The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Structure of Internalin, a Major Invasion Protein of Listeria monocytogenes, in Complex with Its Human Receptor E-Cadherin
Open accessAbstract
Listeria monocytogenes, a food-borne bacterial pathogen, enters mammalian cells by inducing its own phagocytosis. The listerial protein internalin (InlA) mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. We present the crystal structures of the functional domain of InlA alone and in a complex with the extracellular, N-terminal domain of human E-cadherin (hEC1). The leucine rich repeat (LRR) domain of InlA surrounds and specifically recognizes hEC1. Individual interactions were probed by mutagenesis and analytical ultracentrifugation. These include Pro16 of hEC1, a major determinant for human susceptibility to L. monocytogenes infection that is essential for intermolecular recognition. Our studies reveal the structural basis for host tro-pism of this bacterium and the molecular deception L. monocytogenes employs to exploit the E-cadherin system.
Overview
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
Verification
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?
The cited source says what the claim attributes to it.
In the citing paper
“Interestingly, this family of proteins includes internalin A of L. monocytogenes, which mediates epithelial cell invasion by binding to E-cadherin [41,44].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [44]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
Refinement of Macromolecular Structures by the Maximum-Likelihood Method
Murshudov, G. N., Vagin, A. A., & Dodson, E. J. (1997) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444996012255 · Cited by 14,796
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
AMoRe: an automated package for molecular replacement
Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877
The atomic structure of protein-protein recognition sites 1 1Edited by A. R. Fersht
Conte, L. L., Chothia, C., & Janin, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2439 · Cited by 1,967
The leucine-rich repeat as a protein recognition motif
Kobe, B. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(01)00266-4 · Cited by 1,720
Research works printed but not linked: 3
- Brünger, 1998, Crystallography & NMR system, Acta Crystallogr., D54, 905
- CCP4, 1994, The CCP4 (Collaborative Computational Project 4) suite, Acta Crystallogr. D, 50, 760
- Nicholls, 1993, Grasp, Biophys. J., 64, A166
Cited by
Sorted by citations
Items 101–200 of 303
On the usefulness of ion-mobility mass spectrometry and SAXS data in scoring docking decoys
Karaca, E., & Bonvin, A. M. J. J. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913007063 · Cited by 58
Bosse, T., Ehinger, J., Czuchra, A., Benesch, S., Steffen, A., Wu, X., Schloen, K., Niemann, H. H., Scita, G., Stradal, T. E. B., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00367-07 · Cited by 60
A Toll‐like receptor in horseshoe crabs
Inamori, K., Ariki, S., & Kawabata, S. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.0131.x · Cited by 59
Kovačević, J. J., Mesak, L. R., & Allen, K. J. (2012) · Food Microbiology · doi:10.1016/j.fm.2011.12.015 · Cited by 57
Rapid automated superposition of shapes and macromolecular models using spherical harmonics
Konarev, P. V., Petoukhov, M. V., & Svergun, D. I. (2016) · Journal of Applied Crystallography · doi:10.1107/s1600576716005793 · Cited by 57
Reid, S. D., Montgomery, A. G., Voyich, J. M., DeLeo, F. R., Lei, B., Ireland, R. M., Green, N. M., Liu, M., Lukomski, S., & Musser, J. M. (2003) · Infection and Immunity · doi:10.1128/iai.71.12.7043-7052.2003 · Cited by 54
