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Solution structure and basis for functional activity of stromal cell‐derived factor‐1; dissociation of CXCR4 activation from binding and inhibition of HIV‐1
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The three-dimensional structure of stromal cell-derived factor-1 (SDF-1) was determined by NMR spectroscopy. SDF-1 is a monomer with a disordered N-terminal region (residues 1-8), and differs from other chemokines in the packing of the hydrophobic core and surface charge distribution. Results with analogs showed that the N-terminal eight residues formed an important receptor binding site; however, only Lys-1 and Pro-2 were directly involved in receptor activation. Modification to Lys-1 and/or Pro-2 resulted in loss of activity, but generated potent SDF-1 antagonists. Residues 12-17 of the loop region, which we term the RFFESH motif, unlike the N-terminal region, were well defined in the SDF-1 structure. The RFFESH formed a receptor binding site, which we propose to be an important initial docking site of SDF-1 with its receptor. The ability of the SDF-1 analogs to block HIV-1 entry via CXCR4, which is a HIV-1 coreceptor for the virus in addition to being the receptor for SDF-1, correlated with their affinity for CXCR4. Activation of the receptor is not required for HIV-1 inhibition.
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“The protein product of CCL11 resulting from differential signal peptide cleavage is predicted to retain additional amino-acid residues at its N terminus, a key region specifying binding and activity of chemokines.44”
From Whole-genome sequencing suggests a chemokine gene cluster that modifies age at onset in familial Alzheimer's disease (2015) · cites this paper as [44]
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Citations
Cites
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,616
NMR with Proteins and Nucleic Acids
Wüthrich, K. (1986) · Europhysics news · doi:10.1051/epn/19861701011 · Cited by 8,028
NMR of Proteins and Nucleic Acids
(2006) · Royal Society of Chemistry eBooks · doi:10.1039/9781847555236-00336 · Cited by 5,874
Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230
HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor
Feng, Y. Y., Broder, C. C., Kennedy, P. E., & Berger, E. A. (1996) · Science · doi:10.1126/science.272.5263.872 · Cited by 4,169
X-PLOR Version 3.1: A System for X-ray Crystallography and NMR
Brünger, A. T. (1992) · Medical Entomology and Zoology · Cited by 3,424
Raster3D Version 2.0. A program for photorealistic molecular graphics
Merritt, E. A., & Murphy, M. E. P. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994006396 · Cited by 2,493
Nagasawa, T., Hirota, S., Tachibana, K., Takakura, N., Nishikawa, S.-I., Kitamura, Y., Yoshida, N., Kikutani, H., & Kishimoto, T. (1996) · Nature · doi:10.1038/382635a0 · Cited by 2,382
Cited by
Sorted by citations
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Drouillard, D., Halyko, M., Cinquegrani, E., Poimenidou, M., Emosİvbe, M., McAllister, D. M., Peterson, F. C., Marchese, A., & Dwinell, M. B. (2025) · Scientific Reports · doi:10.1038/s41598-025-12005-7 · Cited by 5
“These data are in stark contrast to CXCL12-LD treated cells, in which CXCR4 surface levels were significantly reduced in both U937 and AML-193 cells at both time points.”
