Maintaining integrity under stress: Envelope stress response regulation of pathogenesis in gram-negative bacteria

The Bacterial Cell EnvelopePreprint

Silhavy, T. J., Kahne, D. E., & Walker, S. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000414 · Cited by 3,834 · see citing works

Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia

Govan, J. R. W., & Deretic, V. P. (1996) · Microbiological Reviews · doi:10.1128/mr.60.3.539-574.1996 · Cited by 1,671 · see citing works

Nutritional immunity: transition metals at the pathogen–host interface

Hood, M. I., & Skaar, E. P. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2836 · Cited by 1,535 · see citing works

<i>Pseudomonas aeruginosa</i> : new insights into pathogenesis and host defenses

Gellatly, S. L., & Hancock, R. E. W. (2013) · Pathogens and Disease · doi:10.1111/2049-632x.12033 · Cited by 1,295 · see citing works

A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens.

McDaniel, T. K., Jarvis, K. G., Donnenberg, M. S., & Kaper, J. B. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1664 · Cited by 1,247 · see citing works

Pretreatment of Mice with Streptomycin Provides a <i>Salmonella enterica</i> Serovar Typhimurium Colitis Model That Allows Analysis of Both Pathogen and Host

Barthel, M., Hapfelmeier, S., Quintanilla-Martínez, L., Kremer, M., Rohde, M., Hogardt, M., Pfeffer, K., Rüssmann, H., & Hardt, W.-D. (2003) · Infection and Immunity · doi:10.1128/iai.71.5.2839-2858.2003 · Cited by 1,020 · see citing works

Identification of a protein required for disulfide bond formation in vivo.

Bardwell, J., McGovern, K., & Beckwith, J. (1991) · Cell · doi:10.1016/0092-8674(91)90532-4 · Cited by 961 · see citing works

Quorum-sensing regulators control virulence gene expression in Vibrio cholerae

Zhu, J., Miller, M. B., Vance, R. E., Dziejman, M., Bassler, B. L., & Mekalanos, J. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052694299 · Cited by 849 · see citing works

Unravelling the biology of macrophage infection by gene expression profiling of intracellular <i>Salmonella enterica</i>

Eriksson, S., Lucchini, S., Thompson, A., Rhen, M., & Hinton, J. C. D. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03313.x · Cited by 846 · see citing works

A Temperature-Dependent Switch from Chaperone to Protease in a Widely Conserved Heat Shock Protein

Spiess, C., Beil, A., & Ehrmann, M. (1999) · Cell · doi:10.1016/s0092-8674(00)80743-6 · Cited by 768 · see citing works

Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly

Voulhoux, R., Bos, M. P., Geurtsen, J., Mols, M., & Tommassen, J. (2003) · Science · doi:10.1126/science.1078973 · Cited by 742 · see citing works

ADP-ribosylation of membrane proteins catalyzed by cholera toxin: basis of the activation of adenylate cyclase.

Gill, D. M., & Meren, R. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.7.3050 · Cited by 739 · see citing works

LysM, a widely distributed protein motif for binding to (peptido)glycans

Buist, G., Steen, A., Kok, J., & Kuipers, O. P. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06211.x · Cited by 628 · see citing works

Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design

Li, J., Koh, J.-J., Liu, S., Lakshminarayanan, R., Verma, C. S., & Beuerman, R. W. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00073 · Cited by 613 · see citing works

Covalent lipoprotein from the outer membrane of Escherichia coli

Braun, V. (1975) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(75)90013-1 · Cited by 580 · see citing works

The twin-arginine translocation (Tat) protein export pathway

Palmer, T., & Berks, B. C. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2814 · Cited by 536 · see citing works

Conserved and Variable Functions of the σE Stress Response in Related Genomes

Rhodius, V. A., Suh, W.-C., Nonaka, G., West, J. T., & Gross, C. A. (2005) · PLoS Biology · doi:10.1371/journal.pbio.0040002 · Cited by 521 · see citing works

A cloned pathogenicity island from enteropathogenic Escherichia coli confers the attaching and effacing phenotype on E. coli K‐12

McDaniel, T. K., & Kaper, J. B. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.2311591.x · Cited by 516 · see citing works

OMP Peptide Signals Initiate the Envelope-Stress Response by Activating DegS Protease via Relief of Inhibition Mediated by Its PDZ Domain

Walsh, N. P., Alba, B. M., Bose, B., Gross, C. A., & Sauer, R. T. (2003) · Cell · doi:10.1016/s0092-8674(03)00203-4 · Cited by 508 · see citing works

Citrobacter rodentium: infection, inflammation and the microbiota

Collins, J. W., Keeney, K. M., Crepin, V. F., Rathinam, V. A. K., Fitzgerald, K. A., Finlay, B. B., & Frankel, G. M. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3315 · Cited by 508 · see citing works

Mucoid conversion of Pseudomonas aeruginos by hydrogen peroxide: a mechanism for virulence activation in the cystic fibrosis lung

Mathee, K., Ciofu, O., Sternberg, C., Lindum, P. W., Campbell-Tofte, J., Jensen, P., Johnsen, A. H., Givskov, M., Ohman, D. E., Molin, S., et al. (1999) · Microbiology · doi:10.1099/13500872-145-6-1349 · Cited by 483 · see citing works

Biogenesis of the Gram-Negative Bacterial Outer Membrane

Bos, M. P., Robert, V., & Tommassen, J. (2007) · Annual Review of Microbiology · doi:10.1146/annurev.micro.61.080706.093245 · Cited by 473 · see citing works

ClpXP, an ATP-powered unfolding and protein-degradation machine

Baker, T. A., & Sauer, R. T. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.007 · Cited by 468 · see citing works

Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in <i>Escherichia coli</i>

Sklar, J. G., Wu, T., Kahne, D., & Silhavy, T. J. (2007) · Genes &amp; Development · doi:10.1101/gad.1581007 · Cited by 459 · see citing works

Advances in understanding bacterial outer-membrane biogenesis

Ruiz, N., Kahne, D. E., & Silhavy, T. J. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1322 · Cited by 458 · see citing works

Salmonella SPI-2 Type III Secretion System Effectors: Molecular Mechanisms And Physiological Consequences

Jennings, E. R., Thurston, T. L. M., & Holden, D. W. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.07.009 · Cited by 455 · see citing works

Regulatory cascade controls virulence in Vibrio cholerae.

DiRita, V. J., Parsot, C., Jander, G., & Mekalanos, J. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.12.5403 · Cited by 450 · see citing works

Protein export through the bacterial Sec pathway

Tsirigotaki, A., De Geyter, J., Šoštaric´, N., Economou, A., & Karamanou, S. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.161 · Cited by 447 · see citing works

Pseudomonas aeruginosa PAO1 Kills Caenorhabditis elegans by Cyanide Poisoning

Gallagher, L. A., & Manoil, C. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.21.6207-6214.2001 · Cited by 446 · see citing works

The Yersinia Ysc–Yop 'Type III' weaponry

Cornelis, G. R. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm932 · Cited by 426 · see citing works

Surface sensing and adhesion of Escherichia coli controlled by the Cpx-signaling pathway

Otto, K., & Silhavy, T. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042521699 · Cited by 402 · see citing works

Cholera

Clemens, J. D., Nair, G. B., Ahmed, T., Qadri, F., & Holmgren, J. R. (2017) · The Lancet · doi:10.1016/s0140-6736(17)30559-7 · Cited by 399 · see citing works

Characterization of the Escherichia coliςE Regulon

Dartigalongue, C., Missiakas, D. M., & Raina, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100464200 · Cited by 394 · see citing works

The RNA chaperone Hfq is essential for the virulence of Salmonella typhimurium

Sittka, A., Pfeiffer, V., Tedin, K., & Vogel, J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05489.x · Cited by 393 · see citing works

The Per regulon of enteropathogenic Escherichia coli : identification of a regulatory cascade and a novel transcriptional activator, the locus of enterocyte effacement (LEE)‐encoded regulator (Ler)

Mellies, J. L., Elliott, S. J., Sperandio, V., Donnenberg, M. S., & Kaper, J. B. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01473.x · Cited by 390 · see citing works

Biofilms, flagella, and mechanosensing of surfaces by bacteria

Belas, R. (2014) · Trends in Microbiology · doi:10.1016/j.tim.2014.05.002 · Cited by 388 · see citing works

Structure and Function of TolC: The Bacterial Exit Duct for Proteins and Drugs

Koronakis, V. E., Eswaran, J., & Hughes, C. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074104 · Cited by 362 · see citing works

σ E ‐dependent small RNAs of Salmonella respond to membrane stress by accelerating global omp mRNA decay

Papenfort, K., Pfeiffer, V., Mika, F., Lucchini, S., Hinton, J. C. D., & Vogel, J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05524.x · Cited by 359 · see citing works

The Bacterial Twin-Arginine Translocation Pathway

Lee, P. A., Tullman‐Ercek, D., & Georgiou, G. (2006) · Annual Review of Microbiology · doi:10.1146/annurev.micro.60.080805.142212 · Cited by 348 · see citing works

Salmonella takes control: effector-driven manipulation of the host

McGhie, E. J., Brawn, L. C., Hume, P. J., Humphreys, D., & Koronakis, V. E. (2009) · Current Opinion in Microbiology · doi:10.1016/j.mib.2008.12.001 · Cited by 347 · see citing works

Novel type of murein transglycosylase in Escherichia coli

Höltje, J., Mirelman, D., Sharon, N., & Schwarz, U. T. (1975) · Journal of Bacteriology · doi:10.1128/jb.124.3.1067-1076.1975 · Cited by 340 · see citing works

Effect of Cholera Enterotoxin on Ion Transport across Isolated Ileal Mucosa

Field, M., Fromm, D., Al‐Awqati, Q., & Greenough, W. B. (1972) · Journal of Clinical Investigation · doi:10.1172/jci106874 · Cited by 339 · see citing works

The σ E ‐mediated response to extracytoplasmic stress in Escherichia coli is transduced by RseA and RseB, two negative regulators of σ E

Peñas, A. D. L., Connolly, L. E., & Gross, C. A. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.3611718.x · Cited by 337 · see citing works

TcpP protein is a positive regulator of virulence gene expression in Vibrio cholerae

Häse, C. C., & Mekalanos, J. J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.2.730 · Cited by 329 · see citing works

DegS and YaeL participate sequentially in the cleavage of RseA to activate the ς E -dependent extracytoplasmic stress responsePreprint

Alba, B. M., Leeds, J. A., Onufryk, C., Lu, C. Z., & Gross, C. A. (2002) · Genes & Development · doi:10.1101/gad.1008902 · Cited by 328 · see citing works

Lipoprotein Sorting in Bacteria

Okuda, S., & Tokuda, H. (2010) · Annual Review of Microbiology · doi:10.1146/annurev-micro-090110-102859 · Cited by 327 · see citing works

The Cpx two-component signal transduction pathway of Escherichia coli regulates transcription of the gene specifying the stress-inducible periplasmic protease, DegP.Preprint

Danese, P. N., Snyder, W. B., Cosma, C. L., Davis, L. J., & Silhavy, T. J. (1995) · Genes & Development · doi:10.1101/gad.9.4.387 · Cited by 325 · see citing works

Pushing the envelope: extracytoplasmic stress responses in bacterial pathogens

Rowley, G., Spector, M. P., Kormanec, J., & Roberts, M. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1394 · Cited by 321 · see citing works

Acetyl phosphate and the activation of two-component response regulators.

