Molecular Mechanisms of Two-Component Signal Transduction

Two-Component Signal Transduction

Stock, A., Robinson, V. L., & Goudreau, P. N. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.183 · Cited by 3,653

PAS Domains: Internal Sensors of Oxygen, Redox Potential, and Light

Taylor, B. L., & Zhulin, I. B. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.2.479-506.1999 · Cited by 1,632

Structural identification of a bacterial quorum-sensing signal containing boron

Chen, X., Schauder, S., Potier, N., DORSSELAER, A. V., Pelczer, I., Bassler, B. L., & Hughson, F. M. (2002) · Nature · doi:10.1038/415545a · Cited by 1,572

Identification of direct residue contacts in protein–protein interaction by message passing

Weigt, M., White, R. A., Szurmant, H., Hoch, J. A., & Hwa, T. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805923106 · Cited by 1,025

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

Specificity in Two-Component Signal Transduction Pathways

Laub, M. T., & Goulian, M. (2007) · Annual Review of Genetics · doi:10.1146/annurev.genet.41.042007.170548 · Cited by 752

Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases

Mascher, T., Helmann, J. D., & Unden, G. (2006) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00020-06 · Cited by 723

Robust and accurate prediction of residue–residue interactions across protein interfaces using evolutionary information

Ovchinnikov, S., Kamisetty, H., & Baker, D. (2014) · eLife · doi:10.7554/elife.02030 · Cited by 629

Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domainPreprint

Paul, R., Weiser, S., Amiot, N. C., Chan, C., Schirmer, T., Giese, B., & Jenal, U. (2004) · Genes & Development · doi:10.1101/gad.289504 · Cited by 612

Structure of VanS from vancomycin-resistant enterococci: A sensor kinase with weak ATP binding

Grasty, K. C., Guzik, C., D’Lauro, E. J., Padrick, S. B., Beld, J., & Loll, P. J. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.103001 · Cited by 2

Virtual Screening of Potential RoxS Inhibitors and Evaluation of Their Antimicrobial Activity in Combination with Antibiotics against Clinically Resistant Bacteria

Huang, Y., Li, J., Liang, T., Zhao, Z., Xu, J., & Chen, W. (2023) · Antibiotics · doi:10.3390/antibiotics12091422 · Cited by 2

Characterization of the extracellular domain of sensor histidine kinase NagS from Paenibacillus sp. str. FPU-7: nagS interacts with oligosaccharide binding protein NagB1 in complexes with N, N′-diacetylchitobiose

Itoh, T., Ogawa, T., Hibi, T., & Kimoto, H. (2023) · Bioscience Biotechnology and Biochemistry · doi:10.1093/bbb/zbad173 · Cited by 2

Impact Study of Gene Expression: Osmotic Control, SOS Response, and Heat Shock Responses

Kamath, R., Panda, P., Mukherjee, P., Vimal, P., & Kasturi, P. (2024) · Springer eBooks · doi:10.1007/978-981-97-1912-9_5 · Cited by 2

Development and validation of an experimental life support system to study coral reef microbial communities

Stuij, T. M., Cleary, D. F. R., Rocha, R. J. M., Polónia, A. R. M., Silva, D., Frommlet, J. C., Louvado, A., Huang, Y. M., de Voogd, N. J., Voogd, N. J. D., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-69514-0 · Cited by 3

Adaptative responses of Neurospora crassa by histidine kinases upon the attack of the arthropod Sinella curviseta

Lu, T., Wang, X.-M., Chen, P., Xi, J., Yang, H.-B., Zheng, W., & Zhao, Y. (2024) · Current Genetics · doi:10.1007/s00294-024-01302-9 · Cited by 2

The Campylobacter jejuni BumS sensor phosphatase detects the branched short-chain fatty acids isobutyrate and isovalerate as direct cues for signal transduction

Ruiz, N., Xing, J., Zhulin, I. B., Brautigam, C. A., & Hendrixson, D. R. (2024) · mBio · doi:10.1128/mbio.03278-24 · Cited by 2

Structural and biophysical characterization of the cytoplasmic domains of HprS kinase and its interactions with the cognate regulator HprR

