The DOI matches its Crossref record; 54 of the 55 references it cites were found in a registry or an index.
Heparan sulfate proteoglycan as a cell-surface endocytosis receptor
Open accessAbstract
How various macromolecules are exchanged between cells and how they gain entry into recipient cells are fundamental questions in cell biology with important implications e.g. non-viral drug delivery, infectious disease, metabolic disorders, and cancer. The role of heparan sulfate proteoglycan (HSPG) as a cell-surface receptor of diverse macromolecular cargo has recently been manifested. Exosomes, cell penetrating peptides, polycation–nucleic acid complexes, viruses, lipoproteins, growth factors and morphogens among other ligands enter cells through HSPG-mediated endocytosis. Key questions that partially have been unraveled over recent years include the respective roles of HSPG core protein and HS chain structure specificity for macromolecular cargo endocytosis, the down-stream intracellular signaling events involved in HSPG-dependent membrane invagination and vesicle formation, and the biological significance of the HSPG transport pathway. Here, we discuss the intriguing role of HSPGs as a major entry pathway of macromolecules in mammalian cells with emphasis on recent in vitro and in vivo data that provide compelling evidence of HSPG as an autonomous endocytosis receptor. • Heparan sulfate proteoglycan (HSPG) is a receptor of diverse macromolecular cargo. • HSPG endocytosis is involved in infectious disease, lipid metabolism and cancer. • HSPG represents an interesting target for macromolecular drug delivery. • Recent findings on the intriguing role of HSPG-mediated transport are discussed.
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
“However, HSPGs are known to act both independently and in concert with co-receptors to mediate endocytosis26.”
From LRP1 is a master regulator of tau uptake and spread (2020) · cites this paper as [26]
In the citing paper
“Meanwhile, the extracellular tau can be taken up by neighboring cells, both neurons and glial cells, through various pathways, including phagocytosis [68], macropinocytosis [69], receptor-mediated uptake [67, 70], endocytosis [71], and/or membrane fusion of exosomes [72, 73].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [71]
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
Heparan Sulfate ProteoglycansPreprint
Sarrazin, S., Lamanna, W. C., & Esko, J. D. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004952 · Cited by 1,605
Christianson, H. C., Svensson, K. J., van Kuppevelt, T. H., Li, J.-P., & Belting, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1304266110 · Cited by 903
Self-citationEvidence for the role of proteoglycans in cation-mediated gene transfer.
Mislick, K. A., & Baldeschwieler, J. D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12349 · Cited by 774
Effects of Charge on Antibody Tissue Distribution and Pharmacokinetics
Boswell, C. A., Tesar, D. B., Mukhyala, K., Theil, F.-P., Fielder, P. J., & Khawli, L. A. (2010) · Bioconjugate Chemistry · doi:10.1021/bc100261d · Cited by 398
Capurro, M., Xu, P., Shi, W., Li, F., Jia, A. Y., & Filmus, J. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.03.006 · Cited by 365
Heparan sulfate proteoglycan as a plasma membrane carrier
Belting, M. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00031-8 · Cited by 273
Self-citationInternalization and Trafficking of Cell Surface Proteoglycans and Proteoglycan‐Binding Ligands
Payne, C. K., Jones, S. A., Chen, C., & Zhuang, X. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00540.x · Cited by 270
