The DOI matches its Crossref record; 105 of the 105 references it cites were found in a registry or an index.
REGULATION OF PROTEIN FUNCTION BY GLYCOSAMINOGLYCANS—AS EXEMPLIFIED BY CHEMOKINES
Abstract
▪ Abstract Immune modulators such as cytokines and growth factors exert their biological activity through high-affinity interactions with cell-surface receptors, thereby activating specific signaling pathways. However, many of these molecules also participate in low-affinity interactions with another class of molecules, referred to as proteoglycans. Proteoglycans consist of a protein core to which glycosaminoglycan (GAG) chains are attached. The GAGs are long, linear, sulfated, and highly charged heterogeneous polysaccharides that are expressed throughout the body in different forms, depending on the developmental or pathological state of the organ/organism. They participate in many biological functions, including organogenesis and growth control, cell adhesion, signaling, inflammation, tumorigenesis, and interactions with pathogens. Recently, it was demonstrated that certain chemokines require interactions with GAGs for their in vivo function. The GAG interaction is thought to provide a mechanism for retaining chemokines on cell surfaces, facilitating the formation of chemokine gradients. These gradients serve as directional cues to guide the migration of the appropriate cells in the context of their inflammatory, developmental, and homeostatic functions. In this review, we discuss GAGs and their interaction with proteins, with a special emphasis on the chemokine system.
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The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
Zlotnik, A., & Yoshie, O. (2000) · Immunity · doi:10.1016/s1074-7613(00)80165-x · Cited by 3,859
Chemokines and leukocyte traffic
Baggiolini, M. (1998) · Nature · doi:10.1038/33340 · Cited by 2,709
The Biology of Chemokines and their Receptors
Rossi, D., & Zlotnik, A. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.217 · Cited by 2,410
Hyaluronan: from extracellular glue to pericellular cue
Toole, B. P. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1391 · Cited by 2,125
Order Out of Chaos: Assembly of Ligand Binding Sites in Heparan Sulfate
Esko, J. D., & Selleck, S. B. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135458 · Cited by 1,495
The Purification and Mechanism of Action of Human Antithrombin-Heparin Cofactor
Rosenberg, R. D., & Damus, P. S. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43472-8 · Cited by 1,356
Molecular modeling of protein-glycosaminoglycan interactions.
Cardin, A. D., & Weintraub, H. J. (1989) · Arteriosclerosis: An Official Journal of the American Heart Association, Inc. · doi:10.1161/01.atv.9.1.21 · Cited by 1,301
Lymphocyte traffic control by chemokines
Moser, B., & Loetscher, P. (2001) · Nature Immunology · doi:10.1038/84219 · Cited by 1,240
Schlessinger, J., Plotnikov, A. N., Ibrahimi, O. A., Eliseenkova, A. V., Yeh, B. K., Yayon, A., Linhardt, R. J., & Mohammadi, M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00073-3 · Cited by 1,199
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Development, maintenance and disruption of the blood-brain barrier
Obermeier, B., Daneman, R., & Ransohoff, R. M. (2013) · Nature Medicine · doi:10.1038/nm.3407 · Cited by 2,452
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Van Raemdonck, K., Van den Steen, P. E., Liekens, S., Van Damme, J., & Struyf, S. (2015) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2014.11.009 · Cited by 310
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Deng, T., Gao, D., Song, X., Zhou, Z., Zhou, L., Tao, M., Jiang, Z., Yang, L., Luo, L., Zhou, A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-35907-4 · Cited by 289
Hepatic platelet and leukocyte adherence during endotoxemia
Croner, R. S., Hoerer, E., Kulu, Y., Hackert, T., Gebhard, M.-M., Herfarth, C., & Klar, E. (2006) · Critical Care · doi:10.1186/cc3968 · Cited by 275
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Ori, A., Wilkinson, M. C., & Fernig, D. G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.228114 · Cited by 251
Metadata
- Authors
- Handel, T. M., Johnson, Z., Crown, S. E., Lau, E. K., Sweeney, M., & Proudfoot, A. E.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2005-06-01
- Volume
- 74
- Issue
- 1
- Pages
- 385-410
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2156700198
- Cited by
- 508
- References
- 105
- FWCI
- 0.50
- Type
- journal article
- Language
- en
- Open access
- closed
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- Handel, T. M., Johnson, Z., Crown, S. E., Lau, E. K., Sweeney, M., & Proudfoot, A. E. (2005). REGULATION OF PROTEIN FUNCTION BY GLYCOSAMINOGLYCANS—AS EXEMPLIFIED BY CHEMOKINES. Annual Review of Biochemistry. https://doi.org/10.1146/annurev.biochem.72.121801.161747
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