Structure and sequence features of mussel adhesive protein lead to its salt-tolerant adhesion ability
Open accessAbstract
Aromatic and basic residue form pair in intrinsically disordered adhesive protein, and such pairs dominate protein adsorption.
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?
BA and PEA effectively expel water from the contact interface, and when neighbouring with ATAC, they could enhance electrostatic interactions with the negatively charged glass surface.
“This is because BA and PEA effectively expel water from the contact interface, and, when neighbouring with ATAC (Supplementary Fig. 11), they could enhance electrostatic interactions with the negatively charged glass surface27,40–43 (Supplementary Fig. 12).”
From Data-driven de novo design of super-adhesive hydrogels (2025) · cites this paper as [42]
The Discussion (page not provided) describes an analogous mechanism: aromatic Dopa or Tyr residues scatter interfacial water, allowing paired positively charged residues to bind electrostatically to negatively charged sites on mica. The paper does not establish that BA or PEA expel water or that pairing them with ATAC enhances interactions with glass. (LLM, conf=0.86)
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
VMD: visual molecular dynamics
Humphrey, W., Dalke, A., & Schulten, K. (1996) · Journal of Molecular Graphics · doi:10.1016/0263-7855(96)00018-5 · Cited by 66,952 · see citing works
Comparison of simple potential functions for simulating liquid water
Jorgensen, W. L., Chandrasekhar, J., Madura, J., Impey, R., & Klein, M. (1983) · The Journal of Chemical Physics · doi:10.1063/1.445869 · Cited by 38,335 · see citing works
Molecular dynamics with coupling to an external bath
Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., DiNola, A., & Haak, J. R. (1984) · The Journal of Chemical Physics · doi:10.1063/1.448118 · Cited by 30,626 · see citing works
Particle mesh Ewald: An N⋅log(N) method for Ewald sums in large systems
Darden, T., York, D., & Pedersen, L. (1993) · The Journal of Chemical Physics · doi:10.1063/1.464397 · Cited by 29,588 · see citing works
LINCS: A linear constraint solver for molecular simulations
Hess, B., Bekker, H., Berendsen, H. J. C., & Fraaije, J. G. E. M. (1997) · Journal of Computational Chemistry · doi:10.1002/(sici)1096-987x(199709)18:12 · Cited by 18,369 · see citing works
Canonical sampling through velocity rescaling
Bussi, G., Donadio, D., & Parrinello, M. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2408420 · Cited by 18,034 · see citing works
GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
Hess, B., Kutzner, C., van der Spoel, D., & Lindahl, E. R. (2008) · Journal of Chemical Theory and Computation · doi:10.1021/ct700301q · Cited by 15,830 · see citing works
Comparative Protein Modelling by Satisfaction of Spatial Restraints
Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977 · see citing works
Vanommeslaeghe, K., Hatcher, E., Acharya, C., Kundu, S., Zhong, S., Shim, J., Darian, E., Guvench, O., Lopes, P. E. M., Vorobyov, I., et al. (2009) · Journal of Computational Chemistry · doi:10.1002/jcc.21367 · Cited by 6,986 · see citing works
Replica-exchange molecular dynamics method for protein folding
Sugita, Y., & Okamoto, Y. (1999) · Chemical Physics Letters · doi:10.1016/s0009-2614(99)01123-9 · Cited by 4,499 · see citing works