Histones and Basic Polyamino Acids Stimulate the Uptake of Albumin by Tumor Cells in Culture
Ryser, H. J. ‐., & Hancock, R. (1965) · Science · doi:10.1126/science.150.3695.501 · 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
Stanford, K. I., Bishop, J. R., Foley, E. M., Gonzales, J. C., Niesman, I. R., Witztum, J. L., & Esko, J. D. (2009) · Journal of Clinical Investigation · doi:10.1172/jci38251 · Cited by 226
Cited by
Sorted by citations
Items 201–300 of 423
Theodoraki, A., Hu, Y., Poopalasundaram, S., Oosterhof, A., Guimond, S. E., Disterer, P., Khoo, B. C. E., Hauge-Evans, A. C., Jones, P. M., Turnbull, J. E., et al. (2014) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2014.09.011 · Cited by 21
Heparinoid Complex-Based Heparin-Binding Cytokines and Cell Delivery Carriers
Ishihara, M., Nakamura, S., Sato, Y., Takayama, T., Fukuda, K., Fujita, M., Murakami, K., & Yokoe, H. (2019) · Molecules · doi:10.3390/molecules24244630 · Cited by 21
Heparanase Involvement in Exosome Formation
David, G., & Zimmermann, P. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-34521-1_10 · Cited by 21
The Role of BAR Proteins and the Glycocalyx in Brain Endothelium Transcytosis
Leite, D. M., Matias, D., & Battaglia, G. (2020) · Cells · doi:10.3390/cells9122685 · Cited by 23
Aydın, Y., Köksal, A. R., Thevenot, P., Chava, S. P., Heidari, Z., Lin, D., Sandow, T. A., Moroz, K., Parsi, M. A., Scott, J., et al. (2021) · Journal of Hepatocellular Carcinoma · doi:10.2147/jhc.s327339 · Cited by 21
Ferguson, R., & Subramanian, V. (2018) · PLoS ONE · doi:10.1371/journal.pone.0193302 · Cited by 21
Syndecans and Pancreatic Ductal Adenocarcinoma
Betriu, N., Bertran-Mas, J., Andreeva, A. Y., & Semino, C. E. (2021) · Biomolecules · doi:10.3390/biom11030349 · Cited by 21
The Cytotoxic Necrotizing Factors (CNFs)—A Family of Rho GTPase-Activating Bacterial Exotoxins
Chaoprasid, P., & Dersch, P. (2021) · Toxins · doi:10.3390/toxins13120901 · Cited by 20
Potential roles of heparanase in cancer therapy: Current trends and future direction
Yang, Y., Yuan, F., Zhou, H., Quan, J., Liu, C., Wang, Y., Xiao, F., Liu, Q., Liu, J., Zhang, Y., et al. (2023) · Journal of Cellular Physiology · doi:10.1002/jcp.30995 · Cited by 20
SCHWARTZ, J. L., Capistrano, K. J., Gluck, J., Hezarkhani, A., & Naqvi, A. R. (2024) · Reviews in Medical Virology · doi:10.1002/rmv.2543 · Cited by 20
Tanhaeian, A., Jaafari, M. R., Ahmadi, F. S., Vakili‐Ghartavol, R., & Sekhavati, M. H. (2018) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-018-9496-6 · Cited by 20
Methods for Monitoring Matrix-Induced Autophagy
Chen, C. G., Kapoor, A., & Iozzo, R. V. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9133-4_14 · Cited by 20
Yogalingam, G., Luu, A. R., Prill, H., Lo, M. J., Yip, B. K., Holtzinger, J., Christianson, T., Aoyagi-Scharber, M., Lawrence, R., Crawford, B. E., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0207836 · Cited by 20
Syndecan-4: major player or innocent bystander of the endothelial glycocalyx?
McCarthy, K. J. (2020) · Kidney International · doi:10.1016/j.kint.2020.01.040 · Cited by 19
PDZ scaffolds regulate extracellular vesicle production, composition, and uptake
Castro-Cruz, M., Hyka, L., Daaboul, G. G., Leblanc, R., Meeussen, S., Lembo, F., Oris, A., Herck, L. V., Granjeaud, S., David, G., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2310914120 · Cited by 19
Martín-Antonio, B., Suñé, G., Najjar, A., Pérez-Amill, L., Antoñana-Vildosola, A., Castellà, M., de León, S. J. P., Andrés, M. V., Lozano, F., Lozano, E., et al. (2019) · Journal for ImmunoTherapy of Cancer · doi:10.1186/s40425-019-0739-1 · Cited by 19