McCleary, W. R., & Stock, J. B. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31731-9 · Cited by 320 · see citing works

Outer Membrane Biogenesis

Konovalova, A., Kahne, D. E., & Silhavy, T. J. (2017) · Annual Review of Microbiology · doi:10.1146/annurev-micro-090816-093754 · Cited by 315 · see citing works

Bacterial Stress Responses during Host Infection

Fang, F. C., Frawley, E. R., Tapscott, T., & Vázquez‐Torres, A. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.07.009 · Cited by 313 · see citing works

rpoE, the gene encoding the second heat‐shock sigma factor, sigma E, in Escherichia coli.

Rouvière, P. E., Peñas, A. D. L., Mecsas, J. C., Lu, C. Z., Rudd, K. E., & Gross, C. A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07084.x · Cited by 310 · see citing works

Regulation of Escherichia coli cell envelope proteins involved in protein folding and degradation by the Cpx two-component system.Preprint

Pogliano, J., Lynch, A. S., Belin, D., Lin, E. C. C., & Beckwith, J. (1997) · Genes & Development · doi:10.1101/gad.11.9.1169 · Cited by 306 · see citing works

Sigma factors inPseudomonas aeruginosa

Potvin, É., Sanschagrin, F., & Lévesque, R. C. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00092.x · Cited by 306 · see citing works

The chaperone‐assisted membrane release and folding pathway is sensed by two signal transduction systems

Jones, C. H., Danese, P. N., Pinkner, J. S., Silhavy, T. J., & Hultgren, S. J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.21.6394 · Cited by 299 · see citing works

Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli

Sklar, J. G., Wu, T., Gronenberg, L. S., Malinverni, J. C., Kahne, D. E., & Silhavy, T. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701579104 · Cited by 296 · see citing works

CpxP, a Stress-Combative Member of the Cpx Regulon

Danese, P. N., & Silhavy, T. J. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.4.831-839.1998 · Cited by 294 · see citing works

Transduction of envelope stress in Escherichia coli by the Cpx two-component system

Raivio, T. L., & Silhavy, T. J. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.24.7724-7733.1997 · Cited by 284 · see citing works

The Escherichia coli sigma E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factorPreprint

Ades, S. E., Connolly, L. E., Alba, B. M., & Gross, C. A. (1999) · Genes & Development · doi:10.1101/gad.13.18.2449 · Cited by 274 · see citing works

Small non-coding RNAs and the bacterial outer membrane

Vogel, J., & Papenfort, K. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2006.10.006 · Cited by 272 · see citing works

Vibriobactin, a siderophore from Vibrio cholerae.

Griffiths, G. L., Sigel, S. P., Payne, S. M., & Neilands, J. B. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43671-4 · Cited by 262 · see citing works

YaeL (EcfE) activates the ς E pathway of stress response through a site-2 cleavage of anti-ς E , RseAPreprint

Kanehara, K., Ito, K., & Akiyama, Y. (2002) · Genes & Development · doi:10.1101/gad.1002302 · Cited by 258 · see citing works

Homology between virF, the transcriptional activator of the Yersinia virulence regulon, and AraC, the Escherichia coli arabinose operon regulator

Cornelis, G. R., Sluiters, C., de Rouvroit, C. L., & Michiels, T. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.1.254-262.1989 · Cited by 252 · see citing works

The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity

Behrens, S., Maier, R., de Cock, H., Schmid, F. X., & Gross, C. A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.1.285 · Cited by 247 · see citing works

Conserved Small Non-coding RNAs that belong to the σE Regulon: Role in Down-regulation of Outer Membrane Proteins

Johansen, J., Rasmussen, A. A., Overgaard, M., & Valentin‐Hansen, P. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.09.004 · Cited by 246 · see citing works

SigmaE is an essential sigma factor in Escherichia coli

Peñas, A. D. L., Connolly, L. E., & Gross, C. A. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.21.6862-6864.1997 · Cited by 245 · see citing works

RNA-seq Brings New Insights to the Intra-Macrophage Transcriptome of Salmonella Typhimurium

Srikumar, S., Kröger, C., Hébrard, M., Colgan, A. M., Owen, S. V., Sivasankaran, S. K., Cameron, A. D. S., Hokamp, K., & Hinton, J. C. D. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005262 · Cited by 242 · see citing works

MicL, a new σE-dependent sRNA, combats envelope stress by repressing synthesis of Lpp, the major outer membrane lipoproteinPreprint

Guo, M. S., Updegrove, T. B., Gogol, E. B., Shabalina, S. A., Gross, C. A., & Storz, G. (2014) · Genes & Development · doi:10.1101/gad.243485.114 · Cited by 241 · see citing works

outer membrane remodeling: role in resistance to host innate immunity

Ernst, R. K., Guina, T., & Miller, S. I. (2001) · Microbes and Infection · doi:10.1016/s1286-4579(01)01494-0 · Cited by 238 · see citing works

The Cpx Envelope Stress Response Is Controlled by Amplification and Feedback Inhibition

Raivio, T. L., Popkin, D. L., & Silhavy, T. J. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.17.5263-5272.1999 · Cited by 237 · see citing works

The Alternative Sigma Factor, ςE, Is Critically Important for the Virulence of Salmonella typhimurium

Humphreys, S., Stevenson, A. W., Bacon, A. K., Weinhardt, A. B., & Roberts, M. (1999) · Infection and Immunity · doi:10.1128/.67.4.1560-1568.1999 · Cited by 236 · see citing works

Characterization of the Cpx Regulon in Escherichia coli Strain MC4100

Price, N. L., & Raivio, T. L. (2008) · Journal of Bacteriology · doi:10.1128/jb.00798-08 · Cited by 228 · see citing works

Signal Detection and Target Gene Induction by the CpxRA Two-Component System

Champion, P. A. D., & Silhavy, T. J. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.8.2432-2440.2003 · Cited by 225 · see citing works

Overproduction of NlpE, a new outer membrane lipoprotein, suppresses the toxicity of periplasmic LacZ by activation of the Cpx signal transduction pathway

Snyder, W. B., Davis, L. J., Danese, P. N., Cosma, C. L., & Silhavy, T. J. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.15.4216-4223.1995 · Cited by 223 · see citing works

The complex rcs regulatory cascade.

Wall, E., Majdalani, N., & Gottesman, S. (2018) · Annual Review of Microbiology · doi:10.1146/annurev-micro-090817-062640 · Cited by 220 · see citing works

Everything old is new again: An update on current research on the Cpx envelope stress response

Raivio, T. L. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.10.018 · Cited by 220 · see citing works

A third envelope stress signal transduction pathway in Escherichia coli

Raffa, R. G., & Raivio, T. L. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03112.x · Cited by 216 · see citing works

Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm ofEscherichia coli

Arié, J., Sassoon, N., & Betton, J. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02250.x · Cited by 208 · see citing works

Modulating substrate choice: the SspB adaptor delivers a regulator of the extracytoplasmic-stress response to the AAA+ protease ClpXP for degradationPreprint

Flynn, J. M., Levchenko, I. V., Sauer, R. T., & Baker, T. A. (2004) · Genes & Development · doi:10.1101/gad.1240104 · Cited by 208 · see citing works

A 3′ UTR-Derived Small RNA Provides the Regulatory Noncoding Arm of the Inner Membrane Stress Response

Chao, Y., & Vogel, J. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.12.023 · Cited by 203 · see citing works

Small RNAs endow a transcriptional activator with essential repressor functions for single-tier control of a global stress regulon

Gogol, E. B., Rhodius, V. A., Papenfort, K., Vogel, J., & Gross, C. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109379108 · Cited by 196 · see citing works

The Escherichia coli Cpx Envelope Stress Response Regulates Genes of Diverse Function That Impact Antibiotic Resistance and Membrane Integrity

Raivio, T. L., Leblanc, S. K. D., & Price, N. L. (2013) · Journal of Bacteriology · doi:10.1128/jb.00105-13 · Cited by 193 · see citing works

Identification of the l,d -Transpeptidases for Peptidoglycan Cross-Linking inEscherichia coli

Magnet, S., Dubost, L., Marie, A., Arthur, M., & Gutmann, L. (2008) · Journal of Bacteriology · doi:10.1128/jb.00025-08 · Cited by 187 · see citing works

Salmonellae PhoPQ regulation of the outer membrane to resist innate immunity

Dalebroux, Z. D., & Miller, S. I. (2014) · Current Opinion in Microbiology · doi:10.1016/j.mib.2013.12.005 · Cited by 186 · see citing works

The alternative sigma factor σE controls antioxidant defences required for Salmonella virulence and stationary‐phase survival

Testerman, T. L., Vázquez‐Torres, A., Xu, Y., Jones‐Carson, J., Libby, S. J., & Fang, F. C. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02787.x · Cited by 186 · see citing works

Cpx signaling pathway monitors biogenesis and affects assembly and expression of P pili

Hung, D. L., Raivio, T. L., Jones, C. H., Silhavy, T. J., & Hultgren, S. J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1508 · Cited by 186 · see citing works

Just scratching the surface: an expanding view of the Cpx envelope stress response

Vogt, S., & Raivio, T. L. (2011) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2011.02406.x · Cited by 183 · see citing works

Hfq Modulates the σ E -Mediated Envelope Stress Response and the σ 32 -Mediated Cytoplasmic Stress Response in Escherichia coli

Guisbert, E., Rhodius, V. A., Ahuja, N., Witkin, E., & Gross, C. A. (2006) · Journal of Bacteriology · doi:10.1128/jb.01243-06 · Cited by 178 · see citing works

Vibrio cholerae RND Family Efflux Systems Are Required for Antimicrobial Resistance, Optimal Virulence Factor Production, and Colonization of the Infant Mouse Small Intestine

Bina, X. R., Provenzano, D., Nguyen, N., & Bina, J. E. (2008) · Infection and Immunity · doi:10.1128/iai.01620-07 · Cited by 178 · see citing works

