Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram‐positive bacteria
Abstract
Summary: Clp proteolytic complexes consisting of a proteolytic core flanked by Clp ATPases are widely conserved in bacteria, and their biological roles have received considerable interest. In particular, mutants in the clp genes in the low‐GC‐content Gram‐positive phyla Bacillales and Lactobacillales display a diverse range of phenotypic changes including general stress sensitivity, aberrant cell morphology, failure to initiate developmental programs, and for pathogens, severely attenuated virulence. Extensive research dedicated to unravelling the molecular mechanisms underlying these complex phenotypes has led to fascinating new insights that will be covered by this review. First, Clp ATPases and ClpP‐containing proteolytic complexes play indispensable roles in cellular protein quality control systems by refolding or degrading damaged proteins in both stressed and non‐stressed cells. Secondly, ClpP proteases and the chaperone activity of Clp ATPases are important for controlling stability and activity of central transcriptional regulators, thereby exerting tremendous impact on cell physiology. Targets include major stress regulators like Spx (oxidative stress), the antisigma factor RsiW (alkaline stress) and HdiR (DNA damage) in addition to regulators of developmental programs like ComK (competence development), σ H and Sda (sporulation). Thus, Clp proteins are central in co‐ordinating developmental decisions and stress response in low GC Gram‐positive bacteria.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In Lactobacillaceae, the ClpL gene encodes an ATP-dependent Clp protease with chaperone activity involved in degrading misfolded or damaged intracellular proteins.
“in Lactobacillaceae family, this gene encodes an ATP-dependent Clp protease with chaperone activity which is involved in degrading misfolded or damaged intracellular proteins [76].”
From Bile Salt Hydrolase Activity in the Food-Derived Strain Levilactobacillus brevis M3R3: Genomic and Functional Characterization (2026) · cites this paper as [76]
Clp is inducible under acidic shock and contributes to the fast response of lactobacilli to harsh gastro-intestinal conditions, especially acid and bile stresses.
“Clp is inducible under acidic shock [77] and contributes to the fast response of lactobacilli to harsh gastro-intestinal conditions, especially to acid and bile stresses [76].”
From Bile Salt Hydrolase Activity in the Food-Derived Strain Levilactobacillus brevis M3R3: Genomic and Functional Characterization (2026) · cites this paper as [76]
Cites
Neuwald, A. F., Aravind, L., Spouge, J. L., & Koonin, E. V. (1999) · Genome Research · doi:10.1101/gr.9.1.27 · Cited by 1,811 · see citing works
Autoinduction and signal transduction in the regulation of staphylococcal virulence
Novick, R. P. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03526.x · Cited by 1,271 · see citing works
Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
Keiler, K. C., Waller, P. R. H., & Sauer, R. T. (1996) · Science · doi:10.1126/science.271.5251.990 · Cited by 1,125 · see citing works
Dubnau, D. A., & Losick, R. M. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05249.x · Cited by 729 · see citing works
HSP100/Clp proteins: a common mechanism explains diverse functions
Schirmer, E. C., Glover, J. R., Singer, M. A., & Lindquist, S. L. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10038-4 · Cited by 673 · see citing works
Flynn, J. M., Neher, S. B., Kim, Y., Sauer, R. T., & Baker, T. A. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00060-1 · Cited by 605 · see citing works
Mogk, A., Tomoyasu, T., Goloubinoff, P., Rüdiger, S., Röder, D., Langen, H., & Bukau, B. (1999) · The EMBO Journal · doi:10.1093/emboj/18.24.6934 · Cited by 596 · see citing works
The Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis
Wang, J., Hartling, J. A., & Flanagan, J. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80431-6 · Cited by 591 · see citing works
Dysregulation of bacterial proteolytic machinery by a new class of antibiotics
Brötz-Oesterhelt, H., Beyer, D., Kroll, H.-P., Endermann, R., Ladel, C., Schroeder, W., Hinzen, B., Raddatz, S., Paulsen, H., Henninger, K., et al. (2005) · Nature Medicine · doi:10.1038/nm1306 · Cited by 505 · see citing works
Sculpting the Proteome with AAA+ Proteases and Disassembly Machines
Sauer, R. T., Bolon, D. N. A., Burton, B. M., Burton, R. E., Flynn, J. M., Grant, R. A., Hersch, G. L., Joshi, S. A., Kenniston, J. A., Levchenko, I. V., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.020 · Cited by 462 · see citing works
