The DOI matches its Crossref record; 120 of the 120 references it cites were found in a registry or an index.
Laminins: Roles and Utility in Wound Repair
Open accessAbstract
Significance: Laminins are complex extracellular macromolecules that are major players in the control of a variety of core cell processes, including regulating rates of cell proliferation, differentiation, adhesion, and migration. Laminins, and related extracellular matrix components, have essential roles in tissue homeostasis; however, during wound healing, the same proteins are critical players in re-epithelialization and angiogenesis. Understanding how these proteins influence cell behavior in these different conditions holds great potential in identifying new strategies to enhance normal wound closure or to treat chronic/nonhealing wounds. Recent Advances: Laminin-derived bioactive peptides and, more recently, laminin-peptide conjugated scaffolds, have been designed to improve tissue regeneration after injuries. These peptides have been shown to be effective in decreasing inflammation and granulation tissue, and in promoting re-epithelialization, angiogenesis, and cell migration. Critical Issues: Although there is now a wealth of knowledge concerning laminin form and function, there are still areas of some controversy. These include the relative contribution of two laminin-based adhesive devices (focal contacts and hemidesmosomes) to the re-epithelialization process, the impact and implications of laminin proteolytic processing, and the importance of laminin polymer formation on cell behavior. In addition, the roles in wound healing of the laminin-related proteins, netrins, and LaNts are still to be fully defined. Future Directions: The future of laminin-based therapeutics potentially lies in the bioengineering of specific substrates to support laminin deposition for ex vivo expansion of autologous cells for graft formation and transplantation. Significant recent advances suggest that this goal is within sight.
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?
In the citing paper
“Keratinocytes themselves further activate fibroblasts in a feedback loop through the production of fibronectin, tenascin C, and laminin 332 (Fig. 2) [93].”
From Immunology of Wound Healing (2018) · cites this paper as [93]
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
A simplified laminin nomenclature
Aumailley, M., Bruckner‐Tuderman, L., Carter, W. G., Deutzmann, R., EDGAR, D., Ekblom, P., Engel, J., Engvall, E., Hohenester, E., & Jones, J. (2005) · Matrix Biology · doi:10.1016/j.matbio.2005.05.006 · Cited by 928
Beningo, K. A., Dembo, M., Kaverina, I., Small, J. V., & Wang, Y. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.4.881 · Cited by 750
Supramolecular assembly of basement membranes
Timpl, R., & Brown, J. C. (1996) · BioEssays · doi:10.1002/bies.950180208 · Cited by 701
Miner, J. H., Patton, B. L., Lentz, S. I., Gilbert, D. J., Snider, W. D., Jenkins, N. A., Copeland, N. G., & Sanes, J. R. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.137.3.685 · Cited by 650
Expression and Function of Laminins in the Embryonic and Mature Vasculature
Hallmann, R., Horn, N., Selg, M., Wendler, O., Pausch, F., & Sorokin, L. M. (2005) · Physiological Reviews · doi:10.1152/physrev.00014.2004 · Cited by 597
Miner, J. H., Cunningham, J. M., & Sanes, J. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.6.1713 · Cited by 491
Laminins in basement membrane assembly
Hohenester, E., & Yurchenco, P. D. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.21831 · Cited by 478
Laminin-nidogen complex. Extraction with chelating agents and structural characterization
Paulsson, M., Aumailley, M., Deutzmann, R., Timpl, R., Beck, K., & ENGEL, J. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13476.x · Cited by 450
Functional Diversity of Laminins
Domogatskaya, A., Rodin, S., & Tryggvason, K. (2012) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155750 · Cited by 396
Deletion of the Laminin α4 Chain Leads to Impaired Microvessel Maturation
Thyboll, J., Kortesmaa, J., Cao, R., Soininen, R., Wang, L., Iivanainen, A., Sorokin, L. M., Risling, M., Cao, Y., & Tryggvason, K. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1194-1202.2002 · Cited by 349
Miner, J. H., Li, C., Mudd, J. L., Go, G., & Sutherland, A. E. (2004) · Development · doi:10.1242/dev.01112 · Cited by 343
Ryan, M. C., Lee, K., Miyashita, Y., & Carter, W. G. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.6.1309 · Cited by 315
Schenk, S., Hintermann, E., Bilban, M., Koshikawa, N., Hojilla, C., Khokha, R., & Quaranta, V. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200208145 · Cited by 309
Pulkkinen, L., Christiano, A. M., Airenne, T. T., Haakana, H., Tryggvason, K., & Uitto, J. (1994) · Nature Genetics · doi:10.1038/ng0394-293 · Cited by 296
Usui, M. L., Mansbridge, J. N., Carter, W. G., Fujita, M., & Olerud, J. E. (2008) · Journal of Histochemistry & Cytochemistry · doi:10.1369/jhc.2008.951194 · Cited by 281
Ryan, M. C., Tizard, R., VanDevanter, D. R., & Carter, W. G. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31713-1 · Cited by 279
Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity.