Monoclonal antibody targeting the β-barrel assembly machine of Escherichia coli is bactericidal

Storek, K. M., Auerbach, M. R., Shi, H., Garcia, N. K., Sun, D., Nickerson, N. N., Vij, R., Lin, Z., Chiang, N., Schneider, K., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1800043115 · Cited by 175 · see citing works

Microbial Peptidyl-Prolyl cis / trans Isomerases (PPIases): Virulence Factors and Potential Alternative Drug Targets

Ünal, C., & Steinert, M. (2014) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00015-14 · Cited by 174 · see citing works

HilD-mediated transcriptional cross-talk between SPI-1 and SPI-2

Bustamante, V. H., Martínez-Chavarría, L. C., Santana, F. J., Knodler, L. A., Steele‐Mortimer, O., & Puente, J. L. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801205105 · Cited by 170 · see citing works

The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP

Isaac, D. D., Pinkner, J. S., Hultgren, S. J., & Silhavy, T. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508936102 · Cited by 168 · see citing works

Involvement of cpxA, a sensor of a two-component regulatory system, in the pH-dependent regulation of expression of Shigella sonnei virF gene

Nakayama, S., & Watanabe, H. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.17.5062-5069.1995 · Cited by 164 · see citing works

The disulfide bond formation (Dsb) system

Ito, K., & Inaba, K. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.02.002 · Cited by 163 · see citing works

PhoPQ regulates acidic glycerophospholipid content of the Salmonella Typhimurium outer membrane

Dalebroux, Z. D., Matamouros, S., Whittington, D., Bishop, R. E., & Miller, S. I. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316901111 · Cited by 162 · see citing works

The Extracytoplasmic Stress Factor, σE, Is Required to Maintain Cell Envelope Integrity in Escherichia coli

Hayden, J., & Ades, S. E. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001573 · Cited by 158 · see citing works

Characterization of Copper-Inducible Promoters Regulated by CpxA/CpxR in Escherichia coli

Yamamoto, K., & Ishihama, A. (2006) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.60024 · Cited by 153 · see citing works

The CpxRA Signal Transduction System of Escherichia coli : Growth-Related Autoactivation and Control of Unanticipated Target Operons

Wulf, P. D., Kwon, O., & Lin, E. C. C. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.21.6772-6778.1999 · Cited by 152 · see citing works

Impact of bacterial sRNAs in stress responses

Holmqvist, E., & Wagner, E. G. H. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160363 · Cited by 150 · see citing works

Functional equivalence of Escherichia coli sigma E and Pseudomonas aeruginosa AlgU: E. coli rpoE restores mucoidy and reduces sensitivity to reactive oxygen intermediates in algU mutants of P. aeruginosa

Yu, H. D., Schurr, M. J., & Deretic, V. P. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.11.3259-3268.1995 · Cited by 148 · see citing works

Coordinated Regulation of Virulence during Systemic Infection of Salmonella enterica Serovar Typhimurium

Yoon, H., McDermott, J., Porwollik, S., McClelland, M., & Heffron, F. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000306 · Cited by 134 · see citing works

Loss of Hfq activates the σE‐dependent envelope stress response in Salmonella enterica

Figueroa‐Bossi, N., Lemire, S., Maloriol, D., Balbontín, R., Casadesús, J., & Bossi, L. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05413.x · Cited by 132 · see citing works

P fimbriae enhance the early establishment of Escherichia coli in the human urinary tract

Wullt, B., Bergsten, G., Connell, H., ROLLANO, P., Gebretsadik, N., Hull, R. A., & Svanborg, C. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02165.x · Cited by 131 · see citing works

Role of the Two-Component Regulator CpxAR in the Virulence of Salmonella enterica Serotype Typhimurium

Humphreys, S., Rowley, G., Stevenson, A. W., Anjum, M. F., Woodward, M. J., Gilbert, S., Kormanec, J., & Roberts, M. (2004) · Infection and Immunity · doi:10.1128/iai.72.8.4654-4661.2004 · Cited by 130 · see citing works

Signal Integration by the Two-Component Signal Transduction Response Regulator CpxR

Wolfe, A. J., Parikh, N., Lima, B. P., & Zemaitaitis, B. W. (2008) · Journal of Bacteriology · doi:10.1128/jb.01906-07 · Cited by 129 · see citing works

Bacterial lipoproteins; biogenesis, sorting and quality control

Narita, S., & Tokuda, H. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2016.11.009 · Cited by 128 · see citing works

RovM, a novel LysR‐type regulator of the virulence activator gene rovA , controls cell invasion, virulence and motility of Yersinia pseudotuberculosis

Heroven, A. K., & Dersch, P. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05458.x · Cited by 128 · see citing works

OmpC and the σE regulatory pathway are involved in adhesion and invasion of the Crohn's disease‐associated Escherichia coli strain LF82

Rolhion, N., Carvalho, F. A., & Darfeuille–Michaud, A. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05638.x · Cited by 125 · see citing works

Inhibition of the β-barrel assembly machine by a peptide that binds BamD

Hagan, C. L., Wzorek, J. S., & Kahne, D. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415955112 · Cited by 123 · see citing works

MicA sRNA links the PhoP regulon to cell envelope stress

Coornaert, A., Lu, A., Mandin, P., Springer, M., Gottesman, S., & Guillier, M. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07115.x · Cited by 123 · see citing works

Redefining the essential trafficking pathway for outer membrane lipoproteins

Grabowicz, M., & Silhavy, T. J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1702248114 · Cited by 123 · see citing works

Lpp, the Braun lipoprotein, turns 50—major achievements and remaining issues

Asmar, A. T., & Collet, J. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny199 · Cited by 122 · see citing works

The Response Regulator PhoP of Yersinia pseudotuberculosis Is Important for Replication in Macrophages and for Virulence

Grabenstein, J. P., Marceau, M., Pujol, C., Simonet, M., & Bliska, J. B. (2004) · Infection and Immunity · doi:10.1128/iai.72.9.4973-4984.2004 · Cited by 119 · see citing works

The Phage Shock Protein Response

Flores-Kim, J., & Darwin, A. J. (2016) · Annual Review of Microbiology · doi:10.1146/annurev-micro-102215-095359 · Cited by 119 · see citing works

Down-regulation of Porins by a Small RNA Bypasses the Essentiality of the Regulated Intramembrane Proteolysis Protease RseP in Escherichia coli

Douchin, V., Bohn, C., & Bouloc, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600819200 · Cited by 118 · see citing works

The Cpx stress response system of Escherichia coli senses plasma membrane proteins and controls HtpX, a membrane protease with a cytosolic active site

Shimohata, N., Chiba, S., Saikawa, N., Ito, K., & Akiyama, Y. (2002) · Genes to Cells · doi:10.1046/j.1365-2443.2002.00554.x · Cited by 117 · see citing works

A Csr‐type regulatory system, including small non‐coding RNAs, regulates the global virulence regulator RovA of Yersinia pseudotuberculosis through RovM

Heroven, A. K., Böhme, K., Rohde, M., & Dersch, P. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06218.x · Cited by 116 · see citing works

Design principles of the proteolytic cascade governing the σE-mediated envelope stress response in Escherichia coli: keys to graded, buffered, and rapid signal transductionPreprint

Chaba, R., Grigorova, I., Flynn, J. M., Baker, T. A., & Gross, C. A. (2007) · Genes & Development · doi:10.1101/gad.1496707 · Cited by 116 · see citing works

ClpXP, an ATP-powered unfolding and protein-degradation machine

Sauer, R. T., & Baker, T. A. (2011) · Cited by 113 · see citing works

Proteolytic regulation of alginate overproduction in Pseudomonas aeruginosa

Damron, F. H., & Goldberg, J. B. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08049.x · Cited by 113 · see citing works

The Response Regulator CpxR Directly Regulates Expression of SeveralLegionella pneumophila icm/dotComponents as Well as New Translocated Substrates

Altman, E., & Segal, G. (2008) · Journal of Bacteriology · doi:10.1128/jb.01493-07 · Cited by 112 · see citing works

The Alternative Sigma Factor σ E Plays an Important Role in Intestinal Survival and Virulence in Vibrio cholerae

Kovacikova, G., & Skorupski, K. (2002) · Infection and Immunity · doi:10.1128/iai.70.10.5355-5362.2002 · Cited by 111 · see citing works

Quality Control of Cytoplasmic Membrane Proteins in Escherichia coli

Akiyama, Y. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp071 · Cited by 111 · see citing works

Tethering of CpxP to the inner membrane prevents spheroplast induction of the Cpx envelope stress response

Raivio, T. L., Laird, M. W., Joly, J. C., & Silhavy, T. J. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02074.x · Cited by 108 · see citing works

Fine-Tuning of the Cpx Envelope Stress Response Is Required for Cell Wall Homeostasis in Escherichia coli

Delhaye, A., Collet, J., & Laloux, G. (2016) · mBio · doi:10.1128/mbio.00047-16 · Cited by 108 · see citing works

Identification of CpxR as a Positive Regulator of icm and dot Virulence Genes of Legionella pneumophila

Gal‐Mor, O., & Segal, G. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.16.4908-4919.2003 · Cited by 108 · see citing works

Assembly of Lipopolysaccharide in Escherichia coli Requires the Essential LapB Heat Shock Protein

Klein, G., Kobylak, N., Lindner, B., Stupak, A., & Raina, S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.539494 · Cited by 107 · see citing works

ClpXP proteases positively regulate alginate overexpression and mucoid conversion in Pseudomonas aeruginosa

Qiu, D., Eisinger, V. M., Head, N. E., Pier, G. B., & Yu, H. D. (2008) · Microbiology · doi:10.1099/mic.0.2008/017368-0 · Cited by 105 · see citing works

The Cpx Envelope Stress Response Affects Expression of the Type IV Bundle-Forming Pili of EnteropathogenicEscherichiacoli

Nevesinjac, A. Z., & Raivio, T. L. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.2.672-686.2005 · Cited by 105 · see citing works

Antimicrobial peptides activate the Vibrio cholerae σ E regulon through an OmpU‐dependent signalling pathway

Mathur, J., Davis, B. M., & Waldor, M. K. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05544.x · Cited by 102 · see citing works

Analysis of YfgL and YaeT Interactions through Bioinformatics, Mutagenesis, and Biochemistry

Vuong, P., Bennion, D., Mantei, J., Frost, D., & Misra, R. (2007) · Journal of Bacteriology · doi:10.1128/jb.01477-07 · Cited by 101 · see citing works

The CpxR/CpxA Two-component System Up-regulates Two Tat-dependent Peptidoglycan Amidases to Confer Bacterial Resistance to Antimicrobial Peptide