Koczurowska, A., Carrillo, D. R., García-Alai, M., Zakłos‐Szyda, M., Bujacz, G., & Pietrzyk‐Brzezinska, A. J. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110269 · Cited by 2

Structural Insight Into the Conversion of DhNik1, A Hybrid Histidine Kinase From Debaryomyces hansenii to a Cytotoxic Phosphatase Conformation for Novel Antifungal Agent

Sasan, S. P., Martoliya, Y., Vashishtha, S., Kaur, H., Kundu, D., Gourinath, S., Lynn, A. M., Prasad, R., Kundu, B., & Mondal, A. K. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169116 · Cited by 2

KaiC-like ATPases as Signal Transduction Hubs in Archaea

Makarova, K. S., & Koonin, E. V. (2017) · Springer eBooks · doi:10.1007/978-3-319-65536-9_11 · Cited by 2

Backbone resonance assignment of the response regulator protein PhoBNF20D from Escherichia coli

Kou, X., Liu, X., Liu, Y., Li, C., Liu, M., & Jiang, L. (2018) · Biomolecular NMR Assignments · doi:10.1007/s12104-017-9795-y · Cited by 2

Research progress on two-component signal transduction systems in Porphyromonas gingivalis.

Yao, K., Cai, J.-Y., Zhao, L., Wu, Y.-F., Zhao, Z.-H., & Shen, D.-N. (2021) · PubMed Central · doi:10.7518/hxkq.2021.01.013 · Cited by 2

Sensory Transduction in Bacteria

Galperin, M. Y., & Schultz, J. E. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.02458-2 · Cited by 2

Exploration of kinase phosphotransfer mechanism based onN-phosphoryl amino acids

Fu, S., Li, F., Huang, B., Cai, H., Ni, F., Ying, J., Liu, Y., Fu, C., Gao, X., Li, Y., et al. (2022) · Scientia Sinica Chimica · doi:10.1360/ssc-2022-0208 · Cited by 2

Expression patterns and influence of the two-component system in Vibrio parahaemolyticus of different genotypes

Meng, Y., Mu, L., Li, Y., Yu, M., Liu, H., Pan, Y., & Zhao, Y. (2023) · Gene · doi:10.1016/j.gene.2023.147187 · Cited by 2

Regulatory Systems: Two-Component

Raivio, T. L. (2019) · European Lisp Symposium · doi:10.1002/9780470015902.a0000856.pub3

Learning from Adversity?

Bourret, R. B. (2017) · Journal of Bacteriology · doi:10.1128/jb.00420-17 · Cited by 2

Nutritional inter-dependencies and a carbazole-dioxygenase are key elements of a bacterial consortium relying on a Sphingomonas for the degradation of the fungicide thiabendazolePreprint

Vasileiadis, S., Perruchon, C., Benjamin, S., Adrian, L., Nicole, S., Trevisan, M., Plaza‐Bolaños, P., Agüera, A., Chatzinotas, A., & Karpouzas, D. G. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.03.30.015693 · Cited by 2

Development and validation of an experimental life support system to study the impact of ultraviolet B radiation and temperature on coral reef microbial communitiesPreprint

Stuij, T., Cleary, D., Rocha, R. J., Polónia, A. R. M., Silva, D., Frommlet, J., Louvado, A., Huang, Y.-M., van der Windt, N., de Voogd, N. D., et al. (2023) · bioRxiv · doi:10.1101/2023.03.01.530425 · Cited by 1

Bacteria use spatial sensing to direct chemotaxis on surfacesPreprint

Wheeler, J. H. R., Foster, K. R., & Durham, W. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.13.580113 · Cited by 2

Studying of the regulatory roles of response regulators GlrR and ArcA in xenocoumacins biosynthesis in Xenorhabdus nematophila CB6

Li, X., Zheng, X., Dong, Y., Qin, Y., Jia, F., Yuan, B., Duan, J., Li, B., & Li, G. (2024) · Journal of Integrative Agriculture · doi:10.1016/j.jia.2024.02.014 · Cited by 1

Role of the NtrC family response regulator in nitrogen metabolism of Acinetobacter baumannii