Yurchenco, P. D., Tsilibary, E. C., CHARONIS, A. S., & Furthmayr, H. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39656-4 · Cited by 265
Sorokin, L. M., Pausch, F., Frieser, M., Kröger, S., Ohage, E., & Deutzmann, R. (1997) · Developmental Biology · doi:10.1006/dbio.1997.8668 · Cited by 265
Goldfinger, L. E., Hopkinson, S. B., deHart, G. W., Collawn, S. S., Couchman, J., & Jones, J. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.16.2615 · Cited by 261
Self-assembly and calcium-binding sites in laminin. A three-arm interaction model
Yurchenco, P. D., & Cheng, Y. S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85334-6 · Cited by 244
Aumailley, M., Nurcombe, V., Edgar, D., Paulsson, M., & Timpl, R. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60840-3 · Cited by 239
Bass, M. D., Roach, K. A., Morgan, M. R., Mostafavi‐Pour, Z., Schoen, T., Muramatsu, T., Mayer, U., Ballestrem, C., Spatz, J. P., & Humphries, M. J. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610076 · Cited by 236
Kallunki, P., Sainio, K., Eddy, R. L., Byers, M. G., Kallunki, T., Sariola, H. V., Beck, K., Hirvonen, H., Shows, T. B., & Tryggvason, K. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.119.3.679 · Cited by 233
Kikkawa, Y., Sanzen, N., Fujiwara, H., Sonnenberg, A., & Sekiguchi, K. (2000) · PubMed · doi:10.1242/jcs.113.5.869 · Cited by 231
Defects in keratinocyte activation during wound healing in the syndecan-1-deficient mouse
Stepp, M. A., Gibson, H. E., Gala, P. H., Iglesia, D. D. S., Pajoohesh‐Ganji, A., Pal‐Ghosh, S., Brown, M., Aquino, C. J., Schwartz, A. M., Goldberger, O., et al. (2002) · Journal of Cell Science · doi:10.1242/jcs.00128 · Cited by 230
The syndecans, tuners of transmembrane signaling
Zimmermann, P., & David, G. (1999) · The FASEB Journal · doi:10.1096/fasebj.13.9001.s91 · Cited by 217
Syndecan-4 and focal adhesion function
Woods, A., & Couchman, J. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00254-4 · Cited by 215
A role for pericytes as microenvironmental regulators of human skin tissue regeneration
Paquet‐Fifield, S., Schlüter, H., Li, A., Aitken, T., Gangatirkar, P., Blashki, D., Koelmeyer, R., Pouliot, N., Palatsides, M., Ellis, S. L., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38535 · Cited by 215
Rajasekharan, S., & Kennedy, T. E. (2009) · Genome biology · doi:10.1186/gb-2009-10-9-239 · Cited by 214
Shekarabi, M., & Kennedy, T. E. (2002) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2001.1075 · Cited by 206
Laplante, A., Germain, L., Auger, F. A., & Moulin, V. J. (2001) · The FASEB Journal · doi:10.1096/fj.01-0250com · Cited by 199
Laminin 5 deposition regulates keratinocyte polarization and persistent migration
Frank, D. E., & Carter, W. G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01003 · Cited by 183
Extensive tissue-regenerative capacity of neonatal human keratinocyte stem cells and their progeny
Li, A., Pouliot, N., Redvers, R. P., & Kaur, P. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200419140 · Cited by 182
Kibbey, M. C., Grant, D. S., & Kleinman, H. K. (1992) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/84.21.1633 · Cited by 180
Laminin deposition in the extracellular matrix: a complex picture emerges
Hamill, K. J., Kligys, K. R., Hopkinson, S. B., & Jones, J. (2009) · Journal of Cell Science · doi:10.1242/jcs.041095 · Cited by 179