Weatherspoon‐Griffin, N., Zhao, G., Kong, W., Kong, Y., Morigen, M., Andrews‐Polymenis, H. L., McClelland, M., & Shi, Y. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.200352 · Cited by 99 · see citing works

Identification of cpxR as a Positive Regulator Essential for Expression of the Shigella sonnei virF Gene

Nakayama, S., & Watanabe, H. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.14.3522-3528.1998 · Cited by 96 · see citing works

Mutational activation of the Cpx signal transduction pathway of Escherichia coli suppresses the toxicity conferred by certain envelope‐associated stresses

Cosma, C. L., Danese, P. N., Carlson, J. H., Silhavy, T. J., & Snyder, W. B. (1995) · Molecular Microbiology · doi:10.1111/j.1365-2958.1995.mmi_18030491.x · Cited by 94 · see citing works

Yersinia Enterocolitica: A Brief Review of the Issues Relating to the Zoonotic Pathogen, Public Health Challenges, and the Pork Production Chain

Drummond, N., Murphy, B. P., Ringwood, T., Prentice, M., Buckley, J., & Fanning, S. (2012) · Foodborne pathogens and disease · doi:10.1089/fpd.2011.0938 · Cited by 92 · see citing works

The Cpx Envelope Stress Response Modifies Peptidoglycan Cross-Linking via the l,d-Transpeptidase LdtD and the Novel Protein YgaU

Bernal-Cabas, M., Ayala, J. A., & Raivio, T. L. (2014) · Journal of Bacteriology · doi:10.1128/jb.02449-14 · Cited by 92 · see citing works

Environmental Regulation of Salmonella typhi Invasion-Defective Mutants

Leclerc, G. J., Tartera, C., & Metcalf, E. S. (1998) · Infection and Immunity · doi:10.1128/iai.66.2.682-691.1998 · Cited by 92 · see citing works

Cpx Signal Transduction Is Influenced by a Conserved N-Terminal Domain in the Novel Inhibitor CpxP and the Periplasmic Protease DegP

Buelow, D. R., & Raivio, T. L. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.19.6622-6630.2005 · Cited by 92 · see citing works

From Chaperones to the Membrane with a BAM!

Plummer, A. M., & Fleming, K. G. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.06.005 · Cited by 90 · see citing works

Deletion of lolB , Encoding an Outer Membrane Lipoprotein, Is Lethal for Escherichia coli and Causes Accumulation of Lipoprotein Localization Intermediates in the Periplasm

Tanaka, K., Matsuyama, S., & Tokuda, H. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.22.6538-6542.2001 · Cited by 90 · see citing works

Global Comparison of the Membrane Subproteomes between a Multidrug-Resistant Acinetobacter baumannii Strain and a Reference Strain

Siroy, A., Cosette, P., Seyer, D., Guillier, C., Vallenet, D., DORSSELAER, A. V., Boyer-Mariotte, S., Jouenne, T., & Dé, E. (2006) · Journal of Proteome Research · doi:10.1021/pr060372s · Cited by 89 · see citing works

Lactobacillus reuteri Inhibition of Enteropathogenic Escherichia coli Adherence to Human Intestinal Epithelium

Walsham, A. D. S., MacKenzie, D. A., Cook, V., Wemyss-Holden, S. A., Hews, C. L., Juge, N., & Schüller, S. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.00244 · Cited by 89 · see citing works

New Insights into the Non-orthodox Two Component Rcs Phosphorelay System

Guo, X.-P., & Sun, Y. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02014 · Cited by 88 · see citing works

Biogenesis of inner membrane proteins in Escherichia coli

Luirink, J., Yu, Z. K., Wagner, S., & Gier, J. D. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2011.12.006 · Cited by 87 · see citing works

Regulation of Flagellum Biosynthesis in Response to Cell Envelope Stress in Salmonella enterica Serovar Typhimurium

Spöring, I., Felgner, S., Preuße, M., Eckweiler, D., Rohde, M., Häußler, S., Weiß, S., & Erhardt, M. (2018) · mBio · doi:10.1128/mbio.00736-17 · Cited by 85 · see citing works

Disruption of the Genes for ClpXP Protease inSalmonella entericaSerovar Typhimurium Results in Persistent Infection in Mice, and Development of Persistence Requires Endogenous Gamma Interferon and Tumor Necrosis Factor Alpha

Yamamoto, T., Sashinami, H., Takaya, A., Tomoyasu, T., Matsui, H., Kikuchi, Y., Hanawa, T., Kamiya, S., & Nakane, A. (2001) · Infection and Immunity · doi:10.1128/iai.69.5.3164-3174.2001 · Cited by 85 · see citing works

Salmonella Pathogenicity Island 1(SPI-1) at Work

Que, F., Wu, S., & Huang, R. (2013) · Current Microbiology · doi:10.1007/s00284-013-0307-8 · Cited by 84 · see citing works

Identification of the σ E regulon of Salmonella enterica serovar Typhimurium

Škovierová, H., Rowley, G., Řežuchová, B., Homerová, D., Lewis, C., Roberts, M., & Kormanec, J. (2006) · Microbiology · doi:10.1099/mic.0.28744-0 · Cited by 83 · see citing works

Regulation of the Pap Epigenetic Switch by CpxAR

Hernday, A. D., Braaten, B. A., Broitman-Maduro, G., Engelberts, P. J., & Low, D. A. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.020 · Cited by 82 · see citing works

Small Regulatory RNAs in the Enterobacterial Response to Envelope Damage and Oxidative Stress

Fröhlich, K. S., & Gottesman, S. (2018) · Microbiology Spectrum · doi:10.1128/microbiolspec.rwr-0022-2018 · Cited by 81 · see citing works

Reprogramming of Yersinia from Virulent to Persistent Mode Revealed by Complex In Vivo RNA-seq Analysis

Avican, K., Fahlgren, A., Huss, M., Heroven, A. K., Beckstette, M., Dersch, P., & Fällman, M. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1004600 · Cited by 81 · see citing works

Targeting and Insertion of Membrane Proteins

Kühn, A., Koch, H., & Dalbey, R. (2017) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0012-2016 · Cited by 80 · see citing works

Escherichia coli Isolate for Studying Colonization of the Mouse Intestine and Its Application to Two-Component Signaling Knockouts

Lasaro, M. A., Liu, Z., Bishar, R. A., Kelly, K., Chattopadhyay, S., Paul, S., Sokurenko, E. V., Zhu, J., & Goulian, M. (2014) · Journal of Bacteriology · doi:10.1128/jb.01296-13 · Cited by 79 · see citing works

Role of Periplasmic Chaperones and BamA (YaeT/Omp85) in Folding and Secretion of Intimin from EnteropathogenicEscherichia coliStrains

Bodelón, G., Marín, E., & Fernández, L. Á. (2009) · Journal of Bacteriology · doi:10.1128/jb.00458-09 · Cited by 79 · see citing works

The alternative sigma factor σE is required for resistance of Salmonella enterica serovar Typhimurium to anti‐microbial peptides

Crouch, M. V., Becker, L. A., Bang, I. S., Tanabe, H., Ouellette, A. J., & Fang, F. C. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04578.x · Cited by 79 · see citing works

The Cpx Stress Response System Potentiates the Fitness and Virulence of Uropathogenic Escherichia coli

Debnath, I., Norton, J. P., Barber, A. E., Ott, E. M., Dhakal, B. K., Kulesus, R. R., & Mulvey, M. A. (2013) · Infection and Immunity · doi:10.1128/iai.01213-12 · Cited by 79 · see citing works

Bam Lipoproteins Assemble BamA in Vitro

Hagan, C. L., Westwood, D. B., & Kahne, D. E. (2013) · Biochemistry · doi:10.1021/bi400865z · Cited by 78 · see citing works

Virulence properties of Pseudomonas aeruginosa lacking the extreme-stress sigma factor AlgU (sigmaE)

Yu, H. D., Boucher, J. C., Hibler, N. S., & Deretic, V. P. (1996) · Infection and Immunity · doi:10.1128/iai.64.7.2774-2781.1996 · Cited by 75 · see citing works

The Sigma Factor AlgU Plays a Key Role in Formation of Robust Biofilms by NonmucoidPseudomonas aeruginosa

Bazire, A., Shioya, K., Soum-Soutéra, E., Bouffartigues, E., Ryder, C., Guentas-Dombrowsky, L., Hémery, G., Linossier, I., Chevalier, S., Wozniak, D. J., et al. (2010) · Journal of Bacteriology · doi:10.1128/jb.01633-09 · Cited by 75 · see citing works

Yersinia pestisTwo-Component Gene Regulatory Systems Promote Survival in Human Neutrophils

O’Loughlin, J. L., Spinner, J. L., Minnich, S. A., & Kobayashi, S. D. (2009) · Infection and Immunity · doi:10.1128/iai.00718-09 · Cited by 73 · see citing works

Signal integration by DegS and RseB governs the σ E -mediated envelope stress response in Escherichia coli

Chaba, R., Alba, B. M., Guo, M. S., Sohn, J., Ahuja, N., Sauer, R. T., & Gross, C. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019277108 · Cited by 73 · see citing works

The Pseudomonas aeruginosa AlgZR two-component system coordinates multiple phenotypes

Okkotsu, Y., Little, A. S., & Schurr, M. J. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00082 · Cited by 72 · see citing works

Activation of the Cpx Envelope Stress Response Down-Regulates Expression of Several Locus of Enterocyte Effacement-Encoded Genes in Enteropathogenic Escherichia coli

MacRitchie, D. M., Ward, J. D., Nevesinjac, A. Z., & Raivio, T. L. (2008) · Infection and Immunity · doi:10.1128/iai.01265-07 · Cited by 72 · see citing works

Structural Basis for Two-component System Inhibition and Pilus Sensing by the Auxiliary CpxP Protein

Zhou, X., Keller, R., Volkmer, R., Krauß, N., Scheerer, P., & Hunke, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.194092 · Cited by 71 · see citing works

Effects of Lipoprotein Overproduction on the Induction of DegP (HtrA) Involved in Quality Control in the Escherichia coli Periplasm

Miyadai, H., Tanaka-Masuda, K., Matsuyama, S., & Tokuda, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406390200 · Cited by 70 · see citing works

Global Regulation by Horizontally Transferred Regulators Establishes the Pathogenicity of Escherichia coli

Abe, H., Miyahara, A., Oshima, T., Tashiro, K., Ogura, Y., Kuhara, S., Ogasawara, N., Hayashi, T., & Tobe, T. (2008) · DNA Research · doi:10.1093/dnares/dsm033 · Cited by 70 · see citing works

RseB Binding to the Periplasmic Domain of RseA Modulates the RseA:ςE Interaction in the Cytoplasm and the Availability of ςE·RNA Polymerase