Sawant, A. R., Pagal, S., & Prashanth, K. (2024) · Gene · doi:10.1016/j.gene.2024.148552 · Cited by 1

Archaeal Signalling Networks—New Insights Into the Structure and Function of Histidine Kinases and Response Regulators of the Methanogenic Archaeon Methanosarcina acetivorans

Georgiev, N. F. K., Andersson, A. L., Ruppe, Z., Kattwinkel, L., & Frankenberg‐Dinkel, N. (2025) · Environmental Microbiology · doi:10.1111/1462-2920.70047 · Cited by 1

Multifaceted Evolution of the PhoPQ Two‐Component System in Salmonella enterica Enhanced the Expression of Horizontally Acquired Virulence Genes

Barretto, L. A. F., & Fowler, C. C. (2025) · Molecular Microbiology · doi:10.1111/mmi.15355 · Cited by 1

Genomic profiling of soil nitrifying microorganisms enriched on floating membrane filter

Abiola, C., Gwak, J.-H., Lee, U.-J., Adigun, A. O., & Rhee, S.-K. (2025) · Journal of Microbiology · doi:10.71150/jm.2502002 · Cited by 1

Phylogeny as the basis for the sub-fields of biosemiotics

Lineweaver, C. H. (2025) · Semiotica · doi:10.1515/sem-2023-0175 · Cited by 1

The VanS sensor histidine kinase from type-B vancomycin-resistant enterococci recognizes vancomycin directly

Maciunas, L. J., Rotsides, P., D’Lauro, E. J., Brady, S., Beld, J., & Loll, P. J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110276 · Cited by 4

Regulation of bacterial phosphorelay systems

Foulkes, D. M., Cooper, D. M., Westland, C., & Byrne, D. P. (2025) · RSC Chemical Biology · doi:10.1039/d5cb00016e · Cited by 1

Transcriptomic and Neurotransmitter Insights Into Gray Matter Volume Changes From 1 Hz rTMS in Treating Schizophrenia With Auditory Verbal Hallucinations

Xie, Y., Li, C., Guan, M., Zhang, T., Ma, C., Wang, L., Li, X., Li, Y., Wang, Z., Wang, H., et al. (2025) · Acta Psychiatrica Scandinavica · doi:10.1111/acps.70014 · Cited by 1

The DR2416/DR2415 two-component system is responsible for the radioresistance of Deinococcus radiodurans

Wang, W., Du, Z., Yang, F., & He, S. (2025) · Antonie van Leeuwenhoek · doi:10.1007/s10482-025-02125-5 · Cited by 1

The PAS domain of the polarly localized histidine kinase FlrB in Vibrio cholerae controls class III flagellar transcription and contributes to intestinal colonization

Stanton, V., Himes, B., Mejia-Santana, A., Eppinger, M., Romo, J. A., Xing, J., Zhulin, I. B., Cai, H., Wang, Y., Inniss, N. L., et al. (2025) · mBio · doi:10.1128/mbio.02379-25 · Cited by 1

A Campylobacter jejuni sensor phosphatase–driven two-component system integrates metabolic phosphodonors as cues in signal transduction

Ruiz, N., & Hendrixson, D. R. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2512446122 · Cited by 1

Harnessing quorum sensing for disease management

Desai, V., Sahana, M., Mayegowda, S. B., Gadilingappa, M. N., & Nagshetty, K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-34178-6.00015-4 · Cited by 1

Role of sigma 54 and bamVW in regulation of anaerobic aromatic degradation via benzoate-CoA ligase by Geotalea daltonii

Kiessling, C. M., Bullows, J. E., Ramirez, N., Li, X., & Chin, K. (2025) · The Microbe · doi:10.1016/j.microb.2025.100601 · Cited by 1

The response regulator CrsR positively regulates ansamitocin P-3 biosynthesis in Actinosynnema pretiosum

Zhang, P., Zong, G., Wang, T., Zhao, S., Sun, R., Fu, J., Liu, M., & Cao, G. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1684526 · Cited by 1

Multiple input–multiple output (MIMO) designs in two-component signalling systems of Mycobacterium tuberculosis

Singh, D. P., Gayathri, A. S., Singh, R., Dixit, N. M., & Saini, D. K. (2025) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuaf064 · Cited by 1