Proteolysis in Bacterial Regulatory Circuits
Gottesman, S. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.110701.153228 · Cited by 423 · see citing works
Regulation of the Escherichia coliσE‐dependent envelope stress response
Alba, B. M., & Gross, C. A. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2003.03982.x · Cited by 407 · see citing works
Derré, I., Rapoport, G., & Msadek, T. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01152.x · Cited by 400 · see citing works
Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor
Turgay, K., Hahn, J., Burghoorn, J., & Dubnau, D. A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6730 · Cited by 352 · see citing works
Alternative roles of ClpX and ClpP in Staphylococcus aureus stress tolerance and virulence
Frees, D., Qazi, S. N. A., Hill, P. J., & Ingmer, H. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03524.x · Cited by 328 · see citing works
Self-citationFrees, D., Chastanet, A., Qazi, S. N. A., Sørensen, K., Hill, P. J., Msadek, T., & Ingmer, H. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04368.x · Cited by 327 · see citing works
Self-citationHomology in Structural Organization BetweenE. coliClpAP Protease and the Eukaryotic 26 S Proteasome
Kessel, M., Maurizi, M. R., Kim, B. Y., et al. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0400 · Cited by 299 · see citing works
Gaillot, O., Pellegrini, E., Bregenholt, S., Nair, S., & Berche, P. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01773.x · Cited by 269 · see citing works
Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase.
Kim, Y.-I., Levchenko, I. V., Fraczkowska, K., Woodruff, R. V., Sauer, R. T., & Baker, T. A. (2001) · Nature Structural Biology · doi:10.1038/84967 · Cited by 263 · see citing works
Inhibition of rot translation by RNAIII, a key feature of agr function
Geisinger, E., Adhikari, R. P., Jin, R., Ross, H. F., & Novick, R. P. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05292.x · Cited by 252 · see citing works
Nakano, S., Küster-Schöck, E., Grossman, A. D., & Zuber, P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2235180100 · Cited by 241 · see citing works
Msadek, T., Dartois, V. A., Kunst, F., Herbaud, M., Denizot, F., & Rapoport, G. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00735.x · Cited by 233 · see citing works
New insights into the ATP‐dependent Clp protease: Escherichia coli and beyond
Porankiewicz, J., Wang, J., & Clarke, A. K. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01357.x · Cited by 233 · see citing works
AAA+ proteins and substrate recognition, it all depends on their partner in crime
Dougan, D. A., Mogk, A., Zeth, K., et al. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03179-4 · Cited by 225 · see citing works
Michel, A., Agerer, F., Hauck, C. R., Herrmann, M., Ullrich, J., Hacker, J. H., & Ohlsen, K. (2006) · Journal of Bacteriology · doi:10.1128/jb.00074-06 · Cited by 214 · see citing works
Turgay, K., Hamoen, L. W., Venema, G., & Dubnau, D. A. (1997) · Genes & Development · doi:10.1101/gad.11.1.119 · Cited by 204 · see citing works
Gerth, U., Krüger, E., Derré, I., et al. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00840.x · Cited by 198 · see citing works
The Clp Proteases ofBacillus subtilisAre Directly Involved in Degradation of Misfolded Proteins
Krüger, E., Witt, E., Ohlmeier, S., et al. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.11.3259-3265.2000 · Cited by 196 · see citing works
Chastanet, A., Prudhomme, M., Claverys, J., & Msadek, T. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.24.7295-7307.2001 · Cited by 175 · see citing works
Spx-RNA Polymerase Interaction and Global Transcriptional Control during Oxidative Stress
Zuber, P. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.7.1911-1918.2004 · Cited by 171 · see citing works
Spx Is a Global Effector Impacting Stress Tolerance and Biofilm Formation in Staphylococcus aureus
Pamp, S. J., Frees, D., Engelmann, S., Hecker, M., & Ingmer, H. (2006) · Journal of Bacteriology · doi:10.1128/jb.00194-06 · Cited by 168 · see citing works
Self-citationMecA, an adaptor protein necessary for ClpC chaperone activity
Schlothauer, T., Mogk, A., Dougan, D. A., Bukau, B., & Turgay, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0535717100 · Cited by 162 · see citing works
Clp‐mediated proteolysis in Gram‐positive bacteria is autoregulated by the stability of a repressor
Krüger, E., Zühlke, D., Witt, E., Ludwig, H., & Hecker, M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.4.852 · Cited by 154 · see citing works