Listeria monocytogenes InlP interacts with afadin and facilitates basement membrane crossing
Faralla, C., Bastounis, E. E., Ortega, F. E., Light, S. H., Rizzuto, G. A., Gao, L., Marciano, D. K., Nocadello, S., Anderson, W. F., Robbins, J. R., et al. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007094 · Cited by 53
Listeria monocytogenes and the Genus Listeria
Khelef, N., Lecuit, M., Buchrieser, C., Cabanes, D., Dussurget, O., & Cossart, P. (2006) · Springer eBooks · doi:10.1007/0-387-30744-3_11 · Cited by 52
Innate Immune Recognition and Inflammasome Activation in Listeria Monocytogenes Infection
Eitel, J., Suttorp, N., & Opitz, B. (2011) · Frontiers in Microbiology · doi:10.3389/fmicb.2010.00149 · Cited by 51
Postinfection Irritable Bowel Syndrome
Downs, I. A., Aroniadis, O. C., Kelly, L., & Brandt, L. J. (2017) · Journal of Clinical Gastroenterology · doi:10.1097/mcg.0000000000000924 · Cited by 56
Zilelidou, E. A., & Skandamis, P. N. (2018) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2018.04.011 · Cited by 52
Koch, A., Farooq, A., Shan, W., Zeng, L., Colman, D., & Zhou, M. (2004) · Structure · doi:10.1016/j.str.2004.02.034 · Cited by 53
Zhu, J., Brownlie, R. M., Liu, Q., Babiuk, L. A., Potter, A. A., & Mutwiri, G. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.09.024 · Cited by 53
Zheng, Q., Lu, J., Wang, Y., & Jiao, N. (2019) · FEMS Microbiology Ecology · doi:10.1093/femsec/fiz017 · Cited by 51
Huyton, T., & Wolberger, C. (2007) · Protein Science · doi:10.1110/ps.072803507 · Cited by 50
The mechanism of cell adhesion by classical cadherins: the role of domain 1
Harrison, O. J., Corps, E. M., Berge, T., & Kilshaw, P. J. (2005) · Journal of Cell Science · doi:10.1242/jcs.01665 · Cited by 50
Pathogen‐induced actin filament rearrangement in infectious diseases
Rottner, K., Lommel, S., Wehland, J., & Stradal, T. E. B. (2004) · The Journal of Pathology · doi:10.1002/path.1638 · Cited by 47
Self-citationMachner, M. P., Frese, S., Schubert, W., Orian‐Rousseau, V., Gherardi, E., Wehland, J., Niemann, H. H., & Heinz, D. W. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03532.x · Cited by 46
Self-citationMonk, I. R., Casey, P. G., Hill, C., & Gahan, C. G. M. (2010) · BMC Microbiology · doi:10.1186/1471-2180-10-318 · Cited by 45
Cadherin adhesion depends on a salt bridge at the N-terminus
Harrison, O. J., Corps, E. M., & Kilshaw, P. J. (2005) · Journal of Cell Science · doi:10.1242/jcs.02539 · Cited by 44
Su, X., Cao, G., Zhang, J., Pan, H., Zhang, D., Kuang, D., Yang, X., Xu, X., Shi, X., & Meng, J. (2019) · Gut Pathogens · doi:10.1186/s13099-019-0307-8 · Cited by 43
Fan, Q., & Hendrickson, W. A. (2006) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2005.12.055 · Cited by 43
Pathogenesis of listeriosis during pregnancy
Poulsen, K. P., & Czuprynski, C. J. (2013) · Animal Health Research Reviews · doi:10.1017/s1466252312000242 · Cited by 45
A Minireview of the Methods for Listeria monocytogenes Detection
Liu, A., Shen, L., Zeng, Z., Sun, M., Liu, Y., Liu, S., Cheng, L., & Wang, X. (2017) · Food Analytical Methods · doi:10.1007/s12161-017-0991-2 · Cited by 42
Ortega, F. E., Rengarajan, M., Chavez, N., Radhakrishnan, P., Gloerich, M., Bianchini, J. M., Siemers, K. A., Luckett, W. S., Lauer, P., Nelson, W. J., et al. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-12-0851 · Cited by 45
Velge, P., & Roche, S. M. (2010) · Future Microbiology · doi:10.2217/fmb.10.134 · Cited by 41
Mostowy, S., & Cossart, P. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20353 · Cited by 42
The VIT® technology for rapid detection of Listeria monocytogenes and other Listeria spp.
