Stimulation of collagen synthesis in fibroblast cultures by the tripeptide‐copper complex glycyl‐L‐histidyl‐L‐lysine‐Cu2+
Abstract
Glycyl‐L‐histidyl‐L‐lysine (GHK) is a tripeptide with affinity for copper(II) ions and was isolated from human plasma. This peptide appears to play a physiological role in wound healing. We report the stimulating effect of GHK‐Cu on collagen synthesis by fibroblasts. The stimulation began between 10−12 and 10−11 M, maximized at 10−9 M, and was independent of any change in cell number. The presence of a GHK triplet in the α 2(I) chain of type I collagen suggests that the tripeptide might be liberated by proteases at the site of a wound and exert in situ healing effects.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Both GHK and GHK-Cu, at a very low, non-toxic concentration (0.01-1 nM), stimulated collagen synthesis in cultured fibroblasts while non-collagen proteins were not affected.
“Subsequent studies directed by Borel and Maquart et al. demonstrated that both GHK and GHK-Cu, at a very low, non-toxic concentration (0.01-1 nM), stimulated collagen synthesis in cultured fibroblasts while non-collagen proteins were not affected [23].”
From GHK-Cu may Prevent Oxidative Stress in Skin by Regulating Copper and Modifying Expression of Numerous Antioxidant Genes (2015) · cites this paper as [23]
GHK is probably released locally during collagen or SPARC proteolysis caused by skin damage.
“GHK is probably released locally during collagen or SPARC (Secreted Protein Acidic and Rich in Cysteine) proteolysis caused by skin damage [37,38].”
From Ternary Cu(II) Complex with GHK Peptide and Cis-Urocanic Acid as a Potential Physiologically Functional Copper Chelate (2020) · cites this paper as [38]
The GHK amino acid sequence is present in the alpha 2(I) chain of type I collagen, and when damage activates proteolytic enzymes, GHK is released into the site of injury.
“The GHK amino acid sequence is present in the alpha 2(I) chain of type I collagen, and when damage activates proteolytic enzymes, GHK is released into the site of an injury [7].”
From Regenerative and Protective Actions of the GHK-Cu Peptide in the Light of the New Gene Data (2018) · cites this paper as [7]
The GHK sequence is included in the collagen molecule and SPARC protein, and GHK is naturally released after an injury due to protein breakdown.
“GHK sequence is included in the collagen molecule, and SPARC protein and GHK is naturally released after an injury due to protein breakdown.”
From Regenerative and Protective Actions of the GHK-Cu Peptide in the Light of the New Gene Data (2018) · cites this paper as [7]
GHK at concentrations of 10^-12 and 10^-11 M, maximized at 10^-9 M, stimulates the synthesis of collagen in fibroblasts.
“In 1988, Maquart et al. from Université de Reims Champagne-Ardenne (France) found that GHK at concentrations of 10 -12 and 10 -11 M, maximized at 10 -9 M was able to stimulate the synthesis of collagen in fibroblasts.”
From Modulation of Gene Expression in Human Breast Cancer MCF7 and Prostate Cancer PC3 Cells by the Human Copper-Binding Peptide GHK-Cu (2021) · cites this paper as [5]
Cites
Freshney, R. I. (2005) · Wiley eBooks · doi:10.1002/9780470649367 · Cited by 3,869 · see citing works
Lehrach, H. R., Diamond, D. J., Wozney, J. M., & Boedtker, H. (1977) · Biochemistry · doi:10.1021/bi00640a033 · Cited by 3,415 · see citing works
Peterkofsky, B., & Diegelmann, R. F. (1971) · Biochemistry · doi:10.1021/bi00782a009 · Cited by 1,389 · see citing works
Messenger RNA for myosin polypeptides: Isolation from single myogenic cell cultures
Strohman, R. C., Moss, P. S., Micou-Eastwood, J., Spector, D. H., Przybyla, A., & Paterson, B. M. (1977) · Cell · doi:10.1016/0092-8674(77)90220-3 · Cited by 404 · see citing works
Culture of Animal Cells. A manual for basic techniques
Stampfer, M. R., & Taylor‐Papadimitriou, J. (2000) · Cited by 328 · see citing works
Fiszer‐Szafarz, B., Szafarz, D., & de Murillo, A. G. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90130-5 · Cited by 245 · see citing works
Fibroblasts degrade newly synthesised collagen within the cell before secretion
Bienkowski, R. S., Baum, B. J., & Crystal, R. G. (1978) · Nature · doi:10.1038/276413a0 · Cited by 204 · see citing works
Growth-modulating plasma tripeptide may function by facilitating copper uptake into cells
Pickart, L., Freedman, J. H., Loker, W. J., Peisach, J., Perkins, C. M., Stenkamp, R. E., & Weinstein, B. (1980) · Nature · doi:10.1038/288715a0 · Cited by 175 · see citing works
Self-citationOrganization of the human pro-alpha 2(I) collagen gene.
