Elongation factor Tu is a multifunctional and processed moonlighting protein
Open accessAbstract
Many bacterial moonlighting proteins were originally described in medically, agriculturally, and commercially important members of the low G + C Firmicutes. We show Elongation factor Tu (Ef-Tu) moonlights on the surface of the human pathogens Staphylococcus aureus (Sa Ef-Tu) and Mycoplasma pneumoniae (Mpn Ef-Tu), and the porcine pathogen Mycoplasma hyopneumoniae (Mhp Ef-Tu). Ef-Tu is also a target of multiple processing events on the cell surface and these were characterised using an N-terminomics pipeline. Recombinant Mpn Ef-Tu bound strongly to a diverse range of host molecules, and when bound to plasminogen, was able to convert plasminogen to plasmin in the presence of plasminogen activators. Fragments of Ef-Tu retain binding capabilities to host proteins. Bioinformatics and structural modelling studies indicate that the accumulation of positively charged amino acids in short linear motifs (SLiMs), and protein processing promote multifunctional behaviour. Codon bias engendered by an A + T rich genome may influence how positively-charged residues accumulate in SLiMs.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Mycoplasmas are known for having moonlighting proteins, i.e., multifunctional proteins that are not the result of gene fusions.
“Because of evolutionary pressure to delete nonessential genes, mycoplasmas are known for having such multifunctional proteins.114−117”
From Toward the Complete Functional Characterization of a Minimal Bacterial Proteome (2022) · cites this paper as [117]
The Results identify multifunctional EF-Tu proteins in mycoplasmas, and the Discussion says protein processing can expand moonlighting functions (page unavailable). The cited paper does not link those functions to evolutionary pressure to delete nonessential genes, and the passages found do not address gene fusions. (LLM, conf=0.84)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
Sievers, F., Wilm, A., Dineen, D., Gibson, T., Karplus, K., Li, W.-Z., Lopez, R., McWilliam, H., Remmert, M., Söding, J., et al. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.75 · Cited by 15,576 · see citing works
SignalP 4.0: discriminating signal peptides from transmembrane regions
Petersen, T. N., Brunak, S., von Heijne, G., & Nielsen, H. (2011) · Nature Methods · doi:10.1038/nmeth.1701 · Cited by 8,847 · see citing works
Protein Identification and Analysis Tools in the ExPASy Server
Wilkins, M. R., Gasteiger, E., Bairoch, A., Sanchez, J., Williams, K. L., Appel, R. D., & Hochstrasser, D. F. (2003) · Humana Press eBooks · doi:10.1385/1-59259-584-7:531 · Cited by 6,209 · see citing works
Comparative Protein Structure Modeling Using Modeller
Eswar, N., Webb, B., Martı́-Renom, M. A., Madhusudhan, M. S., Eramian, D., Shen, M., Pieper, U., & Šali, A. (2006) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0506s15 · Cited by 4,564 · see citing works
Comparative Protein Structure Modeling Using MODELLER
Webb, B., & Šali, A. (2016) · Current Protocols in Bioinformatics · doi:10.1002/cpbi.3 · Cited by 4,349 · see citing works
Predicting coiled coils from protein sequences.
Lupas, A., Van Dyke, M., & Stock, J. (1991) · Science · doi:10.1126/science.252.5009.1162 · Cited by 3,953 · see citing works
Boller, T., & Felix, G. (2009) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.57.032905.105346 · Cited by 3,395 · see citing works
Phase separation of integral membrane proteins in Triton X-114 solution.
Bordier, C. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69848-0 · Cited by 3,324 · see citing works
Comparative Protein Structure Modeling Using MODELLER
Eswar, N., Webb, B., Martı́-Renom, M. A., Madhusudhan, M. S., Eramian, D., Shen, M., Pieper, U., & Šali, A. (2007) · Current Protocols in Protein Science · doi:10.1002/0471140864.ps0209s50 · Cited by 2,862 · see citing works
Gómez‐Gómez, L., & Boller, T. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80265-8 · Cited by 2,350 · see citing works
Tmbase-A database of membrane spanning protein segments
Hofmann, K., & Stoffel, W. (1993) · Medical Entomology and Zoology · Cited by 2,257 · see citing works
Zipfel, C., Kunze, G., Chinchilla, D., Caniard, A., Jones, J. D. G., Boller, T., & Felix, G. (2006) · Cell · doi:10.1016/j.cell.2006.03.037 · Cited by 2,068 · see citing works
Ashkenazy, H., Erez, E., Martz, E., Pupko, T., & Ben‐Tal, N. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq399 · Cited by 1,822 · see citing works
de Castro, E., Sigrist, C. J. A., Gattiker, A., Bulliard, V., Langendijk-Genevaux, P. S., Gasteiger, E., Bairoch, A., & Hulo, N. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl124 · Cited by 1,686 · see citing works
Robbins, J., Dilwortht, S. M., Laskey, R. A., & Dingwall, C. (1991) · Cell · doi:10.1016/0092-8674(91)90245-t · Cited by 1,490 · see citing works
Rost, B., Yachdav, G., & Liu, J. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh377 · Cited by 1,462 · see citing works
CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis
Miya, A., Albert, P., Shinya, T., Desaki, Y., Ichimura, K., Shirasu, K., Narusaka, Y., Kawakami, N., Kaku, H., & Shibuya, N. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705147104 · Cited by 1,428 · see citing works
Molecular modeling of protein-glycosaminoglycan interactions.
Cardin, A. D., & Weintraub, H. J. R. (1989) · Arteriosclerosis An Official Journal of the American Heart Association Inc · doi:10.1161/01.atv.9.1.21 · Cited by 1,301 · see citing works
Innate immunity in plants and animals: striking similarities and obvious differences
Nürnberger, T., Brunner, F., Kemmerling, B., & Piater, L. A. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.0119.x · Cited by 1,288 · see citing works
Feature-based prediction of non-classical and leaderless protein secretion
Bendtsen, J. D., Jensen, L. J., Blom, N., von HEIJNE, G., & Brunak, S. (2004) · Protein Engineering Design and Selection · doi:10.1093/protein/gzh037 · Cited by 1,179 · see citing works
Comparative Protein Structure Modeling Using MODELLER
Webb, B., & Šali, A. (2014) · Current Protocols in Bioinformatics · doi:10.1002/0471250953.bi0506s47 · Cited by 1,141 · see citing works
Wright, P. E., & Dyson, H. J. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.12.003 · Cited by 1,012 · see citing works
The N Terminus of Bacterial Elongation Factor Tu Elicits Innate Immunity in Arabidopsis Plants
Kunze, G., Zipfel, C., Robatzek, S., Niehaus, K., Boller, T., & Felix, G. (2004) · The Plant Cell · doi:10.1105/tpc.104.026765 · Cited by 955 · see citing works
Otto, M. J. (2008) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-75418-3_10 · Cited by 903 · see citing works
Wan, J., Zhang, X.-C., Neece, D. J., Ramonell, K. M., Clough, S. J., Kim, S., Stacey, M. G., & Stacey, G. S. (2008) · The Plant Cell · doi:10.1105/tpc.107.056754 · Cited by 800 · see citing works
Weedn, V. W. (1999) · American Journal of Clinical Pathology · doi:10.1093/ajcp/111.2.278 · Cited by 773 · see citing works
Explosive cell lysis as a mechanism for the biogenesis of bacterial membrane vesicles and biofilms
Turnbull, L., Toyofuku, M., Hynen, A. L., Kurosawa, M., Pessi, G., Petty, N. K., Osvath, S. R., Cárcamo-Oyarce, G., Gloag, E. S., Shimoni, R., et al. (2016) · Nature Communications · doi:10.1038/ncomms11220 · Cited by 709 · see citing works
Self-citationStaphylococcus aureus biofilms: recent developments in biofilm dispersal
Lister, J. L., & Horswill, A. R. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00178 · Cited by 705 · see citing works
Current Topics in Microbiology and Immunology
Cooper, M. D., Henle, W., HOFSCHNEIDER, P. H., Koprowski, H., Melchers, F., Rott, R., Schweiger, H., Vogt, P. K., & Zinkernagel, R. M. (1982) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-68528-6 · Cited by 645 · see citing works
Tissue cultures and mycoplasmas.