Collinet, B., Yuzawa, H., Chen, T., Herrera, C., & Missiakas, D. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006214200 · Cited by 69 · see citing works

A Suppressor of Cell Death Caused by the Loss of σ E Downregulates Extracytoplasmic Stress Responses and Outer Membrane Vesicle Production in Escherichia coli

Button, J. E., Silhavy, T. J., & Ruiz, N. (2006) · Journal of Bacteriology · doi:10.1128/jb.01534-06 · Cited by 68 · see citing works

The CpxQ sRNA Negatively Regulates Skp To Prevent Mistargeting of β-Barrel Outer Membrane Proteins into the Cytoplasmic Membrane

Grabowicz, M., Koren, D., & Silhavy, T. J. (2016) · mBio · doi:10.1128/mbio.00312-16 · Cited by 68 · see citing works

Role of bundle-forming pilus of enteropathogenicEscherichia coliin host cell adherence and in microcolony development

Tobe, T., & Sasakawa, C. (2001) · Cellular Microbiology · doi:10.1046/j.1462-5822.2001.00136.x · Cited by 67 · see citing works

Eliminating a Set of Four Penicillin Binding Proteins Triggers the Rcs Phosphorelay and Cpx Stress Responses in Escherichia coli

Evans, K. L., Kannan, S., Li, G., de Pedro, M. A., & Young, K. D. (2013) · Journal of Bacteriology · doi:10.1128/jb.00596-13 · Cited by 67 · see citing works

Salmonella entericaSerovar TyphimuriumsurAMutants Are Attenuated and Effective Live Oral Vaccines

Sydenham, M. A., Douce, G. R., Bowe, F., Ahmed, S., Chatfield, S. N., & Gordon Dougan, B. (2000) · Infection and Immunity · doi:10.1128/iai.68.3.1109-1115.2000 · Cited by 67 · see citing works

Inhibitor of intramembrane protease RseP blocks the σ E response causing lethal accumulation of unfolded outer membrane proteins

Konovalova, A., Grabowicz, M., Balibar, C. J., Malinverni, J. C., Painter, R. E., Riley, D., Mann, P. A., Wang, H., Garlisi, C. G., Sherborne, B. S., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1806107115 · Cited by 65 · see citing works

Regulated Control of the Assembly and Diversity of LPS by Noncoding sRNAs

Klein, G., & Raina, S. (2015) · BioMed Research International · doi:10.1155/2015/153561 · Cited by 64 · see citing works

Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage

Li, X., Wang, B., Feng, L., Kang, H., Qi, Y., Wang, J., & Shi, Y. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903289106 · Cited by 64 · see citing works

A Bacterial Stress Response Regulates Respiratory Protein Complexes To Control Envelope Stress Adaptation

Guest, R. L., Wang, J., Wong, J. L., & Raivio, T. L. (2017) · Journal of Bacteriology · doi:10.1128/jb.00153-17 · Cited by 64 · see citing works

The cell wall amidase AmiB is essential for P seudomonas aeruginosa cell division, drug resistance and viability

Yakhnina, A. A., McManus, H. R., & Bernhardt, T. G. (2015) · Molecular Microbiology · doi:10.1111/mmi.13077 · Cited by 63 · see citing works

ZraP is a periplasmic molecular chaperone and a repressor of the zinc-responsive two-component regulator ZraSR

Appia‐Ayme, C., Hall, A., Patrick, E. H., Rajadurai, S., Clarke, T. A., & Rowley, G. (2011) · Biochemical Journal · doi:10.1042/bj20111639 · Cited by 63 · see citing works

The Lipoprotein NlpE Is a Cpx Sensor That Serves as a Sentinel for Protein Sorting and Folding Defects in the Escherichia coli Envelope

Delhaye, A., Laloux, G., & Collet, J. (2019) · Journal of Bacteriology · doi:10.1128/jb.00611-18 · Cited by 63 · see citing works

The Cpx envelope stress response both facilitates and inhibits elaboration of the enteropathogenic Escherichia coli bundle‐forming pilus

Vogt, S. L., Nevesinjac, A. Z., Humphries, R. M., Donnenberg, M. S., Armstrong, G. D., & Raivio, T. L. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07145.x · Cited by 63 · see citing works

In Vivo Roles of BamA, BamB and BamD in the Biogenesis of BamA, a Core Protein of the β-Barrel Assembly Machine of Escherichia coli

Misra, R., Stikeleather, R., & Gabriele, R. M. C. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.04.021 · Cited by 62 · see citing works

The Lipid Bilayer-Inserted Membrane Protein BamA of Escherichia coli Facilitates Insertion and Folding of Outer Membrane Protein A from Its Complex with Skp

Patel, G. J., & Kleinschmidt, J. H. (2013) · Biochemistry · doi:10.1021/bi400103t · Cited by 62 · see citing works

Stress Relief during Host Infection: The Phage Shock Protein Response Supports Bacterial Virulence in Various Ways

Darwin, A. J. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003388 · Cited by 61 · see citing works

Vibrio cholerae vexH Encodes a Multiple Drug Efflux Pump That Contributes to the Production of Cholera Toxin and the Toxin Co-Regulated Pilus

Taylor, D. L., Bina, X. R., & Bina, J. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038208 · Cited by 61 · see citing works

Dynamic Interaction between the CpxA Sensor Kinase and the Periplasmic Accessory Protein CpxP Mediates Signal Recognition in E. coli

Tschauner, K., Hörnschemeyer, P., Müller, V. S., & Hunke, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0107383 · Cited by 60 · see citing works

The small regulatory RNA molecule MicA is involved in Salmonella enterica serovar Typhimurium biofilm formation

Kint, G., Coster, D. D., Kathleen Marchal, D., Vanderleyden, J., & Keersmaecker, S. C. J. D. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-276 · Cited by 60 · see citing works

Induction of the Cpx Envelope Stress Pathway Contributes to Escherichia coli Tolerance to Antimicrobial Peptides

Audrain, B., Ferrières, L., Zaïri, A., Soubigou, G., Dobson, C. B., Coppée, J., Beloin, C., & Ghigo, J. (2013) · Applied and Environmental Microbiology · doi:10.1128/aem.02593-13 · Cited by 60 · see citing works

degS Is Necessary for Virulence and Is among Extraintestinal Escherichia coli Genes Induced in Murine Peritonitis

Redford, P., Roesch, P. L., & Welch, R. A. (2003) · Infection and Immunity · doi:10.1128/iai.71.6.3088-3096.2003 · Cited by 59 · see citing works

Decreased intracellular survival of an fkpA mutant of Salmonella typhimurium Copenhagen

Horne, S. M., Kottom, T. J., Nolan, L. K., & Young, K. D. (1997) · Infection and Immunity · doi:10.1128/iai.65.2.806-810.1997 · Cited by 59 · see citing works

The MisR/MisS Two-component Regulatory System Influences Inner Core Structure and Immunotype of Lipooligosaccharide in Neisseria meningitidis

Tzeng, Y., Datta, A., Ambrose, K. D., Lo, M., Davies, J. K., Carlson, R. W., Stephens, D. S., & Kahler, C. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401433200 · Cited by 55 · see citing works

The YfgL Lipoprotein Is Essential for Type III Secretion System Expression and Virulence of Salmonella enterica Serovar Enteritidis

Fardini, Y., Chettab, K., Grépinet, O., Rochereau, S., Trotereau, J., Harvey, P., Amy, M., Bottreau, E., Bumstead, N., Barrow, P., et al. (2006) · Infection and Immunity · doi:10.1128/iai.00716-06 · Cited by 54 · see citing works

A Sensor of the Two-Component System CpxA Affects Expression of the Type III Secretion System through Posttranscriptional Processing of InvE

Mitobe, J., Arakawa, E., & Watanabe, H. (2004) · Journal of Bacteriology · doi:10.1128/jb.187.1.107-113.2005 · Cited by 54 · see citing works

Hitting with a BAM: Selective Killing by Lectin-Like Bacteriocins

Ghequire, M. G. K., Swings, T., Michiels, J. J., Buchanan, S. K., & Mot, R. D. (2018) · mBio · doi:10.1128/mbio.02138-17 · Cited by 54 · see citing works

OMP Peptides Activate the DegS Stress-Sensor Protease by a Relief of Inhibition Mechanism

Sohn, J., Grant, R. A., & Sauer, R. T. (2009) · Structure · doi:10.1016/j.str.2009.07.017 · Cited by 53 · see citing works

Structural Studies of the Cpx Pathway Activator NlpE on the Outer Membrane of Escherichia coli

Hirano, Y., Hossain, M. M., Takeda, K., Tokuda, H., & Miki, K. (2007) · Structure · doi:10.1016/j.str.2007.06.014 · Cited by 52 · see citing works

Extracytoplasmic-Stress-Responsive Pathways Modulate Type III Secretion in Yersinia pseudotuberculosis

Carlsson, K. E., Liu, J., Edqvist, P. J., & Francis, M. S. (2007) · Infection and Immunity · doi:10.1128/iai.01346-06 · Cited by 52 · see citing works

Activation of hilA expression at low pH requires the signal sensor CpxA, but not the cognate response regulator CpxR, in Salmonella enterica serovar Typhimurium

Nakayama, S., Kushiro, A., Asahara, T., Tanaka, R., Hu, L., Kopecko, D. J., & Watanabe, H. (2003) · Microbiology · doi:10.1099/mic.0.26229-0 · Cited by 52 · see citing works

Bacterial Stress Responses as Potential Targets in Overcoming Antibiotic Resistance

Dawan, J., & Ahn, J. (2022) · Microorganisms · doi:10.3390/microorganisms10071385 · Cited by 219 · see citing works

Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments

Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works

Pseudomonas Flagella: Generalities and Specificities

Bouteiller, M., Dupont, C. A., Bourigault, Y., Latour, X., Barbey, C., Konto‐Ghiorghi, Y., & Mérieau, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073337 · Cited by 116 · see citing works

Comparative Analysis of Outer Membrane Vesicle Isolation Methods With an Escherichia coli tolA Mutant Reveals a Hypervesiculating Phenotype With Outer-Inner Membrane Vesicle Content

Reimer, S. L., Beniac, D. R., Hiebert, S. L., Booth, T. F., Chong, P. M., Westmacott, G., Zhanel, G. G., & Bay, D. C. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.628801 · Cited by 102 · see citing works

Inhibiting fatty acid synthesis overcomes colistin resistance

Carfrae, L. A., Rachwalski, K., French, S., Gordzevich, R., Seidel, L., Tsai, C. N., Tu, M. M., MacNair, C. R., Ovchinnikova, O. G., Clarke, B. R., et al. (2023) · Nature Microbiology · doi:10.1038/s41564-023-01369-z · Cited by 90 · see citing works