de Wet, W., Bernard, M. P., Benson-Chanda, V., Chu, M., Dickson, L. A., Weil, D., & Ramirez, F. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47691-0 · Cited by 156 · see citing works
Sorenson, J. R. J. (1987) · Humana Press eBooks · doi:10.1007/978-1-4612-4584-1 · Cited by 126 · see citing works
[28] Biological activity of human plasma copper-binding growth factor glycyl-l-histidyl-l-lysine
Pickart, L., & Lovejoy, S. (1987) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(87)47121-8 · Cited by 57 · see citing works
Self-citationBellon, G., Randoux, A., & Jp, B. (1985) · Collagen and Related Research · doi:10.1016/s0174-173x(85)80030-3 · Cited by 18 · see citing works
GARROD, L. P., & Wilson, G. S. (1978) · Nature · doi:10.1038/273413a0 · Cited by 2 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Bioinorganics and biomaterials: Bone repair
Habibovic, P., & Barralet, J. E. (2011) · Acta Biomaterialia · doi:10.1016/j.actbio.2011.03.027 · Cited by 441 · see citing works
Li, Y. (2000) · Cardiovascular Research · doi:10.1016/s0008-6363(00)00003-1 · Cited by 434 · see citing works
Li, Y. Y., Feng, Y., Kadokami, T., McTiernan, C. F., Draviam, R. A., Watkins, S. C., & Feldman, A. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.23.12746 · Cited by 324 · see citing works
Copper complexes as therapeutic agents
Duncan, C., & White, A. R. (2011) · Metallomics · doi:10.1039/c2mt00174h · Cited by 293 · see citing works
Lipopeptides: from self-assembly to bioactivity
Hamley, I. W. (2015) · Chemical Communications · doi:10.1039/c5cc01535a · Cited by 291 · see citing works
Circulating Biomarkers of Collagen Metabolism in Cardiac Diseases
López, B., González, A., & Dı́ez, J. (2010) · Circulation · doi:10.1161/circulationaha.109.912774 · Cited by 252 · see citing works
An introduction to matrikines: extracellular matrix-derived peptides which regulate cell activity
Maquart, F., Brassart‐Pasco, S., Ramont, L., Hornebeck, W., & Monboisse, J. (2004) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2003.06.007 · Cited by 232 · see citing works
Self-citationThe neglected role of copper ions in wound healing
Kornblatt, A. P., Nicoletti, V. G., & Travaglia, A. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.02.012 · Cited by 221 · see citing works
The Use of Copper as an Antimicrobial Agent in Health Care, Including Obstetrics and Gynecology
Arendsen, L. P., Thakar, R., & Sultan, A. H. (2019) · Clinical Microbiology Reviews · doi:10.1128/cmr.00125-18 · Cited by 225 · see citing works
Matricryptins and matrikines: biologically active fragments of the extracellular matrix
Ricard‐Blum, S., & Salza, R. (2014) · Experimental Dermatology · doi:10.1111/exd.12435 · Cited by 224 · see citing works
The human tri-peptide GHK and tissue remodeling
Pickart, L. (2008) · Journal of Biomaterials Science, Polymer Edition · doi:10.1163/156856208784909435 · Cited by 218 · see citing works
Self-citationRole of topical peptides in preventing or treating aged skin
Gorouhi, F., & Maibach, H. I. (2009) · International Journal of Cosmetic Science · doi:10.1111/j.1468-2494.2009.00490.x · Cited by 193 · see citing works
Lupo, M. P., & Cole, A. (2007) · Dermatologic Therapy · doi:10.1111/j.1529-8019.2007.00148.x · Cited by 165 · see citing works
Bioinorganics and Wound Healing
Dalisson, B., & Barralet, J. E. (2019) · Advanced Healthcare Materials · doi:10.1002/adhm.201900764 · Cited by 165 · see citing works
Guiding principles for peptide nanotechnology through directed discovery
Lampel, A., Ulijn, R. V., & Tuttle, T. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00177d · Cited by 162 · see citing works