Hayflick, L. (1965) · PubMed · Cited by 632 · see citing works
Attributes of short linear motifs
Davey, N. E., Roey, K. V., Weatheritt, R. J., Toedt, G., Uyar, B., Altenberg, B., Budd, A., Diella, F., Dinkel, H., & Gibson, T. J. (2011) · Molecular BioSystems · doi:10.1039/c1mb05231d · Cited by 626 · see citing works
Izano, E. A., Amarante, M. A., Kher, W. B., & Kaplan, J. B. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.02073-07 · Cited by 553 · see citing works
Modulation of eDNA Release and Degradation Affects Staphylococcus aureus Biofilm Maturation
Mann, E. E., Rice, K. C., Boles, B. R., Endres, J. L., Ranjit, D. K., Chandramohan, L., Tsang, L. H., Smeltzer, M. S., Horswill, A. R., & Bayles, K. W. (2009) · PLoS ONE · doi:10.1371/journal.pone.0005822 · Cited by 508 · see citing works
Henderson, B. E., & Martin, A. C. R. (2011) · Infection and Immunity · doi:10.1128/iai.00179-11 · Cited by 460 · see citing works
Granato, D., Bergonzelli, G. E., Pridmore, R. D., Marvin, L., Rouvet, M., & Corthésy-Theulaz, I. E. (2004) · Infection and Immunity · doi:10.1128/iai.72.4.2160-2169.2004 · Cited by 410 · see citing works
Mühlradt, P. F., Kieß, M., Meyer, H., Süßmuth, R. D., & Jung, G. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.11.1951 · Cited by 396 · see citing works
The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation
Kjeldgaard, M., Nissen, P., Thirup, S., & Nyborg, J. (1993) · Structure · doi:10.1016/0969-2126(93)90007-4 · Cited by 392 · see citing works
Jones, D. A., & Takemoto, D. (2003) · Current Opinion in Immunology · doi:10.1016/j.coi.2003.11.016 · Cited by 336 · see citing works
MetaDisorder: a meta-server for the prediction of intrinsic disorder in proteins
Kozlowski, L. P., & Bujnicki, J. M. (2012) · BMC Bioinformatics · doi:10.1186/1471-2105-13-111 · Cited by 328 · see citing works
The many roles of the eukaryotic elongation factor 1 complex
Sasikumar, A. N., Perez, W. B., & Kinzy, T. G. (2012) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1118 · Cited by 298 · see citing works
Dallo, S. F., Kannan, T. R., Blaylock, M. W., & Baseman, J. B. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.03207.x · Cited by 293 · see citing works
Housekeeping enzymes as virulence factors for pathogens
Pancholi, V., & Chhatwal, G. S. (2003) · International Journal of Medical Microbiology · doi:10.1078/1438-4221-00283 · Cited by 290 · see citing works
Refined structure of elongation factor EF-Tu from Escherichia coli
Kjeldgaard, M., & Nyborg, J. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90986-t · Cited by 285 · see citing works
eEF1A: Thinking Outside the Ribosome
Mateyak, M. K., & Kinzy, T. G. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.113795 · Cited by 274 · see citing works
Protein-based biofilm matrices in Staphylococci
Speziale, P., Pietrocola, G., Foster, T. J., & Geoghegan, J. A. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00171 · Cited by 269 · see citing works
The root of the universal tree and the origin of eukaryotes based on elongation factor phylogeny.
Baldauf, S. L., Palmer, J. D., & Doolittle, W. F. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.7749 · Cited by 269 · see citing works
Heparin Stimulates Staphylococcus aureus Biofilm Formation
Shanks, R. M. Q., Donegan, N. P., Graber, M. L., Buckingham, S. E., Zegans, M. E., Cheung, A. L., & O’Toole, G. A. (2005) · Infection and Immunity · doi:10.1128/iai.73.8.4596-4606.2005 · Cited by 266 · see citing works
Sharp, J. K., McNeil, M., & Albersheim, P. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90865-3 · Cited by 261 · see citing works
ISIS: interaction sites identified from sequence
Ofran, Y., & Rost, B. (2007) · Bioinformatics · doi:10.1093/bioinformatics/btl303 · Cited by 257 · see citing works
Crowe, J. D., Sievwright, I. K., Auld, G. C., Moore, N. R., Gow, N. A. R., & Booth, N. A. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03390.x · Cited by 246 · see citing works
Kunert, A., Losse, J., Gruszin, C., Hühn, M., Kaendler, K., Mikkat, S., Volke, D., Hoffmann, R., Jokiranta, T. S., Seeberger, H., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.5.2979 · Cited by 228 · see citing works
Helix unwinding in the effector region of elongation factor EF-Tu–GDP
Polekhina, G., Thirup, S., Kjeldgaard, M., Nissen, P., Lippmann, C., & Nyborg, J. (1996) · Structure · doi:10.1016/s0969-2126(96)00122-0 · Cited by 217 · see citing works
Short linear motifs – ex nihilo evolution of protein regulation
Davey, N. E., Cyert, M., & Moses, A. M. (2015) · Cell Communication and Signaling · doi:10.1186/s12964-015-0120-z · Cited by 217 · see citing works
Foulston, L., Elsholz, A. K. W., DeFrancesco, A. S., & Losick, R. M. (2014) · mBio · doi:10.1128/mbio.01667-14 · Cited by 207 · see citing works
Ventura, C. L., Małachowa, N., Hammer, C. H., Nardone, G. A., Robinson, M. A., Kobayashi, S. D., & DeLeo, F. R. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011634 · Cited by 206 · see citing works
The eEF1A Proteins: At the Crossroads of Oncogenesis, Apoptosis, and Viral Infections
Abbas, W., Kumar, A., & Herbein, G. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00075 · Cited by 205 · see citing works
Ejiri, S. (2002) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.66.1 · Cited by 203 · see citing works
The cell wall subproteome of <b><i>Listeria monocytogenes</i></b>
Schaumburg, J., Diekmann, O., Hagendorff, P., Bergmann, S., Rohde, M., Hammerschmidt, S., Jänsch, L., Wehland, J., & Kärst, U. (2004) · PROTEOMICS · doi:10.1002/pmic.200400928 · Cited by 199 · see citing works
Are elicitins cryptograms in plant-Oomycete communications?
Ponchet, M., Panabi�res, F., Milat, M.-L., Mikeš, V., Montillet, J., Suty, L., Triantaphylidès, C., Tirilly, Y., & Blein, J.-P. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050491 · Cited by 187 · see citing works
Content of elongation factor Tu in Escherichia coli.
Furano, A. V. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.12.4780 · Cited by 185 · see citing works
Improved Disorder Prediction by Combination of Orthogonal Approaches
Schlessinger, A., Punta, M., Yachdav, G., Kaján, L., & Rost, B. (2009) · PLoS ONE · doi:10.1371/journal.pone.0004433 · Cited by 177 · see citing works
Nandan, D., Yi, T., Lopez, M., Lai, C., & Reiner, N. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209210200 · Cited by 154 · see citing works
Lamberti, A., Caraglia, M., Longo, O., Marra, M., Abbruzzese, A., & Arcari, P. (2004) · Amino Acids · doi:10.1007/s00726-004-0088-2 · Cited by 153 · see citing works
Schwartz, K., Ganesan, M., Payne, D. E., Solomon, M. J., & Boles, B. R. (2015) · Molecular Microbiology · doi:10.1111/mmi.13219 · Cited by 150 · see citing works
Thornton, S., Anand, N., Purcell, D., & Lee, J. W. J. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0461-8 · Cited by 147 · see citing works
Haunreiter, V. D., Foulston, L., DeFrancesco, A. S., & Losick, R. M. (2015) · Journal of Bacteriology · doi:10.1128/jb.00726-15 · Cited by 145 · see citing works
Xolalpa, W., Vallecillo, A. J., Lara, M., Mendoza‐Hernández, G., Comini, M. A., Spallek, R., Singh, M., & Espitia, C. (2007) · PROTEOMICS · doi:10.1002/pmic.200600876 · Cited by 141 · see citing works
Profiling the surfacome of Staphylococcus aureus
Dreisbach, A., Hempel, K., Buist, G., Hecker, M., Becher, D., & van Dijl, J. M. (2010) · PROTEOMICS · doi:10.1002/pmic.201000062 · Cited by 136 · see citing works
Two-dimensional gel protein database ofSaccharomyces cerevisiae (update 1999)
Perrot, M., Sagliocco, F. A., Mini, T., Monribot, C., Schneider, U., Shevchenko, A., Mann, M., Jenö, P., & Boucherie, H. (1999) · Electrophoresis · doi:10.1002/(sici)1522-2683(19990801)20:11 · Cited by 129 · see citing works
The Roles of Moonlighting Proteins in Bacteria
Wang, G., Xia, Y., Cui, J. R., Gu, Z., Song, Y., Chen, Y. Q., Chen, H., Zhang, H., & Chen, W. (2014) · Current Issues in Molecular Biology · doi:10.21775/cimb.016.015 · Cited by 127 · see citing works
Staphylococcal Major Autolysin (Atl) Is Involved in Excretion of Cytoplasmic Proteins
Pasztor, L., Ziebandt, A., Nega, M., Schlag, M., Haase, S. P., Franz‐Wachtel, M., Madlung, J., Nordheim, A., Heinrichs, D. E., & Götz, F. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.167312 · Cited by 126 · see citing works
Proteolytic Processing of theMycoplasma hyopneumoniaeCilium Adhesin
Djordjevic, S. P., Cordwell, S. J., Djordjevic, M. A., Wilton, J. L., & Minion, F. C. (2004) · Infection and Immunity · doi:10.1128/iai.72.5.2791-2802.2004 · Cited by 119 · see citing works
Self-citationCrystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex.