CHARMM36 all-atom additive protein force field: Validation based on comparison to NMR data
Huang, J., & MacKerell, A. D. (2013) · Journal of Computational Chemistry · doi:10.1002/jcc.23354 · Cited by 4,484 · see citing works
Interactions with Aromatic Rings in Chemical and Biological Recognition
Meyer, E. A., Castellano, R. K., & Diederich, F. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200390319 · Cited by 3,554 · see citing works
Cygan, R. T., Liang, J.-J., & Kalinichev, A. G. (2004) · The Journal of Physical Chemistry B · doi:10.1021/jp0363287 · Cited by 3,244 · see citing works
Statistical potential for assessment and prediction of protein structures
Shen, M., & Šali, A. (2006) · Protein Science · doi:10.1110/ps.062416606 · Cited by 2,294 · see citing works
Single-molecule mechanics of mussel adhesion
Lee, H., Scherer, N. F., & Messersmith, P. B. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605552103 · Cited by 2,112 · see citing works
Peptide Folding: When Simulation Meets Experiment
Daura, X., Gademann, K., Jaun, B., Seebàch, D., van Gunsteren, W. F., & Mark, A. E. (1999) · Angewandte Chemie International Edition · doi:10.1002/(sici)1521-3773(19990115)38:1/2 · Cited by 2,059 · see citing works
Automation of the CHARMM General Force Field (CGenFF) I: bond perception and atom typing
Vanommeslaeghe, K., & MacKerell, A. D. (2012) · Journal of Chemical Information and Modeling · doi:10.1021/ci300363c · Cited by 2,028 · see citing works
The distribution of aluminum in the tetrahedra of silicates and aluminates
Loewenstein, W. B. (1954) · American Mineralogist · Cited by 1,807 · see citing works
Mussel-Inspired Adhesives and Coatings
Lee, B. P., Messersmith, P. B., Israelachvili, J. N., & Waite, J. H. (2011) · Annual Review of Materials Research · doi:10.1146/annurev-matsci-062910-100429 · Cited by 1,668 · see citing works
Polyphenolic Substance of Mytilus edulis : Novel Adhesive Containing L-Dopa and Hydroxyproline
Waite, J. H., & Tanzer, M. L. (1981) · Science · doi:10.1126/science.212.4498.1038 · Cited by 1,051 · see citing works
Adaptive synergy between catechol and lysine promotes wet adhesion by surface salt displacement
Maier, G. P., Rapp, M. V., Waite, J. H., Israelachvili, J. N., & Butler, A. (2015) · Science · doi:10.1126/science.aab0556 · Cited by 722 · see citing works
Bioinspired underwater adhesives by using the supramolecular toolbox
Hofman, A. H., van Hees, I. A., Yang, J., & Kamperman, M. (2018) · Advanced Materials · doi:10.1002/adma.201704640 · Cited by 652 · see citing works
Polyphosphoprotein from the Adhesive Pads of <i>Mytilus edulis</i>
Waite, J. H., & Qin, X. (2001) · Biochemistry · doi:10.1021/bi002718x · Cited by 610 · see citing works
Adhesion mechanisms of the mussel foot proteins mfp-1 and mfp-3
Lin, Q., Gourdon, D., Sun, C., Holten‐Andersen, N., Anderson, T. H., Waite, J. H., & Israelachvili, J. N. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607852104 · Cited by 563 · see citing works
Zhong, W., Gallivan, J. P., Zhang, Y., Li, L., Lester, H. A., & Dougherty, D. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12088 · Cited by 550 · see citing works
A temperature predictor for parallel tempering simulations
