protein D1 + H2O
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substrate of isoform DEG1
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reaction centre protein D1 + H2O
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substrate of isoform DEG1
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reaction centre protein D2 + H2O
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substrate of isoforms DEG1, DEG5, DEG7 and DEG8
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reaction centre protein D2 + H2O
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substrate of isoforms DEG1, DEG5, DEG7 and DEG8
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additional information
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involved in the degradation of damaged proteins
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additional information
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the enzyme plays a role in the Burkholderia cenocepacia stress response, HtrABCAL2829 is required for growth of Burkholderia cenocepacia upon exposure to osmotic stress by NaCl or KCl, and thermal stress at 44°C
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additional information
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heat shock serine protease that degrades misfolded proteins at high temperatures
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins, enzyme is indispensable for bacterial survival at elevated temperatures
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additional information
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involved in the degradation of damaged proteins, enzyme is indispensable for bacterial survival at temperatures above 42°C
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additional information
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involved in the degradation of damaged proteins, enzyme is indispensable for bacterial survival at temperatures above 42°C
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additional information
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involved in the degradation of damaged proteins, participate in removal of aggregated proteins
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additional information
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involved in the degradation of damaged proteins, switches from chaperone to protease function in a temperature-dependent manner
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additional information
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involved in the degradation of denatured and unfolded proteins
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additional information
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involved in the degradation of misfolded proteins
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additional information
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involved in the degradation of unfolded proteins
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additional information
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allosteric activation of DegP by stress signals during bacterial protein quality control, regulation mechanism, pathway scheme, overview
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additional information
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HtrA inhibits the unfolded lysozyme substrate aggregation over the range of temperatures at 30-45°C, HtrA is able to bind to the denatured polypeptides and as a consequence limits their ability to form large aggregates, overview, HtrA may protect the bacterial cells from deleterious effects of heat shock not only by degrading the damaged proteins but by combination of the proteolytic and chaperoning activities
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additional information
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when unfolded proteins bind to CpxP, DegP efficiently degrades this protein complex
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additional information
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identification of beta-barrel outer membrane proteins, OMPs, as major natural substrates by photo-crosslinking using non-natural amino acid DiZPK, 3-(3-methyl-3H-diazirine-3-yl)-propaminocarbonyl-Nepsilon-L-lysine, as the photo-crosslinker. Isoform DegP primarily functions as a protease, at both low and high temperatures, to eliminate unfolded outer membrane proteins, with hardly any appreciable chaperone activity in cells. The toxic and cell membrane-damaging misfolded outer membrane proteins would accumulate in DegP-lacking cells cultured under heat shock conditions
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additional information
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the enzyme shows chaperone-like activity with substrate lysozyme, and protease activity. The PDZ domains are needed for DegQ chaperone activity. Up to six lysozyme substrates bind inside the DegQ dodecamer cage, binding of a well-ordered lysozyme to four DegQ protomers, overview
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additional information
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involved in the degradation of damaged proteins, involved in arthritis, cell growth, stress response, apoptosis and aging, possible tumor suppressor function
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additional information
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HtrA1 expression is regulated by cisplatin and paclitaxel, and upregulation results in catalytic activation of HtrA1, overview, HtrA1 influences tumor response to chemotherapy by modulating hemotherapy-induced cytotoxicity, HtrA1 in ovarian and gastric cancers may contribute to in vivo chemoresistance, overview
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additional information
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HtrA1 plays a role in arthritic disease, within the context of arthritis pathology HtrA1 contributes to cartilage degradation, overview
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additional information
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HTRA1 does not cleave CFH protein, complement component C3 and complement component C3b
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additional information
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HTRA1 interacts with presenilin 1 to cleave one product of gamma-secretase
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additional information
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role in extracellular proteolysis, proteolysis occurs during or after export to the cell surface, involved in the degradation of abnormal exported proteins
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additional information
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role in extracellular proteolysis, proteolysis occurs during or after export to the cell surface, involved in the degradation of abnormal exported proteins
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additional information
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HtrA is involved in the stress response of several important Gram-negative, as well as gram-positive, pathogens, HtrA is required for efficient Listeria monocytogenes biofilm formation at high temperatures
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additional information
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HtrA is involved in the stress response of several important Gram-negative, as well as gram-positive, pathogens, HtrA is required for efficient Listeria monocytogenes biofilm formation at high temperatures
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additional information
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involved in the degradation of damaged proteins, acts as protease, chaperone and regulator of apoptosis
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additional information
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HtrA is specific for mature mucosal mast cells
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additional information
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HtrA1 degrades specific matrix-associated proteins, HtrA1 inhibits mineral deposition by osteoblasts, the protease domain and the PDZ domain are essential for the inhibition of osteoblast mineralization by HtrA1, overview
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additional information
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HtrA is specific for mature mucosal mast cells
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additional information
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MucD negatively regulates alginate production on genetic level, MucD-deficient strain show temperature-dependent alginate production, while MucD-containing strains do not, which is independent of MucD proteolytic activity, overview
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additional information
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DegP degrades unfolded or misfolded, secreted, and accumulated inactive proteins and is important for cell survival, especially in the absence of DsbA
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additional information
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mutants are deficient in their ability to survive in mice or macrophages
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additional information
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the enzyme is involved in survival of the bacteria under heat shock stress conditions in vitro and in vivo, overview
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additional information
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involved in the degradation of damaged proteins
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additional information
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HtrA is essential for the maturation of cysteine protease streptococcal pyrogenic exotoxin B, SpeB, but is unable to directly process SpeB zymogen, proSpeB to the active form in vitro, thus playing an indirect role in the maturation, overview
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additional information
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involved in the degradation of damaged proteins
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additional information
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involved in the degradation of damaged proteins, chaperone and proteolytic activity
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additional information
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HtrA1 promotes posterior development in mRNA-injected Xenopus laevis embryos, e.g. induces secondary tail-like structures, expansion of mesoderm, and formation of ectopic neurons in an FGF-dependent manner, HtrA1 activates FGF/ERK signaling and the transcription of FGF genes by cleaving proteoglycans and releasing cell surface-bound FGF ligands, overview
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additional information
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deletion mutant is unable to grow at an elevated temperature and to survive within macrophages after phagocytosis
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