Andersen, G. R., Valente, L., Pedersen, L., Kinzy, T. G., & Nyborg, J. (2001) · Nature Structural Biology · doi:10.1038/88598 · Cited by 116 · see citing works
Elongation factor Tu: a regulatory GTPase with an integrated effector
Sprinzl, M. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90149-x · Cited by 111 · see citing works
Duensing, T. D., Wing, J. S., & van Putten, J. P. M. (1999) · Infection and Immunity · doi:10.1128/iai.67.9.4463-4468.1999 · Cited by 106 · see citing works
Identification of a fibronectin‐binding domain within the Campylobacter jejuni CadF protein
Konkel, M. E., Christensen, J. E., Keech, A. M., Monteville, M. R., Klena, J. D., & Garvis, S. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04744.x · Cited by 105 · see citing works
Kuit, T. A., Dinkla, K., Rohde, M., Chhatwal, G. S., Uphoff, C. C., Srivastava, M., Cordwell, S. J., Geary, S. J., Liao, X., Minion, F. C., et al. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05139.x · Cited by 105 · see citing works
Self-citationBarel, M., Hovanessian, A. G., Meibom, K. L., Briand, J., Dupuis, M., & Charbit, A. (2008) · BMC Microbiology · doi:10.1186/1471-2180-8-145 · Cited by 101 · see citing works
Fen, L., Wang, H., Wang, S., Jiang, W., Shan, C., Li, B., Yang, J., Zhang, S., & Sun, W. (2014) · Journal of Integrative Plant Biology · doi:10.1111/jipb.12306 · Cited by 100 · see citing works
Solis, N., Larsen, M. R., & Cordwell, S. J. (2010) · PROTEOMICS · doi:10.1002/pmic.200900564 · Cited by 99 · see citing works
Binding of heparan sulfate to Staphylococcus aureus
Liang, O. D., Ascencio, F., Fransson, L. Å., & Wadström, T. (1992) · Infection and Immunity · doi:10.1128/iai.60.3.899-906.1992 · Cited by 99 · see citing works
Two Distinct EF-Tu Epitopes Induce Immune Responses in Rice and Arabidopsis
Furukawa, T., Inagaki, H., Takai, R., Hirai, H., & Che, F. (2013) · Molecular Plant-Microbe Interactions · doi:10.1094/mpmi-10-13-0304-r · Cited by 98 · see citing works
Balasubramanian, S., Kannan, T. R., & Baseman, J. B. (2008) · Infection and Immunity · doi:10.1128/iai.00173-08 · Cited by 97 · see citing works
Wang, W., & Jeffery, C. J. (2016) · Molecular BioSystems · doi:10.1039/c5mb00550g · Cited by 96 · see citing works
Seymour, L. M., Jenkins, C., Deutscher, A. T., Raymond, B. B. A., Padula, M. P., Tacchi, J. L., Bogema, D. R., Eamens, G. J., Woolley, L. K., Dixon, N. E., et al. (2011) · Cellular Microbiology · doi:10.1111/j.1462-5822.2011.01702.x · Cited by 89 · see citing works
Self-citationSeymour, L. M., Deutscher, A. T., Jenkins, C., Kuit, T. A., Falconer, L., Minion, F. C., Crossett, B., Padula, M. P., Dixon, N. E., Djordjevic, S. P., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.104463 · Cited by 89 · see citing works
Self-citationProteins complexed to the P1 adhesin of Mycoplasma pneumoniae
Layh‐Schmitt, G., Podtelejnikov, A. V., & Mann, M. (2000) · Microbiology · doi:10.1099/00221287-146-3-741 · Cited by 88 · see citing works
Bogema, D. R., Deutscher, A. T., Woolley, L. K., Seymour, L. M., Raymond, B. B. A., Tacchi, J. L., Padula, M. P., Dixon, N. E., Minion, F. C., Jenkins, C., et al. (2012) · mBio · doi:10.1128/mbio.00282-11 · Cited by 88 · see citing works
Self-citationBereiter, M., Young, T. F., Joo, H., & Ross, R. F. (1990) · Veterinary Microbiology · doi:10.1016/0378-1135(90)90075-7 · Cited by 86 · see citing works
Wolff, D. G., Valencia, M. M. C., Abe, C. M., Monaris, D., de Morais, Z. M., de Souza, G. O., Vasconcellos, S. A., Isaac, L., Abreu, P. A. E., & Barbosa, A. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081818 · Cited by 84 · see citing works
Li, Q., Liu, H., Du, D., Yu, Y., Ma, C., Jiao, F., Yao, H., Lu, C., & Zhang, W. (2015) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2015.00082 · Cited by 84 · see citing works
Type 1 and type 2 strains of Mycoplasma pneumoniae form different biofilms
Simmons, W. L., Daubenspeck, J. M., Osborne, J. D., Balish, M. F., Waites, K. B., & Dybvig, K. F. (2013) · Microbiology · doi:10.1099/mic.0.064782-0 · Cited by 83 · see citing works
Glowalla, E., Tosetti, B., Krönke, M., & Krut, O. (2009) · Infection and Immunity · doi:10.1128/iai.00617-08 · Cited by 81 · see citing works
Nieves, W., Heang, J., Asakrah, S. K., zu Bentrup, K. H., Roy, C. J., & Morici, L. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014361 · Cited by 80 · see citing works
Deutscher, A. T., Jenkins, C., Minion, F. C., Seymour, L. M., Padula, M. P., Dixon, N. E., Walker, M. J., & Djordjevic, S. P. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07345.x · Cited by 79 · see citing works
Self-citationShimizu, T., Kida, Y., & Kuwano, K. (2008) · Infection and Immunity · doi:10.1128/iai.00257-08 · Cited by 76 · see citing works
Calcutt, M. J., Kim, M. F., Karpas, A. B., Mühlradt, P. F., & Wise, K. S. (1999) · Infection and Immunity · doi:10.1128/iai.67.2.760-771.1999 · Cited by 74 · see citing works
Hempel, K., Pané‐Farré, J., Otto, A., Sievers, S., Hecker, M., & Becher, D. (2010) · Journal of Proteome Research · doi:10.1021/pr901143a · Cited by 70 · see citing works
Wilton, J. L., Jenkins, C., Cordwell, S. J., Falconer, L., Minion, F. C., Oneal, D., Djordjevic, M. A., Connolly, A. M., Barchia, I. M., Walker, M. J., et al. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06546.x · Cited by 70 · see citing works
Self-citationHempel, K., Herbst, F., Moche, M., Hecker, M., & Becher, D. (2011) · Journal of Proteome Research · doi:10.1021/pr1009838 · Cited by 69 · see citing works
Dallo, S. F., Zhang, B., Denno, J., Hong, S., Tsai, A.-Y., Haskins, W., Ye, J. Y., & Weitao, T. (2012) · The Scientific World JOURNAL · doi:10.1100/2012/128705 · Cited by 67 · see citing works
Tuf of Streptococcus pneumoniae is a surface displayed human complement regulator binding protein
Mohan, S., Hertweck, C., Dudda, A., Hammerschmidt, S., Skerka, C., Hallström, T., & Zipfel, P. F. (2014) · Molecular Immunology · doi:10.1016/j.molimm.2014.06.029 · Cited by 64 · see citing works
Jarocki, V. M., Santos, J., Tacchi, J. L., Raymond, B. B. A., Deutscher, A. T., Jenkins, C., Padula, M. P., & Djordjevic, S. P. (2015) · Open Biology · doi:10.1098/rsob.140175 · Cited by 63 · see citing works
Self-citationPinto, P. M., Chemale, G., de Castro, L. A., Costa, A. P. M., Kich, J. D., Vainstein, M. H., Zaha, A., & Ferreira, H. B. (2006) · Veterinary Microbiology · doi:10.1016/j.vetmic.2006.11.018 · Cited by 63 · see citing works
Tacchi, J. L., Raymond, B. B. A., Haynes, P. A., Berry, I. J., Widjaja, M., Bogema, D. R., Woolley, L. K., Jenkins, C., Minion, F. C., Padula, M. P., et al. (2016) · Open Biology · doi:10.1098/rsob.150210 · Cited by 62 · see citing works
Self-citationGibson, T. J., Dinkel, H., Roey, K. V., & Diella, F. (2015) · Cell Communication and Signaling · doi:10.1186/s12964-015-0121-y · Cited by 60 · see citing works