Bardi, G. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2910350 · Cited by 4
The Structural Biology of Chemokines
Lolis, E., & Murphy, J. W. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-020-1_2 · Cited by 4
“The solution structure of CXCL10 interferon inducible protein (IP-10) is monomeric (28), and CXCL12 exists as a monomer or dimer depending on solution conditions (29,30), yet the oligomeric states in the crystal structures are different: CXCL12 is a dimer (31), whereas CXCL10 was crystallized as both a dimer and tetra…”
BackgroundClark‐Lewis, I. (2003) · Humana Press eBooks · doi:10.1385/1-59259-058-6:47 · Cited by 4
Self-citationBi-ligand surfaces with oriented and patterned protein for real-time tracking of cell migration
Vernekar, V. N., Wallace, C. S., Wu, M. Y. M., Chao, J. T., O’Connor, S. K., Raleigh, A. R., Liu, X., Haugh, J. M., & Reichert, W. M. (2014) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2014.09.020 · Cited by 4
Song, J.-Z., Wang, X., Lei, C., Piao, J., Yin, C., Zhang, Z., Lin, Q., & Hualiang, H. (2006) · Biotechnology and Applied Biochemistry · doi:10.1042/ba20060060 · Cited by 4
DPPIV/CD26 as a Target in Anti-inflammatory Therapy
Vliegen, G., & Meester, I. D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805417-8.00011-1 · Cited by 4
Luo, Y., Li, Q., Yang, X., Wei, D., Feng, B., Li, M., Han, Y., Zhao, J., Lin, Y., Li, Q., et al. (2021) · Disease Markers · doi:10.1155/2021/6649579 · Cited by 4
Kurowarabe, K., Endo, M., Kobayashi, D., & Hayasaka, H. (2021) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2021.101128 · Cited by 4
Endogenous Peptide Inhibitors of HIV Entry
Harms, M., Hayn, M., Zech, F., Kirchhoff, F., & Münch, J. (2022) · Advances in experimental medicine and biology · doi:10.1007/978-981-16-8702-0_5 · Cited by 4
Lee, K.-G., Santos, A. R. M. P., Kang, Y. G., Chae, Y. J., Shah, M., Pirzada, R. H., Song, M., Kim, J., Choi, S., & Park, Y. (2022) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.2c00766 · Cited by 4
The complex nature of CXCR4 mutations in WHIM syndrome
Rodrı́guez-Frade, J. M., González‐Granado, L. I., Santiago, C. A., & Mellado, M. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1406532 · Cited by 4
Development And Application Of Fluorescent SDF-1 Derivatives
Masuda, R., Oishi, S., Tanahara, N., Ohno, H., Hirasawa, A., Tsujimoto, G., Kodama, E. N., Matsuoka, M., & Fujii, N. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.31 · Cited by 4
Baryshnikova, O. K., Rainey, J. K., & Sykes, B. D. (2005) · Journal of Peptide Research · doi:10.1111/j.1747-0285.2006.00330.x · Cited by 4
Self-citationPicking the Lock with a Hairpin
Lusso, P. (2003) · Structure · doi:10.1016/s0969-2126(03)00013-3 · Cited by 4
Specific Probes for Chemokine Receptors
Tamamura, H., & Tsutsumi, H. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.12.005 · Cited by 4
Kessler, N., Akabayov, S. R., Cohen, L. S., Scherf, T., Naider, F. R., & Anglister, J. (2023) · FEBS Journal · doi:10.1111/febs.17013 · Cited by 3
“Unliganded CXCL12 is completely monomeric at acidic pH [42].”
BackgroundPereira, R. V. S., EzEldeen, M., & Opdenakker, G. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052165 · Cited by 3
Chemokine receptors – Exemplifying functional divergence in G protein-coupled receptors
Otun, O., Granier, S., Durroux, T., & Bechara, C. (2025) · Molecular Pharmacology · doi:10.1016/j.molpha.2025.100053 · Cited by 3
Chemokine receptors (version 2020.5) in the IUPHAR/BPS Guide to Pharmacology Database
Bachelerie, F., Ben‐Baruch, A., Burkhardt, A. M., Charo, I. F., Combadière, C., Förster, R., Farber, J. M., Graham, G. J., Hills, R., Horuk, R., et al. (2020) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f14/2020.5 · Cited by 4
Yahiro, I., Barnuevo, K. D., Sato, O., Mohapatra, S., Toyoda, A., Itoh, T., Ohno, K., Matsuyama, M., Chakraborty, T., & Ohta, K. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1349119 · Cited by 3
Assessing Protein-Protein Docking Protocols: Case Studies of G-Protein-Coupled Receptor Interactions
Sonawani, A., Naglekar, A., Kharche, S., & Sengupta, D. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3985-6_13 · Cited by 3
Li, H., & Wang, Y. (2013) · Europe PMC (PubMed Central) · Cited by 3
In vitroscreening for chemokine antagonists
Ribeiro, S., & Horuk, R. (2009) · Expert Opinion on Drug Discovery · doi:10.1517/17460440902956628 · Cited by 3
“The discrepancy in potency of AMD3100 for CXCR4 described in these assays is thought to reflect differences in interaction of the antagonist and CXCL12 with CXCR4, which has been reported to be a two-step process [29].”
BackgroundCloning, expression and identification of an isoform of human stromal cell derived factor-1α
Liang, Y., PING, W., & Bian, L. (2015) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2015.2355 · Cited by 3
“Crump et al (10) studied the NMR structure of SDF-1 in different solution conditions.”