The Dynamic SecYEG Translocon

Oswald, J., Njenga, R., Natriashvili, A., Sarmah, P., & Koch, H.-G. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.664241 · Cited by 88 · see citing works

YhdP, TamB, and YdbH Are Redundant but Essential for Growth and Lipid Homeostasis of the Gram-Negative Outer Membrane

Ruiz, N., Davis, R. M., & Kumar, S. (2021) · mBio · doi:10.1128/mbio.02714-21 · Cited by 80 · see citing works

The Wsp system of Pseudomonas aeruginosa links surface sensing and cell envelope stress

O’Neal, L., Baraquet, C., Suo, Z., Dreifus, J. E., Peng, Y., Raivio, T. L., Wozniak, D. J., Harwood, C. S., & Parsek, M. R. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2117633119 · Cited by 75 · see citing works

Impact of the Resistance Responses to Stress Conditions Encountered in Food and Food Processing Environments on the Virulence and Growth Fitness of Non-Typhoidal Salmonellae

Guillén, S., Nadal, L., Álvarez, I., Mañas, P., & Cebrián, G. (2021) · Foods · doi:10.3390/foods10030617 · Cited by 62 · see citing works

Gram-Negative Bacterial Envelope Homeostasis under Oxidative and Nitrosative Stress

Chautrand, T., Souak, D., Chevalier, S., & Poc, C. D. (2022) · Microorganisms · doi:10.3390/microorganisms10050924 · Cited by 57 · see citing works

Antibiotic-induced stress responses in Gram-negative bacteria and their role in antibiotic resistance

Brand, C., Newton-Foot, M., Grobbelaar, M., & Whitelaw, A. (2025) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkaf068 · Cited by 54 · see citing works

Understanding tolerance to cell wall–active antibiotics

Dörr, T. (2020) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14541 · Cited by 46 · see citing works

A comprehensive review on latent role of stress proteins in antibiotic resistance

Dalbanjan, N. P., Kadapure, A. J., & Kumar, S. K. P. (2024) · The Microbe · doi:10.1016/j.microb.2024.100151 · Cited by 51 · see citing works

A genetic platform to investigate the functions of bacterial drug efflux pumps

Teelucksingh, T., Thompson, L. K., Zhu, S., Kuehfuss, N. M., Goetz, J. A., Gilbert, S., MacNair, C. R., Geddes‐McAlister, J., Brown, E. D., & Cox, G. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01119-y · Cited by 46 · see citing works

Expanding the genetic toolkit helps dissect a global stress response in the early-branching species Fusobacterium nucleatum

Ponath, F., Zhu, Y., Cosi, V., & Vogel, J. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201460119 · Cited by 35 · see citing works

Bacterial extracellular vesicles: biotechnological perspective for enhanced productivity

Muñoz-Echeverri, L. M., Benavides-López, S., Geiger, O., Trujillo‐Roldán, M. A., & Valdez‐Cruz, N. A. (2024) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-024-03963-7 · Cited by 34 · see citing works

An Intertwined Network of Regulation Controls Membrane Permeability Including Drug Influx and Efflux in Enterobacteriaceae

Ferrand, A., Vergalli, J., Pagès, J., & Davin‐Regli, A. (2020) · Microorganisms · doi:10.3390/microorganisms8060833 · Cited by 34 · see citing works

Inhibitors targeting BamA in gram-negative bacteria

Storek, K. M., Sun, D., & Rutherford, S. T. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2023.119609 · Cited by 31 · see citing works

Sex Steroids Induce Membrane Stress Responses and Virulence Properties in Pseudomonas aeruginosa

Vidaillac, C., Yong, V. F. L., Aschtgen, M., Qu, J. T., Yang, S., Xu, G., Seng, Z. J., Brown, A. C., Ali, M. K., Jaggi, T. K., et al. (2020) · mBio · doi:10.1128/mbio.01774-20 · Cited by 29 · see citing works

Salmonella enterica Serovar Typhimurium CpxRA Two-Component System Contributes to Gut Colonization in Salmonella-Induced Colitis

Fujimoto, M., Goto, R., Haneda, T., Okada, N., & Miki, T. (2018) · Infection and Immunity · doi:10.1128/iai.00280-18 · Cited by 28 · see citing works

Bacterial envelope stress responses: Essential adaptors and attractive targets

Cho, T. H. S., Pick, K., & Raivio, T. L. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2022.119387 · Cited by 27 · see citing works

The Cpx Stress Response Regulates Turnover of Respiratory Chain Proteins at the Inner Membrane of Escherichia coli

Tsviklist, V., Guest, R. L., & Raivio, T. L. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.732288 · Cited by 27 · see citing works

Bone marrow mesenchymal stem cells offer an immune-privileged niche to Cutibacterium acnes in case of implant-associated osteomyelitis

Dubus, M., Varin, J., Papa, S., Chevrier, J., Quilès, F., Francius, G., Audonnet, S., Mauprivez, C., Gangloff, S. C., Siboni, R., et al. (2021) · Acta Biomaterialia · doi:10.1016/j.actbio.2021.10.026 · Cited by 25 · see citing works

Exploiting the fitness cost of metallo-β-lactamase expression can overcome antibiotic resistance in bacterial pathogens

Tu, M. M., Carfrae, L. A., Rachwalski, K., French, S., Catacutan, D. B., Gordzevich, R., MacNair, C. R., Speagle, M. E., Werah, F., Stokes, J. M., et al. (2025) · Nature Microbiology · doi:10.1038/s41564-024-01883-8 · Cited by 24 · see citing works

A Mildly Acidic Environment Alters Pseudomonas aeruginosa Virulence and Causes Remodeling of the Bacterial Surface

Mozaheb, N., Rasouli, P., Kaur, M., Smissen, P. V. D., Larrouy-Maumus, G. J., & Mingeot‐Leclercq, M. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.04832-22 · Cited by 24 · see citing works

Matching amino acids membrane preference profile to improve activity of antimicrobial peptides

Kim, S., Lee, J., Lee, S., Kim, H., Sim, J.-Y., Pak, B., Kim, K., & Kim, J. I. (2022) · Communications Biology · doi:10.1038/s42003-022-04164-4 · Cited by 23 · see citing works

Stress-Based High-Throughput Screening Assays to Identify Inhibitors of Cell Envelope Biogenesis

Steenhuis, M., ten Hagen‐Jongman, C. M., van Ulsen, P., & Luirink, J. (2020) · Antibiotics · doi:10.3390/antibiotics9110808 · Cited by 23 · see citing works

Physiological and genomic evidence supports the role of Serratia quinivorans PKL:12 as a biopriming agent for the biohardening of micropropagated Picrorhiza kurroa plantlets in cold regions

Kumar, R., Borker, S. S., Thakur, A. D., Thapa, P., Kumar, S., Mukhia, S., Kumari, A., Bhattacharya, A., & Kumar, S. (2021) · Genomics · doi:10.1016/j.ygeno.2021.03.019 · Cited by 22 · see citing works

The Anti-Campylobacter Activity and Mechanisms of Pinocembrin Action

Klančnik, A., Šimunović, K., Kovač, J., Şahin, O., Wu, Z., Vučković, D., Abram, M., Zhang, Q., & Možina, S. S. (2019) · Microorganisms · doi:10.3390/microorganisms7120675 · Cited by 21 · see citing works

A σE-mediated temperature gauge orchestrates type VI secretion system, biofilm formation and cell invasion in pathogen Pseudomonas plecoglossicida

Zhang, Y., Huang, Y., Ding, H., Ma, J., Tong, X., Zhang, Y., Tao, Z., & Wang, Q. (2022) · Microbiological Research · doi:10.1016/j.micres.2022.127220 · Cited by 21 · see citing works

Molecular regulation of virulence in Legionella pneumophila

Graham, C. I., MacMartin, T. L., de Kievit, T. R., & Brassinga, A. K. C. (2023) · Molecular Microbiology · doi:10.1111/mmi.15172 · Cited by 21 · see citing works

Salmonella stress response systems as targets for anti-virulence strategies

Hassanin, A., Lories, B., & Steenackers, H. P. L. (2025) · BMC Microbiology · doi:10.1186/s12866-025-04003-6 · Cited by 20 · see citing works

Adaptive Laboratory Evolution Restores Solvent Tolerance in Plasmid-Cured Pseudomonas putida S12: a Molecular Analysis

Kusumawardhani, H., Furtwängler, B., Blommestijn, M., Kaltenytė, A., van der Poel, J., Kolk, J., Hosseini, R., & de Winde, J. H. (2021) · Applied and Environmental Microbiology · doi:10.1128/aem.00041-21 · Cited by 21 · see citing works

A Critical Review on the Economically Feasible and Sustainable Poly(3-Hydroxybutyrate-co-3-hydroxyvalerate) Production from Alkyl Alcohols

Wong, H. S. J., Bhubalan, K., & Abdullah, A. A. (2022) · Polymers · doi:10.3390/polym14040670 · Cited by 20 · see citing works

The diffusible signal factor synthase, RpfF, in Xanthomonas oryzae pv. oryzae is required for the maintenance of membrane integrity and virulence

Singh, P., Verma, R. K., & Chatterjee, S. (2021) · Molecular Plant Pathology · doi:10.1111/mpp.13148 · Cited by 20 · see citing works

The Small RNA ErsA Plays a Role in the Regulatory Network of Pseudomonas aeruginosa Pathogenicity in Airway Infections

Ferrara, S., Rossi, A., Ranucci, S., Fino, I. D., Bragonzi, A., Cigana, C., & Bertoni, G. (2020) · mSphere · doi:10.1128/msphere.00909-20 · Cited by 19 · see citing works

Metagenomic insights into the microbial communities of inert and oligotrophic outdoor pier surfaces of a coastal city

Tong, X., Leung, M. H. Y., Shen, Z., Lee, J. Y. Y., Mason, C. E., & Lee, P. K. H. (2021) · Microbiome · doi:10.1186/s40168-021-01166-y · Cited by 19 · see citing works

Involvement of E. coli 6S RNA in Oxidative Stress Response

Burenina, O. Y., Elkina, D. A., Ovcharenko, A., Bannikova, V. A., Schlüter, M. A. C., Oretskaya, T. S., Hartmann, R. K., & Kubareva, E. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073653 · Cited by 18 · see citing works

Characterization of the Inflammatory Response Evoked by Bacterial Membrane Vesicles in Intestinal Cells Reveals an RIPK2-Dependent Activation by Enterotoxigenic Escherichia coli Vesicles

Thapa, H. B., Kohl, P., Zingl, F. G., Fleischhacker, D., Wolinski, H., Kufer, T. A., & Schild, S. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.01115-23 · Cited by 19 · see citing works