Regenerative and Protective Actions of the GHK-Cu Peptide in the Light of the New Gene Data
Pickart, L., & Margolina, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19071987 · Cited by 158 · see citing works
Self-citationMaquart, F., Bellon, G., Gillery, P., Wegrowski, Y., & Jp, B. (1990) · Connective Tissue Research · doi:10.3109/03008209009152427 · Cited by 151 · see citing works
Self-citationGHK Peptide as a Natural Modulator of Multiple Cellular Pathways in Skin Regeneration
Pickart, L., Vasquez-Soltero, J. M., & Margolina, A. (2015) · BioMed Research International · doi:10.1155/2015/648108 · Cited by 144 · see citing works
Self-citationMatrikines in the regulation of extracellular matrix degradation
Maquart, F., Bellon, G., Brassart‐Pasco, S., & Monboisse, J. C. (2004) · Biochimie · doi:10.1016/j.biochi.2004.10.006 · Cited by 140 · see citing works
Self-citationExtracellular matrix and wound healing
Maquart, F., & Monboisse, J. C. (2014) · Pathologie Biologie · doi:10.1016/j.patbio.2014.02.007 · Cited by 138 · see citing works
Self-citationFunk, S. E., & Sage, E. H. (1993) · Journal of Cellular Physiology · doi:10.1002/jcp.1041540108 · Cited by 138 · see citing works
Natural Tripeptide-Based Inhibitor of Multifaceted Amyloid β Toxicity
Rajasekhar, K., Madhu, C., & Govindaraju, T. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00175 · Cited by 136 · see citing works
Zhang, L., & Falla, T. J. (2009) · Clinics in Dermatology · doi:10.1016/j.clindermatol.2009.05.013 · Cited by 134 · see citing works
Bonoiu, A. C., Mahajan, S. D., Ye, L., Kumar, R., Ding, H. Y., Yong, K., Roy, I., Aalinkeel, R., Nair, B. B., Reynolds, J. L., et al. (2009) · Brain Research · doi:10.1016/j.brainres.2009.05.047 · Cited by 126 · see citing works
Matrikines as mediators of tissue remodelling
Jariwala, N., Ozols, M., Bell, M., Bradley, E., Gilmore, A. P., Debelle, L., & Sherratt, M. J. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114240 · Cited by 123 · see citing works
Maquart, F. X., Bellon, G., Chaqour, B., Wegrowski, J., Patt, L. M., Trachy, R. E., Monboisse, J. C., Chastang, F., Birembaut, P., & Gillery, P. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116842 · Cited by 110 · see citing works
Self-citationPickart, L., Vasquez-Soltero, J. M., & Margolina, A. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/324832 · Cited by 108 · see citing works
Self-citationBiologically active peptides: from a laboratory bench curiosity to a functional skin care product
Lintner, & Peschard, O. (2000) · International Journal of Cosmetic Science · doi:10.1046/j.1467-2494.2000.00010.x · Cited by 107 · see citing works
Engleka, K. A., & Maciag, T. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49911-0 · Cited by 104 · see citing works
Myocardial proteases and matrix remodeling in inflammatory heart disease
Rutschow, S., LI, J., Schultheiss, H., & Pauschinger, M. (2006) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.12.009 · Cited by 99 · see citing works
Skin ageing and topical rejuvenation strategies
Griffiths, T. W., Watson, R. E. B., & Langton, A. K. (2023) · British Journal of Dermatology · doi:10.1093/bjd/ljad282 · Cited by 108 · see citing works
Cosmeceuticals: peptides, proteins, and growth factors
el Hadmed, H. H., & Castillo, R. F. (2016) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.12229 · Cited by 96 · see citing works
Philips, N., Hwang, H., Chauhan, S., Leonardi, D., & Gonzalez, S. (2010) · Connective Tissue Research · doi:10.3109/03008200903288431 · Cited by 95 · see citing works
Cooperative, ion-sensitive co-assembly of tripeptide hydrogels