Redox‐sensitive transcriptional control by a thiol/disulphide switch in the global regulator, Spx
Nakano, S., Erwin, K. N., Ralle, M., et al. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04395.x · Cited by 154 · see citing works
Msadek, T., Kunst, F., & Rapoport, G. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.13.5788 · Cited by 152 · see citing works
A regulatory protein that interferes with activator-stimulated transcription in bacteria
Nakano, S., NAKANO, M. M., Zhang, Y., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0637648100 · Cited by 150 · see citing works
Robertson, G. T., Ng, W., Foley, J., Gilmour, R., & Winkler, M. E. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.13.3508-3520.2002 · Cited by 150 · see citing works
ClpP participates in the degradation of misfolded protein in Lactococcus lactis
Frees, D., & Ingmer, H. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01149.x · Cited by 144 · see citing works
Self-citationAdaptor protein controlled oligomerization activates the AAA+ protein ClpC
Kirstein, J., Schlothauer, T., Dougan, D. A., Lilie, H., Tischendorf, G. W., Mogk, A., Bukau, B., & Turgay, K. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601042 · Cited by 143 · see citing works
Krüger, E., & Hecker, M. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.24.6681-6688.1998 · Cited by 143 · see citing works
Regulation and Physiological Significance of ClpC and ClpP in Streptococcus mutans
Lemos, J. A. C., & Burne, R. A. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.22.6357-6366.2002 · Cited by 133 · see citing works
A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases
Žółkiewski, M. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05309.x · Cited by 129 · see citing works
CtsR controls class III heat shock gene expression in the human pathogen Listeria monocytogenes
Nair, S., Derré, I., Msadek, T., Gaillot, O., & Berche, P. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01752.x · Cited by 128 · see citing works
The CtsR regulator of stress response is active as a dimer and specifically degraded in vivo at 37°C
Derré, I., Rapoport, G., & Msadek, T. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02124.x · Cited by 124 · see citing works
Kirstein, J., Zühlke, D., Gerth, U., Turgay, K., & Hecker, M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600780 · Cited by 120 · see citing works
Self‐compartmentalized bacterial proteases and pathogenesis
Butler, S. M., Festa, R. A., Pearce, M. J., & Darwin, K. H. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05128.x · Cited by 119 · see citing works
Wojtyra, U., Thibault, G., Tuite, A. R., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307825200 · Cited by 118 · see citing works
Chastanet, A., Derré, I., Nair, S., & Msadek, T. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.4.1165-1174.2004 · Cited by 115 · see citing works
Frees, D., Sørensen, K., & Ingmer, H. (2005) · Infection and Immunity · doi:10.1128/iai.73.12.8100-8108.2005 · Cited by 114 · see citing works
Self-citationPan, Q., Garsin, D. A., & Losick, R. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00362-8 · Cited by 111 · see citing works
Multiple Pathways of Spx (YjbD) Proteolysis in Bacillus subtilis
Nakano, S., Zheng, G., NAKANO, M. M., et al. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.13.3664-3670.2002 · Cited by 107 · see citing works
SsrA-Mediated Tagging in Bacillus subtilis
Wiegert, T., & Schumann, W. (2001) · Journal of Bacteriology · doi:10.1128/jb.183.13.3885-3889.2001 · Cited by 107 · see citing works
Nair, S., Fréhel, C., Nguyen, L., Escuyer, V. E., & Berche, P. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01159.x · Cited by 104 · see citing works
The ClpX chaperone modulates assembly of the tubulin‐like protein FtsZ
Weart, R. B., Nakano, S., Lane, B. E., Zuber, P., & Levin, P. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04673.x · Cited by 102 · see citing works
The Amino-terminal Domain of ClpB Supports Binding to Strongly Aggregated Proteins
Barnett, M. E., Nagy, M., Kędzierska‐Mieszkowska, S., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505653200 · Cited by 100 · see citing works
NAKANO, M. M., Hajarizadeh, F., Zhu, Y., et al. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02639.x · Cited by 99 · see citing works
Effects of metabolic flux on stress response pathways in Lactococcus lactis
Duwat, P., Ehrlich, S. D., & Gruss, A. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01222.x · Cited by 96 · see citing works