Self-citationDeposition of Laminin 5 by Keratinocytes Regulates Integrin Adhesion and Signaling
Nguyen, B. P., Gil, S. G., & Carter, W. G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006379200 · Cited by 171
α3aβ1 integrin localizes to focal contacts in response to diverse extracellular matrix proteins
DiPersio, C. M., Shah, S., & Hynes, R. O. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.6.2321 · Cited by 159
Structure and Function of a Vimentin-associated Matrix Adhesion in Endothelial Cells
Gonzales, M., Weksler, B. B., Tsuruta, D., Goldman, R. D., Yoon, K. J., Hopkinson, S. B., Flitney, F. W., & Jones, J. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.1.85 · Cited by 157
Integrin α3β1 inhibits directional migration and wound re-epithelialization in the skin
Margadant, C., Raymond, K., Kreft, M., Sachs, N., Janssen, H., & Sonnenberg, A. (2008) · Journal of Cell Science · doi:10.1242/jcs.029108 · Cited by 149
Pullar, C. E., Baier, B. S., Kariya, Y., Russell, A. J., Horst, B. A. J., Marinkovich, M. P., & Isseroff, R. R. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-05-0433 · Cited by 144
Talts, J. F., Sasaki, T., Miosge, N., Göhring, W., Mann, K., Mayne, R., & Timpl, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003261200 · Cited by 138
McLean, W. H. I. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg234 · Cited by 138
Gonzalez, A. M., Gonzales, M., Herron, G. S., Nagavarapu, U., Hopkinson, S. B., Tsuruta, D., & Jones, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252649399 · Cited by 133
Laminin 332 in junctional epidermolysis bullosa
Kiritsi, D., Has, C., & Bruckner‐Tuderman, L. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.22418 · Cited by 132
Choma, D. P., Pumiglia, K. M., & DiPersio, C. M. (2004) · Journal of Cell Science · doi:10.1242/jcs.01251 · Cited by 129
Recombinant Human Laminin-10 (α5β1γ1)
Doi, M., Thyboll, J., Kortesmaa, J., Jansson, K., Iivanainen, A., Parvardeh, M., Timpl, R., Hedin, U., Swedenborg, J., & Tryggvason, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111228200 · Cited by 128
Recombinant Laminin-8 (α4β1γ1)
Kortesmaa, J., Yurchenco, P. D., & Tryggvason, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.20.14853 · Cited by 127
The netrin receptor DCC focuses invadopodia-driven basement membrane transmigration in vivo
Hagedorn, E. J., Ziel, J. W., Morrissey, M. A., Linden, L. M., Wang, Z., Chi, Q., Johnson, S. A., & Sherwood, D. R. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201301091 · Cited by 127
Ali, S., Saik, J. E., Gould, D. J., Dickinson, M. E., & West, J. L. (2013) · BioResearch open access · doi:10.1089/biores.2013.0021 · Cited by 127
Integrin β4 Regulates Migratory Behavior of Keratinocytes by Determining Laminin-332 Organization
Sehgal, B. U., DeBiase, P. J., Matzno, S., Chew, T., Claiborne, J. N., Hopkinson, S. B., Russell, A. J., Marinkovich, M. P., & Jones, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606317200 · Cited by 123
Gagnoux-Palacios, L., Allégra, M., Spirito, F., Pommeret, O., Roméro, C., Ortonne, J. P., & Meneguzzi, G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.4.835 · Cited by 122
Tsuruta, D., Hashimoto, T., Hamill, K. J., & Jones, J. (2011) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2011.01.005 · Cited by 122
Self-citationTerminal short arm domains of basement membrane laminin are critical for its self-assembly.