Patriksson, A., & van der Spoel, D. (2008) · Physical Chemistry Chemical Physics · doi:10.1039/b716554d · Cited by 495 · see citing works
Wang, R., Li, J., Chen, W., Xu, T., Yun, S., Xu, Z., Xu, Z., Sato, T., Chi, B., & Xu, H. (2017) · Advanced Functional Materials · doi:10.1002/adfm.201604894 · Cited by 471 · see citing works
Self-citationPerspectives on Mussel-Inspired Wet Adhesion
Ahn, B. K. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.6b13149 · Cited by 444 · see citing works
Adjacent cationic–aromatic sequences yield strong electrostatic adhesion of hydrogels in seawater
Fan, H., Wang, J., Tao, Z., Huang, J., Rao, P., Kurokawa, T., & Gong, J. P. (2019) · Nature Communications · doi:10.1038/s41467-019-13171-9 · Cited by 379 · see citing works
Anderson, T. H., Yu, J., Estrada, A., Hammer, M. U., Waite, J. H., & Israelachvili, J. N. (2010) · Advanced Functional Materials · doi:10.1002/adfm.201000932 · Cited by 364 · see citing works
Cation–π interactions in protein–protein interfaces
Crowley, P. B., & Golovin, A. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20417 · Cited by 360 · see citing works
Heinz, H., Farmer, B. L., Pandey, R. B., Slocik, J. M., Patnaik, S. S., Pachter, R., & Naik, R. R. (2009) · Journal of the American Chemical Society · doi:10.1021/ja900531f · Cited by 353 · see citing works
Stewart, R. J., Ransom, T. C., & Hlady, V. (2011) · Journal of Polymer Science Part B Polymer Physics · doi:10.1002/polb.22256 · Cited by 350 · see citing works
Zheng, J., Li, L., Tsao, H., Sheng, Y., Chen, S., & Jiang, S. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.059428 · Cited by 341 · see citing works
Tuning underwater adhesion with cation–π interactions
Gebbie, M. A., Wei, W., Schrader, A. M., Cristiani, T. R., Dobbs, H. A., Idso, M. N., Chmelka, B. F., Waite, J. H., & Israelachvili, J. N. (2017) · Nature Chemistry · doi:10.1038/nchem.2720 · Cited by 339 · see citing works
Picosecond dynamics of tyrosine side chains in proteins
McCammon, J. A., Wolynes, P. G., & Karplus, M. (1979) · Biochemistry · doi:10.1021/bi00573a001 · Cited by 336 · see citing works
Adhesion of mussel foot proteins to different substrate surfaces
Lu, Q., Danner, E. W., Waite, J. H., Israelachvili, J. N., Zeng, H., & Hwang, D. S. (2012) · Journal of The Royal Society Interface · doi:10.1098/rsif.2012.0759 · Cited by 336 · see citing works
The role of hydrophobic interactions in initiation and propagation of protein folding
Dyson, H. J., Wright, P. E., & Scheraga, H. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605504103 · Cited by 330 · see citing works
Novel Hydrogel Actuator Inspired by Reversible Mussel Adhesive Protein Chemistry
Lee, B. P., & Konst, S. (2014) · Advanced Materials · doi:10.1002/adma.201306137 · Cited by 321 · see citing works
Adaptive hydrophobic and hydrophilic interactions of mussel foot proteins with organic thin films
Yu, J., Kan, Y., Rapp, M. V., Danner, E. W., Wei, W., Das, S., Miller, D. R., Chen, Y., Waite, J. H., & Israelachvili, J. N. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315015110 · Cited by 297 · see citing works
Progressive fuzzy cation-π assembly of biological catecholamines
Hong, S., Wang, Y., Park, S. Y., & Lee, H. (2018) · Science Advances · doi:10.1126/sciadv.aat7457 · Cited by 295 · see citing works
High-performance mussel-inspired adhesives of reduced complexity
