The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The requested target is CXCR3 from horse (Equus caballus), UniProt A0A9L0T1D1, annotated as “C-X-C chemokine receptor type 3” and “interferon-inducible protein 10 receptor.” The supplied UniProt assignment is internally consistent: its GPCR-1/rhodopsin-like seven-transmembrane, chemokine-receptor, CCR1–9-like, and CXCR3-specific domains all describe a conventional CXC chemokine receptor. The literature search found equine studies involving CXCR3 and its ligands and did not reveal a conflicting horse protein with the same symbol. However, the accession itself appears poorly characterized experimentally; its identification therefore remains principally annotation-based.
The most defensible primary-function annotation is: a seven-transmembrane chemokine GPCR that detects interferon-inducible CXCL9, CXCL10/IP-10, and probably CXCL11 at the surface of responsive cells and converts these extracellular gradients into Gi-linked migratory signals, thereby directing activated type-1 effector lymphocytes toward inflamed tissues. Ligand-activated receptor is expected to undergo GRK/β-arrestin-regulated internalization and continue generating spatially differentiated signals from endosomes. This molecular mechanism is established directly for human CXCR3 but remains an orthology/domain-based inference for A0A9L0T1D1. Equine-specific studies directly support regulated CXCR3 transcription and an active CXCL9/CXCL10–lymphocyte-migration axis, but do not yet establish equine receptor binding constants, protein localization, Gi coupling, isoforms, or receptor-dependent migration.
| Annotation component | Conclusion | Evidence type/species | Confidence | Key limitation |
|---|---|---|---|---|
| Identity and architecture | A0A9L0T1D1 is annotated as Equus caballus C-X-C chemokine receptor type 3 (CXCR3), with chemokine-receptor and rhodopsin-like seven-transmembrane GPCR domains. | Supplied UniProt annotation; computational/domain classification | High for database identity; moderate for functional annotation | The accession-level annotation was not independently experimentally validated, and no horse protein study was retrieved. |
| Equine expression during exercise | CXCR3 mRNA increased in peripheral blood immediately after intense exercise; the reported overall change was 2.12-fold (p = 0.001) in 12 young Quarter Horses. | Direct equine RT-qPCR expression evidence (wilson2023differentialexpressionof pages 4-6, wilson2023differentialexpressionof pages 1-2, wilson2023differentialexpressionof pages 2-4) | Moderate | Transcript abundance does not establish receptor protein abundance, cell-surface localization, or activity; cohort was small and context-specific. |
| Equine EHV-1 ligand axis | EHV-1-infected primary equine respiratory epithelial cells increased CXCL9/CXCL10 expression and generated supernatants that recruited equine T lymphocytes; neurovirulent virus produced greater ligand expression/bioactivity, while viral gp2 deletion increased recruitment. This supports an active CXCR3-ligand environment but does not directly prove receptor dependence. | Direct equine ligand-expression and migration assays (poelaert2019equineherpesvirus1 pages 3-4, poelaert2019equineherpesvirus1 pages 1-2) | Moderate for ligand production and migration; low-to-moderate for CXCR3 attribution | CXCR3 was not directly measured, blocked, or genetically disrupted; numerical effect sizes were unavailable in the extracted evidence. |
| Canonical ligand recognition and Gi coupling | Human CXCR3 binds CXCL9–CXCL11; cryo-EM directly resolved a CXCL11–CXCR3–Gi complex and showed the chemokine N terminus entering the orthosteric pocket. Agonists PS372424 and VUF11222 use related but distinct activation modes, whereas SCH546738 binds an allosteric pocket between TM5 and TM6. | Direct human structural, mutagenesis, simulation, and signaling evidence (jiao2024structuralinsightsinto pages 8-9, jiao2024structuralinsightsinto pages 1-2, jiao2024structuralinsightsinto pages 2-3, jiao2024structuralinsightsinto pages 7-8, jiao2024structuralinsightsinto pages 3-5) | High for human CXCR3; moderate as an equine functional inference | Horse ligand binding, residue conservation, coupling selectivity, and pharmacology were not tested. |
| Plasma-membrane and endosomal trafficking | Activated human CXCR3 signals and is regulated at the plasma membrane and after trafficking to endosomes. Ligand-specific recruitment of GRK2/3/5/6 shapes β-arrestin engagement, internalization, and cytosolic versus nuclear ERK signaling; peak recruitment occurred at approximately 2 minutes at the membrane and 13 minutes at endosomes. | Direct cultured-cell trafficking, BRET, imaging, knockout/reconstitution, and signaling evidence (gardner2024gpcrkinasesdifferentially pages 3-4, gardner2024gpcrkinasesdifferentially pages 1-3, gardner2024gpcrkinasesdifferentially pages 32-36, gardner2024gpcrkinasesdifferentially pages 11-13, gardner2024gpcrkinasesdifferentially pages 9-11, gardner2024gpcrkinasesdifferentially pages 27-32) | High for tested human receptor systems; moderate as an equine inference | Overexpression and engineered-cell systems may not reproduce native equine leukocytes; equine trafficking has not been demonstrated. |
| Equine protein localization | Most likely a cell-surface seven-transmembrane receptor that can internalize into endosomes after activation. | Domain/orthology-based inference from canonical CXCR3 | Moderate inference only | No retrieved equine immunohistochemistry, flow cytometry, microscopy, proteomics, or trafficking experiment directly localized A0A9L0T1D1. |
| Equine ligand affinities and signaling potency | CXCL9, CXCL10, and CXCL11 are plausible cognate agonists, expected to promote Gi-dependent chemotactic signaling. | Mammalian orthology and human structural/pharmacological inference (jiao2024structuralinsightsinto pages 8-9, jiao2024structuralinsightsinto pages 1-2, dillemans2024naturalcarboxyterminaltruncation pages 1-3, dillemans2024naturalcarboxyterminaltruncation pages 7-8, dillemans2024naturalcarboxyterminaltruncation pages 5-7) | Moderate for ligand assignment; low for quantitative pharmacology | No equine binding constants, concentration–response curves, calcium-flux measurements, pertussis-toxin tests, or β-arrestin assays were found. |
| Equine isoforms | The existence and function of horse counterparts to human CXCR3A/CXCR3B or other splice forms remain undetermined. | Evidence gap | Unknown | No equine isoform-resolved transcript or protein evidence was retrieved; human isoform behavior should not be transferred automatically. |
| Equine loss-of-function phenotype | No horse knockout, knockdown, natural loss-of-function variant, or receptor-blockade phenotype was found. | Evidence gap | Unknown | Causality for equine leukocyte trafficking, infection, inflammation, exercise responses, or disease cannot presently be assigned specifically to A0A9L0T1D1. |
Table: Evidence-grading matrix separating direct equine findings from canonical human CXCR3 evidence and orthology-based inference. It highlights the strong structural assignment but substantial gaps in horse-specific protein pharmacology, localization, isoforms, and causal genetics.