The Different Cellular Entry Routes for Drug Delivery Using Cell Penetrating Peptides
Okafor, M., Schmitt, D. A., Ory, S., Gasman, S., Hureau, C., Faller, P., & Vitale, N. (2025) · Biology of the Cell · doi:10.1111/boc.70012 · Cited by 22
Lysosome-targeting chimeras enable targeted protein degradation
Li, B., Li, Y., Zhang, J. J., Badama, S., Zhao, X., Wang, L., Zhang, T. W., Wang, X., Yi, X., Ding, G., et al. (2026) · Cell chemical biology · doi:10.1016/j.chembiol.2026.01.008 · Cited by 19
Su, L., Sun, Z., Qi, F., Su, H., Qian, L., Li, J., Zuo, L., Huang, J., Yu, Z., Li, J., et al. (2022) · Journal of Nanobiotechnology · doi:10.1186/s12951-022-01530-6 · Cited by 18
Beaussart, A., Brandhorst, T. T., Dufrêne, Y. F., & Klein, B. S. (2015) · mBio · doi:10.1128/mbio.01403-15 · Cited by 18
Kim, J., Park, J.-Y., Shin, S., Park, S.-W., Jun, S.-Y., Hong, J.-S., Choi, D.-K., & Kim, Y. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.07.008 · Cited by 18
Campeiro, J. D., Dam, W., Monte, G. G., Porta, L. C., de Oliveira, L. C. G., Nering, M. B., Viana, G. M., Carapeto, F. C. L., Oliveira, E. B., van den Born, J., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-39842-7 · Cited by 18
Brink, L., Chichlowski, M., Pastor, N., Athmaram, T. N., & Shah, N. (2021) · Nutrients · doi:10.3390/nu13030870 · Cited by 18
Smart micro/nanorobots for drug delivery in the brain
Shi, D., Wang, X., Deng, Y., Zhou, H., Wang, Y., Chu, P. K.-H., & Li, J. (2025) · Progress in Materials Science · doi:10.1016/j.pmatsci.2025.101533 · Cited by 17
Tumour acidosis remodels the glycocalyx to control lipid scavenging and ferroptosis
Bång-Rudenstam, A., Cerezo-Magaña, M., Horvath, M., Hugo Talbot, A., Gustafsson, E., Jonathan, S., Chakraborty, C., Nissen, I., de Oliveira, K. G., Boukredine, A., et al. (2026) · Nature Cell Biology · doi:10.1038/s41556-026-01879-y · Cited by 17
Self-citationGarcia, M., Hoffer, L., Leblanc, R., Benmansour, F., Feracci, M., Derviaux, C., Egea-Jiménez, A. L., Roche, P., Zimmermann, P., Morelli, X., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113601 · Cited by 17
Mockett, B. G., & Ryan, M. M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.05.014 · Cited by 18
Novel regulators of heparan sulfate proteoglycans modulate cellular uptake of α-synuclein fibrils
Vanderperre, B., Muraleedharan, A., Dorion, M., Larroquette, F., del Cid‐Pellitero, E., Rajakulendran, N., Chen, C. X. ‐., Larivière, R., Michaud-Tardif, C., Goiran, T., et al. (2025) · Communications Biology · doi:10.1038/s42003-025-08786-2 · Cited by 18
Astrada, S., Fernández, J. R., Vallespí, M. G., & Bollati‐Fogolín, M. (2018) · Molecules · doi:10.3390/molecules23040801 · Cited by 17
Sonpho, E., Mann, F. G., Levy, M. J., Ross, E. J., Guerrero‐Hernández, C., Florens, L. A., Saraf, A., Doddihal, V., Ounjai, P., & Alvarado, A. S. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100137 · Cited by 17
Extracellular vesicles in the retina - putative roles in physiology and disease
Kalargyrou, A. A., Guilfoyle, S. E., Smith, A. J., Ali, R. R., & Pearson, R. A. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1042469 · Cited by 19
Mozley, O. L., Thompson, B. C., Fernandez‐Martell, A., & James, D. C. (2014) · Biotechnology Progress · doi:10.1002/btpr.1932 · Cited by 17
Spotlight on HIV-derived TAT peptide as a molecular shuttle in drug delivery
Maani, Z., Rahbarnia, L., Bahadori, A., Chollou, K. M., & Farajnia, S. (2024) · Drug Discovery Today · doi:10.1016/j.drudis.2024.104191 · Cited by 16
Gonul, C. P., Karaçiçek, B., & Genç, Ş. (2025) · Developmental Neurobiology · doi:10.1002/dneu.22984 · Cited by 17