Stephan, R., Schumacher, S., & Zychowska, M. A. (2003) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(03)00307-6 · Cited by 40
Polle, L., Rigano, L. A., Julian, R., Ireton, K., & Schubert, W. (2013) · Structure · doi:10.1016/j.str.2013.10.017 · Cited by 39
Self-citationMcGann, P., Raengpradub, S., Ivanek, R., Wiedmann, M., & Boor, K. J. (2008) · Foodborne Pathogens and Disease · doi:10.1089/fpd.2008.0085 · Cited by 38
N-Terminal Gly224–Gly411 Domain in Listeria Adhesion Protein Interacts with Host Receptor Hsp60
Jagadeesan, B., Littlejohn, A. E. F., Amalaradjou, M. A. R., Singh, A. K., Mishra, K. K., La, D., Kihara, D., & Bhunia, A. K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020694 · Cited by 37
Bober, M., Mörgelin, M., Olin, A. I., von Pawel‐Rammingen, U., & Collin, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020345 · Cited by 37
Chatterjee, S., Basak, A. J., Nair, A. V., Duraivelan, K., & Samanta, D. (2020) · FEMS Microbiology Letters · doi:10.1093/femsle/fnaa220 · Cited by 33
Schimmele, B., & Plückthun, A. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.06.073 · Cited by 37
Waldemarsson, J., Areschoug, T., Lindahl, G., & Johnsson, E. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.2.378-388.2006 · Cited by 36
Structural insights into Met receptor activation
Niemann, H. H. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.11.014 · Cited by 36
Structural Insights into the Evolution of the Adaptive Immune System
Deng, L., Luo, M., Velikovsky, A., & Mariuzza, R. A. (2013) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-083012-130422 · Cited by 37
Hao, G., Boyle, M., Zhou, L., & Duan, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0068921 · Cited by 36
Architecturally complex O -glycopeptidases are customized for mucin recognition and hydrolysis
Pluvinage, B., Ficko‐Blean, E., Noach, I., Stuart, C. P., Thompson, N. K., McClure, H., Buenbrazo, N., Wakarchuk, W. W., & Boraston, A. B. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2019220118 · Cited by 37
Bublitz, M., Holland, C., Sabet, C., Reichelt, J., Cossart, P., Heinz, D. W., Bierne, H., & Schubert, W. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.100 · Cited by 35
Self-citationA common clathrin-mediated machinery coordinates cell-cell adhesion and bacterial internalization
Bonazzi, M., Kühbacher, A., Toledo-Arana, A., Mallet, A., Vasudevan, L., Pizarro-Cerdá, J., Brodsky, F. M., & Cossart, P. (2012) · Traffic : the International Journal of Intracellular Transport · doi:10.1111/tra.12009 · Cited by 40
Lowe, D. E., Robbins, J. R., & Bakardjiev, A. I. (2018) · Infection and Immunity · doi:10.1128/iai.00801-17 · Cited by 33
Péter, B., Farkas, E., Kurunczi, S., Szittner, Z., Bősze, S. E., Ramsden, J. J., Székács, I., & Horváth, R. (2022) · Biosensors · doi:10.3390/bios12040188 · Cited by 33
Dames, S. A., Bang, E., Häußinger, D., Ahrens, T., Engel, J., & Grzesiek, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708335200 · Cited by 33
Thermodynamically reengineering the listerial invasion complex InlA/E-cadherin
Wollert, T., Heinz, D. W., & Schubert, W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702199104 · Cited by 32
Self-citationWieczorek, K., Bomba, A., & Osek, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249419 · Cited by 31
Pizarro‐Cerdá, J., Sousa, S., & Cossart, P. (2004) · Comptes Rendus Biologies · doi:10.1016/j.crvi.2003.11.007 · Cited by 31
Moal, V. L.-L., Servin, A. L., & Coconnier, M. H. (2005) · Cellular Microbiology · doi:10.1111/j.1462-5822.2005.00532.x · Cited by 30