Excretion of cytosolic proteins (ECP) in bacteria
Götz, F., Yu, W., Dube, L., Prax, M., & Ebner, P. (2014) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2014.12.021 · Cited by 60 · see citing works
Deutscher, A. T., Tacchi, J. L., Minion, F. C., Padula, M. P., Crossett, B., Bogema, D. R., Jenkins, C., Kuit, T. A., Walker, M. J., & Djordjevic, S. P. (2012) · Journal of Proteome Research · doi:10.1021/pr201115v · Cited by 59 · see citing works
Self-citationRobinson, M. W., Buchtmann, K. A., Jenkins, C., Tacchi, J. L., Raymond, B. B. A., To, J., Roy Chowdhury, P., Woolley, L. K., Labbate, M., Turnbull, L., et al. (2013) · Open Biology · doi:10.1098/rsob.130017 · Cited by 58 · see citing works
Self-citationIdentification of Lipoprotein MslA as a Neoteric Virulence Factor ofMycoplasma gallisepticum
Szczepanek, S. M., Frasca, S., Schumacher, V. L., Liao, X., Padula, M. P., Djordjevic, S. P., & Geary, S. J. (2010) · Infection and Immunity · doi:10.1128/iai.00154-10 · Cited by 58 · see citing works
Self-citationThomas, C., Jacobs, E., & Dumke, R. (2012) · Microbiology · doi:10.1099/mic.0.061184-0 · Cited by 57 · see citing works
Self-citationStructural determination of the functional sites of E. coli elongation factor Tu
Clark, B. F. C., Kjeldgaard, M., la Cour, T. F. M., Thirup, S., & Nyborg, J. (1990) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(90)90167-z · Cited by 57 · see citing works
Excretion of cytoplasmic proteins ( ECP ) in S taphylococcus aureus
Ebner, P., Prax, M., Nega, M., Koch, I., Dube, L., Yu, W., Rinker, J., Popella, P., Floetenmeyer, M., & Götz, F. (2015) · Molecular Microbiology · doi:10.1111/mmi.13065 · Cited by 57 · see citing works
Mhp107 Is a Member of the Multifunctional Adhesin Family of Mycoplasma hyopneumoniae
Seymour, L. M., Falconer, L., Deutscher, A. T., Minion, F. C., Padula, M. P., Dixon, N. E., Djordjevic, S. P., & Walker, M. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.208140 · Cited by 55 · see citing works
Self-citationBogema, D. R., Scott, N. E., Padula, M. P., Tacchi, J. L., Raymond, B. B. A., Jenkins, C., Cordwell, S. J., Minion, F. C., Walker, M. J., & Djordjevic, S. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.226084 · Cited by 54 · see citing works
Self-citationRaymond, B. B. A., Tacchi, J. L., Jarocki, V. M., Minion, F. C., Padula, M. P., & Djordjevic, S. P. (2013) · Journal of Proteome Research · doi:10.1021/pr400903s · Cited by 52 · see citing works
Self-citationCurrent Topics in Microbiology and Immunology
Sch, E. (1970) · Journal of Pest Science · doi:10.1007/bf02330261 · Cited by 51 · see citing works
Nishiyama, K., Ochiai, A., Tsubokawa, D., Ishihara, K., Yamamoto, Y., & Mukai, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083703 · Cited by 51 · see citing works
Gründel, A., Pfeiffer, M., Jacobs, E., & Dumke, R. (2015) · Infection and Immunity · doi:10.1128/iai.01071-15 · Cited by 50 · see citing works
Self-citationGründel, A., Jacobs, E., & Dumke, R. (2016) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2016.09.001 · Cited by 46 · see citing works
Self-citationThe Overlap of Small Molecule and Protein Binding Sites within Families of Protein Structures
Davis, F. P., & Šali, A. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000668 · Cited by 45 · see citing works
Matsubayashi, M., Kimata, I., Uni, S., Lillehoj, H. S., Matsuda, H., Furuya, M., Tani, H., & Sasai, K. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515544 · Cited by 45 · see citing works
Gründel, A., Friedrich, K., Pfeiffer, M., Jacobs, E., & Dumke, R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126600 · Cited by 44 · see citing works
Self-citationScarman, A. L., Chin, J. J.-C., Earmens, G. J., Delaney, S. F., & Djordjevic, S. P. (1997) · Microbiology · doi:10.1099/00221287-143-2-663 · Cited by 44 · see citing works
Self-citationBoone, T. J., & Tyrrell, G. J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.361261 · Cited by 42 · see citing works
Factors influencing the nuclear targeting ability of nuclear localization signals
Sun, Y., Xian, L., Xing, H., Yu, J., Yang, Z. L., Yang, T., Yang, L., & Ding, P. (2016) · Journal of drug targeting · doi:10.1080/1061186x.2016.1184273 · Cited by 42 · see citing works
The Mycoplasma gallisepticum OsmC-like protein MG1142 resides on the cell surface and binds heparin
Jenkins, C., Geary, S. J., Gladd, M. F., & Djordjevic, S. P. (2007) · Microbiology · doi:10.1099/mic.0.2006/004937-0 · Cited by 41 · see citing works
Self-citationBergh, P. V., Heller, M., Braga-Lagache, S., & Joachim Frey, A. (2013) · Proteome Science · doi:10.1186/1477-5956-11-44 · Cited by 41 · see citing works
Raymond, B. B. A., Jenkins, C., Seymour, L. M., Tacchi, J. L., Widjaja, M., Jarocki, V. M., Deutscher, A. T., Turnbull, L., Whitchurch, C. B., Padula, M. P., et al. (2014) · Cellular Microbiology · doi:10.1111/cmi.12377 · Cited by 39 · see citing works
Self-citationTacchi, J. L., Raymond, B. B. A., Jarocki, V. M., Berry, I. J., Padula, M. P., & Djordjevic, S. P. (2014) · Journal of Proteome Research · doi:10.1021/pr500087c · Cited by 39 · see citing works
Self-citationAdhesion and biofilm formation of Mycoplasma pneumoniae on an abiotic surface
Kornspan, D., Tarshis, M. A., & Rottem, S. (2011) · Archives of Microbiology · doi:10.1007/s00203-011-0749-y · Cited by 38 · see citing works
Davis, K. L., & Wise, K. S. (2002) · Infection and Immunity · doi:10.1128/iai.70.3.1129-1135.2002 · Cited by 37 · see citing works
Liu, L., Liu, X., Sun, W., Li, M., & Gao, Y. (2013) · Proteome Science · doi:10.1186/1477-5956-11-1 · Cited by 37 · see citing works
Muñoz-Provencio, D., Pérez‐Martínez, G., & Monedero, V. (2011) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-011-9065-8 · Cited by 35 · see citing works
Balasubramanian, S., Kannan, T. R., Hart, P. J., & Baseman, J. B. (2009) · Infection and Immunity · doi:10.1128/iai.00081-09 · Cited by 35 · see citing works
Scott, N. E., Marzook, N. B., Deutscher, A. T., Falconer, L., Crossett, B., Djordjevic, S. P., & Cordwell, S. J. (2009) · PROTEOMICS · doi:10.1002/pmic.200900440 · Cited by 33 · see citing works
Self-citationJiang, F., Jin-yan, H., Navarro–Álvarez, N., Xu, J., Li, X., Li, P., & Wu, W. (2016) · PLoS ONE · doi:10.1371/journal.pone.0161170 · Cited by 33 · see citing works
Gaucher, E. A., Das, U. K., Miyamoto, M. M., & Benner, S. A. (2002) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a004113 · Cited by 28 · see citing works
Guillot, A., Boulay, M., Chambellon, É., Gitton, C., Monnet, V., & Juillard, V. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00424 · Cited by 26 · see citing works
Chlamydia trachomatis Outer Membrane Complex Protein B (OmcB) Is Processed by the Protease CPAF
Hou, S., Lei, L., Yang, Z., Qi, M., Liu, Q., & Zhong, G. (2012) · Journal of Bacteriology · doi:10.1128/jb.02087-12 · Cited by 25 · see citing works