Pteropine orthoreoviruses use cell surface heparan sulphate as an attachment receptor
Tan, C. W., Gamage, A. M., Yap, W. C., Tang, L. J. W., Sun, Y. M., Yang, X., Pyke, A. T., Chua, K. B., & Wang, L. (2023) · Emerging Microbes & Infections · doi:10.1080/22221751.2023.2208683 · Cited by 16
Mandarini, E., Tollapi, E., Zanchi, M., Depau, L., Pini, A., Brunetti, J., Bracci, L., & Falciani, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218282 · Cited by 16
SARS-COV-2 spike binding to ACE2 in living cells monitored by TR-FRET
Cecon, E., Burridge, M., Cao, L., Carter, L. P., Ravichandran, R., Dam, J., & Jockers, R. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.06.008 · Cited by 17
Receptor control by membrane-tethered ubiquitin ligases in development and tissue homeostasis
Lebensohn, A. M., Bazán, J. F., & Rohatgi, R. (2022) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2022.03.003 · Cited by 17
Proteoglycans: a common portal for SARS-CoV-2 and extracellular vesicle uptake
Cerezo-Magaña, M., Bång-Rudenstam, A., & Belting, M. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00453.2022 · Cited by 16
Self-citationMaya, W. D. C., du Plessis, S. S., & Velilla, P. A. (2016) · Journal of Assisted Reproduction and Genetics · doi:10.1007/s10815-016-0747-8 · Cited by 16
PG545 sensitizes ovarian cancer cells to PARP inhibitors through modulation of RAD51-DEK interaction
Ray, U., Thirusangu, P., Jin, L., Xiao, Y., Pathoulas, C. L., Staub, J. K., Erskine, C. L., Dredge, K. S., Hammond, E., Block, M. S., et al. (2023) · Oncogene · doi:10.1038/s41388-023-02785-5 · Cited by 15
Jhaveri, J. R., Khare, P., Pinky, P. P., Kamte, Y. S., Chandwani, M. N., Milošević, J., Abraham, N., Sun, M., Stolz, D. B., Dave, K. M., et al. (2024) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2024.114500 · Cited by 15
Heparanase: Potential roles in multiple sclerosis
Changyaleket, B., Deliu, Z., Chignalia, A. Z., & Feinstein, D. L. (2017) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2017.07.001 · Cited by 15
Kim, M. G., Kim, C. L., Kim, Y. S., Jang, J. W., & Lee, G. M. (2021) · Scientific Reports · doi:10.1038/s41598-021-82955-1 · Cited by 15
Mechanisms of the epithelial-to-mesenchymal transition in sea urchin embryos
Katow, H. (2015) · Tissue Barriers · doi:10.1080/21688370.2015.1059004 · Cited by 15
A Developmental Perspective on Paragangliar Tumorigenesis
Lotti, L. V., Vespa, S., Pantalone, M. R., Perconti, S., Esposito, D. L., Visone, R., Veronese, A., Paties, C. T., Sanna, M., Verginelli, F., et al. (2019) · Cancers · doi:10.3390/cancers11030273 · Cited by 14
Kuo, P.-H., Teng, Y.-H., Cin, A.-L., Han, W., Huang, P.-W., Wang, L. H.-C., Chou, Y., Yang, J., Tseng, Y., Kao, M.-H., et al. (2020) · Drug Delivery · doi:10.1080/10717544.2020.1745326 · Cited by 14
Köksal, A. R., Thevenot, P., Aydın, Y., Núñez, K., Sandow, T. A., Widmer, K., Nayak, L., Scott, J., Delk, M., Moehlen, M., et al. (2022) · Journal of Hepatocellular Carcinoma · doi:10.2147/jhc.s376210 · Cited by 14
The role of heparan sulfate in host macrophage infection byLeishmaniaspecies
Maciej-Hulme, M. L., Skidmore, M. A., & Price, H. P. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170398 · Cited by 15
Ferrer, I., Andrés‐Benito, P., Sala‐Jarque, J., Gil, V., & del Rı́o, J. A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00101 · Cited by 14
A Novel, Broad-Acting Peptide Inhibitor of Double-Stranded DNA Virus Gene Expression and Replication
Ruzsics, Z., Hoffmann, K., Riedl, A., Krawczyk, A., Widera, M., Sertznig, H., Schipper, L., Kapper-Falcone, V., Debreczeny, M., Ernst, W., et al. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.601555 · Cited by 14
