The complex rcs regulatory cascade.

Many roads to maturity: microRNA biogenesis pathways and their regulation

Winter, J. J., Jung, S., Keller, S., Gregory, R. I., & Diederichs, S. (2009) · Nature Cell Biology · doi:10.1038/ncb0309-228 · Cited by 2,646 · see citing works

Biosynthesis and Assembly of Capsular Polysaccharides in Escherichia coli

Whitfield, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142545 · Cited by 993 · see citing works

Biological Insights from Structures of Two-Component Proteins

Gao, R., & Stock, A. (2009) · Annual Review of Microbiology · doi:10.1146/annurev.micro.091208.073214 · Cited by 793 · see citing works

Exopolysaccharide Production Is Required for Development of Escherichia coli K-12 Biofilm Architecture

Danese, P. N., Pratt, L. A., & Kolter, R. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.12.3593-3596.2000 · Cited by 656 · see citing works

THE RCS PHOSPHORELAY: A Complex Signal Transduction System

Majdalani, N., & Gottesman, S. (2005) · Annual Review of Microbiology · doi:10.1146/annurev.micro.59.050405.101230 · Cited by 560 · see citing works

Molecular Mechanisms of Two-Component Signal Transduction

Zschiedrich, C. P., Keidel, V., & Szurmant, H. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.003 · Cited by 540 · see citing works

The EcoCyc database: reflecting new knowledge aboutEscherichia coliK-12

Keseler, I. M., Mackie, A. M., Santos-Zavaleta, A., Billington, R., Bonavides-Martínez, C., Caspi, R., Fulcher, C. A., Gama‐Castro, S., Kothari, A., Krummenacker, M., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1003 · Cited by 525 · see citing works

Structure of the outer membrane protein A transmembrane domain

Pautsch, A., & Schulz, G. E. (1998) · Nature Structural Biology · doi:10.1038/2983 · Cited by 476 · see citing works

Large‐scale monitoring of pleiotropic regulation of gene expression by the prokaryotic nucleoid‐associated protein, H‐NS

Hommais, F., Krin, E., Laurent‐Winter, C., Soutourina, O. A., Malpertuy, A., Caër, J. L., Danchin, A., & Bertin, P. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02358.x · Cited by 436 · see citing works

Regulation and mode of action of the second small RNA activator of RpoS translation, RprA

Majdalani, N., Hernández, D., & Gottesman, S. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03203.x · Cited by 371 · see citing works

Microbial Genetic Composition Tunes Host Longevity

Han, B., Sivaramakrishnan, P., Lin, C.-C., Neve, I. A. A., He, J., Tay, L. W. R., Sowa, J. N., Sizovs, A., Du, G., Wang, J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.05.036 · Cited by 349 · see citing works

Structure of the entire cytoplasmic portion of a sensor histidine‐kinase protein

Marina, A., Waldburger, C. D., & Hendrickson, W. A. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600886 · Cited by 299 · see citing works

The Rcs Phosphorelay Is a Cell Envelope Stress Response Activated by Peptidoglycan Stress and Contributes to Intrinsic Antibiotic Resistance

Laubacher, M. E., & Ades, S. E. (2008) · Journal of Bacteriology · doi:10.1128/jb.01740-07 · Cited by 276 · see citing works

RcsB and RcsC: a two-component regulator of capsule synthesis in Escherichia coli

Stout, V., & Gottesman, S. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.2.659-669.1990 · Cited by 275 · see citing works

Regulation of capsular polysaccharide synthesis in Escherichia coli K-12: characterization of three regulatory genes

Gottesman, S., Trisler, P., & Torres-Cabassa, A. (1985) · Journal of Bacteriology · doi:10.1128/jb.162.3.1111-1119.1985 · Cited by 273 · see citing works

RmpA Regulation of Capsular Polysaccharide Biosynthesis in Klebsiella pneumoniae CG43

Cheng, H., Chen, Y., Wu, C.-C., Chang, H. Y., Lai, Y., & Peng, H. (2010) · Journal of Bacteriology · doi:10.1128/jb.00031-10 · Cited by 270 · see citing works

A small RNA acts as an antisilencer of the H-NS-silenced rcsA gene of Escherichia coli.

Sledjeski, D. D., & Gottesman, S. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.6.2003 · Cited by 246 · see citing works

The RcsC sensor kinase is required for normal biofilm formation in Escherichia coli K‐12 and controls the expression of a regulon in response to growth on a solid surface

Ferrières, L., & Clarke, D. J. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03815.x · Cited by 245 · see citing works

Capsule synthesis in Escherichia coli K-12 is regulated by proteolysis

Torres-Cabassa, A., & Gottesman, S. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.3.981-989.1987 · Cited by 244 · see citing works

A Comprehensive Genetic Characterization of Bacterial Motility

Girgis, H. S., Liu, Y., Ryu, W. S., & Tavazoie, S. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030154 · Cited by 237 · see citing works

Snapshots of DsbA in Action: Detection of Proteins in the Process of Oxidative Folding

Kadokura, H., Tian, H., Zander, T., Bardwell, J. C. A., & Beckwith, J. (2004) · Science · doi:10.1126/science.1091724 · Cited by 234 · see citing works

A novel feature of the multistep phosphorelay in Escherichia coli: a revised model of the RcsC → YojN → RcsB signalling pathway implicated in capsular synthesis and swarming behaviour

Takeda, S., Fujisawa, Y., Matsubara, M., Aiba, H., & Mizuno, T. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02393.x · Cited by 215 · see citing works

Gene expression patterns during swarming in Salmonella typhimurium: genes specific to surface growth and putative new motility and pathogenicity genes

Wang, Q., Frye, J. G., McClelland, M., & Harshey, R. M. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2003.03977.x · Cited by 214 · see citing works

Connecting two-component regulatory systems by a protein that protects a response regulator from dephosphorylation by its cognate sensorPreprint

Kato, A., & Groisman, E. A. (2004) · Genes & Development · doi:10.1101/gad.1230804 · Cited by 208 · see citing works

GadE (YhiE): a novel activator involved in the response to acid environment in Escherichia coli

Hommais, F., Krin, E., Coppée, J., Lacroix, C., Yeramian, E., Danchin, A., & Bertin, P. (2003) · Microbiology · doi:10.1099/mic.0.26659-0 · Cited by 182 · see citing works

The RcsAB Box

Wehland, M., & Bernhard, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.7013 · Cited by 169 · see citing works

Detecting Envelope Stress by Monitoring β-Barrel Assembly

Cho, S.-H., Szewczyk, J., Pesavento, C., Zietek, M., Banzhaf, M., Roszczenko, P., Asmar, A. T., Laloux, G., Hov, A. K., Leverrier, P., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.045 · Cited by 166 · see citing works

Genome-Wide Analyses Revealing a Signaling Network of the RcsC-YojN-RcsB Phosphorelay System in Escherichia coli

Hagiwara, D., Sugiura, M., Oshima, T., Mori, H., Aiba, H., Yamashino, T., & Mizuno, T. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.19.5735-5746.2003 · Cited by 163 · see citing works

Fine-structure mapping and identification of two regulators of capsule synthesis in Escherichia coli K-12

Brill, J. A., Quinlan-Walshe, C., & Gottesman, S. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.6.2599-2611.1988 · Cited by 157 · see citing works

lon transcriptional regulation of genes necessary for capsular polysaccharide synthesis in Escherichia coli K-12

Trisler, P., & Gottesman, S. (1984) · Journal of Bacteriology · doi:10.1128/jb.160.1.184-191.1984 · Cited by 152 · see citing works

Retracing the Evolutionary Path that Led to Flea-Borne Transmission of Yersinia pestis