Schittny, J. C., & Yurchenco, P. D. (1990) · The Journal of Cell Biology · doi:10.1083/jcb.110.3.825 · Cited by 118
Ljubimov, A. V., Huang, Z.-S., Huang, G. H., Burgeson, R. E., Miner, J. H., Gullberg, D., Ninomiya, Y., Sado, Y., & Kenney, M. C. (1998) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549804600907 · Cited by 116
Regulation of hemidesmosome disassembly by growth factor receptors
Margadant, C., Frijns, E., Wilhelmsen, K., & Sonnenberg, A. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.05.001 · Cited by 115
DCC constrains tumour progression via its dependence receptor activity
Castets, M., Broutier, L., Molin, Y., Brevet, M., Chazot, G., Gadot, N., Paquet, A., Mazelin, L., Jarrosson, L., Scoazec, J., et al. (2011) · Nature · doi:10.1038/nature10708 · Cited by 114
Kivirikko, S., McGrath, J. A., Pulkkinen, L., Uitto, J., & Christiano, A. M. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.2.231 · Cited by 114
Netrin-1 role in angiogenesis: To be or not to be a pro-angiogenic factor?
Castets, M., & Mehlen, P. (2010) · Cell Cycle · doi:10.4161/cc.9.8.11197 · Cited by 113
Kainulainen, T., Häkkinen, L., Hamidi, S., Larjava, K., Kallioinen, M. J., Peltonen, J. T. K., Salo, T. A., Larjava, H., & Oikarinen, A. (1998) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549804600309 · Cited by 109
McLean, W. H. I. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddh031 · Cited by 109
Laminin‐1 peptide‐conjugated chitosan membranes as a novel approach for cell engineering
Mochizuki, M., Kadoya, Y., Wakabayashi, Y., Kato, K., Okazaki, I., YAMADA, M., Sato, T. J., Sakairi, N., Nishi, N., & Nomizu, M. (2003) · The FASEB Journal · doi:10.1096/fj.02-0564fje · Cited by 105
Staquicini, F. I., Dias‐Neto, E., Li, J., Snyder, E. Y., Sidman, R. L., Pasqualini, R., & Arap, W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813286106 · Cited by 102
Binding of Netrin-4 to Laminin Short Arms Regulates Basement Membrane Assembly
Schneiders, F. I., Maertens, B., Böse, K., Li, Y. H., Brunken, W. J., Paulsson, M., Smyth, N. R., & Koch, M. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703137200 · Cited by 99
Ogawa, T., Tsubota, Y., Hashimoto, J., Kariya, Y., & Miyazaki, K. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-09-0806 · Cited by 98
Pouliot, N., Saunders, N. A., & Kaur, P. (2002) · Experimental Dermatology · doi:10.1034/j.1600-0625.2002.110501.x · Cited by 92
Pouliot, N., & Kusuma, N. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.22125 · Cited by 90
Kim, J., Park, W. H., & MIN, B. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.11.009 · Cited by 87
The C-terminal Region of Laminin β Chains Modulates the Integrin Binding Affinities of Laminins
Taniguchi, Y., Ido, H., Sanzen, N., Hayashi, M., Nishiuchi, R., Futaki, S., & Sekiguchi, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809332200 · Cited by 80
Wilhelmsen, K., Litjens, S. H. M., Kuikman, I., Margadant, C., van Rheenen, J., & Sonnenberg, A. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0306 · Cited by 76
Netrin-1 Simultaneously Suppresses Corneal Inflammation and Neovascularization
Han, Y., Shao, Y., Lin, Z., Qu, Y., Wang, H., Zhou, Y., Chen, W., Chen, Y., Chen, W., Hu, F., et al. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.11-8722 · Cited by 74
Wondimu, Z., Geberhiwot, T., Ingerpuu, S., Juronen, E., Xie, X., Lindbom, L., Doi, M., Kortesmaa, J., Thyboll, J., Tryggvason, K., et al. (2004) · Blood · doi:10.1182/blood-2004-01-0396 · Cited by 73
Hussain, S., Carafoli, F., & Hohenester, E. (2011) · EMBO Reports · doi:10.1038/embor.2011.3 · Cited by 72
Clement, A. L., Moutinho, T. J., & Pins, G. D. (2013) · Acta Biomaterialia · doi:10.1016/j.actbio.2013.08.017 · Cited by 71
Herlitz Junctional Epidermolysis Bullosa
Laimer, M., Lanschuetzer, C. M., Diem, A., & Bauer, J. W. (2009) · Dermatologic Clinics · doi:10.1016/j.det.2009.10.006 · Cited by 71