Dahms, S. O., Mayer, M., Roeser, D., Multhaup, G., & Than, M. E. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004714027114 · Cited by 14
Abraham, J. N., Rawat, D., Srikanth, P., Sunny, L. P., & Abraham, N. M. (2025) · Mammalian Genome · doi:10.1007/s00335-025-10128-w · Cited by 13
Cohen, E., Mariotton, J., Rozenberg, F., Sams, A. G., van Kuppevelt, T. H., Delongchamps, N. B., Zerbib, M., Bomsel, M., & Ganor, Y. (2022) · Mucosal Immunology · doi:10.1038/s41385-022-00521-y · Cited by 13
Nidhi, G., Yadav, V., Singh, T., Sharma, D., Bohot, M., & Satapathy, S. R. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1593834 · Cited by 14
Suzuki, T., Sato, Y., Okuno, Y., Goshima, F., Mikami, T., Umeda, M., Murata, T., Watanabe, T., Watashi, K., Wakita, T., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03581-9 · Cited by 13
Cellular-Defined Microenvironmental Internalization of Exosomes
Gonda, A., Moyron, R. B., Kabagwira, J., Vallejos, P. A., & Wall, N. R. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.86020 · Cited by 12
PRELP Enhances Host Innate Immunity against the Respiratory Tract Pathogen Moraxella catarrhalis
Liu, G., Ermert, D., Johansson, M., Singh, B., Su, Y., Paulsson, M., Riesbeck, K., & Blom, A. M. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601319 · Cited by 12
A Brief History of Adherons: The Discovery of Brain Exosomes
Schubert, D. A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207673 · Cited by 12
Physiology of Midkine and Its Potential Pathophysiological Role in COVID-19
Sanino, G., Bosco, M., & Terrazzano, G. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.616552 · Cited by 12
Alshehri, M. A., Alshehri, M. M., Albalawi, N. S., Al-ghamdi, M. A., & Al-Gayyar, M. M. H. (2021) · Oncology Letters · doi:10.3892/ol.2021.12434 · Cited by 12
An Intrinsically Disordered Peptide Facilitates Non‐Endosomal Cell Entry
Medina, S. H., Miller, S. E., Keim, A. I., Gorka, A. P., Schnermann, M. J., & Schneider, J. P. (2016) · Angewandte Chemie · doi:10.1002/ange.201510518 · Cited by 12
Lee, S., Lee, J., & Lee, K. (2026) · Biomaterials Science · doi:10.1039/d5bm01582k · Cited by 11
Han, M. (2024) · American Journal of Cancer Research · doi:10.62347/rxve7097 · Cited by 11
Shrestha, P., Adepu, S., Vivès, R. R., Masri, R. E., Klooster, A., Kaptein, F. H. J., Dam, W., Bakker, S. J. L., van Goor, H., van de Sluis, B., et al. (2021) · Journal of the American Society of Nephrology · doi:10.1681/asn.2020091376 · Cited by 12
The Non-Specific Binding of Fluorescent-Labeled MiRNAs on Cell Surface by Hydrophobic Interaction
Lu, T., Lin, Z., Ren, J., Yao, P., Wang, X., Wang, Z., & Zhang, Q. (2016) · PLoS ONE · doi:10.1371/journal.pone.0149751 · Cited by 11
Garcia, J., Patel, N. S., Basehore, S. E., & Clyne, A. M. (2019) · Annals of Biomedical Engineering · doi:10.1007/s10439-019-02202-7 · Cited by 11
Guanidinylated Neomycin Conjugation Enhances Intranasal Enzyme Replacement in the Brain
Tong, W., Dwyer, C. A., Thacker, B. E., Glass, C. A., Brown, J. R.-M., Hamill, K. M., Moremen, K. W., Sarrazin, S., Gordts, P. L. S. M., Dozier, L. E., et al. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2017.08.007 · Cited by 11
The Roles of Exosomes in Anti‐Cancer Drugs
Feng, P., Zhang, X., Gao, J., Jiang, L., & Li, Y. (2025) · Cancer Medicine · doi:10.1002/cam4.70897 · Cited by 11
Alo, B., & Lamers, C. (2025) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.5c00153 · Cited by 10
Pingyangmycin inhibits glycosaminoglycan sulphation in both cancer cells and tumour tissues
Lan, Y., Li, X., Liu, Y., He, Y., Hao, C., Wang, H., Jin, L., Zhang, G., Zhang, S., Zhou, A., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15017 · Cited by 10