Sun, Y., Jarrett, C. O., Bosio, C. F., & Hinnebusch, B. J. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.04.003 · Cited by 151 · see citing works

Acid stress response in Escherichia coli: mechanism of regulation of gadA transcription by RcsB and GadE

Castanié‐Cornet, M., Cam, K., Bastiat, B., Cros, A., Bordes, P., & Gutierrez, C. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq097 · Cited by 146 · see citing works

Role of RcsF in Signaling to the Rcs Phosphorelay Pathway inEscherichia coli

Majdalani, N., Heck, M. C., Stout, V., & Gottesman, S. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.19.6770-6778.2005 · Cited by 146 · see citing works

Salmonella enterica Serovar Typhimurium Response Involved in Attenuation of Pathogen Intracellular Proliferation

Cano, D. A., Martı́nez-Moya, M., Pucciarelli, M. G., Groisman, E. A., Casadesús, J., & del Portillo, F. G. (2001) · Infection and Immunity · doi:10.1128/iai.69.10.6463-6474.2001 · Cited by 138 · see citing works

Communication across the bacterial cell envelope depends on the size of the periplasm

Asmar, A. T., Ferreira, J. L., Cohen, E. J., Cho, S.-H., Beeby, M., Hughes, K. T., & Collet, J. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2004303 · Cited by 132 · see citing works

The Rcs Phosphorelay: More Than Just A Two-Component Pathway

Clarke, D. J. (2010) · Future Microbiology · doi:10.2217/fmb.10.83 · Cited by 129 · see citing works

Control of the Salmonella ugd gene by three two‐component regulatory systems

Mouslim, C., & Groisman, E. A. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03318.x · Cited by 127 · see citing works

Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins

Konovalova, A., Perlman, D. H., Cowles, C. E., & Silhavy, T. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417138111 · Cited by 122 · see citing works

Outer membrane lipoprotein biogenesis: Lol is not the end

Konovalova, A., & Silhavy, T. J. (2015) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2015.0030 · Cited by 122 · see citing works

Antimicrobial Peptides Activate the Rcs Regulon through the Outer Membrane Lipoprotein RcsF

Farris, C., Sanowar, S., Bader, M. W., Pfuetzner, R. A., & Miller, S. I. (2010) · Journal of Bacteriology · doi:10.1128/jb.00505-10 · Cited by 121 · see citing works

The RcsCDB Signaling System and Swarming Motility inSalmonella entericaSerovar Typhimurium: Dual Regulation of Flagellar and SPI-2 Virulence Genes

Wang, Q., Zhao, Y., McClelland, M., & Harshey, R. M. (2007) · Journal of Bacteriology · doi:10.1128/jb.01198-07 · Cited by 121 · see citing works

Regulation of Capsule Synthesis and Cell Motility in Salmonella enterica by the Essential Gene igaA

Cano, D. A., Domínguez‐Bernal, G., Tiérrez, A., del Portillo, F. G., & Casadesús, J. (2002) · Genetics · doi:10.1093/genetics/162.4.1513 · Cited by 118 · see citing works

Involvement of Two-Component Signaling on Bacterial Motility and Biofilm Development

Prüß, B. M. (2017) · Journal of Bacteriology · doi:10.1128/jb.00259-17 · Cited by 118 · see citing works

A lipoprotein/β-barrel complex monitors lipopolysaccharide integrity transducing information across the outer membrane

Konovalova, A., Mitchell, A. M., & Silhavy, T. J. (2016) · eLife · doi:10.7554/elife.15276 · Cited by 113 · see citing works

Acetyl phosphate‐sensitive regulation of flagellar biogenesis and capsular biosynthesis depends on the Rcs phosphorelay

Fredericks, C. E., Shibata, S., Aizawa, S.-I., Reimann, S. A., & Wolfe, A. J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05260.x · Cited by 112 · see citing works

Genetic and Biochemical Dissection of a HisKA Domain Identifies Residues Required Exclusively for Kinase and Phosphatase Activities

Willett, J. W., & Kirby, J. R. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1003084 · Cited by 111 · see citing works

Experimental evidence for negative selection in the evolution of a Yersinia pestis pseudogene

Sun, Y., Hinnebusch, B. J., & Darby, C. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0803525105 · Cited by 109 · see citing works

RcsF Is an Outer Membrane Lipoprotein Involved in the RcsCDB Phosphorelay Signaling Pathway in Escherichia coli

Castanié‐Cornet, M., Cam, K., & Jacq, A. (2006) · Journal of Bacteriology · doi:10.1128/jb.00004-06 · Cited by 108 · see citing works

Escherichia coli RcsA, a Positive Activator of Colanic Acid Capsular Polysaccharide Synthesis, Functions To Activate Its Own Expression

Ebel, W., & Trempy, J. E. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.2.577-584.1999 · Cited by 105 · see citing works

Activation of the Rcs Signal Transduction System Is Responsible for the Thermosensitive Growth Defect of anEscherichia coliMutant Lacking Phosphatidylglycerol and Cardiolipin

Shiba, Y., Yokoyama, Y., Aono, Y., Kiuchi, T., Kusaka, J., Matsumoto, K., & Hara, H. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.19.6526-6535.2004 · Cited by 103 · see citing works

Novel genes that upregulate the Proteus mirabilis flhDC master operon controlling flagellar biogenesis and swarming

Dufour, A., Furness, R. B., & Hughes, C. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00967.x · Cited by 100 · see citing works

Regulation of osmC Gene Expression by the Two-Component System rcsB-rcsC in Escherichia coli

Davalos, M., Conter, A., Toesca, I. J., Gutierrez, C., & Cam, K. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.20.5870-5876.2001 · Cited by 99 · see citing works

The Rcs phosphorelay system is specific to enteric pathogens/commensals and activates ydeI , a gene important for persistent Salmonella infection of mice

Erickson, K. D., & Detweiler, C. S. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05420.x · Cited by 98 · see citing works

Enhancement of extracapsular polysaccharide synthesis in Klebsiella pneumoniae by RmpA2, which shows homology to NtrC and FixJ

Wacharotayankun, R., Arakawa, Y., Ohta, M., Tanaka, K., Akashi, T., Mori, M., & Kato, N. (1993) · Infection and Immunity · doi:10.1128/iai.61.8.3164-3174.1993 · Cited by 97 · see citing works

Xenogeneic Silencing and Its Impact on Bacterial Genomes

Singh, K., Milstein, J. N., & Navarre, W. W. (2016) · Annual Review of Microbiology · doi:10.1146/annurev-micro-102215-095301 · Cited by 95 · see citing works

Identification, cloning, and characterization of rcsF, a new regulator gene for exopolysaccharide synthesis that suppresses the division mutation ftsZ84 in Escherichia coli K-12

Gervais, F. G., & Drapeau, G. R. (1992) · Journal of Bacteriology · doi:10.1128/jb.174.24.8016-8022.1992 · Cited by 94 · see citing works

Transcriptional organization and regulation of the Escherichia coli K30 group 1 capsule biosynthesis (cps) gene cluster

Rahn, A., & Whitfield, C. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03354.x · Cited by 93 · see citing works

Fe(III)‐mediated cellular toxicity

Chamnongpol, S., Dodson, W., Cromie, M. J., Harris, Z. L., & Groisman, E. A. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03041.x · Cited by 93 · see citing works

Repression of the RcsC‐YojN‐RcsB phosphorelay by the IgaA protein is a requisite for Salmonella virulence

Domínguez‐Bernal, G., Pucciarelli, M. G., Ramos‐Morales, F., García‐Quintanilla, M., Cano, D. A., Casadesús, J., & del Portillo, F. G. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04213.x · Cited by 92 · see citing works