Evolution and role of manganese-transforming bacterial microorganisms during natural manganese-tailing succession

Wu, C., Wu, Y., Pan, J., Lv, Y., Li, W., Hu, M., Wang, J., Su, S., Zou, Q., & Xue, S. (2026) · Journal of Environmental Sciences · doi:10.1016/j.jes.2026.01.018 · Cited by 1

Characterising complex metabolic responses in an engineered, cross-feeding microbial co-culture using quantitative proteomics

Shi, M., McQuillan, J. L., Evans, C. A., Liu, Y., Lin, X., Barney, B. M., & Pandhal, J. (2026) · New Biotechnology · doi:10.1016/j.nbt.2026.02.001 · Cited by 1

Controllable protein design via autoregressive direct coupling analysis conditioned on principal components

(2026) · doi:10.1371/journal.pcbi.1013996 · Cited by 1

Transcription of photosynthetic genes in the plant chloroplast: lessons from bacteria

Moon, J., Dudey, A., Cruces, A. V., Tasker‐Brown, W., Pearce, D., & Webster, M. W. (2026) · The Plant Journal · doi:10.1111/tpj.70959 · Cited by 1

Anti-Virulence Factor Therapeutics

Johnson, D. I. (2017) · Springer eBooks · doi:10.1007/978-3-319-67651-7_34 · Cited by 1

Evolutionary couplings of amino acid residues reveal structure and function of bacterial signaling proteins

Szurmant, H. (2019) · Molecular Microbiology · doi:10.1111/mmi.14282 · Cited by 1

Insights into the structure and function of the histidine kinase ComP from Bacillus amyloliquefaciens based on molecular modeling

Wang, L., Fan, R., Li, Z., Wang, L., Bai, X., Bu, T., Dong, Y., Xu, Y., & Quan, C. (2022) · Bioscience Reports · doi:10.1042/bsr20220352 · Cited by 1

Cross-regulation of Aps-promoters in Lacticaseibacillus paracasei by the PsdR response regulator in response to lantibiotics

Zhang, Q., Zúñiga, M., Alcántara, C., Wolf, D., Mascher, T., & Revilla-Guarinos, A. (2024) · Scientific Reports · doi:10.1038/s41598-024-53592-1 · Cited by 2

Ligand binding represses bacterial histidine kinase activity by inhibiting its dimerization

Sankhe, G. D., Xing, J., Xiao, X., Buglino, J. A., Li, H., Zhulin, I. B., & Glickman, M. S. (2026) · FEBS Journal · doi:10.1111/febs.70621 · Cited by 1

A Close Look at the Mechanisms of Signal Transduction

Hodak, H. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.006 · Cited by 1

Niche differentiation of microbes and their functional signatures in Assam type tea (Camellia sinensis var. assamica)Preprint

Bora, S. S., Dey, K. K., Borah, M., Rahman, M., Gogoi, M., Modi, M. K., & Barooah, M. (2021) · Research Square · doi:10.21203/rs.3.rs-347764/v1 · Cited by 1

Brucella

Caswell, C. C., Arenas-Gamboa, Á. M., & Foster, J. T. (2022) · doi:10.1002/9781119754862.ch16 · Cited by 1

Phosphorylation‐Based Molecular Switches

Reményi, A. (2022) · Wiley eBooks · doi:10.1002/9783527830503.ch17 · Cited by 1

The VanS sensor histidine kinase from type-B VRE recognizes vancomycin directlyPreprint

Maciunas, L. J., Rotsides, P., D’Lauro, E. J., Brady, S., Beld, J., & Loll, P. J. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.07.09.548278 · Cited by 1

PhoPQ-mediated lipopolysaccharide modification regulates intrinsic resistance to tetracycline and glycylcycline antibiotics in Escherichia coliPreprint

Choi, B. J., Choi, U., Ryu, D.-B., & Lee, C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.01.601565 · Cited by 1

Functional and pangenomic exploration of Roc two-component regulatory systems identifies novel players across Pseudomonas speciesPreprint

Simon, V., Trouillon, J., Attrée, I., & Elsen, S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.18.618891 · Cited by 1