Cloning and expression of chemokine receptor CXCR4 in eukaryotic cells CHO, HEK293 and BHK21
Strods, A., Petrovska, R., Jackeviča, L., & Renhofa, R. (2010) · Proceedings of the Latvian Academy of Sciences Section B Natural Exact and Applied Sciences · doi:10.2478/v10046-010-0033-6 · Cited by 3
“Dace Skrastiòa, called anti-543; these antibodies were prepared using as antigen, himeric virus-like particles formed from bacteriophage coat protein fused with a thirty nine N-terminal aminoacid long fragment of the CXCR4 sequence (Crump et al., 1997).”
MethodLiu, H., Sun, H., Li, L., Mo, X. M., Li, X., & Zhang, G. (2012) · Tropical Journal of Pharmaceutical Research · doi:10.4314/tjpr.v11i2.4 · Cited by 3
“The N-terminal region of a chemokine is an important candidate site for development of antagonists, since it initially combines with receptors to start a series of signal cascades [13].”
BackgroundChen, Z., & Ding, J. (2011) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmr026 · Cited by 3
Chemokine Receptors and NeuroAIDS
Meucci, O. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0793-6 · Cited by 3
Peptide-binding induced inhibition of chemokine CXCL12
Duan, H., Zhu, L., Peng, J., Yang, M., Xie, H., Lin, Y., Li, W., Liu, C., Li, X., Guo, H., et al. (2017) · RSC Advances · doi:10.1039/c7ra01735a · Cited by 3
Kufareva, I., Abagyan, R. A., & Handel, T. M. (2014) · Topics in medicinal chemistry · doi:10.1007/7355_2014_77 · Cited by 3
The use of Envelope for HIV therapeutics: from vaccines to co-receptors
Doranz, B. J. (2000) · Emerging Therapeutic Targets · doi:10.1517/14728222.4.4.423 · Cited by 3
“Binding of the cognate chemokine SDF to CXCR4 follows the two-site model of many other chemokine receptors: the amino terminus of CXCR4 provides the primary high affinity binding site for SDF and ECL2 provides the activation site for signalling [146,147,153].”
BackgroundProudfoot, A. E. I., Shaw, J. P., Power, C., & Wells, T. N. C. (2002) · Elsevier eBooks · doi:10.1016/b978-044451002-0/50006-3 · Cited by 3
MacLean, F., Tsegaye, A. T., Graham, J. B., Swarts, J. L., Vick, S. C., Potchen, N. B., Talavera, I. C., Warrier, L., Dubrulle, J., Schroeder, L. K., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.03.601916 · Cited by 3
Satani, K. H., & Spencer, J. V. (2025) · Virology · doi:10.1016/j.virol.2025.110693 · Cited by 2
Computational studies of target-specific radiopharmaceuticals for theranostics
Gervasoni, S. I., Guccione, C., & Malloci, G. (2025) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2025.109264 · Cited by 2
Zhou, J., Liu, X., Xu, Y., Cruz, A., An, J., Warshel, A., & Huang, Z. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.6c01087 · Cited by 2
Li, H., Yan, Z., Cao, H., & Wang, Y. (2011) · Medical Hypotheses · doi:10.1016/j.mehy.2011.11.003 · Cited by 2
Våbenø, J., Oliva-Santiago, M., Jørgensen, A. S., Karlshøj, S., & ROSENKILDE, M. M. (2023) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00070 · Cited by 2
Xu, T., Schou, A. S., Lackman, J. J., Barrio-Calvo, M., Verhallen, L., Goth, C. K., Jensen, B. A. H., Veldkamp, C. T., Volkman, B. F., Peterson, F. C., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251910854 · Cited by 2
“…one or more ligands in common like CCR1 and CCR5, although expressed by the same type of cell, may be under differential control, due to their differential dependence on PTMs, that changes in immune cells going from immature to mature states and dependent on, e.g., the activating substances [33].”
BackgroundInfluentialMurphy, J. W., Rajasekaran, D., Merkel, J., Skeens, E., Keeler, C., Hodsdon, M. E., Lisi, G. P., & Lolis, E. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00164 · Cited by 2
“The agonist exists as a monomer (Crump et al., 1997), dimer (Dealwis et al., 1998), and a decamer (Murphy et al., 2010).”