The TviA auxiliary protein renders the Salmonella enterica serotype Typhi RcsB regulon responsive to changes in osmolarity

Winter, S., Winter, M. G., Thiennimitr, P., Gerriets, V. A., Nuccio, S., Rüssmann, H., & Bäumler, A. J. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06859.x · Cited by 90 · 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

The yjbEFGH locus in Escherichia coli K-12 is an operon encoding proteins involved in exopolysaccharide production

Ferrières, L., Aslam, S. N., Cooper, R. M., & Clarke, D. J. (2007) · Microbiology · doi:10.1099/mic.0.2006/002907-0 · Cited by 85 · see citing works

An essential sensor histidine kinase controlled by transmembrane helix interactions with its auxiliary proteins

Szurmant, H., Bu, L., Brooks, C. L., & Hoch, J. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800247105 · Cited by 83 · see citing works

The Rcs Stress Response and Accessory Envelope Proteins Are Required for De Novo Generation of Cell Shape in Escherichia coli

Ranjit, D. K., & Young, K. D. (2013) · Journal of Bacteriology · doi:10.1128/jb.00160-13 · Cited by 82 · see citing works

Small RNA-based feedforward loop with AND-gate logic regulates extrachromosomal DNA transfer in Salmonella

Papenfort, K., Espinosa, E., Casadesús, J., & Vogel, J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1507825112 · Cited by 79 · 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

Two variable active site residues modulate response regulator phosphoryl group stability

Thomas, S., Brewster, J. A., & Bourret, R. B. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06296.x · Cited by 75 · see citing works

BglJ-RcsB Heterodimers Relieve Repression of theEscherichia coli bglOperon by H-NS

Venkatesh, G. R., Koungni, F. C. K., Paukner, A., Stratmann, T., Blissenbach, B., & Schnetz, K. (2010) · Journal of Bacteriology · doi:10.1128/jb.00807-10 · Cited by 74 · see citing works

Salmonella Biofilm Development Depends on the Phosphorylation Status of RcsB

Latasa, C., García, B., Echeverz, M., Toledo‐Arana, A., Valle, J., Campoy, S., del Portillo, F. G., Solano, C., & Lasa, Í. (2012) · Journal of Bacteriology · doi:10.1128/jb.00361-12 · Cited by 74 · see citing works

Signal-dependent Requirement for the Co-activator Protein RcsA in Transcription of the RcsB-regulated ugd Gene

Mouslim, C., Latifi, T. N., & Groisman, E. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309433200 · Cited by 72 · see citing works

Role of the Heat Shock Protein DnaJ in the Lon-dependent Degradation of Naturally Unstable Proteins

Jubete, Y., Maurizi, M. R., & Gottesman, S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30798 · Cited by 72 · see citing works

The glutamate-dependent acid resistance system in Escherichia coli: essential and dual role of the His–Asp phosphorelay RcsCDB/AF

Castanié‐Cornet, M., Daniels‐Treffandier, H., Francez‐Charlot, A., Gutierrez, C., & Cam, K. (2006) · Microbiology · doi:10.1099/mic.0.29278-0 · Cited by 71 · see citing works

Capsule Production and Glucose Metabolism Dictate Fitness during Serratia marcescens Bacteremia

Anderson, M. T., Mitchell, L. A., Zhao, L., & Mobley, H. L. T. (2017) · mBio · doi:10.1128/mbio.00740-17 · Cited by 70 · see citing works

Genome-Wide Mutant Fitness Profiling Identifies Nutritional Requirements for Optimal Growth of Yersinia pestis in Deep Tissue

Palace, S. G., Proulx, M. K., Lu, S., Baker, R. E., & Goguen, J. D. (2014) · mBio · doi:10.1128/mbio.01385-14 · Cited by 68 · see citing works

Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC

Leverrier, P., Declercq, J., Denoncin, K., Vertommen, D., Hiniker, A. O., Cho, S.-H., & Collet, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.224865 · Cited by 68 · see citing works

Alternative pathways for Escherichia coli biofilm formation revealed by sRNA overproduction

Parker, A., Cureoglu, S., Lay, N. R. D., Majdalani, N., & Gottesman, S. (2017) · Molecular Microbiology · doi:10.1111/mmi.13702 · Cited by 65 · see citing works

DjlA Is a Third DnaK Co-chaperone of Escherichia coli, and DjlA-mediated Induction of Colanic Acid Capsule Requires DjlA-DnaK Interaction

Genevaux, P., Wawrzynów, A., Żylicz, M., Georgopoulos, C. P., & Kelley, W. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m003855200 · Cited by 64 · see citing works

Involvement of WalK ( VicK ) phosphatase activity in setting WalR ( VicR ) response regulator phosphorylation level and limiting cross‐talk in S treptococcus pneumoniae D 39 cells

Wayne, K. J., Li, S., Kazmierczak, K. M., Tsui, H. T., & Winkler, M. E. (2012) · Molecular Microbiology · doi:10.1111/mmi.12006 · Cited by 63 · see citing works

LrhA RegulatesrpoSTranslation in Response to the Rcs Phosphorelay System inEscherichia coli

Peterson, C. N., Carabetta, V. J., Chowdhury, T., & Silhavy, T. J. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.9.3175-3181.2006 · Cited by 60 · see citing works

Virulence attenuation in Salmonella enterica rcsC mutants with constitutive activation of the Rcs system

García-Calderón, C. B., García‐Quintanilla, M., Casadesús, J., & Ramos‐Morales, F. (2005) · Microbiology · doi:10.1099/mic.0.27520-0 · Cited by 60 · see citing works

The Rcs Two-Component System Regulates Expression of Lysozyme Inhibitors and Is Induced by Exposure to Lysozyme

Callewaert, L., Vanoirbeek, K. G. A., Lurquin, I., Michiels, C. W., & Aertsen, A. (2009) · Journal of Bacteriology · doi:10.1128/jb.01549-08 · Cited by 59 · see citing works

Genome-Wide Identification of Genes Regulated by the Rcs Phosphorelay System in Erwinia amylovora

Wang, D., Qi, M., Calla, B., Korban, S. S., Clough, S. J., Cock, P., Sundin, G. W., Toth, I. K., & Zhao, Y. F. (2011) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-08-11-0207 · Cited by 57 · see citing works

Genome Expression Analyses Revealing the Modulation of the Salmonella Rcs Regulon by the Attenuator IgaA

Mariscotti, J. F., & del Portillo, F. G. (2009) · Journal of Bacteriology · doi:10.1128/jb.01604-08 · Cited by 57 · see citing works

Distinct domains of Escherichia coli IgaA connect envelope stress sensing and down-regulation of the Rcs phosphorelay across subcellular compartments

Hussein, N. A., Cho, S.-H., Laloux, G., Siam, R., & Collet, J. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007398 · Cited by 55 · see citing works

The Rcs-Regulated Colanic Acid Capsule Maintains Membrane Potential in Salmonella enterica serovar Typhimurium

Pando, J. M., Karlinsey, J. E., Lara, J. C., Libby, S. J., & Fang, F. C. (2017) · mBio · doi:10.1128/mbio.00808-17 · Cited by 53 · see citing works

The Rcs regulon in Proteus mirabilis: implications for motility, biofilm formation, and virulence

Howery, K. E., Clemmer, K. M., & Rather, P. N. (2016) · Current Genetics · doi:10.1007/s00294-016-0579-1 · Cited by 52 · see citing works

RcsB‐BglJ activates the Escherichia coli leuO gene, encoding an H‐NS antagonist and pleiotropic regulator of virulence determinants

Stratmann, T., Pul, Ü., Wurm, R., Wagner, R., & Schnetz, K. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.07993.x · Cited by 50 · see citing works