Protein Phosphorylation-Dephosphorylation and Signal Processing in the Archaea

Kennelly, P. J. (2017) · Springer eBooks · doi:10.1007/978-3-319-65536-9_13

Sensing, Signaling, and Uptake: An Introduction

Krell, T. (2018) · Springer eBooks · doi:10.1007/978-3-319-50542-8_29

Overview of Gas-sensing Systems

Aono, S. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781788012836-00001

Two-component systems regulate swarming in Pseudomonas aeruginosa PA14Preprint

Joge, S., Kollaran, A. M., Kotian, H. S., Badal, D., Prakash, D., Mishra, A., Varma, M. M., & Singh, V. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/445015

Analysis of Transcriptional Regulators Involved in Pseudomonas aeruginosa Antibiotic Resistance and Tolerance

Hall, C. W. (2019) · uO Research (University of Ottawa) · doi:10.20381/ruor-23727

The Role of Two-Component and Small RNA Regulatory Systems in Pseudomonas aeruginosa Biofilms

Taylor, P. (2019) · uO Research (University of Ottawa) · doi:10.20381/ruor-23857

Post-Translational Modifications in Corynebacterium glutamicum

Kosono, S. (2020) · Microbiology monographs · doi:10.1007/978-3-030-39267-3_6

We’re in this Together: Sensation of the Host Cell Environment by Endosymbiotic Bacteria

Dunn, C. D., Somborac, T., & Akpınar, B. A. (2020) · Results and problems in cell differentiation · doi:10.1007/978-3-030-51849-3_6

Intergenerational Cellular Signal Transfer and Erasure

McElfresh, G., & Ray, J. C. J. (2019) · SFI Press eBooks · doi:10.37911/9781947864078.05

A Cyclic di-GMP Two-Component System Contributes to Legionella pneumophila Differentiation and Resilience

Hughes, E. (2019) · Deep Blue (University of Michigan)

Bases moleculares de la especificidad en el mecanismo de transducción de señal en los sistemas de dos componentes bacterianos

Mora, C. M. (2021) · doi:10.4995/thesis/10251/161920

Assay developments for detection of biological analytes

Tan, J. (2019) · doi:10.32657/10356/143757

Wybrane zagadnienia z zakresu ochrony i zagrożeń środowiska

Babicz, M., & Nowakowicz-Dębek, B. (2021) · doi:10.24326/mon.2021.6

Bacterial chemoperception during the plant infection process

Cerna‐Vargas, J. P. (2021) · UPM Digital Archive (Technical University of Madrid) · doi:10.20868/upm.thesis.68073

Faculty Opinions recommendation of Integrated sensing of host stresses by inhibition of a cytoplasmic two-component system controls M. tuberculosis acute lung infection.

Kana, B. D. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.740134272.793585908

Papel de las Especies Reactivas de Oxígeno en la biosíntesis de Penicilina G, Cefalosporina C y Lovastatina

León, M. E. B. (2021) · doi:10.24275/uami.pg15bf11c

Biological Sensors for Microbiome Diagnostics

Breedon, A. M. E., Beabout, K., Coia, H. G., Davis, C. M., Harbaugh, S. V., Mauzy, C. A., Nelson, M., Saldanha, R., Stamps, B. W., & Goodson, M. S. (2022) · Wiley eBooks · doi:10.1002/9783527825462.ch6

Advanced transcriptomic analysis reveals the role of efflux pumps and media composition in antibiotic responses of Pseudomonas aeruginosaPreprint

Rajput, A., Tsunemoto, H., Sastry, A. V., Szubin, R., Rychel, K., Chauhan, S., Pogliano, J., & Palsson, B. Ø. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.04.487074

Sensing, Signaling, and Uptake: An Introduction

Krell, T. (2017) · Springer eBooks · doi:10.1007/978-3-319-20796-4_29-1

Understanding the Genetics and Evolution of Antimicrobial Resistance in Escherichia Coli

Bhatnagar, K. (2019) · Carleton University's Institutional Repository (MacOdrum Library, Carleton University) · doi:10.22215/etd/2019-13711

Faculty Opinions recommendation of Phyletic Distribution and Lineage-Specific Domain Architectures of Archaeal Two-Component Signal Transduction Systems.