Fine-Tuning in Regulation of Clp Protein Content in Bacillus subtilis
Gerth, U., Kirstein, J., Mostertz, J., et al. (2003) · Journal of Bacteriology · doi:10.1128/jb.186.1.179-191.2004 · Cited by 90 · see citing works
Kock, H., Gerth, U., & Hecker, M. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03875.x · Cited by 88 · see citing works
Involvement ofBacillus subtilisClpE in CtsR Degradation and Protein Quality Control
Miethke, M., Hecker, M., & Gerth, U. (2006) · Journal of Bacteriology · doi:10.1128/jb.00287-06 · Cited by 81 · see citing works
Kong, L., & Dubnau, D. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.13.5793 · Cited by 80 · see citing works
Involvement of Clp protease activity in modulating the Bacillus subtilis σ W stress response
Zellmeier, S., Schumann, W., & Wiegert, T. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05323.x · Cited by 80 · see citing works
Ibrahim, Y. M., Kerr, A. R., Silva, N. A., & Mitchell, T. J. (2005) · Infection and Immunity · doi:10.1128/iai.73.2.730-740.2005 · Cited by 78 · see citing works
CtsR Is the Master Regulator of Stress Response Gene Expression inOenococcus oeni
Grandvalet, C., Coucheney, F., Beltramo, C., & Guzzo, J. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.16.5614-5623.2005 · Cited by 78 · see citing works
Liu, J., Cosby, W. M., & Zuber, P. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01489.x · Cited by 73 · see citing works
The ClpP Peptidase Is the Major Determinant of Bulk Protein Turnover in Bacillus subtilis
Kock, H., Gerth, U., & Hecker, M. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.17.5856-5864.2004 · Cited by 73 · see citing works
Nanamiya, H., Ohashi, Y., Asai, K., et al. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00943.x · Cited by 72 · see citing works
Ingmer, H., Vogensen, F. K., Hammer, K., & Kilstrup, M. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.7.2075-2083.1999 · Cited by 65 · see citing works
Self-citationVarmanen, P., Ingmer, H., & Vogensen, F. K. (2000) · Microbiology · doi:10.1099/00221287-146-6-1447 · Cited by 61 · see citing works
Self-citationGaillot, O., Bregenholt, S., Jaubert, F., Santo, J. P. D., & Berche, P. (2001) · Infection and Immunity · doi:10.1128/iai.69.8.4938-4943.2001 · Cited by 58 · see citing works
Regulation of Repair by the 26S Proteasome
Sweder, K., & Madura, K. (2002) · Journal of Biomedicine and Biotechnology · doi:10.1155/s1110724302205033 · Cited by 56 · see citing works
Frees, D., Varmanen, P., & Ingmer, H. (2001) · Molecular Microbiology · doi:10.1046/j.1365-2958.2001.02503.x · Cited by 56 · see citing works
Self-citationRuvolo, M., Mach, K. E., & Burkholder, W. F. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05167.x · Cited by 55 · see citing works
Savijoki, K., Ingmer, H., Frees, D., Vogensen, F. K., Palva, A., & Varmanen, P. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03713.x · Cited by 53 · see citing works
Self-citationLiu, J., & Zuber, P. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.02053.x · Cited by 50 · see citing works
A New Tyrosine Phosphorylation Mechanism Involved in Signal Transduction in Bacillus subtilis
Kirstein, J., & Turgay, K. (2005) · Microbial Physiology · doi:10.1159/000089646 · Cited by 48 · see citing works
Oscarsson, J. (2005) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2005.05.003 · Cited by 47 · see citing works
Essentiality of clpX , but Not clpP , clpL , clpC , or clpE , in Streptococcus pneumoniae R6
Robertson, G. T., Ng, W., Gilmour, R., & Winkler, M. E. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.9.2961-2966.2003 · Cited by 43 · see citing works
Chastanet, A., & Msadek, T. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.2.683-687.2003 · Cited by 39 · see citing works
Nair, S., Poyart, C., Béretti, J., Veiga‐Fernandes, H., Berche, P., & Trieu‐Cuot, P. (2003) · Microbiology · doi:10.1099/mic.0.25783-0 · Cited by 36 · see citing works
Staphylococcus aureus ClpYQ plays a minor role in stress survival
Frees, D., Thomsen, L. E., & Ingmer, H. (2005) · Archives of Microbiology · doi:10.1007/s00203-005-0773-x · Cited by 34 · see citing works
Self-citationUnique Degradation Signal for ClpCP inBacillus subtilis
Pan, Q., & Losick, R. M. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.17.5275-5278.2003 · Cited by 34 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Genes and Molecules of Lactobacilli Supporting Probiotic Action
Lebeer, S., Vanderleyden, J., & De Keersmaecker, S. C. J. (2008) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00017-08 · Cited by 1,013 · see citing works
Stress Physiology of Lactic Acid Bacteria.