Role of the Umo Proteins and the Rcs Phosphorelay in the Swarming Motility of the Wild Type and an O-Antigen ( waaL ) Mutant of Proteus mirabilis

Morgenstein, R. M., & Rather, P. N. (2011) · Journal of Bacteriology · doi:10.1128/jb.06047-11 · Cited by 50 · see citing works

Exploring the relationship between lipoprotein mislocalization and activation of the Rcs signal transduction system in Escherichia coli

Shiba, Y., Miyagawa, H., Nagahama, H., Matsumoto, K., Kondo, D., Matsuoka, S., Matsumoto, K., & Hara, H. (2012) · Microbiology · doi:10.1099/mic.0.056945-0 · Cited by 49 · see citing works

The Response Regulator RcsB Activates Expression of Mat Fimbriae in Meningitic Escherichia coli

Lehti, T. A., Heikkinen, J., Korhonen, T., & Westerlund‐Wikström, B. (2012) · Journal of Bacteriology · doi:10.1128/jb.06596-11 · Cited by 47 · see citing works

The fimbriae activator MatA switches off motility in Escherichia coli by repression of the flagellar master operon flhDC

Lehti, T. A., Bauchart, P., Dobrindt, U., Korhonen, T., & Westerlund‐Wikström, B. (2012) · Microbiology · doi:10.1099/mic.0.056499-0 · Cited by 46 · see citing works

Multistress Regulation inEscherichia coli: Expression ofosmBInvolves Two Independent Promoters Responding either to σSor to the RcsCDB His-Asp Phosphorelay

Boulanger, A., Francez‐Charlot, A., Conter, A., Castanié‐Cornet, M., Cam, K., & Gutierrez, C. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.9.3282-3286.2005 · Cited by 45 · see citing works

Colanic Acid Intermediates Prevent De Novo Shape Recovery of Escherichia coli Spheroplasts, Calling into Question Biological Roles Previously Attributed to Colanic Acid

Ranjit, D. K., & Young, K. D. (2016) · Journal of Bacteriology · doi:10.1128/jb.01034-15 · Cited by 45 · see citing works

Major Tom to Ground Control: How Lipoproteins Communicate Extracytoplasmic Stress to the Decision Center of the Cell

Laloux, G., & Collet, J. (2017) · Journal of Bacteriology · doi:10.1128/jb.00216-17 · Cited by 45 · see citing works

Osmotic Regulation of theEscherichia coli bdm(Biofilm-Dependent Modulation) Gene by the RcsCDB His-Asp Phosphorelay

Francez‐Charlot, A., Castanié‐Cornet, M., Gutierrez, C., & Cam, K. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.11.3873-3877.2005 · Cited by 44 · see citing works

RcsAB is a major repressor of Yersinia biofilm development through directly acting on hmsCDE, hmsT and hmsHFRS

Fang, N., Yang, H., Fang, H., Liu, L., Zhang, Y., Wang, L., Han, Y., Zhou, D., & Yang, R. (2015) · Scientific Reports · doi:10.1038/srep09566 · Cited by 42 · see citing works

A New Structural Domain in the Escherichia coli RcsC Hybrid Sensor Kinase Connects Histidine Kinase and Phosphoreceiver Domains

Rogov, V. V., Rogova, N. Y., Bernhard, F., Koglin, A., Löhr, F., & Dötsch, V. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.07.052 · Cited by 39 · see citing works

Transcriptional regulation by BglJ–RcsB, a pleiotropic heteromeric activator in Escherichia coli

Salscheider, S. L., Jahn, A., & Schnetz, K. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1298 · Cited by 37 · see citing works

Analysis of theEscherichia coliAlp Phenotype: Heat Shock Induction inssrAMutants

Munavar, H., Zhou, Y., & Gottesman, S. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.14.4739-4751.2005 · Cited by 37 · see citing works

A Disulfide Bridge Network within the Soluble Periplasmic Domain Determines Structure and Function of the Outer Membrane Protein RCSF

Rogov, V. V., Rogova, N. Y., Bernhard, F., Löhr, F., & Dötsch, V. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.230185 · Cited by 34 · see citing works

Defective Lipoprotein Sorting Induces lolA Expression through the Rcs Stress Response Phosphorelay System

Tao, K., Narita, S., & Tokuda, H. (2012) · Journal of Bacteriology · doi:10.1128/jb.00553-12 · Cited by 34 · see citing works

Lysis induction of Escherichia coli by the cloned lysis protein of the phage MS2 depends on the presence of osmoregulatory membrane-derived oligosaccharides.

Höltje, J. V., Fiedler, W., Rotering, H., Walderich, B., & DUIN, J. V. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68956-2 · Cited by 32 · see citing works

Solution Structure of the Escherichia coli YojN Histidine-phosphotransferase Domain and its Interaction with Cognate Phosphoryl Receiver Domains

Rogov, V. V., Bernhard, F., Löhr, F., & Dötsch, V. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.096 · Cited by 31 · see citing works

The Salmonella Membrane Protein IgaA Modulates the Activity of the RcsC-YojN-RcsB and PhoP-PhoQ Regulons

Tiérrez, A., & del Portillo, F. G. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.22.7481-7489.2004 · Cited by 30 · see citing works

The Virulence of aDickeya dadantii3937 Mutant Devoid of Osmoregulated Periplasmic Glucans Is Restored by Inactivation of the RcsCD-RcsB Phosphorelay

Bouchart, F., Boussemart, G., Prouvost, A.-F., Cogez, V., Madec, E., Vidal, O., Delrue, B., Bohin, J., & Lacroix, J.-M. (2010) · Journal of Bacteriology · doi:10.1128/jb.00143-10 · Cited by 28 · see citing works

An IgaA/UmoB Family Protein from Serratia marcescens Regulates Motility, Capsular Polysaccharide Biosynthesis, and Secondary Metabolite Production

Stella, N. A., Brothers, K. M., Callaghan, J. D., Passerini, A. M., Sigindere, C., Hill, P. J., Liu, X., Wozniak, D. J., & Shanks, R. M. Q. (2018) · Applied and Environmental Microbiology · doi:10.1128/aem.02575-17 · Cited by 28 · see citing works

Regulation of the Min Cell Division Inhibition Complex by the Rcs Phosphorelay in Proteus mirabilis

Howery, K. E., Clemmer, K. M., Şimşek, E., Kim, M., & Rather, P. N. (2015) · Journal of Bacteriology · doi:10.1128/jb.00094-15 · Cited by 26 · see citing works

Instability of the Salmonella RcsCDB signalling system in the absence of the attenuator IgaA

Mariscotti, J. F., & del Portillo, F. G. (2008) · Microbiology · doi:10.1099/mic.0.2007/015891-0 · Cited by 26 · see citing works

Elevated levels of σ S inhibit biofilm formation in Escherichia coli: a role for the Rcs phosphorelay

Ferrières, L., Thompson, A. P., & Clarke, D. J. (2009) · Microbiology · doi:10.1099/mic.0.032722-0 · Cited by 26 · see citing works

Intrapersonal mutation of rmpA and rmpA2: A reason for negative hypermucoviscosity phenotype and low virulence of rmpA-positive Klebsiella pneumoniae isolates

Yu, W., Lee, M.-F., Chang, M.-C., & Chuang, Y.-C. (2015) · Journal of Global Antimicrobial Resistance · doi:10.1016/j.jgar.2015.03.008 · Cited by 24 · see citing works

Missense substitutions reflecting regulatory control of transmitter phosphatase activity in two‐component signalling

Huynh, T. N., Noriega, C. E., & Stewart, V. J. (2013) · Molecular Microbiology · doi:10.1111/mmi.12195 · Cited by 22 · see citing works

A Novel Insight on Signal Transduction Mechanism of RcsCDB System in Salmonella enterica Serovar Typhimurium