Pouliot, N., Nice, E. C., & Burgess, A. W. (2001) · Experimental Cell Research · doi:10.1006/excr.2001.5197 · Cited by 68
Fu, X., Xu, M., Liu, J., Qi, Y., Li, S., & Wang, H. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.11.013 · Cited by 65
Laminin chain assembly is regulated by specific coiled-coil interactions
Macdonald, P. R., Lustig, A., Steinmetz, M. O., & Kammerer, R. A. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.02.004 · Cited by 61
Origin and Evolution of Laminin Gene Family Diversity
Fahey, B., & Degnan, B. M. (2012) · Molecular Biology and Evolution · doi:10.1093/molbev/mss060 · Cited by 61
Hamill, K. J., Hopkinson, S. B., Debiase, P., & Jones, J. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-01-0051 · Cited by 60
Self-citationJakobsson, L., Domogatskaya, A., Tryggvason, K., Edgar, D., & Claesson, L. (2007) · The FASEB Journal · doi:10.1096/fj.07-9617com · Cited by 58
The α4 laminin subunit regulates endothelial cell survival
DeHahn, K. C., Gonzales, M., Gonzalez, A. M., Hopkinson, S. B., Chandel, N. S., Brunelle, J. K., & Jones, J. (2003) · Experimental Cell Research · doi:10.1016/j.yexcr.2003.11.006 · Cited by 57
Processing of Laminin α Chains Generates Peptides Involved in Wound Healing and Host Defense
Senyürek, I., Kempf, W. E., Klein, G., Maurer, A., Kalbacher, H., Schäfer, L., Wanke, I., Christ, C., Stevanović, S., Schaller, M., et al. (2014) · Journal of Innate Immunity · doi:10.1159/000357032 · Cited by 55
α6β4 Integrin, a Master Regulator of Expression of Integrins in Human Keratinocytes
Kligys, K. R., Wu, Y., Hopkinson, S. B., Kaur, S., Platanias, L. C., & Jones, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.310458 · Cited by 54
Angiogenic laminin-derived peptides stimulate wound healing
Malinda, K. M., Wysocki, A. B., Koblinski, J. E., Kleinman, H. K., & Ponce, M. L. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.05.025 · Cited by 54
Laminin peptide‐conjugated chitosan membrane: Application for keratinocyte delivery in wounded skin
Ikemoto, S., Mochizuki, M., YAMADA, M., Takeda, A., Uchinuma, E., Yamashina, S., Nomizu, M., & Kadoya, Y. (2006) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.30804 · Cited by 54
Netrin-4 Promotes Glioblastoma Cell Proliferation through Integrin β4 Signaling
Hu, Y., Ylivinkka, I., Chen, P., Li, L., Hautaniemi, S., Nyman, T. A., Keski‐Oja, J., & Hyytiäinen, M. M. (2012) · Neoplasia · doi:10.1593/neo.111396 · Cited by 51
M�hle, C., Jiang, Q., Charlesworth, A., Bruckner‐Tuderman, L., Meneguzzi, G., & Schneider, H. (2004) · Human Genetics · doi:10.1007/s00439-004-1210-y · Cited by 51
Picard, M., Petrie, R. J., Antoine‐Bertrand, J., Saint-Cyr-Proulx, E., Villemure, J.-F., & Lamarche‐Vane, N. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.09.004 · Cited by 51
Min, S., Lee, S., Hong, S., Chung, C., Park, W. H., & Min, B. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.02.045 · Cited by 50
Jones, J., Yokoo, K. M., & Goldman, R. D. (1986) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970060604 · Cited by 50
Globular domains 4/5 of the laminin α3 chain mediate deposition of precursor laminin 5
Sigle, R. O., Gil, S. G., Bhattacharya, M., Ryan, M. C., Yang, T.-M., Brown, T. A., Boutaud, A., Miyashita, Y., Olerud, J. E., & Carter, W. G. (2004) · Journal of Cell Science · doi:10.1242/jcs.01310 · Cited by 50
Nakamura, M., Mie, M., Mihara, H., Nakamura, M., & Kobatake, E. (2008) · Biomaterials · doi:10.1016/j.biomaterials.2008.04.006 · Cited by 49
Araki, E., Momota, Y., Togo, T., Tanioka, M., Hozumi, K., Nomizu, M., Miyachi, Y., & Utani, A. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-09-0977 · Cited by 49
DCC promoter hypermethylation in esophageal squamous cell carcinoma