Abul‐Haija, Y. M., Scott, G. G., Sahoo, J. K., Tuttle, T., & Ulijn, R. V. (2017) · Chemical Communications · doi:10.1039/c7cc04796g · Cited by 87 · see citing works
Arul, V., Kartha, R., & Jayakumar, R. (2007) · Life Sciences · doi:10.1016/j.lfs.2006.09.018 · Cited by 85 · see citing works
Peptides: Emerging Candidates for the Prevention and Treatment of Skin Senescence: A Review
Pintea, A., Manea, A., Pintea, C., Vlad, R.-A., Bîrsan, M., Antonoaea, P., RÉDAI, E. M., & Ciurba, A. (2025) · Biomolecules · doi:10.3390/biom15010088 · Cited by 89 · see citing works
Bishop, J. B., Phillips, L. G., Mustoe, T. A., VanderZee, A. J., Wiersema, L., Roach, D. E., Heggers, J. P., Hill, D. P., Taylor, E. L., & Robson, M. C. (1992) · Journal of Vascular Surgery · doi:10.1016/0741-5214(92)90115-o · Cited by 74 · see citing works
Jose, S., Hughbanks, M. L., Binder, B. Y. K., Ingavle, G. C., & Leach, J. K. (2014) · Acta Biomaterialia · doi:10.1016/j.actbio.2014.01.020 · Cited by 73 · see citing works
Chen, C., Huang, S. K. S., Lin, J.-L., Lai, L., Lai, S.-C., Liu, C.-W., Chen, W., Wen, C.-H., & Lin, C.-S. (2008) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2008.07.007 · Cited by 73 · see citing works
Wegrowski, Y., Maquart, F. X., & Borel, J. P. (1992) · Life Sciences · doi:10.1016/0024-3205(92)90504-i · Cited by 72 · see citing works
Self-citationSiméon, A., Monier, F., Emonard, H., Gillery, P., Hornebeck, W., Maquart, F.-X., & Birembaut, P. (1999) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.1999.00606.x · Cited by 68 · see citing works
Self-citationThe effect of topical tripeptide-copper complex on healing of ischemic open wounds
Canapp, S. O., Farese, J. P., Schultz, G. S., Gowda, S., Ishak, A. M., Swaim, S. F., Vangilder, J., Lee‐Ambrose, L., & Martin, F. G. (2003) · Veterinary Surgery · doi:10.1111/j.1532-950x.2003.00515.x · Cited by 68 · see citing works
Harrison, C. A., Gossiel, F., Bullock, A. J., Sun, T., Blumsohn, A., & Neil, S. M. (2005) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2005.07022.x · Cited by 67 · see citing works
Lupo, M. P. (2005) · Dermatologic Surgery · doi:10.1111/j.1524-4725.2005.31728 · Cited by 66 · see citing works
Anti-aging products and cosmeceuticals
Glaser, D. A. (2004) · Facial Plastic Surgery Clinics of North America · doi:10.1016/j.fsc.2004.03.004 · Cited by 65 · see citing works
Pollard, J. D., Quan, S., Kang, T., & Koch, R. J. (2005) · Archives of Facial Plastic Surgery · doi:10.1001/archfaci.7.1.27 · Cited by 58 · see citing works
Draelos, Z. D. (2019) · Dermatologic Clinics · doi:10.1016/j.det.2018.07.001 · Cited by 58 · see citing works
Bioactive oligopeptides in dermatology: Part I
Reddy, B. Y., Jow, T., & Hantash, B. M. (2012) · Experimental Dermatology · doi:10.1111/j.1600-0625.2012.01528.x · Cited by 56 · see citing works
Biomarkers of the extracellular matrix and of collagen fragments
Chalikias, G. K., & Tziakas, D. N. (2014) · Clinica Chimica Acta · doi:10.1016/j.cca.2014.06.028 · Cited by 56 · see citing works
Microneedle-Mediated Delivery of Copper Peptide Through Skin
Li, H., Low, Y. S. J., Chong, H. P., Zin, M. T., Lee, C., Li, B., Leolukman, M., & Kang, L. (2015) · Pharmaceutical Research · doi:10.1007/s11095-015-1652-z · Cited by 55 · see citing works
Conato, C., Gavioli, R., Guerrini, R., Kozłowski, H., Młynarz, P., Pasti, C., Pulidori, F., & Remelli, M. (2001) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(01)00127-1 · Cited by 55 · see citing works
Pauschinger, M., Chandrasekharan, K., & Schultheiß, H. (2004) · Heart Failure Reviews · doi:10.1023/b:hrev.0000011391.81676.3c · Cited by 54 · see citing works
Copper–GHK increases integrin expression and p63 positivity by keratinocytes