Pescaretti, M. D. L. M., Farizano, J. V., Morero, R. D., & Delgado, M. A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072527 · Cited by 21 · see citing works

Structural Insights into Rcs Phosphotransfer: The Newly Identified RcsD-ABL Domain Enhances Interaction with the Response Regulator RcsB

Schmöe, K., Rogov, V. V., Rogova, N. Y., Löhr, F., Güntert, P., Bernhard, F., & Dötsch, V. (2011) · Structure · doi:10.1016/j.str.2011.01.012 · Cited by 20 · see citing works

Conformational dynamism for DNA interaction in the Salmonella RcsB response regulator

Casino, P., Miguel-Romero, L., Huesa, J., García, P., del Portillo, F. G., & Marina, A. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1164 · Cited by 19 · see citing works

An integrated computational-experimental approach reveals Yersinia pestis genes essential across a narrow or a broad range of environmental conditions

Senior, N. J., Sasidharan, K., Saint, R. J., Scott, A., Sarkar‐Tyson, M., Ireland, P. M., Bullifent, H. L., Yang, Z., Moore, K., Oyston, P. C. F., et al. (2017) · BMC Microbiology · doi:10.1186/s12866-017-1073-8 · Cited by 18 · see citing works

Systematic Analysis of Two-Component Systems in Citrobacter rodentium Reveals Positive and Negative Roles in Virulence

Thomassin, J., Leclerc, J., Giannakopoulou, N., Zhu, L., Salmon, K., Portt, A. E., Daigle, F., Moual, H. L., & Gruenheid, S. (2016) · Infection and Immunity · doi:10.1128/iai.00654-16 · Cited by 17 · see citing works

A Disulfide Bond in the Membrane Protein IgaA Is Essential for Repression of the RcsCDB System

Pucciarelli, M. G., Rodrı́guez, L., & del Portillo, F. G. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02605 · Cited by 15 · see citing works

Importance of the proline-rich region for the regulatory function of RcsF, an outer membrane lipoprotein component of the Escherichia coli Rcs signal transduction system

Umekawa, M., Miyagawa, H., Kondo, D., Matsuoka, S., Matsumoto, K., & Hara, H. (2013) · Microbiology · doi:10.1099/mic.0.069328-0 · Cited by 12 · see citing works

Crystal structure of nonphosphorylated receiver domain of the stress response regulator RcsB from Escherichia coli

Filippova, E. V., Wawrzak, Z., Ruan, J., Pshenychnyi, S., Schultz, R. M., Wolfe, A. J., & Anderson, W. F. (2016) · Protein Science · doi:10.1002/pro.3050 · Cited by 10 · see citing works

RcsB-BglJ-mediated activation of Cascade operon does not induce the maturation of CRISPR RNAs inE. coliK12

Arslan, Z., Stratmann, T., Wurm, R., Wagner, R., Schnetz, K., & Pul, Ü. (2013) · RNA Biology · doi:10.4161/rna.23765 · Cited by 9 · see citing works

Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis

Allen, M. D., Christie, M., Jones, P. M., Porebski, B. T., Roome, B., Freund, S. M. V., Buckle, A. M., Bycroft, M., & Christ, D. (2015) · Protein Engineering Design and Selection · doi:10.1093/protein/gzv021 · Cited by 7 · see citing works

Letter to the Editor: Assignment of 1H, 13C and 15N resonances of the Escherichia coli YojN Histidine-Phosphotransferase (HPt) domain

Rogov, V. V., Löhr, F., Bernhard, F., & Dötsch, V. (2004) · Journal of Biomolecular NMR · doi:10.1023/b:jnmr.0000042964.09428.4e · Cited by 3 · see citing works

Virulence Factors in Hypervirulent Klebsiella pneumoniae

Zhu, J., Wang, T., Chen, L., & Du, H. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.642484 · Cited by 324 · see citing works

Assembly of Bacterial Capsular Polysaccharides and Exopolysaccharides

Whitfield, C., Wear, S. S., & Sande, C. (2020) · Annual Review of Microbiology · doi:10.1146/annurev-micro-011420-075607 · Cited by 312 · see citing works

Envelope stress responses: balancing damage repair and toxicity

Mitchell, A. M., & Silhavy, T. J. (2019) · Nature Reviews Microbiology · doi:10.1038/s41579-019-0199-0 · Cited by 292 · see citing works

Trouble is coming: Signaling pathways that regulate general stress responses in bacteria

Gottesman, S. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev119.005593 · Cited by 253 · see citing works

Trans-Acting Small RNAs and Their Effects on Gene Expression in Escherichia coli and Salmonella enterica

Hör, J., Matera, G., Vogel, J., Gottesman, S., & Storz, G. (2020) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0030-2019 · Cited by 188 · see citing works

The intersection of capsule gene expression, hypermucoviscosity and hypervirulence in Klebsiella pneumoniae

Walker, K. A., & Miller, V. L. (2020) · Current Opinion in Microbiology · doi:10.1016/j.mib.2020.01.006 · Cited by 181 · see citing works

High-throughput mapping of the phage resistance landscape in E. coli

Mutalik, V. K., Adler, B. A., Rishi, H. S., Piya, D., Zhong, C., Koskella, B., Kutter, E. M., Calendar, R., Novichkov, P. S., Price, M. N., et al. (2020) · PLOS Biology · doi:10.1371/journal.pbio.3000877 · Cited by 171 · see citing works

How the PhoP/PhoQ System Controls Virulence and Mg 2+ Homeostasis: Lessons in Signal Transduction, Pathogenesis, Physiology, and Evolution

Groisman, E. A., Duprey, A., & Choi, J. (2021) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00176-20 · Cited by 166 · see citing works

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

Hews, C. L., Cho, T., Rowley, G., & Raivio, T. L. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00313 · Cited by 168 · see citing works

The Capsule Regulatory Network of Klebsiella pneumoniae Defined by density-TraDISort

Dorman, M. J., Feltwell, T., Goulding, D., Parkhill, J., & Short, F. L. (2018) · mBio · doi:10.1128/mbio.01863-18 · Cited by 151 · see citing works

Membrane Vesicle Production as a Bacterial Defense Against Stress

Mozaheb, N., & Mingeot‐Leclercq, M. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.600221 · Cited by 140 · see citing works

RpoS and the bacterial general stress response

Bouillet, S., Bauer, T., & Gottesman, S. (2024) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00151-22 · Cited by 122 · see citing works

Surface Sensing and Adaptation in Bacteria

Laventie, B., & Jenal, U. (2020) · Annual Review of Microbiology · doi:10.1146/annurev-micro-012120-063427 · Cited by 116 · see citing works

Small RNAs, Large Networks: Posttranscriptional Regulons in Gram-Negative Bacteria

Papenfort, K., & Melamed, S. (2023) · Annual Review of Microbiology · doi:10.1146/annurev-micro-041320-025836 · Cited by 120 · see citing works

The multifarious roles of Tol-Pal in Gram-negative bacteria

Szczepaniak, J., Press, C., & Kleanthous, C. (2020) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaa018 · Cited by 119 · see citing works

Klebsiella pneumoniae capsular polysaccharide: Mechanism in regulation of synthesis, virulence, and pathogenicity

Xu, L., Li, J., Wu, W., Wu, X., & Ren, J. (2024) · Virulence · doi:10.1080/21505594.2024.2439509 · Cited by 106 · see citing works

Coping with stress: How bacteria fine-tune protein synthesis and protein transport

Njenga, R. K., Boele, J., Öztürk, Y., & Koch, H. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105163 · Cited by 107 · 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

The Rcs System in Enterobacteriaceae: Envelope Stress Responses and Virulence Regulation