Ahn, B. K., Das, S., Linstadt, R., Kaufman, Y., Martinez-Rodriguez, N. R., Mirshafian, R., Kesselman, E., Talmon, Y., Lipshutz, B., Israelachvili, J. N., et al. (2015) · Nature Communications · doi:10.1038/ncomms9663 · Cited by 285 · see citing works
Protein- and Metal-dependent Interactions of a Prominent Protein in Mussel Adhesive Plaques
Hwang, D. S., Zeng, H., Mašić, A., Harrington, M. J., Israelachvili, J. N., & Waite, J. H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.133157 · Cited by 281 · see citing works
de Planque, M. R. R., Bonev, B. B., Demmers, J., Greathouse, D. V., Koeppe, R. E., Separovic, F., Watts, A. G., & Killian, J. A. (2003) · Biochemistry · doi:10.1021/bi027000r · Cited by 273 · see citing works
Cheng, H., Yue, K., Kazemzadeh‐Narbat, M., Liu, Y., Khalilpour, A., Li, B., Zhang, Y. S., Annabi, N., & Khademhosseini, A. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b16779 · Cited by 263 · see citing works
Adhesion of Mussel Foot Protein-3 to TiO2 Surfaces: the Effect of pH
Yu, J., Wei, W., Menyo, M. S., Mašić, A., Waite, J. H., & Israelachvili, J. N. (2013) · Biomacromolecules · doi:10.1021/bm301908y · Cited by 252 · see citing works
Kim, S., Yoo, H. Y., Huang, J. S., Lee, Y., Park, S., Park, Y., Jin, S., Jung, Y. M., Zeng, H., Hwang, D. S., et al. (2017) · ACS Nano · doi:10.1021/acsnano.7b01370 · Cited by 233 · see citing works
Petrone, L., Kumar, A., Sutanto, C. N., Patil, N. J., Kannan, S., Palaniappan, A., Amini, S., Zappone, B., Verma, C. S., & Miserez, A. (2015) · Nature Communications · doi:10.1038/ncomms9737 · Cited by 203 · see citing works
Schlegel, M. L., Nagy, K. L., Fenter, P., Cheng, L. K., Sturchio, N. C., & Jacobsen, S. D. (2006) · Geochimica et Cosmochimica Acta · doi:10.1016/j.gca.2006.04.011 · Cited by 187 · see citing works
Guerette, P. A., Hoon, S. S., Seow, Y., Raida, M., Mašić, A., Wong, F. T., Ho, V. H. B., Kong, K. W., Demirel, M. C., Pena‐Francesch, A., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2671 · Cited by 186 · see citing works
Buijs, J., & Hlady, V. (1997) · Journal of Colloid and Interface Science · doi:10.1006/jcis.1997.4876 · Cited by 168 · see citing works
Probing the Adhesive Footprints of Mytilus californianus Byssus
Zhao, H., Robertson, N., Jewhurst, S. A., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510792200 · Cited by 158 · see citing works
Mapping protein dynamics by X-ray diffraction
Ringe, D., & Petsko, G. A. (1985) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(85)90002-1 · Cited by 155 · see citing works
Potential Energy Curves for Cation−π Interactions: Off-Axis Configurations Are Also Attractive
Marshall, M. S., Steele, R. P., Thanthiriwatte, K. S., & Sherrill, C. D. (2009) · The Journal of Physical Chemistry A · doi:10.1021/jp906086x · Cited by 153 · see citing works
Millisecond dynamics of RNA polymerase II translocation at atomic resolution
Silva, D., Weiss, D. R., Pardo-Avila, F., Da, L.-T., Levitt, M., Wang, D., & Huang, X.-H. (2014) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1315751111 · Cited by 144 · see citing works
He, Y., Chang, Y., Hower, J. C., et al. (2008) · Physical Chemistry Chemical Physics · doi:10.1039/b807129b · Cited by 121 · see citing works
Interfacial Tryptophan Residues: A Role for the Cation-π Effect?