BackgroundQin, C., Memon, N. H., Gong, Q., Shi, Q., & Yang, Q. (2021) · Chronobiology International · doi:10.1080/07420528.2021.1927070 · Cited by 2
“In addition, the CXCL12 served as the CXCR4 docking site in the RFFESH motif, and was well conserved from the mammalian orthologue within the N-terminal region (Crump et al. 1997).”
BackgroundMiyakawa, K., Fujita, R., Katane, M., Kubo, Y., & Amanuma, H. (2008) · Journal of General Virology · doi:10.1099/vir.0.2008/006031-0 · Cited by 2
“1b) (Crump et al., 1997), we first examined the effects of truncations from the C terminus of SDF-1a.”
BackgroundInfluentialKraemer, S., Weber, C., & Bernhagen, J. (2012) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789814335362_0002 · Cited by 2
Accurate structural correlations from maximum likelihood superpositions
Theobald, D. L., & Wuttke, D. S. (2005) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0040043.eor · Cited by 2
Structure and function of engineered stromal cell-derived factor-1α.
Abe, F., Nakano, A., Hirata, I., Tanimoto, K., & Kato, K. (2024) · Dental materials journal · doi:10.4012/dmj.2023-247 · Cited by 1
Chemokine receptors (version 2019.5) in the IUPHAR/BPS Guide to Pharmacology Database
Bachelerie, F., Ben‐Baruch, A., Charo, I. F., Combadière, C., Förster, R., Farber, J. M., Graham, G. J., Hills, R., Horuk, R., Locati, M., et al. (2019) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f14/2019.5 · Cited by 2
Chemokines in Behçet’s Disease, a Field to Be Explored as a Potential Basis for Therapy
Baggiolini, M. (2006) · Kluwer Academic Publishers eBooks · doi:10.1007/0-306-48382-3_48 · Cited by 2
Self-citationDwir, O., Grabovsky, V., & Alon, R. (2004) · Springer eBooks · doi:10.1007/978-3-662-05397-3_7 · Cited by 2
Chemokine Receptors and HIV-1 Pathogenesis
Norcross, M. A. (1999) · Elsevier eBooks · doi:10.1016/b978-012200741-5/50011-8 · Cited by 2
Monitoring Ligand-Induced Changes in Receptor Conformation with NanoBiT Conjugated NanobodiesPreprint
Soave, M., Heukers, R., Kellam, B., Woolard, J., Smit, M. J., Briddon, S. J., & Hill, S. J. (2020) · SSRN Electronic Journal · doi:10.2139/ssrn.3578138 · Cited by 2
Khan, M. Z. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0793-6_10 · Cited by 1
Suzuki, S., Miura, T., Shimoyama, Y., Ohara‐Nemoto, Y., Nemoto, T., Yamada, H., & Ishikawa, T. (2025) · Journal of Oral Biosciences · doi:10.1016/j.job.2025.100723 · Cited by 1
The CXCL12/CXCR4 Axis in Sepsis-Induced Acute Lung Injury: Mechanisms and Therapeutic Potential
Luo, R., Fan, Q., Chen, Q., Nie, Z., Dan, L., & Xie, S. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47121052 · Cited by 1
“These domains are required for high-affinity receptor binding and for inducing the conformational changes necessary to initiate CXCR4-dependent intracellular signaling [31,32].”
Guitart, A. V., Lee, C., Santo, A. I. E., Ruan, J.-L., Mao, S.-H., William, L., Redfield, C., Fedorov, O., Burgess-Brown, N., Yue, W. W., et al. (2026) · iScience · doi:10.1016/j.isci.2026.117140 · Cited by 1
“…protein to allow for periplasmic secretion with an N-terminal fusion protein in the pDsbC-HT-CBio vector (DsbC-SUMO-CXCL12) to avoid addition of N-terminal residues to the protein which could affect its activity 50,51 whilst obtaining folded, oxidized CXCL12 via the DsbC fusion protein system.”
Chemokine Proteolytic Processing in HIV Infection: Neurotoxic and Neuroimmune Consequences
Vergote, D., Overall, C. M., & Power, C. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0793-6_7 · Cited by 1
Chemokine receptors (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database
Bachelerie, F., Ben‐Baruch, A., Charo, I. F., Combadière, C., Förster, R., Farber, J. M., Graham, G. J., Hills, R., Horuk, R., Locati, M., et al. (2019) · IUPHAR/BPS Guide to Pharmacology CITE · doi:10.2218/gtopdb/f14/2019.4 · Cited by 1
Chen, Y. (2023) · Frontiers in Medical Science Research · doi:10.25236/fmsr.2023.051103 · Cited by 1
“CXCL12 initially plays a role as a chemokine [28][29] and is trimmed by DPP4 in the FAP family to act together with CXCR4 in immune rejection [30,31] .”