Park, H. L., Kim, M. S., Yamashita, K., Westra, W. H., Carvalho, A. L., Lee, J., Jiang, W., Baek, J. H., Liu, J., Osada, M., et al. (2008) · International Journal of Cancer · doi:10.1002/ijc.23434 · Cited by 48
Role of Dermal-Epidermal Basement Membrane Zone in Skin, Cancer, and Developmental Disorders
Ko, M. S., & Marinkovich, M. P. (2009) · Dermatologic Clinics · doi:10.1016/j.det.2009.10.001 · Cited by 45
Identification of redundant angiogenic sites in laminin α1 and γ1 chains
Ponce, M. L., & Kleinman, H. K. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(03)00056-9 · Cited by 42
Sato, N. (1999) · Japanese Journal of Ophthalmology · doi:10.1016/s0021-5155(99)00095-7 · Cited by 38
Riddelle, K. S., Hopkinson, S. B., & Jones, J. (1992) · Journal of Cell Science · doi:10.1242/jcs.103.2.475 · Cited by 38
Li, J., Zhou, L. Y., Tran, H. T., Chen, Y., Nguyen, N. T., Karasek, M. A., & Marinkovich, M. P. (2005) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700089 · Cited by 37
Kurpakus, M. A., Stock, E. L., & Jones, J. (1990) · Journal of Cell Science · doi:10.1242/jcs.96.4.651 · Cited by 35
Characterization of Laminin 5B and NH2-terminal Proteolytic Fragment of Its α3B Chain
Kariya, Y., Yasuda, C., Nakashima, Y., Ishida, K., Tsubota, Y., & Miyazaki, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400670200 · Cited by 34
The expression and function of netrin-4 in murine ocular tissues
Li, Y. N., Pinzón‐Duarte, G., Dattilo, M., Claudepierre, T., Koch, M., & Brunken, W. J. (2012) · Experimental Eye Research · doi:10.1016/j.exer.2012.01.007 · Cited by 33
Kidd, K. R., & Williams, S. K. (2004) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.20133 · Cited by 33
Kidd, K. R., Ponte, D. B. D., Stone, A. L., Hoying, J. B., Nagle, R. B., & Williams, S. K. (2005) · Tissue Engineering · doi:10.1089/ten.2005.11.1379 · Cited by 32
Hamill, K. J., Hopkinson, S. B., Jonkman, M. F., & Jones, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.203646 · Cited by 31
Self-citationA new homozygous nonsense mutation inLAMA3Aunderlying laryngo-onycho-cutaneous syndrome
Barzegar, M., Mozafari, N., Kariminejad, A., Asadi‐Kani, Z., Ozoemena, L., & McGrath, J. A. (2013) · British Journal of Dermatology · doi:10.1111/bjd.12522 · Cited by 28
Identification of a Novel Family of Laminin N-terminal Alternate Splice Isoforms
Hamill, K. J., Langbein, L., Jones, J., & McLean, W. H. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.052811 · Cited by 27
Self-citationKelker, W., Dyke, D. L. V., Worsham, M. J., Christopherson, P. L., James, C. D., Conlon, M. R., & Carey, T. E. (1996) · PubMed · Cited by 26
Jiang, Q.-J., Izakovic, J., Zenker, M., Fartasch, M., Meneguzzi, G., Rascher, W., & Schneider, H. (2002) · The Journal of Pediatrics · doi:10.1067/mpd.2002.127794 · Cited by 23
Greciano, P. G., Moyano, J. V., Buschmann, M. M., Tang, J. M., Lu, Y., Rudnicki, J., Manninen, A., & Matlin, K. S. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-08-0718 · Cited by 20
Kariya, Y., Mori, T., Yasuda, C., Watanabe, N., Kaneko, Y., Nakashima, Y., Ogawa, T., & Miyazaki, K. (2008) · Journal of Molecular Histology · doi:10.1007/s10735-008-9183-0 · Cited by 20
Peptides derived from the human laminin α4 and α5 chains exhibit antimicrobial activity
Senyürek, I., Klein, G., Kalbacher, H., Deeg, M., & Schittek, B. (2010) · Peptides · doi:10.1016/j.peptides.2010.04.016 · Cited by 20
Figueira, E. C., Anne, C., Challinor, C. J., Coroneo, M. T., & Murrell, D. F. (2007) · Clinical and Experimental Ophthalmology · doi:10.1111/j.1442-9071.2006.01436.x · Cited by 19
Damodaran, G., Tiong, W. H. C., Collighan, R. J., Griffin, M., Navsaria, H. A., & Pandit, A. S. (2013) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.34583 · Cited by 18
Lian, J., Dai, X., Li, X., & He, F. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.06.069 · Cited by 18
The syndecan binding sequence KKLRIKSKEK in laminin α3 LG4 domain promotes epidermal repair.