Quantifying the regulatory role of individual transcription factors in Escherichia coli

Guharajan, S., Chhabra, S., Parisutham, V., & Brewster, R. C. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109952 · Cited by 18 · see citing works

Cpx-signalling facilitates Hms-dependent biofilm formation by Yersinia pseudotuberculosis

Gahlot, D. K., Wai, S. N., Erickson, D. L., & Francis, M. S. (2022) · npj Biofilms and Microbiomes · doi:10.1038/s41522-022-00281-4 · Cited by 17 · see citing works

Breaking Barriers: Exploiting Envelope Biogenesis and Stress Responses to Develop Novel Antimicrobial Strategies in Gram-Negative Bacteria

Bisht, R., Charlesworth, P. D., Sperandeo, P., & Polissi, A. (2024) · Pathogens · doi:10.3390/pathogens13100889 · Cited by 17 · see citing works

Identification of Bacterial Drug-Resistant Cells by the Convolutional Neural Network in Transmission Electron Microscope Images

Hayashi, M., Aoki, K., Kishimoto, A., Takeuchi, Y., Fukushima, A., Uchida, K., Echigo, T., Yagi, Y., Hirose, M., Iwasaki, K., et al. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.839718 · Cited by 17 · see citing works

Molecular insights into Escherichia coli Cpx envelope stress response activation by the sensor lipoprotein Nl p E

Marotta, J., May, K. L., Bae, C. Y., & Grabowicz, M. (2023) · Molecular Microbiology · doi:10.1111/mmi.15054 · Cited by 17 · see citing works

A review of pathogen removal from municipal wastewater using advanced oxidation processes: Agricultural application, regrowth risks, and new perspectives

Oluoch, B., Mandizvo, T., Musazura, W., Badza, T., Otieno, B., Ojwach, S. O., & Odindo, A. O. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e39625 · Cited by 16 · see citing works

Putative Bifunctional Chorismate Mutase/Prephenate Dehydratase Contributes to the Virulence of Acidovorax citrulli

Kim, M., Lee, J. C., Heo, L., & Han, S. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.569552 · Cited by 17 · see citing works

The LiaSR Two-Component System Regulates Resistance to Chlorhexidine in Streptococcus mutans

Huang, S. H., Huang, J., Du, J., Li, Y., Wu, M., Chen, S., Zhan, L., & Huang, X. (2024) · Microorganisms · doi:10.3390/microorganisms12030468 · Cited by 15 · see citing works

Interplay between Regulatory RNAs and Signal Transduction Systems during Bacterial Infection

Piattelli, E., Johann, P., & Soutourina, O. A. (2020) · Genes · doi:10.3390/genes11101209 · Cited by 15 · see citing works

The Role of OmpR in Bile Tolerance and Pathogenesis of Adherent-Invasive Escherichia coli

Lucchini, V., Sivignon, A., Pieren, M., Gitzinger, M., Lociuro, S., Barnich, N., Kemmer, C., & Trebosc, V. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.684473 · Cited by 15 · see citing works

The choline-binding proteins PspA, PspC, and LytA of Streptococcus pneumoniae and their interaction with human endothelial and red blood cells

Vilhena, C., Du, S., Battista, M., Westermann, M., Kohler, T. P., Hammerschmidt, S., & Zipfel, P. F. (2023) · Infection and Immunity · doi:10.1128/iai.00154-23 · Cited by 14 · see citing works

A Biological Signature for the Inhibition of Outer Membrane Lipoprotein Biogenesis

Lehman, K. M., Smith, H. C., & Grabowicz, M. (2022) · mBio · doi:10.1128/mbio.00757-22 · Cited by 13 · see citing works

E. coli Common pili promote the fitness and virulence of a hybrid aEPEC/ExPEC strain within diverse host environments

Munhoz, D. D., Richards, A. C., Santos, F. F., Mulvey, M. A., & Piazza, R. M. F. (2023) · Gut Microbes · doi:10.1080/19490976.2023.2190308 · Cited by 13 · see citing works

Regulatory role of the Cpx ESR in bacterial behaviours

Wan, J., Gao, X., & Liu, F. (2024) · Virulence · doi:10.1080/21505594.2024.2404951 · Cited by 13 · see citing works

Bacillus subtilis ensures high spore quality in competition with Salmonella Typhimurium via the SigB-dependent pathway

Podnar, E., Dendinovic, K., Danevčič, T., Lories, B., Kovačec, E., Steenackers, H. P. L., & Mandić-Mulec, I. (2025) · The ISME Journal · doi:10.1093/ismejo/wraf052 · Cited by 13 · see citing works

Peptidoglycan Endopeptidase Spr of Uropathogenic Escherichia coli Contributes to Kidney Infections and Competitive Fitness During Bladder Colonization

Huang, W.-C., Hashimoto, M., Shih, Y., Wu, C., Lee, M.-F., Chen, Y.-L., Wu, J.-J., Wang, M.-C., Lin, W., Hong, M., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.586214 · Cited by 13 · see citing works

The Periplasmic Oxidoreductase DsbA Is Required for Virulence of the Phytopathogen Dickeya solani

Przepióra, T., Figaj, D., Bogucka, A. E., Fikowicz-Krośko, J., Czajkowski, R., Hugouvieux‐Cotte‐Pattat, N., & Skórko‐Glonek, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23020697 · Cited by 13 · see citing works

Global analysis of the RNA–RNA interactome in Acinetobacter baumannii AB5075 uncovers a small regulatory RNA repressing the virulence-related outer membrane protein CarO

Hamrock, F. J., Ryan, D., Shaibah, A., Ershova, A. S., Mogre, A., Sulimani, M. M., Taarit, S. B., Reichardt, S., Hokamp, K., Westermann, A. J., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae668 · Cited by 12 · see citing works

Antibacterial activity of geraniin from sugar maple leaves: an ultrastructural study with the phytopathogen Xanthomonas campestris pv. vitians

Delisle‐Houde, M., Blais, M., Tweddell, R. J., & Rioux, D. (2021) · Journal of Plant Pathology · doi:10.1007/s42161-021-00743-2 · Cited by 12 · see citing works

Stress response mechanisms and description of three novel species Shewanella avicenniae sp. nov., Shewanella sedimentimangrovi sp. nov. and Shewanella yunxiaonensis sp. nov., isolated from mangrove ecosystem

Liu, G., Zhang, Q., Rao, M. P. N., Yang, S., Tang, R., Shi, H., Wang, J., Huang, G., Liu, B., Zhou, S., et al. (2021) · Antonie van Leeuwenhoek · doi:10.1007/s10482-021-01666-9 · Cited by 12 · see citing works

The role of nitrogen-responsive regulators in controlling inorganic polyphosphate synthesis in Escherichia coli

Bowlin, M. Q., Long, A. R., Huffines, J. T., & Gray, M. J. (2022) · Microbiology · doi:10.1099/mic.0.001185 · Cited by 10 · see citing works

Type III-A CRISPR systems as a versatile gene knockdown technology

Woodside, W. T., Vantsev, N., Catchpole, R. J., Garrett, S. C., Olson, S., Graveley, B. R., & Terns, M. P. (2022) · RNA · doi:10.1261/rna.079206.122 · Cited by 12 · see citing works

Bacterial cell widening alters periplasmic size and activates envelope stress responses

Zietek, M., Miguel, A. V., Shi, H., Khusainov, I. S., Asmar, A. T., Ram, S., Wartel, M., Sueki, A., Schorb, M., Goulian, M., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00534-w · Cited by 11 · see citing works

Staphylococcal secreted cytotoxins are competition sensing signals for Pseudomonas aeruginosaPreprint

Wang, G. Z., Warren, E. A., Haas, A. L., Peña, A. S., Kiedrowski, M. R., Lomenick, B., Chou, T., Bomberger, J. M., Tirrell, D. A., & Limoli, D. H. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.29.526047 · Cited by 12 · see citing works

Transcriptome Analysis Reveals Cr(VI) Adaptation Mechanisms in Klebsiella sp. Strain AqSCr

Lara, P., Vega‐Alvarado, L., Sahonero‐Canavesi, D. X., Koenen, M., Villanueva, L., Riveros-Mckay, F., Morett, E., & Juárez, K. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.656589 · Cited by 11 · see citing works

Vibrio cholerae RND efflux systems: mediators of stress responses, colonization and pathogenesis

Bina, X. R., & Bina, J. E. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1203487 · Cited by 11 · see citing works

Aeromonas salmonicida AI-1 and AI-2 quorum sensing pathways are differentially regulated by rainbow trout mucins and during in vivo colonization

Loibman, S. O., Quintana‐Hayashi, M. P., Santos, L., & Lindén, S. K. (2024) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2024.109862 · Cited by 10 · see citing works

Dynamic feedback regulation for efficient membrane protein production using a small RNA-based genetic circuit in Escherichia coli

Guidi, C., Wannemaeker, L. D., Baets, J. D., Demeester, W., Maertens, J., Paepe, B. D., & Mey, M. D. (2022) · Microbial Cell Factories · doi:10.1186/s12934-022-01983-2 · Cited by 8 · see citing works

Exposure to High Dosage of Gold Nanoparticles Accelerates Growth Rate by Modulating Ribosomal Protein Expression.