BackgroundIdentification and characterization of genes with specific expression in dendritic cells
Heinz, S. (2003) · University of Regensburg Publication Server (University of Regensburg) · doi:10.5283/epub.10104 · Cited by 1
HIV Coreceptors and Chemokines as Therapeutic Targets Against HIV/AIDS
DeVico, A. L., & Gallo, R. C. (2001) · Cited by 1
Chemokine and Cytokine Modulators
Fuentes, M. E., Mirzadegan, T., & Wilhelm, R. S. (2003) · Wiley eBooks · doi:10.1002/0471266949.bmc062 · Cited by 1
Bioengineering of novel 3D scaffolds for cell-based therapy in heart failure and diabetes mellitus
Sondermeijer (2019) · Research Publications (Maastricht University) · doi:10.26481/dis.20190517hs
Heveker, N., Tissot, M., Thuret, A., Schneider‐Mergener, J., Alizon, M., Roch-Arveiller, M., & Marullo, S. (2001) · Molecular Pharmacology · doi:10.1016/s0026-895x(24)12268-7 · Cited by 1
Stem Cells Signaling Pathways in the Heart
Marín-García, J. (2011) · Springer eBooks · doi:10.1007/978-1-4419-9461-5_19
which can functionally be expressed and provide NOD/SCID repopulation
Kollet, Ó., Petit, I., Kahn, J., Samira, S., Dar, A., Peled, A., Deutsch, V. R., Gunetti, M., Piacibello, W., Nagler, A., et al. (2016)
Chow, K. Y. C., & Bachelerie, F. (2010) · Methods and principles in medicinal chemistry · doi:10.1002/9783527631995.ch11
Monfregola, L. (2010) · Università degli Studi di Napoli Federico II · doi:10.6092/unina/fedoa/8026
Structural Insights for Homology Modeling of Chemokine Receptors
Pardo, L., Deupí, X., Cordomí, A., Govaerts, C., & Campillo, M. (2010) · Methods and principles in medicinal chemistry · doi:10.1002/9783527631995.ch2
The Role of Neuroinflammation in Regulating the Age-Related Decline in Neurogenesis
Bachstetter, A. D. (2009) · Digital Commons - University of South Florida (University of South Florida)
Peri- and extravascular inflammation : impact on atherosclerosis
Daissormont, I. (2012) · Research Publications (Maastricht University) · doi:10.26481/dis.20120413id
Chemokine Receptors and HIV/AIDS
Stantchev, T. S., & Broder, C. C. (2007) · Humana Press eBooks · doi:10.1007/978-1-59745-020-1_13
Busillo, J. M. (2008) · The Medicine Forum
Occurrence of Stromal Derived Factor-1 Polymorphism In Kenyan Population
Ongonda, J. K., Gicheru, M. M., & Khamadi, S. A. (2012)
Targeting Homing to Enhance Engraftment Following Umbilical Cord Blood Stem Cell Transplantation
Farag, S. S., & Davis, T. (2014) · Stem cell biology and regenerative medicine · doi:10.1007/978-3-319-06444-4_13
Structure-based design of inhibitors of CXCR4.
Meier, J. (2011) · ThinkIR: The University of Louisville's Institutional Repository (University of Louisville) · doi:10.18297/etd/962
“Interaction between the N-terminus of CXCl12 and extracellular surfaces of the TM helixes produces signal transduction [121, 125, 126].”
BackgroundBrennecke, P. (2011) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-a-006838452
The Role of CCL5/CCR5 Signal Transduction in T cell Function and Breast Cancer
Murooka, T. T. (2009) · TSpace (University of Toronto)
Jegede, O. (2007) · OhioLink ETD Center (Ohio Library and Information Network)
Vasser, G. (2008) · doi:10.21007/etd.cghs.2008.0336
“Previous studies had shown that the C-terminal end of SDF-1α has little to no bearing on its ability to bind to or activate the CXCR-4 receptor [68, 72], therefore we were comfortable experimenting with varying lengths of SDF-1α in the hope that slightly reducing its size might be more conducive to proper folding.”