Rousselle, P., Carulli, S., Chajra, H., Dayan, G., Pin, D., & Herbage, B. (2013) · PubMed · doi:10.1684/ejd.2013.1974 · Cited by 15
Kittelberger, R., Davis, P. F., & Stehbens, W. E. (1990) · PubMed · Cited by 15
Sakai, N., Waterman, E. A., Nguyen, N. T., Keene, D. R., & Marinkovich, M. P. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2010.85 · Cited by 5
Effects of fibroblasts, collagen, and laminin on healing of superficial split wounds
Blinova, M. I., Paramonov, B. A., Кухарева, Л. В., Gorelik, Y. V., Nikitina, Y. M., & Voronkina, I. V. (1997) · Bulletin of Experimental Biology and Medicine · doi:10.1007/bf02445104 · Cited by 4
Mi, B., Paramonov, B. A., Кухарева, Л. В., Gorelik, I. V., Nikitina, I. M., & Voronkina, I. V. (1997) · PubMed · Cited by 4
Cited by
Sorted by citations
Extracellular matrix structure
Theocharis, A. D., Skandalis, S. S., Gialeli, C., & Karamanos, N. K. (2016) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2015.11.001 · Cited by 2,598
Extracellular matrix and its therapeutic potential for cancer treatment
Huang, J., Zhang, L., Wan, D., Zhou, L., Zheng, S., Lin, S., & Qiao, Y. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00544-0 · Cited by 962
Re-epithelialization of adult skin wounds: Cellular mechanisms and therapeutic strategies
Rousselle, P., Braye, F., & Dayan, G. (2018) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.06.019 · Cited by 679
Ellis, S., Lin, E. J., & Tartar, D. (2018) · Current Dermatology Reports · doi:10.1007/s13671-018-0234-9 · Cited by 625
Experimental models and methods for cutaneous wound healing assessment
Masson‐Meyers, D. S., de Andrade, T. A. M., Caetano, G. F., Guimarães, F. R., Leite, M. N., Leite, S. N., & Frade, M. A. C. (2020) · International Journal of Experimental Pathology · doi:10.1111/iep.12346 · Cited by 560
Metadata
- Authors
- Iorio, V., Troughton, L. D., & Hamill, K. J.
- Affiliations
- University of Liverpool (GB)
- Corresponding author
- Hamill, Kevin J.
- Venue
- Advances in Wound Care
- Publisher
- SAGE Publications
- Published
- 2015-04
- Volume
- 4
- Issue
- 4
- Pages
- 250-263
- ISSN
- 2162-1918 (ISSN-L)
- 2162-1934
- PMC
- PMC4397997
- OpenAlex
- W2315246287
- Cited by
- 169
- References
- 120
- Citations by year
- 2026: 14 · 2025: 11 · 2024: 23 · 2023: 23 · 2022: 13 · 2021: 17 · 2020: 23 · 2019: 8 · 2018: 16 · 2017: 12 · 2016: 6 · 2015: 3
- FWCI
- 0.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Advances in Wound Care (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- British Skin Foundation
- University of Liverpool
- Biotechnology and Biological Sciences Research Council (BB/L020513/1)
- Topics
- Health Sciences › Medicine › Surgery › Wound Healing and Treatments
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Health Sciences › Medicine › Surgery › Tissue Engineering and Regenerative Medicine
- Keywords
- laminin, wound healing, re-epithelialization, angiogenesis, chronic wounds, focal adhesions, hemidesmosomes, netrin, cell migration, cell adhesion, tissue regeneration, ex vivo cell expansion
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