Fragmentation of CagA Reduces Hummingbird Phenotype Induction by Helicobactor pylori
Chang, C.-C., Kuo, W.-S., Chen, Y.-C., Perng, C., Lin, H., & Ou, Y.-H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0150061 · Cited by 25 · see citing works
Liew, Y. K., Hamat, R. A., van Belkum, A., Chong, P. P., & Neela, V. (2015) · Clinical and Vaccine Immunology · doi:10.1128/cvi.00493-14 · Cited by 23 · see citing works
Alves, L. R., de Oliveira, C. I., & Goldenberg, S. (2015) · BMC Microbiology · doi:10.1186/s12866-015-0436-2 · Cited by 23 · see citing works
Widjaja, M., Berry, I. J., Pont, E., Padula, M. P., & Djordjevic, S. P. (2015) · Proteomes · doi:10.3390/proteomes3040512 · Cited by 23 · see citing works
Self-citationFallgren, C., Utt, M., & Ljungh, Å. (2001) · Journal of Medical Microbiology · doi:10.1099/0022-1317-50-6-547 · Cited by 22 · see citing works
Microarray‐based identification of human antibodies against Staphylococcus aureus antigens
Kloppot, P., Selle, M., Köhler, C., Stentzel, S., Fuchs, S., Liebscher, V., Müller, E., Devika, K., Ohlsen, K., Bröker, B. M., et al. (2015) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.201400123 · Cited by 21 · see citing works
Monteiro, R., Hébraud, M., Chafsey, I., Chambon, C., Viala, D., Torres, C., Poeta, P. A. C. Q. D., & Igrejas, G. (2015) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2015.07.004 · Cited by 19 · see citing works
Heparin interacts with elongation factor 1α of Cryptosporidium parvum and inhibits invasion
Inomata, A., Murakoshi, F., Ishiwa, A., Takano, R., Takemae, H., Sugi, T., Recuenco, F. C., Horimoto, T., & Kato, K. (2015) · Scientific Reports · doi:10.1038/srep11599 · Cited by 19 · see citing works
Description of a Novel Adhesin ofMycobacterium aviumSubsp.paratuberculosis
Viale, M. N., Echeverría-Valencia, G., Romasanta, P. N., Mon, M. L., Fernández, M. M., Malchiodi, E. L., Romano, M. I., Gioffré, A., & Santangelo, M. D. L. P. (2014) · BioMed Research International · doi:10.1155/2014/729618 · Cited by 15 · see citing works
Churchward, C. P., Rosales, R. S., Gielbert, A., Domínguez, M., Nicholas, R. A. J., & Ayling, R. D. (2014) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12344 · Cited by 10 · see citing works
PhosSA: Fast and accurate phosphorylation site assignment algorithm for mass spectrometry data
Saeed, F., Pisitkun, T., Hoffert, J. D., Rashidian, S., Wang, G., Guček, M., & Knepper, M. A. (2013) · Proteome Science · doi:10.1186/1477-5956-11-s1-s14 · Cited by 10 · see citing works
Barel, M., & Charbit, A. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-1261-2_7 · Cited by 8 · see citing works
Boone, T. J., & Tyrrell, G. J. (2012) · Canadian Journal of Microbiology · doi:10.1139/w2012-015 · Cited by 8 · see citing works
Balbo, M., Barel, M., Lottin, S., Jean, D., & Frade, R. (2005) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2005.06.052 · Cited by 6 · see citing works
Flagged first, then by citations
Research works printed but not linked: 3
- [35]Viale MN Description of a novel adhesin of Mycobacterium avium subsp. paratuberculosis BioMed research international 2014 2014 729618 25136616 PMC4130151
- [85]Tacchi JL Post-translational processing targets functionally diverse proteins in Mycoplasma hyopneumoniae Open biology 2016 6 150210 10.1098/rsob.150210 26865024 PMC4772806 · DOI · Paper page
- [148]P, H. Diploma thesis, Technische Universität München, (2012).
Cited by
Sorted by citations
Nitrogen-fixing organelle in a marine alga
Coale, T. H., Loconte, V., Turk‐Kubo, K. A., Vanslembrouck, B., Mak, E. W. K., Cheung, S., Ekman, A. A., Chen, J.-H., Hagino, K., Takano, Y., et al. (2024) · Science · doi:10.1126/science.adk1075 · Cited by 221 · see citing works
The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis
Harvey, K. L., Jarocki, V. M., Charles, I. G., & Djordjevic, S. P. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.02351 · Cited by 216 · see citing works
Self-citationMycoplasma pneumoniae Infections: Pathogenesis and Vaccine Development
Jiang, Z., Li, S., Zhu, C., Zhou, R., & Leung, P. H. M. (2021) · Pathogens · doi:10.3390/pathogens10020119 · Cited by 184 · see citing works
Intracellular proteins moonlighting as bacterial adhesion factors
Jeffery, C. J. (2018) · AIMS Microbiology · doi:10.3934/microbiol.2018.2.362 · Cited by 94 · see citing works
Infection strategies of mycoplasmas: Unraveling the panoply of virulence factors
Yi-wen, C., Wu, Y., Qin, L., Cuiming, Z., & You, X. (2021) · Virulence · doi:10.1080/21505594.2021.1889813 · Cited by 84 · see citing works
Bacterial Excretion of Cytoplasmic Proteins (ECP): Occurrence, Mechanism, and Function
Ebner, P., & Götz, F. (2018) · Trends in Microbiology · doi:10.1016/j.tim.2018.10.006 · Cited by 79 · see citing works
Tartaglia, N. R., Breyne, K., Meyer, E., Cauty, C., Jardin, J., Chrétien, D., Dupont, A., Demeyere, K., Berkova, N., Azevedo, V., et al. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00277 · Cited by 83 · see citing works
Pathogenicity & virulence ofMycoplasma hyopneumoniae
Zimmer, F. M. A. L., Paes, J. A., Zaha, A., & Ferreira, H. B. (2020) · Virulence · doi:10.1080/21505594.2020.1842659 · Cited by 77 · see citing works
Hiltunen, A. K., Savijoki, K., Nyman, T. A., Miettinen, I., Ihalainen, P., Peltonen, J. P. K., & Fallarero, A. (2019) · Microorganisms · doi:10.3390/microorganisms7120584 · Cited by 72 · see citing works
A novel decoy strategy for polymyxin resistance in Acinetobacter baumannii
Park, J.-E., Kim, M.-S., Shin, B., Kang, M., Yang, J.-H., Lee, T. K., & Park, W. (2021) · eLife · doi:10.7554/elife.66988 · Cited by 68 · see citing works
Tartaglia, N. R., Nicolas, A., Rodovalho, V. D. R., da Luz, B. S. R., Briard‐Bion, V., Krupova, Z., Thierry, A., Coste, F., Burel, A., Martin, P., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-64952-y · Cited by 67 · see citing works
Mycoplasma hyopneumoniae resides intracellularly within porcine epithelial cells
Raymond, B. B. A., Turnbull, L., Jenkins, C., Madhkoor, R., Schleicher, I., Uphoff, C. C., Whitchurch, C. B., Rohde, M., & Djordjevic, S. P. (2018) · Scientific Reports · doi:10.1038/s41598-018-36054-3 · Cited by 57 · see citing works
Self-citationAntibiotic Resistance Diagnosis in ESKAPE Pathogens—A Review on Proteomic Perspective
Kalpana, S., Lin, W.-Y., Wang, Y.-C., Fu, Y., Lakshmi, A. M., & Wang, H. (2023) · Diagnostics · doi:10.3390/diagnostics13061014 · Cited by 58 · see citing works
Korshoj, L. E., & Kielian, T. (2024) · Nature Communications · doi:10.1038/s41467-024-54581-8 · Cited by 55 · see citing works
The Evolution, Ecology, and Mechanisms of Infection by Gram-Positive, Plant-Associated Bacteria
Thapa, S. P., Davis, E. W., Lyu, Q., Weisberg, A. J., Stevens, D. M., Clarke, C. R., Coaker, G., & Chang, J. H. (2019) · Annual Review of Phytopathology · doi:10.1146/annurev-phyto-082718-100124 · Cited by 48 · see citing works