Meng, J., Young, G. M., & Chen, J. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.627104 · Cited by 93 · see citing works

Genomic Profiling Reveals Distinct Routes To Complement Resistance in Klebsiella pneumoniae

Short, F. L., Sario, G. D., Reichmann, N. T., Kleanthous, C., Parkhill, J., & Taylor, P. W. (2020) · Infection and Immunity · doi:10.1128/iai.00043-20 · Cited by 86 · see citing works

Lipoproteins in Gram-negative bacteria: new insights into their biogenesis, subcellular targeting and functional roles

Rayes, J. E., Rodríguez-Alonso, R., & Collet, J. (2021) · Current Opinion in Microbiology · doi:10.1016/j.mib.2021.02.003 · Cited by 83 · 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

A Stress Response Monitoring Lipoprotein Trafficking to the Outer Membrane

May, K. L., Lehman, K. M., Mitchell, A. M., & Grabowicz, M. (2019) · mBio · doi:10.1128/mbio.00618-19 · Cited by 78 · see citing works

Multikinase Networks: Two-Component Signaling Networks Integrating Multiple Stimuli

Francis, V. I., & Porter, S. L. (2019) · Annual Review of Microbiology · doi:10.1146/annurev-micro-020518-115846 · Cited by 75 · see citing works

A Skeptic's Guide to Bacterial Mechanosensing

Chawla, R., Gupta, R., Lele, T. P., & Lele, P. P. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.09.004 · Cited by 65 · see citing works

Survive and thrive: Control mechanisms that facilitate bacterial adaptation to survive manufacturing-related stress

Marmion, M., Macori, G., Ferone, M., Whyte, P., & Scannell, A. G. M. (2022) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2022.109612 · Cited by 73 · 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

Salmonella enterica Serovar Typhimurium Uses PbgA/YejM To Regulate Lipopolysaccharide Assembly during Bacteremia

Cian, M. B., Giordano, N. P., Masilamani, R., Minor, K., & Dalebroux, Z. D. (2019) · Infection and Immunity · doi:10.1128/iai.00758-19 · Cited by 61 · see citing works

Capsules and Extracellular Polysaccharides in Escherichia coli and Salmonella

Sande, C., & Whitfield, C. (2021) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0033-2020 · Cited by 62 · see citing works

Colanic acid biosynthesis in Escherichia coli is dependent on lipopolysaccharide structure and glucose availability

Wang, C., Zhang, H., Wang, J., Chen, S., Wang, Z., Zhao, L., & Wang, X. (2020) · Microbiological Research · doi:10.1016/j.micres.2020.126527 · Cited by 62 · see citing works

Individual bacteria in structured environments rely on phenotypic resistance to phage

Attrill, E. L., Claydon, R., Łapińska, U., Recker, M., Meaden, S., Brown, A. T., Westra, E. R., Harding, S. V., & Pagliara, S. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001406 · Cited by 61 · see citing works

Bacterial Multicellularity: The Biology of Escherichia coli Building Large-Scale Biofilm Communities

Serra, D. O., & Hengge, R. (2021) · Annual Review of Microbiology · doi:10.1146/annurev-micro-031921-055801 · Cited by 59 · see citing works

Precise timing of transcription by c-di-GMP coordinates cell cycle and morphogenesis in Caulobacter

Kaczmarczyk, A., Hempel, A. M., von Arx, C., Böhm, R., Dubey, B. N., Nesper, J., Schirmer, T., Hiller, S., & Jenal, U. (2020) · Nature Communications · doi:10.1038/s41467-020-14585-6 · Cited by 58 · see citing works

A Fly on the Wall: How Stress Response Systems Can Sense and Respond to Damage to Peptidoglycan

Delhaye, A., Collet, J., & Laloux, G. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00380 · Cited by 55 · 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

The Rcs stress response inversely controls surface and CRISPR–Cas adaptive immunity to discriminate plasmids and phages

Smith, L. M., Jackson, S. A., Malone, L. M., Ussher, J. E., Gardner, P. P., & Fineran, P. C. (2021) · Nature Microbiology · doi:10.1038/s41564-020-00822-7 · Cited by 51 · see citing works

Structural insight into the formation of lipoprotein-β-barrel complexes

Rodríguez-Alonso, R., Létoquart, J., Nguyen, V. S., Louis, G., Calabrese, A. N., Iorga, B. I., Radford, S. E., Cho, S.-H., Remaut, H. K., & Collet, J. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0575-0 · Cited by 49 · see citing works

Collateral fitness effects of mutations

Mehlhoff, J. D., Stearns, F. W., Rohm, D., Wang, B., Tsou, E.-Y., Dutta, N., Hsiao, M.-H., Gonzalez, C. E., Rubin, A. F., & Ostermeier, M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1918680117 · Cited by 48 · see citing works

How the assembly and protection of the bacterial cell envelope depend on cysteine residues

Collet, J., Cho, S.-H., Iorga, B. I., & Goemans, C. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011201 · Cited by 46 · see citing works

IgaA negatively regulates the Rcs Phosphorelay via contact with the RcsD Phosphotransfer Protein

Wall, E. A., Majdalani, N., & Gottesman, S. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008610 · Cited by 46 · see citing works

Strategies for Enhancing Microbial Production of 2′-Fucosyllactose, the Most Abundant Human Milk Oligosaccharide

Liu, Y., Zhu, Y., Wang, H., Wan, L., Zhang, W., & Mu, W. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c04539 · Cited by 45 · see citing works

Defining the function of OmpA in the Rcs stress response

Létoquart, J., Dekoninck, K., Laguri, C., Demange, P., Bevernaegie, R., Simorre, J., Dehu, O., Iorga, B. I., Elias, B., Cho, S.-H., et al. (2020) · eLife · doi:10.7554/elife.60861 · Cited by 44 · see citing works

A multifaceted cellular damage repair and prevention pathway promotes high-level tolerance to β-lactam antibiotics

Shin, J., Choe, D., Ransegnola, B. P., Hong, H., Onyekwere, I., Cross, T. S., Shi, Q., Cho, B., Westblade, L. F., Brito, I., et al. (2021) · EMBO Reports · doi:10.15252/embr.202051790 · Cited by 40 · see citing works

The Synthetic Phenotype of Δ bamB Δ bamE Double Mutants Results from a Lethal Jamming of the Bam Complex by the Lipoprotein RcsF

Hart, E. M., Gupta, M., Wühr, M., & Silhavy, T. J. (2019) · mBio · doi:10.1128/mbio.00662-19 · Cited by 40 · see citing works

The role of two-component regulatory systems in environmental sensing and virulence inSalmonella

de Pina, L. C., da Silva, F. S. H., Galvão, T. C., Pauer, H., Ferreira, R. B. R., & Antunes, L. C. M. (2021) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2021.1895067 · Cited by 39 · see citing works

Regulation of type VI secretion systems at the transcriptional, posttranscriptional and posttranslational level

Hespanhol, J. T., Nóbrega-Silva, L., & Bayer‐Santos, E. (2023) · Microbiology · doi:10.1099/mic.0.001376 · Cited by 39 · see citing works

Envelope-Stress Sensing Mechanism of Rcs and Cpx Signaling Pathways in Gram-Negative Bacteria

Cho, S.-H., Dekoninck, K., & Collet, J. (2023) · The Journal of Microbiology · doi:10.1007/s12275-023-00030-y · Cited by 37 · see citing works

Improper Coordination of BamA and BamD Results in Bam Complex Jamming by a Lipoprotein Substrate

Tata, M., & Konovalova, A. (2019) · mBio · doi:10.1128/mbio.00660-19 · Cited by 32 · see citing works

Viscoelastic response of Escherichia coli biofilms to genetically altered expression of extracellular matrix components