Petersen, F. N. R., Jensen, M. Ø., & Hélix‐Nielsen, C. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.061804 · Cited by 118 · see citing works
Cation–π interaction in DOPA-deficient mussel adhesive protein mfp-1
Kim, S., Faghihnejad, A., Lee, Y., Jho, Y., Zeng, H., & Hwang, D. S. (2014) · Journal of Materials Chemistry B · doi:10.1039/c4tb01646g · Cited by 103 · see citing works
Levine, Z. A., Rapp, M. V., Wei, W., Mullen, R. G., Wu, C. F., Zerze, G. H., Mittal, J., Waite, J. H., Israelachvili, J. N., & Shea, J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603065113 · Cited by 99 · see citing works
Bridging Adhesion of Mussel-Inspired Peptides: Role of Charge, Chain Length, and Surface Type
Wei, W., Yu, J., Gebbie, M. A., Tan, Y., Rodriguez, N. R. M., Israelachvili, J. N., & Waite, J. H. (2014) · Langmuir · doi:10.1021/la504316q · Cited by 94 · see citing works
Molecular surface chemistry in marine bioadhesion
Petrone, L. (2013) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2013.03.006 · Cited by 89 · see citing works
A Method for Measuring the Adhesion Strength of Marine Mussels
Burkett, J. R., Wojtas, J. L., Cloud, J. L., et al. (2009) · The Journal of Adhesion · doi:10.1080/00218460902996903 · Cited by 84 · see citing works
Simulations of Membranes and Other Interfacial Systems Using P21 and Pc Periodic Boundary Conditions
Dolan, E. A., Venable, R. M., Pastor, R. W., et al. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75577-x · Cited by 83 · see citing works
Fant, C., Sott, K., Elwing, H. B., & Höök, F. (2000) · Biofouling · doi:10.1080/08927010009378437 · Cited by 81 · see citing works
Shin, M., Shin, J. Y., Kim, K., Yang, B., Han, J. W., Kim, N., & Chi, H. J. (2019) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2019.12.082 · Cited by 79 · see citing works
Molecular mechanics of mussel adhesion proteins
Qin, Z., & Buehler, M. J. (2013) · Journal of the Mechanics and Physics of Solids · doi:10.1016/j.jmps.2013.08.015 · Cited by 74 · see citing works
Bulk adhesive strength of recombinant hybrid mussel adhesive protein
Chi, H. J., Hwang, D. S., Lim, S., et al. (2008) · Biofouling · doi:10.1080/08927010802563108 · Cited by 74 · see citing works
Hydration and Dewetting near Graphite−CH3 and Graphite−COOH Plates
Li, J., Liu, T., Li, X., et al. (2005) · The Journal of Physical Chemistry B · doi:10.1021/jp044090w · Cited by 74 · see citing works
Self-citationDensity functional study of the TiO2–dopamine complex
Vega-Arroyo, M., LeBreton, P. R., Rajh, T., et al. (2005) · Chemical Physics Letters · doi:10.1016/j.cplett.2005.03.029 · Cited by 73 · see citing works
Hu, H., Dyke, J. C., Bowman, B. A., et al. (2016) · Langmuir · doi:10.1021/acs.langmuir.6b02141 · Cited by 64 · see citing works
Natural and bio-inspired underwater adhesives: Current progress and new perspectives
Cui, M., Ren, S., Wei, S., Sun, C., & Zhong, C. (2017) · APL Materials · doi:10.1063/1.4985756 · Cited by 62 · see citing works
Martı́, J., Sala, J., & Guàrdia, E. (2009) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2009.09.015 · Cited by 61 · see citing works
Mussel-inspired hybrid network hydrogel for continuous adhesion in water
Fu, Y., Ren, P., Wang, F., et al. (2020) · Journal of Materials Chemistry B · doi:10.1039/c9tb02863c · Cited by 60 · see citing works
Yeh, I., Lenhart, J. L., & Rinderspacher, B. C. (2015) · The Journal of Physical Chemistry C · doi:10.1021/jp512780s · Cited by 56 · see citing works
Emerging β-Sheet Rich Conformations in Supercompact Huntingtin Exon-1 Mutant Structures
Kang, H., Vázquez, F. X., Zhang, L., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b00838 · Cited by 52 · see citing works
Lundin, M., Elofsson, U. M., Blomberg, E., et al. (2010) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2009.12.019 · Cited by 49 · see citing works
The RGD finger of Del‐1 is a unique structural feature critical for integrin binding