Kesavan, D. K., Vasudevan, A., Wu, L., Chen, J., Su, Z., Wang, S., & Xu, H. (2020) · BMC Microbiology · doi:10.1186/s12866-020-1722-1 · Cited by 46 · see citing works
Dawood, A. S., Algharib, S. A., Zhao, G., Zhu, T., Qi, M., Delai, K., Hao, Z., Marawan, M. A., Shirani, I., & Guo, A. (2022) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.855731 · Cited by 48 · see citing works
Extracellular Actin Is a Receptor for Mycoplasma hyopneumoniae
Raymond, B. B. A., Madhkoor, R., Schleicher, I., Uphoff, C. C., Turnbull, L., Whitchurch, C. B., Rohde, M., Padula, M. P., & Djordjevic, S. P. (2018) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2018.00054 · Cited by 44 · see citing works
Self-citationMycoplasmas are no exception to extracellular vesicles release: Revisiting old concepts
Gaurivaud, P., Ganter, S., Villard, A., Manso-Silván, L., Chevret, D., Boulé, C., Monnet, V., & Tardy, F. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208160 · Cited by 42 · see citing works
Beware of Mycoplasma Anti-immunoglobulin Strategies
Arfi, Y., Lartigue, C., Sirand‐Pugnet, P., & Blanchard, A. (2021) · mBio · doi:10.1128/mbio.01974-21 · Cited by 41 · see citing works
Yu, Y., Liu, M., Hua, L., Qiu, M., Zhang, W., Wei, Y., Gan, Y., Feng, Z., Shao, G., & Xiong, Q. (2018) · Veterinary Research · doi:10.1186/s13567-018-0610-2 · Cited by 36 · see citing works
Widjaja, M., Berry, I. J., Jarocki, V. M., Padula, M. P., Dumke, R., & Djordjevic, S. P. (2020) · Scientific Reports · doi:10.1038/s41598-020-63136-y · Cited by 35 · see citing works
Self-citationNatural Aggregation of Lactobacillus: Mechanisms and Influencing Factors
Wang, S., Li, L., Yu, L., Tian, F., Zhao, J., Zhai, Q., & Chen, W. (2024) · Food Bioscience · doi:10.1016/j.fbio.2024.105007 · Cited by 34 · see citing works
Spatially Targeted Proteomics of the Host–Pathogen Interface during Staphylococcal Abscess Formation
Guiberson, E. R., Weiss, A., Ryan, D. J., Monteith, A. J., Sharman, K., Gutierrez, D. B., Perry, W., Caprioli, R. M., Skaar, E. P., & Spraggins, J. M. (2020) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.0c00647 · Cited by 32 · see citing works
Grimmer, J., & Dumke, R. (2018) · Microbiological Research · doi:10.1016/j.micres.2018.09.006 · Cited by 30 · see citing works
Self-citationIn-Depth Characterization of the Staphylococcus aureus Phosphoproteome Reveals New Targets of Stk1
Prust, N., van der Laarse, S. A. M., van den Toorn, H., van Sorge, N. M., & Lemeer, S. (2021) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra120.002232 · Cited by 28 · see citing works
Baig, M. A., Turner, M. S., Liu, S., Al‐Nabulsi, A. A., Shah, N. P., & Ayyash, M. M. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.731410 · Cited by 28 · see citing works
Liu, D., Yang, Z., Chen, Y., Zhuang, W., Niu, H., Wu, J., & Ying, H. (2018) · Biotechnology for Biofuels · doi:10.1186/s13068-018-1316-4 · Cited by 26 · see citing works
Persistence in Livestock Mycoplasmas—a Key Role in Infection and Pathogenesis
Hoelzle, K., Ade, J., & Hoelzle, L. E. (2020) · Current Clinical Microbiology Reports · doi:10.1007/s40588-020-00149-1 · Cited by 27 · see citing works
Toward the Complete Functional Characterization of a Minimal Bacterial Proteome
Bianchi, D. M., Pelletier, J. F., Hutchison, C. A., Glass, J. I., & Luthey-Schulten, Z. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04188 · Cited by 22 · see citing works
Verdugo-Fuentes, A. A., Gastélum, G., Rocha, J., & de la Torre, M. M. (2020) · Journal of Bacteriology · doi:10.1128/jb.00721-19 · Cited by 25 · see citing works
Paes, J. A., Machado, L. D. P. N., Leal, F. M. D. A., Moraes, S. N., Moura, H., Barr, J. R., & Ferreira, H. B. (2018) · Virulence · doi:10.1080/21505594.2018.1499379 · Cited by 25 · see citing works
Torres, A. N., Chamorro-Veloso, N., Costa, P. S., Cádiz, L., Canto, F. D., Venegas, S., Nitsche, M. L., Coloma-Rivero, R. F., Montero, D. A., & Vidal, R. M. (2020) · Microorganisms · doi:10.3390/microorganisms8081184 · Cited by 21 · see citing works
Wang, J., Li, S., Chen, J., Gan, L., Wang, J., Xiong, Q., Feng, Z., Li, Q., Deng, Z., Yuan, X., et al. (2023) · Microbiology Spectrum · doi:10.1128/spectrum.00218-23 · Cited by 21 · see citing works
Thofte, O., Su, Y.-C., Brant, M., Littorin, N., Duell, B. L., Alvarado, V., Jalalvand, F., & Riesbeck, K. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02910 · Cited by 21 · see citing works
Arming the troops: Post-translational modification of extracellular bacterial proteins
Forrest, S., & Welch, M. (2020) · Science Progress · doi:10.1177/0036850420964317 · Cited by 19 · see citing works
Briggs, R. E., Billing, S. R., Boatwright, W. D., Chriswell, B. O., Casas, E., Dassanayake, R. P., Palmer, M. V., Register, K. B., & Tatum, F. M. (2021) · Microbial Pathogenesis · doi:10.1016/j.micpath.2021.105159 · Cited by 19 · see citing works
Moonlighting proteins: beacon of hope in era of drug resistance in bacteria
Yadav, P., Singh, R., Sur, S., Bansal, S., Chaudhry, U., & Tandon, V. (2022) · Critical Reviews in Microbiology · doi:10.1080/1040841x.2022.2036695 · Cited by 18 · see citing works
Nicholson, P., Furrer, J., Hässig, M., Strauss, C., Heller, M., Braga-Lagache, S., & Frey, J. (2019) · Anaerobe · doi:10.1016/j.anaerobe.2019.02.011 · Cited by 18 · see citing works
The Mycoplasma spp. ‘Releasome’: A New Concept for a Long-Known Phenomenon
Gaurivaud, P., & Tardy, F. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.853440 · Cited by 17 · see citing works
Epitope Mapping of Streptococcus agalactiae Elongation Factor Tu Protein Recognized by Human Sera
Pyclik, M. J., Górska, S., Brzozowska, E., Dobrut, A., Ciekot, J., Gamian, A., & Brzychczy‐Włoch, M. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.00125 · Cited by 17 · see citing works
Liu, D., & Bhunia, A. K. (2024) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.4c00323 · Cited by 16 · see citing works
Bacterial bug-out bags: outer membrane vesicles and their proteins and functions
Kesavan, D. K., Aparna, V. S., Wu, L., Wan, J., Abdelaziz, M. H., Su, Z., Wang, S., & Xu, H. (2020) · The Journal of Microbiology · doi:10.1007/s12275-020-0026-3 · Cited by 16 · see citing works
Dobrut, A., & Brzychczy‐Włoch, M. (2021) · Pathogens · doi:10.3390/pathogens11010043 · Cited by 16 · see citing works
Su, Y., Mattsson, E., Singh, B., Jalalvand, F., Murphy, T. F., & Riesbeck, K. (2019) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiz217 · Cited by 15 · see citing works
Huang, Y., Zhu, F., Koh, J., Stanton, D., Chen, S., & Wang, N. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.977710 · Cited by 14 · see citing works
Wagner, T. M., Torres-Puig, S., Yimthin, T., Irobalieva, R. N., Heller, M., Kaessmeyer, S., Démoulins, T., & Jores, J. (2025) · Communications Biology · doi:10.1038/s42003-025-08099-4 · Cited by 14 · see citing works