Horvat, M., Pannuri, A., Romeo, T., Dogša, I., & Stopar, D. (2019) · Soft Matter · doi:10.1039/c9sm00297a · Cited by 32 · see citing works

Cryo-EM structures of LolCDE reveal the molecular mechanism of bacterial lipoprotein sorting in Escherichia coli

Bei, W., Luo, Q., Shi, H., Zhou, H., Zhou, M., Zhang, X., & Huang, Y. (2022) · PLoS Biology · doi:10.1371/journal.pbio.3001823 · Cited by 31 · 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

Who’s in control? Regulation of metabolism and pathogenesis in space and time

King, A. N., Mets, F. D., & Brinsmade, S. R. (2020) · Current Opinion in Microbiology · doi:10.1016/j.mib.2020.05.009 · Cited by 27 · see citing works

Blowing epithelial cell bubbles with GumB: ShlA-family pore-forming toxins induce blebbing and rapid cellular death in corneal epithelial cells

Brothers, K. M., Callaghan, J. D., Stella, N. A., Bachinsky, J. M., AlHigaylan, M., Lehner, K. M., Franks, J. M., Lathrop, K. L., Collins, E., Schmitt, D. M., et al. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007825 · Cited by 28 · see citing works

The phosphorelay BarA/SirA activates the non-cognate regulator RcsB in Salmonella enterica

Salvail, H., & Groisman, E. A. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008722 · Cited by 28 · see citing works

Tracking Colanic Acid Repeat Unit Formation from Stepwise Biosynthesis Inactivation in Escherichia coli

Reid, A. J., Eade, C. R., Jones, K. J., Jorgenson, M. A., & Troutman, J. M. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00314 · Cited by 28 · see citing works

RcsAB and Fur Coregulate the Iron-Acquisition System via entC in Klebsiella pneumoniae NTUH-K2044 in Response to Iron Availability

Yuan, L., Li, X., Du, L., Su, K., Zhang, J., Liu, P., He, Q., Zhang, Z., Peng, D., Shen, L., et al. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.00282 · Cited by 27 · 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

Microevolution of acquired colistin resistance in Enterobacteriaceae from ICU patients receiving selective decontamination of the digestive tract

Janssen, A. B., van Hout, D., Bonten, M. J. M., Willems, R. J. L., & van Schaik, W. (2020) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkaa305 · Cited by 28 · see citing works

Molecular and Genetic Mechanisms That Mediate Transmission of Yersinia pestis by Fleas

Hinnebusch, B. J., Jarrett, C. O., & Bland, D. M. (2021) · Biomolecules · doi:10.3390/biom11020210 · Cited by 27 · see citing works

Programmable Bacteria with Dynamic Virulence Modulation System for Precision Antitumor Immunity

Wu, L., Li, L., Qiao, L., Li, C., Zhang, S., Yin, X., Du, Z., Sun, Y., Qiu, J., Chang, X., et al. (2024) · Advanced Science · doi:10.1002/advs.202404069 · Cited by 24 · see citing works

Activation of colanic acid biosynthesis linked to heterologous expression of the polyhydroxybutyrate pathway in Escherichia coli

Wu, H., Chen, S., Ji, M., Chen, Q., Shi, J., & Sun, J. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.02.004 · Cited by 26 · see citing works

Regulator RcsB Controls Prodigiosin Synthesis and Various Cellular Processes in Serratia marcescens JNB5-1

Pan, X., Tang, M., You, J., Liu, F., Sun, C., Osire, T., Fu, W., Yi, G., Yang, T., Yang, S., et al. (2020) · Applied and Environmental Microbiology · doi:10.1128/aem.02052-20 · Cited by 26 · see citing works

High-throughput suppressor screen demonstrates that RcsF monitors outer membrane integrity and not Bam complex function

Tata, M., Kumar, S., Lach, S. R., Saha, S., Hart, E. M., & Konovalova, A. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2100369118 · Cited by 26 · see citing works

Evaluation of Cronobacter sakazakii biofilm formation after sdiA knockout in different osmotic pressure conditions

Cao, Y., Li, L., Zhang, Y., Liu, F., Xiao, X., Li, X., & Yu, Y. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110886 · Cited by 26 · see citing works

Interdependence of Shigella flexneri O Antigen and Enterobacterial Common Antigen Biosynthetic Pathways

Maczuga, N. T., Tran, E. N. H., Qin, J., & Morona, R. (2022) · Journal of Bacteriology · doi:10.1128/jb.00546-21 · Cited by 25 · see citing works

Molecules involved in motility regulation in Escherichia coli cells: a review

Khan, F., Tabassum, N., Pham, D. T. N., Oloketuyi, S., & Kim, Y.-M. (2020) · Biofouling (Print) · doi:10.1080/08927014.2020.1826939 · Cited by 23 · see citing works

Combining Cell Envelope Stress Reporter Assays in a Screening Approach to Identify BAM Complex Inhibitors

Steenhuis, M., Corona, F., ten Hagen‐Jongman, C. M., Vollmer, W., Lambin, D., Selhorst, P., Klaassen, H., Versele, M., Chaltin, P., & Luirink, J. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00728 · Cited by 23 · see citing works

Recent advances in a functional deoxy hexose l-fucose: Occurrence, physiological effects, and preparation

Meng, J., Zhu, Y., Wang, N., Zhang, W., & Mu, W. (2023) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2023.05.011 · 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 24 · see citing works

Two-Component Response Regulator OmpR Regulates Mucoviscosity through Energy Metabolism in Klebsiella pneumoniae

Wang, L., Huang, X., Jin, Q., Tang, J., Zhang, H., Zhang, J.-R., & Wu, H. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.00544-23 · Cited by 22 · see citing works

LptM promotes oxidative maturation of the lipopolysaccharide translocon by substrate binding mimicry

Yang, Y., Chen, H., Corey, R. A., Morales, V., Quentin, Y., Froment, C., Caumont-Sarcos, A., Albenne, C., Burlet-Schiltz, O., Ranava, D., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42007-w · Cited by 20 · see citing works

Colanic Acid: Biosynthetic Overproduction by Engineering Escherichia coli and Physical Property Characterization

Qiao, J., Zhan, Y., Tan, X., Liu, Y., Hu, X., & Wang, X. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c04823 · Cited by 21 · see citing works

Impact of Sub-MIC Eugenol on Klebsiella pneumoniae Biofilm Formation via Upregulation of rcsB

Elken, E. M., Tan, Z.-N., Wang, Q., Jiang, X.-Y., Wang, Y., Wang, Y.-M., & Ma, H. (2022) · Frontiers in Veterinary Science · doi:10.3389/fvets.2022.945491 · Cited by 21 · see citing works

Cyclic AMP-CRP Modulates the Cell Morphology of Klebsiella pneumoniae in High-Glucose Environment

Liu, L., Li, F., Xu, L., Wang, J., Li, M., Yuan, J., Wang, H., Yang, R., & Li, B. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02984 · Cited by 20 · see citing works

Transcriptomic analysis reveals the role of RcsB in suppressing bacterial chemotaxis, flagellar assembly and infection in Yersinia enterocolitica

Meng, J., Bai, J., & Chen, J. (2020) · Current Genetics · doi:10.1007/s00294-020-01083-x · Cited by 20 · see citing works

Parallel within-host evolution alters virulence factors in an opportunistic Klebsiella pneumoniae during a hospital outbreak

Zaborskytė, G., Hjort, K., Lytsy, B., & Sandegren, L. (2025) · Nature Communications · doi:10.1038/s41467-025-64521-9 · Cited by 19 · see citing works

How Klebsiella pneumoniae controls its virulence

Nguyen, T. N. T., Howells, G., & Short, F. L. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013499 · Cited by 18 · see citing works