Minsky, B. B., Abzalimov, R. R., Niu, C., Zhao, Y., Kirsch, Z. J., Dubin, P. L., Savinov, S. N., & Kaltashov, I. A. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00199 · Cited by 10
Cheudjeu, A. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119508 · Cited by 10
Biopolymer‐based Carriers for DNA Vaccine Design
Franck, C. O., Fanslau, L., Bistrović, A., Tyagi, P., & Fruk, L. (2020) · Angewandte Chemie · doi:10.1002/ange.202010282 · Cited by 10
Pérez‐Rubio, P., Vendrell-Flotats, M., Lorenzo, E., Enemark‐Rasmussen, K., Cervera, L., Gòdia, F., & Lavado‐García, J. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116893 · Cited by 9
The Challenge of Modulating Heparan Sulfate Turnover by Multitarget Heparin Derivatives
Veraldi, N., Zouggari, N., & de Agostini, A. I. (2020) · Molecules · doi:10.3390/molecules25020390 · Cited by 10
Enhanced nuclear delivery of H1-S6A, F8A peptide by NrTP6-modified polymeric platform
Xie, D., Wang, F., Xiang, Y., & Huang, Y. (2020) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2020.119224 · Cited by 9
Zhang, S., Guo, M., Guo, T., Yang, M.-Y., Cheng, J., Cui, C., Kang, J., Wang, J., Nian, Y., Ma, W., et al. (2021) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-021-04268-1 · Cited by 9
Lee, J. H., Kim, Y., Yoon, Y.-E., Kim, Y.-J., Oh, S., Jang, J., & Kim, E. (2017) · New Biotechnology · doi:10.1016/j.nbt.2017.02.001 · Cited by 9
New SDC function prediction based on protein-protein interaction using bioinformatics tools
Zandonadi, F. D. S., Cruz, E. C. S., & Korvala, J. (2019) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2019.107087 · Cited by 10
Calixarene-decorated liposomes for intracellular cargo delivery
Morbioli, I., Casnati, A., Esko, J. D., Tor, Y., & Sansone, F. (2021) · Organic & Biomolecular Chemistry · doi:10.1039/d1ob01055g · Cited by 9
Transduction of Recombinant M3-p53-R12 Protein Enhances Human Leukemia Cell Apoptosis
Lu, T.-C., Zhao, G. H., Chen, Y. Y., Chien, C.-Y., Huang, C.-H., Lin, K., & Chen, S. L. (2016) · Journal of Cancer · doi:10.7150/jca.15155 · Cited by 9
Cell biology of prion strains in vivo and in vitro
Shoup, D. W., & Priola, S. A. (2022) · Cell and Tissue Research · doi:10.1007/s00441-021-03572-y · Cited by 9
Park, P. W., Hayashida, K., Aquino, R. S., & Jinno, A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.10032-x · Cited by 10
Goto, A., Yamamoto, S., Igari, T., Matsumoto, S.-I., Chisaki, I., Iida, K., Nakayama, M., Oda, A., Kakoi, Y., Uchida, A., et al. (2022) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.122.001331 · Cited by 8
Syndecan-4 Mediates the Cellular Entry of Adeno-Associated Virus 9
Hudák, A., Roach, M., Pusztai, D., Pettkó‐Szandtner, A., Letoha, A., Szilák, L., Azzouz, M., & Letoha, T. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043141 · Cited by 8
Transcriptome profiling of whisker follicles in methamphetamine self-administered rats
Song, S.-H., Jang, W., Hwang, J., Park, B., Jang, J., Seo, Y.-H., Yang, C. H., Lee, S., & Jeong, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-29772-1 · Cited by 8
Habeler, M., Lindner, H. H., & Redl, B. (2020) · Biological Chemistry · doi:10.1515/hsz-2020-0132 · Cited by 8
Malkmus, J., Morabito, A., Lopez‐Delisle, L., Aviñó-Esteban, L., Mayran, A., Zúñiga, A., Sharpe, J. A., Zeller, R., & Sheth, R. (2025) · Development · doi:10.1242/dev.204606 · Cited by 7
Volovăț, S. R., Augustin, I. G., Volovat, C. D., Ingrid, T. V., Ostafe, M. R., Panaite, D. I., Burlacu, A. I., & Volovăț, C. C. (2026) · Pharmaceutics · doi:10.3390/pharmaceutics18010084 · Cited by 8