Papadimitriou, K., Alegría, Á., Bron, P. A., de Angelis, M., Gobbetti, M., Kleerebezem, M., Lemos, J. A., Linares, D. M., Ross, P., Stanton, C., et al. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00076-15 · Cited by 914 · see citing works
Self-citationBacterial Proteases and Virulence
Frees, D., Brøndsted, L., & Ingmer, H. (2013) · Subcellular Biochemistry · doi:10.1007/978-94-007-5940-4_7 · Cited by 159 · see citing works
Self-citationWall, T., Båth, K., Britton, R. A., Jonsson, H., Versalovic, J., & Roos, S. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.01502-06 · Cited by 131 · see citing works
Regulation of host hemoglobin binding by the Staphylococcus aureus Clp proteolytic system
Farrand, A. J., Reniere, M. L., Ingmer, H., Frees, D., & Skaar, E. P. (2013) · Journal of Bacteriology · doi:10.1128/jb.00505-13 · Cited by 56 · see citing works
Self-citationMazzoli, R., Pessione, E., Dufour, M., Laroute, V., Giuffrida, M. G., Giunta, C., Cocaign-Bousquet, M., & Loubière, P. (2010) · Amino Acids · doi:10.1007/s00726-010-0507-5 · Cited by 61 · see citing works
Nugroho, A. D. W., Kleerebezem, M., & Bachmann, H. (2021) · Current Opinion in Food Science · doi:10.1016/j.cofs.2020.12.005 · Cited by 48 · see citing works
Agolino, G., Cristofolini, M., Ronsivalle, M. A., Cattivelli, A., Tagliazucchi, D., Caggia, C., Solieri, L., & Randazzo, C. L. (2026) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-025-10810-0 · Cited by 1 · see citing works
“Clp is inducible under acidic shock [77] and contributes to the fast response of lactobacilli to harsh gastro-intestinal conditions, especially to acid and bile stresses [76].”
- Authors
- Frees, D., Savijoki, K., Varmanen, P., & Ingmer, H.
- Affiliations
- University of Copenhagen (DK)
- University of Helsinki (FI)
- Corresponding author
- Ingmer, Hanne
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2007-01-15
- Volume
- 63
- Issue
- 5
- Pages
- 1285-1295
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2165412123
- Cited by
- 288
- References
- 82
- Citations by year
- 2026: 11 · 2025: 10 · 2024: 9 · 2023: 16 · 2022: 11 · 2021: 13 · 2020: 17 · 2019: 16 · 2018: 13 · 2017: 13 · 2016: 16 · 2015: 6 · 2014: 15 · 2013: 25 · 2012: 21
- FWCI
- 1.38
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- Bacillales, Lactobacillales, protein quality control, protein refolding, protein degradation, chaperone activity, transcription factors, stress response, oxidative stress, alkaline stress, DNA damage, competence development, sporulation, virulence attenuation, cell morphology
- MeSH terms
- Adenosine Triphosphatases, Bacterial Proteins, Gram-Positive Bacteria, Endopeptidase Clp
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review