Research graph
References from Function, molecular mechanisms, and therapeutic potential of bacterial HtrA proteins: An evolving view. Local targets link to admitted publications; unresolved targets remain external evidence.
10.1128/jb.171.3.1574-1584.1989
10.1128/jb.171.3.1574-1584.1989 · External reference
10.1038/nrm3065
10.1038/nrm3065 · External reference
10.1038/416455a
10.1038/416455a · External reference
10.1038/nsmb.1840
10.1038/nsmb.1840 · External reference
Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease
10.1016/s0092-8674(04)00454-4 · 2004 · External reference
10.1016/j.str.2013.12.003
10.1016/j.str.2013.12.003 · External reference
10.1016/s0092-8674(03)00203-4
10.1016/s0092-8674(03)00203-4 · External reference
The structural basis of mode of activation and functional diversity: a case study with HtrA family of serine proteases
10.1016/j.abb.2011.10.007 · 2011 · External reference
10.1517/14728222.2010.487867
10.1517/14728222.2010.487867 · External reference
HtrA protease family as therapeutic targets
10.2174/1381612811319060003 · 2013 · External reference
DegP functions as a critical protease for bacterial acid resistance
10.1111/febs.14627 · 2018 · External reference
Conserved DegP protease in gram-positive bacteria is essential for thermal and oxidative tolerance and full virulence in Streptococcus pyogenes
10.1128/iai.69.9.5538-5545.2001 · 2001 · External reference
Structural analysis of DegS, a stress sensor of the bacterial periplasm
10.1016/j.febslet.2004.06.012 · 2004 · External reference
10.1016/j.str.2011.06.013
10.1016/j.str.2011.06.013 · External reference
10.1074/jbc.m111.243832
10.1074/jbc.m111.243832 · External reference
Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa
2021 · External reference
New Insights into Beta-Lactam Resistance of Streptococcus pneumoniae: Serine Protease HtrA Degrades Altered Penicillin-Binding Protein 2x
10.3390/microorganisms9081685 · 2021 · External reference
10.1038/embor.2010.114
10.1038/embor.2010.114 · External reference
Chemical validation of DegS as a target for the development of antibiotics with a novel mode of action
10.1002/cmdc.201900193 · 2019 · External reference
10.1016/j.ejmech.2021.113692
10.1016/j.ejmech.2021.113692 · External reference
Bacterial serine protease HtrA as a promising new target for antimicrobial therapy?
10.1186/s12964-017-0162-5 · 2017 · External reference
10.1038/nrd3846
10.1038/nrd3846 · External reference
Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response
10.1007/s00018-012-1076-4 · 2013 · External reference
The HtrA family of proteases: implications for protein composition and cell fate
10.1016/s1097-2765(02)00658-5 · 2002 · External reference
Functional analysis and cryo-electron microscopy of Campylobacter jejuni serine protease HtrA
10.1080/19490976.2020.1810532 · 2020 · External reference
Extracellular HtrA serine proteases: an emerging new strategy in bacterial pathogenesis
10.1111/cmi.12845 · 2018 · External reference
PDZ scape: a comprehensive PDZ-protein database
10.1186/s12859-018-2156-8 · 2018 · External reference
10.1038/nrg1324
10.1038/nrg1324 · External reference
10.5483/bmbrep.2005.38.3.266
10.5483/bmbrep.2005.38.3.266 · External reference
Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli
10.1016/j.resmic.2009.07.012 · 2009 · External reference
The LA loop as an important regulatory element of the HtrA (DegP) protease from Escherichia coli: structural and functional studies
10.1074/jbc.m113.532895 · 2014 · External reference
Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro
10.1046/j.1365-2958.1996.1231493.x · 1996 · External reference
10.1046/j.1365-2958.1997.5601928.x
10.1046/j.1365-2958.1997.5601928.x · External reference
HtrA-mediated E-cadherin cleavage is limited to DegP and DegQ homologs expressed by gram-negative pathogens
10.1186/s12964-016-0153-y · 2016 · External reference
10.1073/pnas.2109732118
10.1073/pnas.2109732118 · External reference
10.1111/j.1365-2958.2010.07145.x
10.1111/j.1365-2958.2010.07145.x · External reference
Shigella flexneri DegP facilitates IcsA surface expression and is required for efficient intercellular spread
10.1128/iai.70.11.6355-6364.2002 · 2002 · External reference
10.1016/j.chembiol.2018.10.014
10.1016/j.chembiol.2018.10.014 · External reference
Pseudomonas aeruginosa MucD protease mediates keratitis by inhibiting neutrophil recruitment and promoting bacterial survival
10.1167/iovs.13-13151 · 2014 · External reference
Identification of a periplasmic AlgK–AlgX–MucD multiprotein complex in Pseudomonas aeruginosa involved in biosynthesis and regulation of alginate