Williams, D. J., Castleman, J. D., Lee, C., Mote, B. L., & Smith, M. A. (2009) · Risk Analysis · doi:10.1111/j.1539-6924.2009.01308.x · Cited by 30
Cadherin‐mediated host–pathogen interactions
Dash, S., Duraivelan, K., & Samanta, D. (2021) · Cellular Microbiology · doi:10.1111/cmi.13316 · Cited by 28
Hsu, S., & Yang, C. (2022) · Membranes · doi:10.3390/membranes12030300 · Cited by 34
Miras, I., Saul, F. A., Nowakowski, M., Weber, P., Haouz, A., Shepard, W., & Picardeau, M. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s139900471500704x · Cited by 29
Folding and Stability of the Leucine-rich Repeat Domain of Internalin B from Listeria monocytogenes
Freiberg, A. N., Machner, M. P., Pfeil, W., Schubert, W., Heinz, D. W., & Seckler, R. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.01.044 · Cited by 29
Self-citationCurtiss, R. (2005) · Elsevier eBooks · doi:10.1016/b978-012491543-5/50060-7 · Cited by 29
Disarm The Bacteria: What Temperate Phages Can Do
Zhou, S., Liu, Z., Song, J., & Chen, Y. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45020076 · Cited by 29
Characterization of Listeria monocytogenes protein Lmo0327 with murein hydrolase activity
Popowska, M., & Markiewicz, Z. (2006) · Archives of Microbiology · doi:10.1007/s00203-006-0122-8 · Cited by 28
Xia, D., Tao, J., He, Y., Zhu, Q., Chen, D., Yu, M., Cui, F., & Gan, Y. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.10.038 · Cited by 27
Crystal Structure of the Ligand Binding Domain of Netrin G2
Brasch, J., Harrison, O. J., Ahlsén, G., Liu, Q., & Shapiro, L. S. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.10.030 · Cited by 26
Structure of Internalin InlK from the Human Pathogen Listeria monocytogenes
Neves, D., Job, V., Dortet, L., Cossart, P., & Dessen, A. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.08.010 · Cited by 26
Kuespert, K., Weibel, S., & Hauck, C. R. (2006) · Journal of Microbiological Methods · doi:10.1016/j.mimet.2006.10.003 · Cited by 25
Han, J., Kim, H. J., Lee, S., Hong, S. P., Park, K., Jeon, Y. H., Kim, D., Cheong, H., & Kim, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030929 · Cited by 25
Mariya, T., Huppertz, T., Beerthuyzen, M. M., van Schalkwijk, S., Janssen, P. W. M., Wels, M., Kok, J., & Bachmann, H. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01691 · Cited by 25
Structure of Toll-Like Receptors
Gay, N. J., & Gangloff, M. (2007) · Handbook of experimental pharmacology · doi:10.1007/978-3-540-72167-3_9 · Cited by 25
Kyoui, D., Takahashi, H., Miya, S., Kuda, T., & Kimura, B. (2014) · BMC Microbiology · doi:10.1186/1471-2180-14-15 · Cited by 24
Neurexins, Neuroligins and LRRTMs: synaptic adhesion getting fishy
Wright, G. J., & Washbourne, P. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07141.x · Cited by 26
Hierarchical Regulation of Wound Healing by NOD-Like Receptors in Cardiovascular Disease
Bracey, N. A., Duff, H. J., & Muruve, D. A. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6125 · Cited by 24
Mariuzza, R. A., Velikovsky, C. A., Deng, L., Xu, G., & Pancer, Z. (2010) · Biological Chemistry · doi:10.1515/bc.2010.091 · Cited by 25
Mathipa-Mdakane, M. G., Thantsha, M. S., & Bhunia, A. K. (2019) · Microbial Biotechnology · doi:10.1111/1751-7915.13407 · Cited by 24
AdpC Is aPrevotella intermedia17 Leucine-Rich Repeat Internalin-Like Protein
Iyer, D., Anaya-Bergman, C., Jones, K., Yanamandra, S., Sengupta, D., Miyazaki, H., & Lewis, J. P. (2010) · Infection and Immunity · doi:10.1128/iai.00510-09 · Cited by 24