Protein cleavage influences surface protein presentation in Mycoplasma pneumoniae
Berry, I. J., Widjaja, M., Jarocki, V. M., Steele, J. R., Padula, M. P., & Djordjevic, S. P. (2021) · Scientific Reports · doi:10.1038/s41598-021-86217-y · Cited by 13 · see citing works
Self-citationIncomplete autophagy promotes the replication of Mycoplasma hyopneumoniae
Wang, Z., Wen, Y., Zhou, B., Tian, Y., Ning, Y., & Ding, H. (2021) · The Journal of Microbiology · doi:10.1007/s12275-021-1232-3 · Cited by 13 · see citing works
Machado, L. D. P. N., Paes, J. A., dos Santos, P. S., & Ferreira, H. B. (2019) · Microbial Pathogenesis · doi:10.1016/j.micpath.2019.103958 · Cited by 12 · see citing works
Zhao, F., Liu, J., Xiao, D., Liu, L., Gong, J., Xu, J., Li, H., Zhao, S., & Zhang, J. (2020) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.553739 · Cited by 12 · see citing works
da Silva, W. M., Seyffert, N., Silva, A., & Azevedo, V. (2021) · PeerJ · doi:10.7717/peerj.12456 · Cited by 11 · see citing works
Villa, F., Secundo, F., Forlani, F., Cattò, C., & Cappitelli, F. (2021) · Annals of Microbiology · doi:10.1186/s13213-020-01617-1 · Cited by 11 · see citing works
Yu, S. Y., Wang, X., Li, J., Xue, F., Tang, F., & Dai, J. (2022) · Virulence · doi:10.1080/21505594.2022.2066274 · Cited by 10 · see citing works
Molecular Detection of Hemoplasma in animals in Tamil Nadu, India and Hemoplasma genome analysis
Chitra, M. A., Kumaragurubaran, K., Gunasekaran, K., Murugasamy, S. A., Arunachalam, S., Annamalai, R., Venkataramanan, R., & Ramaswamy, S. (2023) · Veterinary Research Communications · doi:10.1007/s11259-023-10263-2 · Cited by 10 · see citing works
Mucin adsorbed by E. coli can affect neutrophil activation in vitro
Mikhalchik, E. V., Георгиевна, Б. Н., Vakhrusheva, T. V., Av, S., Baykova, J., Rakitina, D. V., Scherbakov, P., Гусев, С. А., Gusev, A., Хараева, З. Ф., et al. (2019) · FEBS Open Bio · doi:10.1002/2211-5463.12770 · Cited by 10 · see citing works
Tavares, B. A. D. R., Paes, J. A., Zaha, A., & Ferreira, H. B. (2021) · Microbial Pathogenesis · doi:10.1016/j.micpath.2021.105344 · Cited by 9 · see citing works
Vidlund, J., Gelalcha, B. D., Gillespie, B. E., Agga, G. E., Schneider, L. G., Swanson, S. M., Frady, K. D., & Dego, O. K. (2024) · Vaccine · doi:10.1016/j.vaccine.2024.01.067 · Cited by 9 · see citing works
Comparison of Staphylococcus aureus surface protein extraction methods and immunogenicity
Abdi, R. D., Dunlap, J. R., Gillespie, B. E., Ensermu, D. B., Almeida, R. A., & Dego, O. K. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e02528 · Cited by 9 · see citing works
Li, G., Obeng, E., Shu, J., Shu, J., Chen, J., Wu, Y., & He, Y. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.510943 · Cited by 9 · see citing works
Stancheva, S. G., Frömbling, J., Sassu, E. L., Hennig‐Pauka, I., Ladinig, A., Gerner, W., Grunert, T., & Ehling‐Schulz, M. (2022) · Microbial Pathogenesis · doi:10.1016/j.micpath.2022.105759 · Cited by 8 · see citing works
Liu, P., Long, H., He, S., Cheng, H., Li, E., Cheng, S., Liang, M., Liu, Z., Guo, Z., & Shi, H. S. (2024) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2300738 · Cited by 7 · see citing works
Pseudomonas aeruginosa elongation factor-Tu (EF-Tu) is an immunogenic protective protein antigen
Moustafa, D. A., Lou, E., Schafer-Kestenman, M. E., Mateu-Borrás, M., Doménech‐Sánchez, A., Albertí, S., & Goldberg, J. B. (2024) · Vaccine · doi:10.1016/j.vaccine.2024.126476 · Cited by 7 · see citing works
Xu, B., Sun, Y. H., Wang, S., Yao, W., Wang, Q., Yuan, T., Ma, S., Wang, X., Lyu, L., Yu, Y., et al. (2024) · Veterinary Microbiology · doi:10.1016/j.vetmic.2024.110275 · Cited by 6 · see citing works
Sokolova, D., Smolarska, A., Bartnik, P., Rąbalski, Ł., Kosiński, M., Narajczyk, M., Krzyżanowska, D. M., Rajewska, M., Mruk, I., Czaplewska, P., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-34803-7 · Cited by 6 · see citing works
Elongation factor Tu promotes the onset of periodontitis through mediating bacteria adhesion
Xiao, L., Pu, Y., Cui, Y., Chen, C., Xiao, Q., Wang, Y., Wei, Y., Feng, M., Zhang, T., Yang, S., et al. (2025) · npj Biofilms and Microbiomes · doi:10.1038/s41522-025-00680-3 · Cited by 6 · see citing works
Searching for Biological Function of the Mysterious PA2504 Protein from Pseudomonas aeruginosa
Drabinska, J., Steczkiewicz, K., Kujawa, M., & Kraszewska, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22189833 · Cited by 6 · see citing works
Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae
Barbosa, M. S., Marques, L. M., Timenetsky, J., Rosengarten, R., Spergser, J., & Chopra‐Dewasthaly, R. (2022) · BMC Microbiology · doi:10.1186/s12866-022-02512-2 · Cited by 6 · see citing works
Impact of c-di-GMP on the Extracellular Proteome of Rhizobium etli
Lorite, M. J., Casas-Román, A., Girard, L., Encarnación‐Guevara, S., Díaz‐Garrido, N., Badı́a, J., Baldomà, L., Pérez‐Mendoza, D., & Sanjuán, J. (2022) · Biology · doi:10.3390/biology12010044 · Cited by 6 · see citing works
Prezioso, S. M., Duong, D. M., Kuiper, E. G., Deng, Q., Albertí, S., Conn, G. L., & Goldberg, J. B. (2019) · Scientific Reports · doi:10.1038/s41598-019-39331-x · Cited by 6 · see citing works
Pinto, L., Torres, C., Gil, C., Santos, H. M., Capelo, J. L., Borges, V., Gomes, J. P., Silva, C., Vieira, L., Poeta, P. A. C. Q. D., et al. (2020) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2019.0164 · Cited by 5 · see citing works
Sami, A. J., Bilal, S., Ahsan, N.-U.-A., Hameed, N., & Saleem, S. (2023) · Environmental Monitoring and Assessment · doi:10.1007/s10661-023-12077-w · Cited by 5 · see citing works
Guan, X., Bu, F., Fu, Y., Zhang, H., Xiang, H., Chen, X., Chen, T., Wu, X.-J., Wu, K., Liu, L., et al. (2024) · iScience · doi:10.1016/j.isci.2024.111338 · Cited by 5 · see citing works
Thofte, O., Kaur, R., Su, Y., Brant, M., Rudin, A., Hood, D. W., & Riesbeck, K. (2018) · European Journal of Immunology · doi:10.1002/eji.201847871 · Cited by 5 · see citing works
Sun, Y., Xu, B., Zhuge, X., Tang, F., Wang, X., Gong, Q., Chen, R., Xue, F., & Dai, J. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2020.592906 · Cited by 5 · see citing works
Substrate recognition by the Pseudomonas aeruginosa EF-Tu–modifying methyltransferase EftM
Kuiper, E. G., Dey, D., LaMore, P. A., Owings, J. P., Prezioso, S. M., Goldberg, J. B., & Conn, G. L. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011213 · Cited by 5 · see citing works
Baillo, A. A., Albarracín, L., Ojeda, E. E. H., Elean, M., Gong, W., Kitazawa, H., Villena, J., & Fadda, S. (2026) · Antibiotics · doi:10.3390/antibiotics15010096 · Cited by 4 · see citing works