Proteomic and Transcriptomic Analysis of Microviridae φX174 Infection Reveals Broad Upregulation of Host Escherichia coli Membrane Damage and Heat Shock Responses

Wright, B. W., Logel, D. Y., Mirzai, M., Pascovici, D., Molloy, M. P., & Jaschke, P. R. (2021) · mSystems · doi:10.1128/msystems.00046-21 · Cited by 18 · see citing works

Impact of Salmonella genome rearrangement on gene expression

Waters, E. V., Tucker, L. A., Ahmed, J. K., Wain, J. R., & Langridge, G. C. (2022) · Evolution Letters · doi:10.1002/evl3.305 · Cited by 18 · see citing works

Rcs Phosphorelay Responses to Truncated Lipopolysaccharide-Induced Cell Envelope Stress in Yersinia enterocolitica

Meng, J., Xu, J., Huang, C., & Chen, J. (2020) · Molecules · doi:10.3390/molecules25235718 · Cited by 18 · 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

Synthesis of the NarP response regulator of nitrate respiration in Escherichia coli is regulated at multiple levels by Hfq and small RNAs

Brosse, A., Boudry, P., Walburger, A., Magalon, A., & Guillier, M. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac504 · Cited by 15 · see citing works

The essential Rhodobacter sphaeroides CenKR two-component system regulates cell division and envelope biosynthesis

Lakey, B. D., Myers, K. S., Alberge, F., Mettert, E. L., Kiley, P. J., Noguera, D. R., & Donohue, T. J. (2022) · PLoS Genetics · doi:10.1371/journal.pgen.1010270 · 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

Flagellar regulation mediated by the Rcs pathway is required for virulence in the fish pathogen Yersinia ruckeri

Jozwick, A. K. S., LaPatra, S. E., Graf, J., & Welch, T. J. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2019.05.036 · Cited by 17 · see citing works

Osmoregulated Periplasmic Glucans Transmit External Signals Through Rcs Phosphorelay Pathway in Yersinia enterocolitica

Meng, J., Huang, C., Huang, X., Liu, D., Han, B., & Chen, J. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.00122 · Cited by 17 · see citing works

Envelope Stress and Regulation of the Salmonella Pathogenicity Island 1 Type III Secretion System

Palmer, A. D., & Slauch, J. M. (2020) · Journal of Bacteriology · doi:10.1128/jb.00272-20 · Cited by 17 · see citing works

At what cost? The impact of bacteriophage resistance on the growth kinetics and protein synthesis of Escherichia coli

Landor, L., Tjendra, J., Erstad, K., Krabberød, A. K., Töpper, J. P., & Våge, S. (2024) · Environmental Microbiology Reports · doi:10.1111/1758-2229.70046 · Cited by 16 · see citing works

Proton motive force and antibiotic tolerance in bacteria

Wan, Y., Zheng, J., Chan, E. W., & Chen, S. (2024) · Microbial Biotechnology · doi:10.1111/1751-7915.70042 · Cited by 16 · see citing works

Molecular Epidemiology of Hypervirulent K. pneumoniae and Problems of Health-Care Associated Infections

Tutelyan, A. V., Shlykova, D. S., Voskanyan, S. L., Михайлович, Г. А., & Писарев, В. М. (2022) · Bulletin of Experimental Biology and Medicine · doi:10.1007/s10517-022-05424-3 · Cited by 16 · see citing works

Structure-based analyses ofSalmonellaRcsB variants unravel new features of the Rcs regulon

Huesa, J., Giner‐Lamia, J., Pucciarelli, M. G., Paredes‐Martínez, F., del Portillo, F. G., Marina, A., & Casino, P. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab060 · Cited by 16 · see citing works

Maintenance and generation of proton motive force are both essential for expression of phenotypic antibiotic tolerance in bacteria

Wan, Y., Chan, E. W., & Chen, S. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.00832-23 · Cited by 15 · see citing works

Synthesis and Structure–Activity Studies of β-Barrel Assembly Machine Complex Inhibitor MRL-494

Wade, N., Wesseling, C. M. J., Innocenti, P., Slingerland, C. J., Koningstein, G. M., Luirink, J., & Martin, N. I. (2022) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.2c00459 · Cited by 15 · see citing works

Conformational rearrangements in the sensory RcsF/OMP complex mediate signal transduction across the bacterial cell envelope

Lach, S. R., Kumar, S., Kim, S., Im, W., & Konovalova, A. (2023) · PLoS Genetics · doi:10.1371/journal.pgen.1010601 · Cited by 15 · see citing works

Rcs signal transduction system in Escherichia coli: Composition, related functions, regulatory mechanism, and applications

Li, Z., Zhu, Y., Zhang, W., & Mu, W. (2024) · Microbiological Research · doi:10.1016/j.micres.2024.127783 · Cited by 14 · see citing works

Allostery and protein plasticity: the keystones for bacterial signaling and regulation

Imelio, J. A., Trajtenberg, F., & Buschiazzo, A. (2021) · Biophysical Reviews · doi:10.1007/s12551-021-00892-9 · Cited by 14 · see citing works

The role of RcsA in the adaptation and survival of Escherichia coli K92

Navasa, N., Ferrero, M. Á. M., Rodrı́guez-Aparicio, L. B., Monteagudo-Mera, A., Gutiérrez, S., & Martı́nez-Blanco, H. (2019) · FEMS Microbiology Letters · doi:10.1093/femsle/fnz082 · Cited by 14 · see citing works

The cascade regulation of small RNA and quorum sensing system: Focusing on biofilm formation of foodborne pathogens in food industry

Zhang, Y., Wu, Q., Forsythe, S. J., Liu, C., Chen, N., Li, Y., Zhang, J., Wang, J., & Ding, Y. (2023) · Food Bioscience · doi:10.1016/j.fbio.2023.102472 · Cited by 13 · see citing works

Escherichia coli has robust regulatory mechanisms against elevated peptidoglycan cleavage by lytic transglycosylases

Liang, Y., Zhao, Y., Kwan, J. M. C., Wang, Y., & Qiao, Y. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104615 · Cited by 13 · see citing works

The Rcs Stress Response System Regulator GumB Modulates Serratia marcescens-Induced Inflammation and Bacterial Proliferation in a Rabbit Keratitis Model and Cytotoxicity In Vitro

Romanowski, E. G., Stella, N. A., Romanowski, J. E., Yates, K. A., Dhaliwal, D. K., Leger, A. J. S., & Shanks, R. M. Q. (2021) · Infection and Immunity · doi:10.1128/iai.00111-21 · Cited by 13 · see citing works

Role of RcsF in Signaling to the Rcs Phosphorelay Pathway inEscherichia coli

Majdalani, N., Heck, M. C., Stout, V., & Gottesman, S. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.19.6770-6778.2005 · Cited by 146 · see citing works

THE RCS PHOSPHORELAY: A Complex Signal Transduction System

Majdalani, N., & Gottesman, S. (2005) · Annual Review of Microbiology · doi:10.1146/annurev.micro.59.050405.101230 · Cited by 560 · see citing works

Genetic Dissection of Signaling Through the Rcs Phosphorelay

Majdalani, N., & Gottesman, S. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)23016-2 · Cited by 25 · see citing works

Interaction of the RcsB Response Regulator with Auxiliary Transcription Regulators in Escherichia coli

Pannen, H. D., Fabisch, M., Gausling, L., & Schnetz, K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.696815 · Cited by 64 · see citing works

Analysis of transcriptional regulation by RcsB homo- and heterodimers in Escherichia coli

Pannen, H. D. (2015) · Kölner Universitäts PublikationsServer (Universität zu Köln)