de la Rosa, A., Metzendorf, N. G., Morrison, J. I., Faresjö, R., Rofo, F., Petrovic, A., O’Callaghan, P., Syvänen, S., & Hultqvist, G. (2022) · Scientific Reports · doi:10.1038/s41598-022-25965-x · Cited by 7
Down‐regulating Proteolysis to Enhance Anticancer Activity of Peptide Nanofibers
Li, J., Du, X., Powell, D. J., Zhou, R., Shi, J., He, H., Feng, Z., & Xu, B. (2018) · Chemistry - An Asian Journal · doi:10.1002/asia.201800875 · Cited by 7
A dimeric α-helical cell penetrating peptide mounted with an HER2-selective affibody
Chong, S., Lee, D., Oh, J. H., Kang, S., Choi, S., Nam, S. H., Yu, J., Koo, H., & Lee, Y. (2021) · Biomaterials Science · doi:10.1039/d1bm00819f · Cited by 7
Antonio, L. C., Ribovski, L., Lins, P. M. P., & Zucolotto, V. (2022) · Journal of Materials Chemistry B · doi:10.1039/d2tb01296k · Cited by 7
Role of sulfatase 2 in lipoprotein metabolism and angiogenesis
Dallinga, M. G., & Dallinga‐Thie, G. M. (2016) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000271 · Cited by 7
Extracellular vesicles at the cross‐line between basic science and clinical needs
Sasso, L., Hosamuddin, H., & Emanueli, C. (2016) · Microcirculation · doi:10.1111/micc.12333 · Cited by 8
Cell-Translocation Mechanisms of CPPs
Langel, Ü. (2019) · Springer eBooks · doi:10.1007/978-981-13-8747-0_10 · Cited by 7
Ansari, A. S., Remant, K. C., Jiang, X., & Uludağ, H. (2021) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.37214 · Cited by 7
SDC4-rs1981429 and ATM-rs228590 may provide early biomarkers of breast cancer risk
Vuorinen, S. I., Okolicsanyi, R. K., Gyimesi, M., Meyjes-Brown, J., Saini, D., Pham, S. H., Griffiths, L. R., & Haupt, L. M. (2022) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-022-04236-2 · Cited by 6
Okafor, M., Champomier, O., Raibaut, L., Ozkan, S., Kholti, N. E., Ory, S., Chasserot‐Golaz, S., Gasman, S., Hureau, C., Faller, P., et al. (2024) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2024.1355963 · Cited by 6
Metadata
- Authors
- Christianson, H. C., & Belting, M.
- Affiliations
- Lund University (SE)
- Corresponding author
- Belting, Mattias
- ORCID
- Belting, Mattias
- Venue
- Matrix Biology
- Publisher
- Elsevier BV
- Published
- 2014-04
- Volume
- 35
- Pages
- 51-55
- ISSN
- 0945-053X (ISSN-L)
- OpenAlex
- W1980226233
- Cited by
- 429
- References
- 55
- Citations by year
- 2026: 20 · 2025: 29 · 2024: 29 · 2023: 44 · 2022: 43 · 2021: 44 · 2020: 54 · 2019: 37 · 2018: 27 · 2017: 29 · 2016: 30 · 2015: 28 · 2014: 14
- FWCI
- 14.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Matrix Biology (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Lund University Publications (Lund University) (submittedVersion)
- Funders
- Swedish Cancer Fund
- Swedish Research Council
- Gunnar Nilsson Cancer Foundation
- Anna Lisa and Sven Eric Lundgren Foundation
- Kamprad Family Foundation
- Skåne University Hospital
- Governmental funding of clinical research within the national health services (ALF)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Physical Sciences › Materials Science › Biomaterials › Nanoparticle-Based Drug Delivery
- Keywords
- heparan sulfate proteoglycans, endocytosis, cell surface receptors, exosomes, cell-penetrating peptides, nucleic acid delivery, viral entry, lipoprotein uptake, growth factor signaling, membrane invagination, intracellular signaling, lipid metabolism, cancer, infectious diseases, drug delivery
- MeSH terms
- Animals, Biological Transport, Endocytosis, Humans, Ligands, Models, Biological, Receptors, Cell Surface, Signal Transduction, Heparan Sulfate Proteoglycans
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