Structural microbiology at the pathogen-host interface
Stebbins, C. E. (2005) · Cellular Microbiology · doi:10.1111/j.1462-5822.2005.00564.x · Cited by 24
Genetic Diversity and Relationships of Listeria monocytogenes Serogroup IIa Isolated in Poland
Lachtara, B., Wieczorek, K., & Osek, J. (2022) · Microorganisms · doi:10.3390/microorganisms10030532 · Cited by 23
Khan, F., Jeong, G., Javaid, A., Pham, D. T. N., Tabassum, N., & Kim, Y. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.12.013 · Cited by 23
Application of hybrid LRR technique to protein crystallization
Jin, M.-S., & Lee, J. (2008) · BMB Reports · doi:10.5483/bmbrep.2008.41.5.353 · Cited by 22
Structure of internalin C fromListeria monocytogenes
Ooi, A., Hussain, S., Seyedarabi, A., & Pickersgill, R. W. (2006) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444906026746 · Cited by 23
Shirai, R., 力哉, R. G. 後., 文康, 平., 潔, K. I. 池., & Inoue, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.122788 · Cited by 23
On the relationship between the protein structure and protein dynamics
Lu, C., Huang, S., Lai, Y., Lin, C., Shih, C., Huang, C., Hsu, W.-L., & Hwang, J. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21954 · Cited by 22
Molecular mechanism of protrusion formation during cell-to-cell spread of Listeria
Ireton, K., Rigano, L. A., Polle, L., & Schubert, W. (2014) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2014.00021 · Cited by 22
Self-citationInfluence of internalin a murinisation on host resistance to orally acquired listeriosis in mice
Bergmann, S., Beard, P. M., Pasche, B., Lienenklaus, S., Weiß, S., Gahan, C. G. M., Schughart, K., & Lengeling, A. (2013) · BMC Microbiology · doi:10.1186/1471-2180-13-90 · Cited by 22
Heroes, E., der Hoeven, G. V., Choy, M. S., García, J. D. P., Ferreira, M., Nys, M., Derua, R., Beullens, M., Ulens, C., Peti, W., et al. (2019) · Structure · doi:10.1016/j.str.2018.12.002 · Cited by 22
Microscale communication between bacterial pathogens and the host epithelium
Mix, A.-K., Goob, G., Sontowski, E., & Hauck, C. R. (2021) · Genes and Immunity · doi:10.1038/s41435-021-00149-1 · Cited by 21
Tracing innate immune defences along the path of Listeria monocytogenes infection
Regan, T. W., MacSharry, J. A., & Brint, E. K. (2014) · Immunology and Cell Biology · doi:10.1038/icb.2014.27 · Cited by 20
Afzal, A. J., Srour, A. Y., Goil, A., Vasudaven, S., Liu, T., Samudrala, R., Dogra, N., Kohli, P., Malakar, A., & Lightfoot, D. A. (2013) · BMC Plant Biology · doi:10.1186/1471-2229-13-43 · Cited by 20
Phosphoinositides and Cellular Pathogens
Payrastre, B., Gaits‐Iacovoni, F., Sansonetti, P. J., & Tronchère, H. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-3015-1_12 · Cited by 20
Gene, R. W., Kumaran, J., Aroche, C., van Faassen, H., Hall, J. C., MacKenzie, C. R., & Arbabi‐Ghahroudi, M. (2014) · Journal of Immunological Methods · doi:10.1016/j.jim.2014.10.009 · Cited by 20
Schubert, W., & Heinz, D. W. (2003) · ChemBioChem · doi:10.1002/cbic.200300624 · Cited by 21
Self-citationLuo, X., & Cai, X. (2012) · Current Microbiology · doi:10.1007/s00284-012-0238-9 · Cited by 19
Hydrophobic clusters in protein structures
Arunachalam, J., & Gautham, N. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21881 · Cited by 19
Structural insights into bacterial modulation of the host cytoskeleton
Stebbins, C. E. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.09.011 · Cited by 19
The Role of Gram-Positive Surface Proteins in Bacterial Niche- and Host-Specialization