Stock, A. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732337248.793568817

Faculty Opinions recommendation of Structure, function, and mechanism of the core circadian clock in cyanobacteria.

Ueda, H. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732665172.793558636

Information Theory in Molecular Evolution: From Models to Structures and Dynamics

Morcos, F. (2021) · MDPI eBooks · doi:10.3390/books978-3-0365-1212-9

Virulence adaptation of Pseudomonas aeruginosa phospholipase mutant with altered membrane phospholipid compositionPreprint

Caliskan, M., Poschmann, G., Gudzuhn, M., Waldera-Lupa, D. M., Streit, W. R., Jaeger, K., Stühler, K., & Kovačić, F. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.25.517918

Biochemical analysis of protein–protein interfaces underlying the regulation of bacterial secretion systems

Salar, S., & Schubot, F. D. (2022) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2022.07.030

System biology study on MtrAB protein-protein interaction network of Mycobacterium tuberculosis

Satsangi, A. T., Kumar, R., Jha, S. K., Chopra, A. P., & Haider, S. (2023) · Journal of Applied Biology & Biotechnology · doi:10.7324/jabb.2023.114465

Two component systems as attractive therapeutic target in methicillin resistant Staphylococcus aureus (MRSA)

Jaiswal, G., Singh, N., Monika, Devendra, D., & Srivastava, S. K. (2023) · AIP conference proceedings · doi:10.1063/5.0139115

Cross-regulation and cross-talk of conserved and accessory two-component regulatory systems orchestrate Pseudomonas copper resistancePreprint

Elsen, S., Simon, V., & Attrée, I. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.26.559466

Antipseudomonal Therapy and Quorum Quenching: A Prospective Marker

Babaniyi, G. G., Babaniyi, B. R., & Akor, U. J. (2023) · Royal Society of Chemistry eBooks · doi:10.1039/bk9781837671380-00059

Metabolism of ʟ -arabinose converges with virulence regulation to promote enteric pathogen fitnessPreprint

Cottam, C., White, R. T., Beck, L. C., Stewart, C. J., Beatson, S. A., Lowe, E. C., Grinter, R., & Connolly, J. P. R. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.21.572775

An ATP “Synthase” Derived from a Single Structural Domain of Bacterial Histidine Kinase

Ji, S., Zhou, Y., Chen, J. C., Yang, M., Li, C., Liu, M., Liu, Y., & Jiang, L. (2024) · Angewandte Chemie · doi:10.1002/ange.202318503

Phosphorylation Mechanism Switching in Histidine Kinases Is a Tool for Fast Protein Evolution: Insights From AlphaFold Models

Olivieri, F., Marti, M. A., & Wetzler, D. E. (2024) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26708

Diversity and functional annotation of bacteria community associated with the epithelial surface of Hippocampus kuda (yellow seahorse) and its surrounding environment

Maguate, N. J. I. F. S., & Tabugo, S. R. M. (2024) · Biodiversitas Journal of Biological Diversity · doi:10.13057/biodiv/d250541

Protein kinase PknB as a promising target for the development of antibacterial drugs toward Staphylococcus aureus

Moskovets, A. O., Pletnova, L. V., Maiula, T. G., Tverdyy, D. O., & Volynets, G. P. (2023) · Ukrainica Bioorganica Acta · doi:10.15407/bioorganica2023.01.003

A General Mechanism for the General Stress Response in BacteriaPreprint

Baral, R., Ho, K., Kumar, R. P., Hopkins, J. B., Watkins, M. B., LaRussa, S., Caban-Penix, S., Calderone, L. A., & Bradshaw, N. (2024) · eLife · doi:10.7554/elife.100376.1

Archaeal signalling networks - new insights into the structure and function of histidine kinases and response regulators of the methanogenic archaeon Methanosarcina acetivoransPreprint

Georgiev, N. F., Andersson, A. L., Ruppe, Z., Kattwinkel, L., & Frankenberg‐Dinkel, N. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.04.616672

Diversification of signal identity and modus operandi of the Haemophilus influenzae PAS-less ArcB sensor kinase