Kang, Y.-A., Choi, H.-R., Na, J.-I., Huh, C.-H., Kim, M.-J., Youn, S.-W., Kim, K.-H., & Park, K.-C. (2009) · Archives of Dermatological Research · doi:10.1007/s00403-009-0942-x · Cited by 51 · see citing works
Effective Active Ingredients Obtained through Biotechnology
Zappelli, C., Barbulova, A., Apone, F., & Colucci, G. (2016) · Cosmetics · doi:10.3390/cosmetics3040039 · Cited by 50 · see citing works
Yamamoto, K., Mano, T., Yoshida, J., Sakata, Y., Nishikawa, N., Nishio, M., Ohtani, T., Hori, M., Miwa, T., & Masuyama, T. (2005) · Journal of Hypertension · doi:10.1097/00004872-200502000-00022 · Cited by 50 · see citing works
Pickart, L., Vasquez-Soltero, J., & Margolina, A. (2015) · Cosmetics · doi:10.3390/cosmetics2030236 · Cited by 48 · see citing works
Self-citationSynytsya, A., Poučková, P., Zadinová, M., Troshchynska, Y., Štětina, J., Synytsya, A., Saloň, I., & Král, V. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.09.251 · Cited by 48 · see citing works
Skin Peptides: Biological Activity and Therapeutic Opportunities
Namjoshi, S., Caccetta, R., & Benson, H. A. (2007) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.21198 · Cited by 49 · see citing works
Rat Epigastric Flap Survival and VEGF Expression after Local Copper Application
Frangoulis, M., Georgiou, P., Chrisostomidis, C., Perrea, D. N., Dontas, I. A., Kavantzas, N., Kostakis, A. G., & Papadopoulos, O. N. (2007) · Plastic & Reconstructive Surgery · doi:10.1097/01.prs.0000252000.59231.5e · Cited by 48 · see citing works
Rodziewicz‐Motowidło, S., Dzierżyńska, M., Justyna, S., Deptuła, M., Sosnowski, P., Sass, P., Peplińska, B., Pietralik-Molińska, Z., Fularczyk, M., Kasprzykowski, F., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-33464-w · Cited by 47 · see citing works
Role of matrix metalloproteinases in hypertension-associated cardiac fibrosis
pez, B. A. L., lez, A. G., & ez, J. D. (2004) · Current Opinion in Nephrology & Hypertension · doi:10.1097/00041552-200403000-00008 · Cited by 46 · see citing works
Self-Assembly of Palmitoyl Lipopeptides Used in Skin Care Products
Castelletto, V., Hamley, I. W., Whitehouse, C., Matts, P. J., Osborne, R., & Baker, E. S. (2013) · Langmuir · doi:10.1021/la401771j · Cited by 45 · see citing works
Das, R., Gayakvad, B., Shinde, S. D., Rani, J., Jain, A. K., & Sahu, B. (2020) · ACS Applied Bio Materials · doi:10.1021/acsabm.0c00544 · Cited by 45 · see citing works
Philips, N., Samuel, P., Parakandi, H., Gopal, S., Siomyk, H., Ministro, A., Thompson, T., & Borkow, G. (2012) · Connective Tissue Research · doi:10.3109/03008207.2012.665970 · Cited by 44 · see citing works
Spiers, P., Kelso, E. J., Siah, W. F., Edge, G., Song, G., McDermott, B. J., & Hennessy, M. (2005) · Journal of Hypertension · doi:10.1097/01.hjh.0000176787.04753.ee · Cited by 44 · see citing works
Faghani, G., & Azarniya, A. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e39611 · Cited by 45 · see citing works
Lysyl oxidase copper-talon complex: a model
Krebs, C. J., & Krawetz, S. A. (1993) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(93)90056-w · Cited by 43 · see citing works
The effects of topical tripeptide copper complex and helium-neon laser on wound healing in rabbits
Gul, N. Y., Topal, A., Cangul, I. T., & Yanik, K. (2008) · Veterinary Dermatology · doi:10.1111/j.1365-3164.2007.00647.x · Cited by 41 · see citing works
Matrix Metalloproteinases in the Progression of Heart Failure
Li, Y. Y., & Feldman, A. M. (2001) · Drugs · doi:10.2165/00003495-200161090-00002 · Cited by 41 · see citing works
Myocardial extracellular matrix remodeling in ischemic heart failure