10.1007/s00253-011-3430-0 · 2012 · External reference
10.1016/j.csbj.2021.04.045 · Admitted local publication
The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease
10.1101/gad.9.4.387 · 1995 · External reference
CpxR/CpxA controls scsABCD transcription to counteract copper and oxidative stress in Salmonella enterica serovar Typhimurium
10.1128/jb.00126-18 · 2018 · External reference
10.1128/jb.187.19.6622-6630.2005
10.1128/jb.187.19.6622-6630.2005 · External reference
The lipoprotein NlpE is a Cpx sensor that serves as a sentinel for protein sorting and folding defects in the Escherichia coli envelope
10.1128/jb.00611-18 · 2019 · External reference
Role of the two-component regulator CpxAR in the virulence of Salmonella enterica serotype Typhimurium
10.1128/iai.72.8.4654-4661.2004 · 2004 · External reference
10.1073/pnas.0508936102
10.1073/pnas.0508936102 · External reference
Cage-like polyhedrons of DegQ from Cytophaga hutchinsonii show stable proteolytic activity and strong chaperone activity
10.1016/j.bej.2020.107585 · 2020 · External reference
Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease
10.1128/jb.178.4.1146-1153.1996 · 1996 · External reference
Unresolved reference
External reference
Control of the alternative sigma factor σE in Escherichia coli
10.1016/j.mib.2004.02.010 · 2004 · External reference
Molecular basis of the lipid-induced MucA-MucB dissociation in Pseudomonas aeruginosa
2020 · External reference
10.3390/ijms22083900
10.3390/ijms22083900 · External reference
Modulation of the Escherichia coli sigmaE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins
10.1046/j.1365-2958.1997.3601713.x · 1997 · External reference
The serine protease HtrA plays a key role in heat-induced dispersal of pneumococcal biofilms
10.1038/s41598-020-80233-0 · 2020 · External reference
10.1093/jac/dkab260
10.1093/jac/dkab260 · External reference
10.1016/j.celrep.2018.12.063
10.1016/j.celrep.2018.12.063 · External reference
Distinct contribution of the HtrA protease and PDZ domains to its function in stress resilience and virulence of Bacillus anthracis
10.3389/fmicb.2019.00255 · 2019 · External reference
Extracellular bacterial proteases in chronic wounds: a potential therapeutic target?
10.1089/wound.2015.0673 · 2016 · External reference
HtrA is a major virulence determinant of Bacillus anthracis
10.1111/j.1365-2958.2011.07790.x · 2011 · External reference
H. pylori isolates with amino acid sequence polymorphisms as presence of both HtrA-L171 & CagL-Y58/E59 increase the risk of gastric cancer
2019 · External reference
Invasive Pathobionts Contribute to Colon Cancer Initiation by Counterbalancing Epithelial Antimicrobial Responses. Cell Mol
2021 · External reference
Campylobacter jejuni enters gut epithelial cells and impairs intestinal barrier function through cleavage of occludin by serine protease HtrA
10.1186/s13099-019-0283-z · 2019 · External reference
10.3389/fcimb.2020.590186
10.3389/fcimb.2020.590186 · External reference
10.1007/s00018-008-8281-1
10.1007/s00018-008-8281-1 · External reference
Importance of two PDZ domains for the proteolytic and chaperone activities of Helicobacter pylori serine protease HtrA
10.1111/cmi.13299 · 2021 · External reference
10.1038/nrn1517
10.1038/nrn1517 · External reference
10.1006/jmbi.1999.3320
10.1006/jmbi.1999.3320 · External reference
10.1073/pnas.1204791109
10.1073/pnas.1204791109 · External reference
10.1002/cbic.200900616
10.1002/cbic.200900616 · External reference
Discovery of novel peptidomimetic boronate ClpP inhibitors with noncanonical enzyme mechanism as potent virulence blockers in vitro and in vivo
10.1021/acs.jmedchem.9b01746 · 2020 · External reference
Inhibiting Mycobacterium tuberculosis ClpP1P2 by addressing the equatorial handle domain of ClpP1 subunit
2019 · External reference
HtrA-family proteases of bacterial pathogens: pros and cons for their therapeutic use
10.1016/j.cmi.2020.12.017 · 2021 · External reference
Fragment-based de novo design reveals a small-molecule inhibitor of Helicobacter pylori HtrA
10.1002/ange.201504035 · 2015 · External reference
A novel FRET peptide assay reveals efficient Helicobacter pylori HtrA inhibition through zinc and copper binding
10.1038/s41598-020-67578-2 · 2020 · External reference
Recent advances in FRET-Based biosensors for biomedical applications
10.1016/j.ab.2021.114323 · 2021 · External reference
10.1016/j.cell.2011.02.024
10.1016/j.cell.2011.02.024 · External reference
10.1038/nature07004
10.1038/nature07004 · External reference