Pickering, A. C., & Fitzgerald, J. R. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.594737 · Cited by 18
Vedove, A. D., Lucarelli, A. P., Nardone, V., Matino, A., & Parisini, E. (2015) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x15003878 · Cited by 16
Comparative structural analysis of the binding domain of follicle stimulating hormone receptor
Fan, Q., & Hendrickson, W. A. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21937 · Cited by 16
Quantitative analysis and prediction of curvature in leucine‐rich repeat proteins
Hindle, K. L., Bella, J., & Lovell, S. C. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22440 · Cited by 16
Helical Parameters and Correlations of Tandem Leucine Rich Repeats in Proteins
Enkhbayar, P. (2014) · Journal of Proteomics & Bioinformatics · doi:10.4172/jpb.1000314 · Cited by 16
Harter, E., Lassnig, C., Wagner, E. M., Zaiser, A., Wagner, M., & Rychli, K. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01644 · Cited by 15
Mäesaar, M., Mamede, R., Elias, T., & Roasto, M. (2021) · International Journal of Genomics · doi:10.1155/2021/6636138 · Cited by 15
Novel Leucine Rich Repeat Domains in Proteins from Unicellular Eukaryotes and Bacteria
Miyashita, H., Kuroki, Y., & Matsushima, N. (2014) · Protein and Peptide Letters · doi:10.2174/09298665113206660112 · Cited by 15
The Cell Wall of Listeria monocytogenes and its Role in Pathogenicity
Pucciarelli, M. G., Bierne, H., & del Portillo, F. G. (2007) · Springer eBooks · doi:10.1007/978-0-387-49376-3_5 · Cited by 15
Stange, C., Matus, J. T., Domínguez, C., Pérez‐Acle, T., & Arce‐Johnson, P. (2007) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2007.05.006 · Cited by 15
Role of the αI domain in ligand binding by integrin αEβ7
Corps, E. M., Robertson, A., Dauncey, M. J., & Kilshaw, P. J. (2003) · European Journal of Immunology · doi:10.1002/eji.200324156 · Cited by 14
Dellafiora, L., Filipello, V., Dall’Asta, C., Finazzi, G., Galaverna, G., & Losio, M. N. (2020) · Toxins · doi:10.3390/toxins12010060 · Cited by 13
Metadata
- Authors
- Schubert, W.-D., Urbanke, C., Ziehm, T., Beier, V., Machner, M. P., Domann, E., Wehland, J., Chakraborty, T., & Heinz, D. W.
- Affiliations
- Helmholtz Centre for Infection Research (DE)
- Medizinische Hochschule Hannover (DE)
- Justus-Liebig-Universität Gießen (DE)
- Corresponding author
- Heinz, Dirk W.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2002-12
- Volume
- 111
- Issue
- 6
- Pages
- 825-836
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2019496511
- Cited by
- 302
- References
- 55
- Citations by year
- 2026: 14 · 2025: 8 · 2024: 4 · 2023: 11 · 2022: 9 · 2021: 7 · 2020: 7 · 2019: 9 · 2018: 5 · 2017: 4 · 2016: 6 · 2015: 6 · 2014: 15 · 2013: 13 · 2012: 13
- FWCI
- 16.42
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Listeria monocytogenes in Food Safety
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Listeria monocytogenes, internalin A, integrated nested Laplace approximation, E-cadherin, bacterial invasion, host cell receptors, leucine-rich repeat domain, protein-protein interaction, host tropism, host susceptibility to infection, epithelial cell adhesion, crystal structure
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Cloning, Molecular, Cytoplasm, Humans, Intestinal Mucosa, Ions, Leucine, Listeria monocytogenes, Models, Molecular, Molecular Sequence Data, Mutation, Protein Binding, Ultracentrifugation, X-Ray Diffraction, Cadherins, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Crystallography, X-Ray
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