Jarocki, V. M., Steele, J. R., Widjaja, M., Tacchi, J. L., Padula, M. P., & Djordjevic, S. P. (2019) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2019.03.005 · Cited by 4 · see citing works
Self-citationSvetličić, E., Alarcón, L. A., Karlsson, R., Jers, C., & Mijakovic̀, I. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c00321 · Cited by 3 · see citing works
Metaviromic and metagenomic study of the pathogens in unexplained pneumonia cases in goats
Xia, Z., Luo, G., Gou, L.-Y., Zhang, W., Ji, E.-G., Li, S., Gao, T., Abi, K.-M., & Yang, F. (2025) · Veterinary Microbiology · doi:10.1016/j.vetmic.2025.110469 · Cited by 3 · see citing works
Brokaw, A. M., Wallen, G., Orvis, A., Kwon, H. J., Seepersaud, R., Nguyen, S., Sharma, K., Coleman, M., Quach, P., Twentyman, J., et al. (2025) · PLoS Pathogens · doi:10.1371/journal.ppat.1013562 · Cited by 3 · see citing works
Lin, Y., He, J., Zhang, Q., Li, Y., Ke, J., Lin, C., Yao, B., Zhang, C., & Tan, N. (2025) · Functional & Integrative Genomics · doi:10.1007/s10142-025-01730-x · Cited by 3 · see citing works
Pagurayan, A. G. B., Fabia, J. Z. P., Agcaoili, M. J. T., Acang, J. P. A., Peralta, J. P. K., Domingo, A., & Gann, P. J. I. (2026) · The Open Microbiology Journal · doi:10.2174/0118742858448770260210051054 · Cited by 3 · see citing works
Si, D., Sun, J., Guo, L., Yang, F., Li, J., & He, S. (2023) · Frontiers in Veterinary Science · doi:10.3389/fvets.2023.1249499 · Cited by 3 · see citing works
Host-endosymbiont co-evolution shaped chloroplast translational regulation
Marchis, F. D., Pompa, A., Ballottari, M., & Bellucci, M. (2019) · Botany Letters · doi:10.1080/23818107.2019.1623716 · Cited by 3 · see citing works
Lactobacillus spp. belonging to the Casei group display a variety of adhesins
Konieczna, C., Olejnik‐Schmidt, A., & SCHMIDT, M. T. (2018) · Acta Scientiarum Polonorum Technologia Alimentaria · doi:10.17306/j.afs.0538 · Cited by 3 · see citing works
Lactobacillus spp. belonging to the Casei group display a variety of adhesins [pdf]
Konieczna, C., Olejnik‐Schmidt, A., & SCHMIDT, M. T. (2018) · Acta Scientiarum Polonorum Technologia Alimentaria · doi:10.17306/j.afs.2018.0538 · Cited by 2 · see citing works
Dobrut, A., Skibiński, J., Bekier, A., Drożdż, K., Rudnicka, K., Płociński, P., Siemińska, I., & Brzychczy‐Włoch, M. (2024) · BMC Veterinary Research · doi:10.1186/s12917-024-04028-5 · Cited by 2 · see citing works
Sanford, J. W., Mobley, J. A., Dybvig, K. F., Atkinson, T. P., & Daubenspeck, J. M. (2025) · PLoS ONE · doi:10.1371/journal.pone.0329506 · Cited by 2 · see citing works
Sami, A. J., Bilal, S., Alam, S., Khalid, M., & Mangat, H. A. (2024) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-024-04892-9 · Cited by 2 · see citing works
Brahma, U., Suresh, A., Kamila, A., Usha, S., Kumar, S. V. A., Baddi, H., Singothu, S., Sharma, P., Bandaru, R. K., Suravaram, S., et al. (2026) · Microbiology Spectrum · doi:10.1101/2025.10.02.680171 · Cited by 2 · see citing works
Zhang, S., Zhang, Y., Luo, Y., Zhang, S., Song, Y., Li, B., Zheng, F., Gao, P., Xu, J., & Chu, Y. (2025) · Microbial Pathogenesis · doi:10.1016/j.micpath.2025.108127 · Cited by 1 · see citing works
Mycoplasma genitaliumlipoproteins inhibit tumour necrosis factor α-induced apoptosis in HeLa cells
Zuo, L., Sun, H., Yu, M., You, X., Zeng, Y., & Wu, Y. (2018) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2018.1523688 · Cited by 1 · see citing works
Adewara, O. A., Ogunbanwo, S. T., & Adegoke, C. O. (2024) · Journal of Advances in Microbiology · doi:10.9734/jamb/2024/v24i2798 · Cited by 1 · see citing works
Sabat, A. J., Durfee, T., Baldwin, S., Akkerboom, V., Voß, A., Friedrich, A. W., & Bathoorn, E. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1368923 · Cited by 1 · see citing works
Quiroz-Castañeda, R. E., Aguilar-Díaz, H., Coronado-Villanueva, E., Catalán-Ochoa, D. I., & Amaro-Estrada, I. (2024) · Pathogens · doi:10.3390/pathogens13100845 · Cited by 1 · see citing works
Mendez-Romero, J. I., Beltrán‐Barrientos, L. M., Heredia-Castro, P. Y., Reyes‐Díaz, R., Hernández‐Mendoza, A., González-Córdova, A. F., & Vallejo‐Córdoba, B. (2024) · Food Biotechnology · doi:10.1080/08905436.2024.2423049 · Cited by 1 · see citing works
The immune responses elicited by six recombinant antigens of Mycoplasma hyopneumoniae in mice
Li, S., Yin, R., Xiong, Q., Liu, M., Wang, J., Zhang, Z., Shao, G., Deng, Z., ZhiXin, F., & Yu, Y. (2024) · Veterinary Microbiology · doi:10.1016/j.vetmic.2024.110295 · Cited by 1 · see citing works
Zarzecka, U., Repetto, O., Ambroziak, P., Bielecka, M., Czaplewska, P., Mruk, I., Musiał, N., Figaj, D., Roncarati, D., Diechler, S., et al. (2025) · Microbial Pathogenesis · doi:10.1016/j.micpath.2025.107979 · Cited by 1 · see citing works
Paul, A. G., Wellslager, B., Williamson, M., & Yilmaz, Ö. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.11.602567 · Cited by 1 · see citing works
- Authors
- Widjaja, M., Harvey, K. L., Hagemann, L., Berry, I. J., Jarocki, V. M., Raymond, B. B. A., Tacchi, J. L., Gründel, A., Steele, J. R., Padula, M. P., Charles, I. G., Dumke, R., & Djordjevic, S. P.
- Affiliations
- University of Technology Sydney (AU)
- Technische Universität Dresden (DE)
- Norwich Research Park (GB)
- Corresponding author
- Djordjevic, Steven Philip
- ORCID
- Venue
- Scientific Reports
- Published
- 2017-09-11
- Volume
- 7
- Issue
- 1
- Pages
- 11227-11227
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC5593925
- OpenAlex
- W2750987002
- Cited by
- 131
- References
- 154
- Citations by year
- 2026: 7 · 2025: 17 · 2024: 20 · 2023: 7 · 2022: 16 · 2021: 20 · 2020: 14 · 2019: 13 · 2018: 17
- FWCI
- 4.92
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UEA Digital Repository (University of East Anglia) (acceptedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- UTS ePRESS (University of Technology Sydney) (submittedVersion)
- Funders
- Bristol-Myers Squibb Foundation
- Deutsche Forschungsgemeinschaft (1280/1-1, DU 1280/1-1)
- University of Technology Sydney
- NSW Department of Primary Industries
- Australian Research Council (LE130100096)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Immunology and Microbiology › Microbiology › Microbial infections and disease research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- elongation factor Tu, moonlighting proteins, protein processing, Staphylococcus aureus, Mycoplasma pneumoniae, Mycoplasma hyopneumoniae, plasmin, short linear motifs, positively charged amino acids, codon usage bias, AT-rich genome, host-pathogen interaction, bacterial cell surface, N-terminomics
- MeSH terms
- Fibrinolysin, Membrane Proteins, Models, Molecular, Mycoplasma pneumoniae, Peptide Elongation Factor Tu, Plasminogen, Protein Binding, Staphylococcus aureus, Computational Biology, Virulence Factors, Mycoplasma hyopneumoniae, Host-Pathogen Interactions
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