BackgroundMethodMolecular and cellular mediators in radiation-induced lung injury
Yang, X. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/mf1m-y866
Sulfotyrosine Recognition as Marker for Druggable Sites in the
Ziarek, J. J., Heroux, M. S., Veldkamp, C. T., Peterson, F. C., & Volkman, B. F. (2011)
München, F. D. L.-M.-U. (2013)
Therapeutic Targeting of Chemokines and Chemokine Receptors
Zimmermann, N., & Rothenberg, M. E. (2002) · Lung biology in health and disease · doi:10.1201/b14066-9
Joubert, B. R. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/q5th-rw94
Die Rolle und Funktionsweise der Chemokinrezeptoren CXCR4 und CXCR7 in Mikroglia und Astrozyten
Lipfert, J. (2013) · Qucosa (Saxon State and University Library Dresden)
The distribution of stromal derived factor-1 mutation in Kenyan population
Ong'onda, K. J. (2011) · Kenyatta University Institutional Repository (Kenyatta University)
Establishing the interaction between the CC chemokine ligand 5 and the receptors CCR1 and CCR5
Kramp, B. K., & Koenen, R. R. (2014) · Research Publications (Maastricht University)
Design, Synthesis and Analysis of Small Molecule Heterocyclic Aromatic-Based CXCR4 Modulators
Gaines, T. (2017) · Digital Archive @ GSU · doi:10.57709/10455291
Smolarek, D., Bertrand, O., Czerwiński, M., Colin, Y., Etchebest, C., & de Brevern, A. G. (2010)
CXCR4 expressed in somatotrophs mediates GH production and cell proliferation
이용호 (2008) · YUHSpace (Yonsei University Medical Library)
Mapping the intracellular molecular mechanisms of chemokine signalling within cancer
Keil, G. (2019) · UEA Digital Repository (University of East Anglia)
Characterization of the Coca Chemokine Receptor Four Agonist Activity of Ubiquitin
Staren, D. M. (2012) · Loyola eCommons (Loyola University of Chicago)
Kojima, M. (2013) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.717962854.793470138
Baggiolini, M., & Loetscher, P. (2010) · Wiley eBooks · doi:10.1002/9780470688618.taw0094
Self-citationGerm cell development and migration
Stebler, J. (2005) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-1290
Boehncke, W.-H. (2004) · CRC Press eBooks · doi:10.1201/b15729-5
Metadata
- Authors
- Crump, M. P., Gong, J., Loetscher, P., Rajarathnam, K., Amara, A., Arenzana‐Seisdedos, F., Virelizier, J., Baggiolini, M., Sykes, B. D., & Clark‐Lewis, I.
- Affiliations
- University of Alberta (CA)
- University of British Columbia (CA)
- University of Bern (CH)
- Institut Pasteur (FR)
- Corresponding author
- Sykes, Brian D.
- Clark‐Lewis, Ian
- Venue
- The EMBO Journal
- Published
- 1997-12-01
- Volume
- 16
- Issue
- 23
- Pages
- 6996-7007
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1170303
- OpenAlex
- W1964083898
- Cited by
- 731
- References
- 45
- Citations by year
- 2026: 10 · 2025: 12 · 2024: 19 · 2023: 14 · 2022: 17 · 2021: 15 · 2020: 29 · 2019: 32 · 2018: 20 · 2017: 35 · 2016: 26 · 2015: 34 · 2014: 30 · 2013: 44 · 2012: 35
- FWCI
- 10.34
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Research Council Canada
- Medical Research Council
- Topics
- Health Sciences › Medicine › Oncology › Chemokine receptors and signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Health Sciences › Medicine › Infectious Diseases › HIV/AIDS drug development and treatment
- Keywords
- CXCL12, chemokine structure, N-terminal disordered region, receptor binding sites, CXCR4, HIV-1 coreceptor, HIV-1 entry inhibition, receptor activation, chemokine antagonists
- MeSH terms
- Amino Acid Sequence, Binding Sites, Models, Biological, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Structure-Activity Relationship, Virus Replication, HIV-1, Sequence Homology, Amino Acid, Chemokines, Anti-HIV Agents, Receptors, CXCR4, Chemokines, CXC, Nuclear Magnetic Resonance, Biomolecular, Chemokine CXCL12
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.
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