Gabrielle, L. G. (2006) · Frontiers in bioscience · doi:10.2741/2157 · Cited by 38 · see citing works
Adjunctive Skin Care of the Brow and Periorbital Region
Bucay, V., & Day, D. (2012) · Clinics in Plastic Surgery · doi:10.1016/j.cps.2012.09.003 · Cited by 38 · see citing works
Molecular analysis of chicken embryo SPARC (osteonectin)
Bassuk, J. A., Iruela‐Arispe, M. L., Lane, T. F., BENSON, J. M., Berg, R. A., & Sage, E. H. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18358.x · Cited by 36 · see citing works
Stem cell recovering effect of copper‐free GHK in skin
Choi, H., Kang, Y., Ryoo, S., Shin, J., Na, J., Huh, C., & Park, K. (2012) · Journal of Peptide Science · doi:10.1002/psc.2455 · Cited by 35 · see citing works
Cui, N., Jiajia, J., Li, M., Qi, H., Wu, X., & Tingli, L. (2019) · Materials Science and Engineering C · doi:10.1016/j.msec.2019.109746 · Cited by 35 · see citing works
Over-the-counter anti-ageing topical agents and their ability to protect and repair photoaged skin
Bradley, E. J., Griffiths, C. E. M., Sherratt, M. J., Bell, M., & Watson, R. E. B. (2015) · Maturitas · doi:10.1016/j.maturitas.2014.12.019 · Cited by 35 · see citing works
Ufnalska, I., Drew, S. C., Zhukov, I., Szutkowski, K., Wawrzyniak, U. E., Wróblewski, W., Frączyk, T., & Bal, W. (2021) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.1c02669 · Cited by 35 · see citing works
Deng, M., Zhang, Q., Yan, L., Bian, Y., Li, R., Gao, J., Wang, Y., Miao, J., Li, J., Zhou, X., et al. (2023) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13213 · Cited by 33 · see citing works
Effects of Glycyl-Histidyl-Lysyl Chelated Cu(II) on Ferritin Dependent Lipid Peroxidation
Miller, D. M., DeSilva, D., Pickart, L., & Aust, S. D. (1990) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4684-5730-8_11 · Cited by 33 · see citing works
Self-citationTopical Over-the-Counter Antiaging Agents: An Update and Systematic Review
Imhof, L., & Leuthard, D. (2020) · Dermatology · doi:10.1159/000509296 · Cited by 32 · see citing works
Mitochondrial mitophagic mechanisms of myocardial matrix metabolism and remodelling
Vacek, T. P., Vacek, J. C., & Tyagi, S. C. (2011) · Archives of Physiology and Biochemistry · doi:10.3109/13813455.2011.635660 · Cited by 32 · see citing works
Badenhorst, T., Svirskis, D., & Merrilees, M. (2016) · Journal of Aging Science · doi:10.4172/2329-8847.1000166 · Cited by 31 · see citing works
Beretta, G., Artali, R., Regazzoni, L., Panigati, M., & Facino, R. M. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700185s · Cited by 30 · see citing works
Arumugam, P., Gopi, V., Subramanian, U., Anoop, S., Sheik, M. J. Y., Divya, H., & Vellaichamy, E. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1612-z · Cited by 30 · see citing works
Picard, F., Brehm, M. U., Fassbach, M., Pelzer, B., Scheuring, S., Küry, P., Strauer, B. E., & Schwartzkopff, B. (2006) · Clinical Research in Cardiology · doi:10.1007/s00392-006-0373-z · Cited by 29 · see citing works
Arumugam, P., Gopi, V., Shyamala Devi, K. M., Balaji, N., & Vellaichamy, E. (2014) · Life Sciences · doi:10.1016/j.lfs.2014.09.030 · Cited by 28 · see citing works
Bilodeau, D., Dupont, É., Journet, M., Oula, M.-L., Gómez, J. G., Léveillé, C., & Loing, E. (2014) · Clinical Cosmetic and Investigational Dermatology · doi:10.2147/ccid.s53580 · Cited by 28 · see citing works
Synthesis of lipoic acid–peptide conjugates and their effect on collagen and melanogenesis
Lu, C., Kim, B. M., Lee, D., Lee, M. H., Kim, J. H., Pyo, H.-B., & Chai, K. Y. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.09.011 · Cited by 27 · see citing works