Quadir, S., Khan, N. A., Singh, D., Faraz, A., Jhingan, G., & Joshi, M. C. (2023) · ACS Nano · doi:10.1021/acsnano.3c01973 · Cited by 9 · see citing works

A protease and a lipoprotein jointly modulate the conserved ExoR-ExoS-ChvI signaling pathway critical in Sinorhizobium meliloti for symbiosis with legume hosts

Bustamante, J. A., Ceron, J. S., Gao, I. T., Ramirez, H. A., Aviles, M., Adam, D. B., Brice, J. R., Cuellar, R. A., Dockery, E., Jabagat, M. K., et al. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010776 · Cited by 9 · see citing works

Genetic Analysis of the Role of the Conserved Inner Membrane Protein CvpA in Enterohemorrhagic Escherichia coli Resistance to Deoxycholate

Warr, A. R., Giorgio, R. T., & Waldor, M. K. (2020) · Journal of Bacteriology · doi:10.1128/jb.00661-20 · Cited by 9 · see citing works

Tolerance to Haemophilus influenzae infection in human epithelial cells: Insights from a primary cell-based model

Kappler, U., Henningham, A., Nasreen, M., Yamamoto, A., Buultjens, A. H., Stinear, T. P., Sly, P. D., & Fantino, E. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1012282 · Cited by 8 · see citing works

Stress Response of Mesosutterella multiformis Mediated by Nitrate Reduction

Ikeyama, N., Ohkuma, M., & Sakamoto, M. (2020) · Microorganisms · doi:10.3390/microorganisms8122003 · Cited by 6 · see citing works

The Global Transcription Regulator XooClp Governs Type IV Pili System-Mediated Bacterial Virulence by Directly Binding to TFP-Chp Promoters to Coordinate Virulence Associated Functions

Verma, R. K., Gondu, P., Saha, T., & Chatterjee, S. (2023) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-07-23-0100-r · Cited by 8 · see citing works

Scs system links copper and redox homeostasis in bacterial pathogens

Mendez, A. A. E., ARGÜELLO, J. M., Soncini, F. C., & Checa, S. K. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105710 · Cited by 8 · see citing works

EbfC/YbaB: A Widely Distributed Nucleoid-Associated Protein in Prokaryotes

Cordeiro, T. F. V. B., Gontijo, M. T. P., Jorge, G. P., & Brocchi, M. (2022) · Microorganisms · doi:10.3390/microorganisms10101945 · Cited by 8 · see citing works

A putative glucose 6-phosphate isomerase has pleiotropic functions on virulence and other mechanisms in Acidovorax citrulli

Heo, L., Han, Y., Cho, Y., Choi, J., Lee, J.-W., & Han, S. (2023) · Frontiers in Plant Science · doi:10.3389/fpls.2023.1275438 · Cited by 7 · see citing works

Survival and Expression of rpoS and grxB of Cronobacter sakazakii in Powdered Infant Formula Under Simulated Gastric Conditions of Newborns

Kireina, D., Parreira, V. R., Goodridge, L. D., & Farber, J. M. (2024) · Journal of Food Protection · doi:10.1016/j.jfp.2024.100269 · Cited by 7 · see citing works

Long-chain fatty acids as nutrients for Gram-negative bacteria: stress, proliferation, and virulence

Shrivastava, M., Roy, D., & Chaba, R. (2025) · Current Opinion in Microbiology · doi:10.1016/j.mib.2025.102609 · Cited by 7 · see citing works

Elucidation of Essential Genes and Mutant Fitness during Adaptation toward Nitrogen Fixation Conditions in the Endophyte Azoarcus olearius BH72 Revealed by Tn-Seq

Harten, T., Nimzyk, R., Gawlick, V. E. A., & Reinhold‐Hurek, B. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.02162-22 · Cited by 7 · see citing works

Identification of genes involved in exoprotein release using a high-throughput exoproteome screening assay in Yersinia entomophaga

Schoof, M., O’Callaghan, M., Sheen, C. R., Glare, T. R., & Hurst, M. R. H. (2022) · PLoS ONE · doi:10.1371/journal.pone.0263019 · Cited by 7 · see citing works

Simulated Colonic Fluid Replicates the In Vivo Growth Capabilities of Citrobacter rodentium cpxRA Mutants and Uncovers Additive Effects of Cpx-Regulated Genes on Fitness

Gilliland, A., Gavino, C., Gruenheid, S., & Raivio, T. L. (2022) · Infection and Immunity · doi:10.1128/iai.00314-22 · Cited by 7 · see citing works

Identification of Genes Required for Long-Term Survival of Legionella pneumophila in Water

Auraß, P., Kim, S., Pinedo, V., Cava, F., & Isberg, R. R. (2023) · mSphere · doi:10.1128/msphere.00454-22 · Cited by 8 · see citing works

The BfmRS stress response protects Acinetobacter baumannii against defects in outer membrane lipoprotein biogenesis

Marotta, J., Zhao, A., Rather, P. N., & Grabowicz, M. (2024) · Journal of Bacteriology · doi:10.1128/jb.00332-24 · Cited by 6 · see citing works

Transcriptional and post-transcriptional mechanisms modulate cyclopropane fatty acid synthase through small RNAs in Escherichia coli

Bianco, C. M., Caballero-Rothar, N. N., Ma, X., Farley, K. R., & Vanderpool, C. K. (2024) · Journal of Bacteriology · doi:10.1128/jb.00049-24 · Cited by 6 · see citing works

AlgU mediates hyperosmotic tolerance in Pseudomonas protegens SN15-2 by regulating membrane stability, ROS scavenging, and osmolyte synthesis

Wang, J., Wang, Y., Lu, S., Lou, H., Wang, X., & Wang, W. (2024) · Applied and Environmental Microbiology · doi:10.1128/aem.00596-24 · Cited by 6 · see citing works

Essential role of extracytoplasmic proteins in the resistance of Gluconacetobacter diazotrophicus to cadmium

Moreira, J. R., Leandro, M. R., Vespoli, L. D. S., Andrade, L. F., Pimentel, V. R., Soares, F. S., de Souza, S. A., Intorne, A. C., Silveira, V., & Filho, G. A. D. S. (2022) · Research in Microbiology · doi:10.1016/j.resmic.2022.103922 · Cited by 6 · see citing works

Boron nutrition affects growth, adaptation to stressful environments, and exopolysaccharide synthesis of Ensifer meliloti

Quijada, N. M., Abreu, I., Reguera, M., Bonilla, I., & Bolaños, L. (2022) · Rhizosphere · doi:10.1016/j.rhisph.2022.100534 · Cited by 6 · see citing works

Stress response in Escherichia coli following sublethal phenalene-1-one mediated antimicrobial photodynamic therapy: an RNA-Seq study

Muehler, D., Morini, S. R., Geißert, J., Engesser, C., Hiller, K., Widbiller, M., Maisch, T., Buchalla, W., & Cieplik, F. (2024) · Photochemical & Photobiological Sciences · doi:10.1007/s43630-024-00617-3 · Cited by 5 · see citing works

Lactobacillus brevis ZFM820 Attenuates LPS-Induced Inflammation via Biofilm Formation and Metabolic Reprogramming

Li, Y., Yan, S., Chen, Y., Chen, S., Zhang, M., Jiang, L., Song, H., Wu, C., Bi, Y., Yu, J., et al. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c09513 · Cited by 5 · see citing works

A Two-Component-System-Governed Regulon That Includes a β-Lactamase Gene is Responsive to Cell Envelope Disturbance

Lee, D., Park, J., Yi, H., Cho, K., & Kim, H. S. (2022) · mBio · doi:10.1128/mbio.01749-22 · Cited by 5 · see citing works

Hfq protein and GcvB small RNA tailoring of oppA target mRNA to levels allowing translation activation by MicF small RNA in Escherichia coli

Carrier, M., Lalaouna, D., & Massé, É. (2023) · RNA Biology · doi:10.1080/15476286.2023.2179582 · Cited by 5 · see citing works

A Single Residue within the MCR-1 Protein Confers Anticipatory Resilience

Frantz, R., Gwozdzinski, K., Gisch, N., Doijad, S. P., Hudel, M., Wille, M., Mraheil, M. A., Schwudke, D., Imirzalioglu, C., Falgenhauer, L., et al. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.03592-22 · Cited by 5 · see citing works

The role of CenKR in the coordination ofRhodobacter sphaeroidescell elongation and division

Lakey, B. D., Alberge, F., Parrell, D., Wright, E., Noguera, D. R., & Donohue, T. J. (2023) · mBio · doi:10.1128/mbio.00631-23 · Cited by 5 · see citing works

Increased Synthesis of a Magnesium Transporter MgtA During Recombinant Autotransporter Expression in Escherichia coli

Petrovskaya, L. E., Ziganshin, R., Kryukova, E. A., Zlobinov, A. V., Gapizov, S. S., Shingarova, L. N., Mironov, V. A., Lomakina, G. Y., Dolgikh, D. A., & Kirpichnikov, M. P. (2021) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-021-03634-5 · Cited by 5 · see citing works

Microbial Chemical Sensing of Microplastic-Derived Compounds in Insect Gut Ecosystems

Shah, S., Ilyas, M., Refaie, A., & Yang, F. (2026) · Environmental Science & Technology · doi:10.1021/acs.est.5c12962 · Cited by 6 · see citing works

The structures and functions of Salmonella outer membrane

Liu, X., Zheng, H., J, J., Zhao, J., Ma, Y., Sun, J., Guo, Z., Wang, Y., Li, Y., Wang, Y., et al. (2026) · Archives of Microbiology · doi:10.1007/s00203-026-04716-w · Cited by 5 · see citing works

RNA-seq reveals multifaceted gene expression response to Fab production in Escherichia coli fed-batch processes with particular focus on ribosome stalling

Vazulka, S., Schiavinato, M., Tauer, C., Wagenknecht, M., Cserjan‐Puschmann, M., & Striedner, G. (2024) · Microbial Cell Factories · doi:10.1186/s12934-023-02278-w · Cited by 4 · see citing works

The CpxAR signaling system confers a fitness advantage for flea gut colonization by the plague bacillus

Robin, B., Dewitte, A., Alaimo, V., Lecœur, C., Pierre, F., Gabriel Billon, A., Sebbane, F., & Bontemps‐Gallo, S. (2024) · Journal of Bacteriology · doi:10.1128/jb.00173-24 · Cited by 4 · see citing works

Unveiling Salmonella Derby Survival: Stress Responses to Prolonged Hyperosmotic Stress

Gong, Y., Li, X., Wang, J., Zhao, Y., Meng, J., & Zhai, L. (2025) · Foods · doi:10.3390/foods14091440 · Cited by 4 · see citing works

Transcriptional Responses of Pseudomonas aeruginosa to Inhibition of Lipoprotein Transport by a Small Molecule Inhibitor

Lorenz, C., Dougherty, T. J., & Lory, S. J. (2020) · Journal of Bacteriology · doi:10.1128/jb.00452-20 · Cited by 4 · see citing works

MicroReview: Envelope stress responses and Gram‐negative bacterial pathogenesis

Raivio, T. L. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04625.x · Cited by 307 · see citing works

Homeostasis of the Gram-negative cell envelope

Saha, S., Lach, S. R., & Konovalova, A. (2021) · Current Opinion in Microbiology · doi:10.1016/j.mib.2021.03.008 · Cited by 43 · see citing works

Regulatory role of the Cpx ESR in bacterial behaviours

Wan, J., Gao, X., & Liu, F. (2024) · Virulence · doi:10.1080/21505594.2024.2404951 · Cited by 13 · see citing works

Pushing the envelope: extracytoplasmic stress responses in bacterial pathogens

Rowley, G., Spector, M. P., Kormanec, J., & Roberts, M. (2006) · Nature Reviews Microbiology · doi:10.1038/nrmicro1394 · Cited by 321 · see citing works

Regulation of bacterial virulence gene expression by cell envelope stress responses

Flores-Kim, J., & Darwin, A. J. (2014) · Virulence · doi:10.4161/21505594.2014.965580 · Cited by 45 · see citing works