Álvarez, A. F., Santillán-Jiménez, A. D. J., Flores-Tamayo, E., Terán-Melo, J. L., Vázquez-Ciros, O. J., & Georgellis, D. (2024) · PLoS ONE · doi:10.1371/journal.pone.0315238

The histidine kinase VraS orchestrates the cell-wall stress response in Staphylococcus aureus via its direct interaction with glycopeptides and β-lactamsPreprint

Antinori, M. B., Sychantha, D., Koteva, K. K., Suárez, I. P., Peralta, M. D., Wright, G. D., & Llarrull, L. I. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.23.634444

A Short-Term View of Protein Sequence Evolution from Salmonella

Cherry, J. L. (2025) · Genome Biology and Evolution · doi:10.1093/gbe/evaf040 · Cited by 1

Functional and Pangenomic Exploration of Roc Two‐Component Regulatory Systems Identifies Novel Players Across Pseudomonas Species

Simon, V., Trouillon, J., Attrée, I., & Elsen, S. (2025) · Molecular Microbiology · doi:10.1111/mmi.15357

MibR and LibR are involved in the transcriptional regulation of the ipdC gene in Azospirillum brasilense Sp7

Reyes-Carmona, S. R., Jijón-Moreno, S., Ramírez-Mata, A., Xiqui-Vázquez, M. L., & Baca, B. E. (2025) · Research in Microbiology · doi:10.1016/j.resmic.2025.104295

Salt stress alters the selectivity of mature pecan for the rhizosphere community and its associated functional traits

Shi, M., Qin, T., Pu, Z., Yang, Z., Lim, K., Yang, M., & Wang, Z. (2025) · Frontiers in Plant Science · doi:10.3389/fpls.2025.1473473

A General Mechanism for Initiating the General Stress Response in BacteriaPreprint

Baral, R., Ho, K., Kumar, R. P., Hopkins, J. B., Watkins, M. B., LaRussa, S., Caban-Penix, S., Calderone, L. A., & Bradshaw, N. (2025) · eLife · doi:10.7554/elife.100376.2

NasR2 promoter-driven bioluminescent detection of bioavailable nitrogen

Abu‐Elreesh, G., & Abd-El-Haleem, D. A. M. (2025) · Discover Sensors · doi:10.1007/s44397-025-00011-3

Engineered bacteriophytochrome heterodimers for research and applications

Tuure, I., Böhm, C., Rumfeldt, J., Multamäki, E., & Takala, H. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110452

Dual regulatory role of cyclic di-GMP via the DgcY/HhmR complex in salt response of Halomonas hydrothermalis Y2

Zhang, Y., Wang, W., Liu, Y., Li, C., Liu, J., Feng, L., Gao, Y., Peng, Y., Wang, W., Li, C., et al. (2025) · mBio · doi:10.1128/mbio.01498-25

Sistemas de dos componentes y sus mecanismos de regulación

Contreras, F. U., & Georgellis, D. (2025) · TIP Revista Especializada en Ciencias Químico-Biológicas · doi:10.22201/fesz.23958723e.2025.742

The effect of cCMP and cUMP on growth of Pseudomonas aeruginosa

Risser, C., Rothschuh, J., Bähre, H., Neumann, D., Seifert, R., & Schirmer, B. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1675794

Two-Component Systems

Biondi, E. G. (2013) · Springer eBooks · doi:10.1007/978-1-4419-9863-7_744 · Cited by 1

Untangling the Complexity of Two-Component Signal Transduction in Bacteria

Wadach, P., Jakimowicz, D., & Gongerowska-Jac, M. (2025) · Microorganisms · doi:10.3390/microorganisms13092013 · Cited by 14

Bacterial Two-Component Systems: Structures and Signaling Mechanisms

Wang, S. (2012) · InTech eBooks · doi:10.5772/48277 · Cited by 45

Targeting New Functions and Applications of Bacterial Two‐Component Systems

Ji, S., Li, C., Liu, M., Liu, Y., & Jiang, L. (2024) · ChemBioChem · doi:10.1002/cbic.202400392 · Cited by 5

The role of sensory kinase proteins in two-component signal transduction

Álvarez, A. F., & Georgellis, D. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220848 · Cited by 19