Development of a LC–MS/MS method to monitor palmitoyl peptides content in anti-wrinkle cosmetics
Chirita, R.-I., Chaimbault, P., Archambault, J.-C., Robert, I., & Elfakir, C. (2009) · Analytica Chimica Acta · doi:10.1016/j.aca.2009.03.015 · Cited by 27 · see citing works
Bossak-Ahmad, K., Wiśniewska, M. D., Bal, W., Drew, S. C., & Frączyk, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176190 · Cited by 25 · see citing works
McCormack, M. C., Nowak, K. C., & Koch, R. J. (2001) · Archives of Facial Plastic Surgery · doi:10.1001/archfacial.qoa90013.28 · Cited by 26 · see citing works
Morganroth, P. A., Wilmot, A. C., & Miller, C. J. (2009) · Journal of the American Academy of Dermatology · doi:10.1016/j.jaad.2009.02.046 · Cited by 25 · see citing works
Development of an in vitro model of menopause using primary human dermal fibroblasts
Remoué, N., Molinari, J., Andres, E., Lago, J. C., Barrichello, C., & Moreira, P. L. (2013) · International Journal of Cosmetic Science · doi:10.1111/ics.12075 · Cited by 24 · see citing works
Hsiao, C., Wu, H.-H., Malhotra, N., Liu, Y.-C., Wu, Y.-H., Lin, Y.-N., Saputra, F., Santoso, F., & Chen, K. H. ‐. (2020) · Biomolecules · doi:10.3390/biom10091202 · Cited by 23 · see citing works
MAZUROWSKA, L., & MOJSKI, M. (2007) · Talanta · doi:10.1016/j.talanta.2006.11.034 · Cited by 23 · see citing works
Rinaldi, F., Marzani, B., Pinto, D., & Sorbellini, E. (2018) · Journal of Dermatological Treatment · doi:10.1080/09546634.2018.1544405 · Cited by 21 · see citing works
Fibroblast — Cytokine — Extracellular Matrix Interactions in Wound Repair
Siméon, A., Monier, F., Emonard, H., Wegrowski, Y., Bellon, G., Monboisse, J. C., Gillery, P., Hornebeck, W., & Maquart, F. (1999) · Current topics in pathology · doi:10.1007/978-3-642-58456-5_10 · Cited by 21 · see citing works
Self-citationLee, A.-R. C. (2019) · Journal of Pharmaceutical Investigation · doi:10.1007/s40005-019-00438-y · Cited by 19 · see citing works
Chapter 31. To Market, To Market - 1996
Galatsis, P. (1997) · Annual reports in medicinal chemistry · doi:10.1016/s0065-7743(08)61489-x · Cited by 17 · see citing works
Rahaman, M. S., Arin, A., Farwa, U., Park, M., Bae, S. H., & Lee, B.-T. (2024) · Biomaterials · doi:10.1016/j.biomaterials.2024.122698 · Cited by 16 · see citing works
Extracellular vesicles and bioactive peptides for regenerative medicine in cosmetology
Yuan, Y., Cao, K., Gao, P., Wang, Y., An, W., & Dong, Y. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102712 · Cited by 17 · see citing works
- Authors
- Maquart, F.-X., Pickart, L., Laurent, M., Gillery, P., Monboisse, J.-C., & Borel, J.-P.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Maquart, François-Xavier
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1988-10-10
- Volume
- 238
- Issue
- 2
- Pages
- 343-346
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2033753997
- Cited by
- 181
- References
- 13
- Citations by year
- 2026: 10 · 2025: 8 · 2024: 9 · 2023: 7 · 2022: 4 · 2021: 5 · 2020: 6 · 2019: 7 · 2018: 5 · 2017: 1 · 2016: 12 · 2015: 12 · 2014: 9 · 2013: 4 · 2012: 7
- FWCI
- 1.58
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Rehabilitation › Wound Healing and Treatments
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Health Sciences › Medicine › Hepatology › Liver physiology and pathology
- Keywords
- copper(II) complexes, collagen synthesis, fibroblasts, wound healing, tripeptides, protease cleavage, plasma peptides
- MeSH terms
- Cells, Cultured, Chromatography, Thin Layer, Collagen, Fibroblasts, Growth Substances, Humans, Oligopeptides, Procollagen, Proline, Wound Healing
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