Schürpf, T., Chen, Q., Liu, J., Wang, R., Springer, T. A., & Wang, J. (2012) · The FASEB Journal · doi:10.1096/fj.11-202036 · Cited by 49 · see citing works
Zhang, Y., Ren, B., Xie, S., Cai, Y., Wang, T., Feng, Z., Tang, J., Chen, Q., Xu, J., Xu, L., et al. (2019) · ACS Applied Polymer Materials · doi:10.1021/acsapm.8b00232 · Cited by 49 · see citing works
Hidden complexity of synergistic roles of Dopa and lysine for strong wet adhesion
Li, Y., Liang, C., Gao, L., Li, S., Zhang, Y., Zhang, J., & Cao, Y. (2017) · Materials Chemistry Frontiers · doi:10.1039/c7qm00402h · Cited by 44 · see citing works
Self-citationWang, R., Zhou, B., Liu, W., et al. (2014) · Journal of Biomaterials Applications · doi:10.1177/0885328214553960 · Cited by 38 · see citing works
Bilotto, P., Labate, C., Santo, M. P. D., et al. (2019) · Langmuir · doi:10.1021/acs.langmuir.9b01730 · Cited by 37 · see citing works
Recombinant mussel protein Pvfp-5β: A potential tissue bioadhesive
Santonocito, R., Venturella, F., Piaz, F. D., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009531 · Cited by 36 · see citing works
Adraa, K. E., Timón, V., Lambert, J., Al-Rabaa, A., Jaber, F., Jaber, M., & Tielens, F. (2012) · The Journal of Physical Chemistry C · doi:10.1021/jp3094148 · Cited by 27 · see citing works
l-3,4-dihydroxyphenylalanine-collagen modified PDMS surface for controlled cell culture
Gao, C., Guo, Y., He, J., et al. (2012) · Journal of Materials Chemistry · doi:10.1039/c2jm00104g · Cited by 24 · see citing works
Karplus, M. (1984) · Advances in Biophysics · doi:10.1016/0065-227x(84)90011-x · Cited by 23 · see citing works
Adsorption and Orientation of 3,4-Dihydroxy- l -phenylalanine onto Tunable Monolayer Films
Chen, T., Yang, H., Gao, H., et al. (2017) · The Journal of Physical Chemistry C · doi:10.1021/acs.jpcc.7b02795 · Cited by 18 · see citing works
Tyrosine Rotamer States in Beta Amyloid: Signatures of Aggregation and Fibrillation
Mancini, O., Rolinski, O. J., Kubiak-Ossowska, K., et al. (2018) · ACS Omega · doi:10.1021/acsomega.8b02408 · Cited by 9 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Data-driven de novo design of super-adhesive hydrogels
Liao, H., Hu, S., Yang, H., Wang, L., Tanaka, S., Takigawa, I., Li, W., Fan, H., & Gong, J. P. (2025) · Nature · doi:10.1038/s41586-025-09269-4 · Cited by 169 · see citing works
- Authors
- Ou, X., Xue, B., Lao, Y., Wutthinitikornkit, Y., Tian, R., Zou, A., Yang, L., Wang, W., Cao, Y., & Li, J.
- Affiliations
- Zhejiang University (CN)
- Collaborative Innovation Center of Advanced Microstructures (CN)
- ShanghaiTech University (CN)
- Corresponding author
- Ou, Xinwen
- Xue, Bin
- Cao, Yi
- Li, Jingyuan
- ORCID
- Venue
- Science Advances
- Published
- 2020-09-25
- Volume
- 6
- Issue
- 39
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC7518861
- OpenAlex
- W3088203618
- Cited by
- 109
- References
- 87
- Citations by year
- 2026: 25 · 2025: 28 · 2024: 14 · 2023: 17 · 2022: 8 · 2021: 16 · 2020: 1
- FWCI
- 2.89
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Science Advances (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (11722434, 11874319, 11674153, 21904088, 11804148)
- China Postdoctoral Science Foundation (2018M642401, 2019T120499)
- National Natural Science Foundation of Jiangsu Province (BK2018032)
- Topics
- Physical Sciences › Materials Science › Surfaces, Coatings and Films › Polymer Surface Interaction Studies
- Physical Sciences › Engineering › Ocean Engineering › Marine Biology and Environmental Chemistry
- Physical Sciences › Engineering › Mechanics of Materials › Adhesion, Friction, and Surface Interactions
- Keywords
- mussel adhesive proteins, wet adhesion, DOPA, tyrosine, intrinsically disordered proteins, basic residues, protein conformation, surface binding, post-translational modification
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