The symbol CXCR3 matches the supplied protein description, “C-X-C chemokine receptor type 3.” The alternative name “interferon-inducible protein 10 receptor” is also consistent because IP-10 is the historical name for CXCL10, a canonical CXCR3 ligand. The organism is explicitly horse, Equus caballus. Searches for equine CXCR3 retrieved horse immune-expression and CXCL9/CXCL10 studies rather than a different gene with a coincident symbol.
A limitation is that no accession-specific publication or independent experimental validation of A0A9L0T1D1 was retrieved. Accordingly, the exact mapping between this UniProt entry and the experimentally measured equine CXCR3 transcripts should be treated as highly plausible but not demonstrated at the protein level.
The supplied InterPro assignments—GPCR_Rhodpsn_7TM, GPCR_Rhodpsn, Chemokine_rcpt, CCR1–9-like, and Chemokine_CXCR3—are mutually concordant. They predict an integral membrane, class-A/rhodopsin-like GPCR with an extracellular amino-terminal chemokine-recognition region, seven transmembrane helices, extracellular and intracellular loops, and a cytoplasmic carboxyl terminus involved in G-protein, GRK, and arrestin regulation.
This architecture agrees with the 2024 human CXCR3 cryo-EM structures. Those structures resolved active CXCR3 coupled to heterotrimeric Gi and bound to CXCL11 or synthetic agonists, as well as an antagonist-stabilized inactive receptor (published online 4 January 2024; DOI 10.1038/s41594-023-01175-5). (jiao2024structuralinsightsinto pages 1-2, jiao2024structuralinsightsinto pages 2-3)
CXCR3 is not an enzyme or transporter. It is a signaling receptor whose relevant “substrates” are extracellular chemokine ligands rather than molecules that are chemically transformed or transported. Canonical mammalian CXCR3 recognizes the interferon-inducible chemokines CXCL9, CXCL10, and CXCL11. Ligand gradients provide positional information, while receptor activation changes leukocyte adhesion, polarity, and motility.
The strongest current mechanistic evidence comes from human CXCR3. Cryo-EM directly visualized the CXCL11 amino terminus inserted into the receptor’s central orthosteric pocket. A proximal receptor Pro42–Cys43 region participates in chemokine recognition, while CXCL11’s N-terminal FPMF and KRGR motifs contact residues distributed across the extracellular receptor and transmembrane pocket. Mutating interacting receptor residues reduced CXCL11-stimulated signaling. (jiao2024structuralinsightsinto pages 2-3, jiao2024structuralinsightsinto pages 3-5)
Activation reorganizes the transmembrane bundle: extracellular portions of TM1, TM2, and TM5 move inward, while cytoplasmic TM6 moves outward and TM7 inward to expose the Gi-binding cavity. This breaks and reforms hydrophobic packing among TM3, TM5, TM6, and TM7. These structural changes provide a direct physical explanation for how chemokine binding is converted into intracellular Gi activation. (jiao2024structuralinsightsinto pages 7-8)
For the equine protein, assignment of CXCL9–CXCL11 as ligands is moderate-confidence orthology inference, not direct pharmacological proof. CXCL9 and CXCL10 are experimentally present and bioactive in equine inflammatory systems, but no retrieved study measured their affinity or potency at purified or heterologously expressed A0A9L0T1D1.
A0A9L0T1D1 is predicted to function principally in the plasma membrane, where its extracellular amino terminus and loops encounter chemokines and its cytoplasmic surface couples to signaling proteins. In canonical mammalian immunity, CXCR3 is especially associated with activated type-1 effector populations, including Th1-like CD4 cells and cytotoxic CD8 cells. The immediate functional outcome is directed migration toward CXCL9/CXCL10/CXCL11-rich tissue.
No retrieved equine study directly localized the A0A9L0T1D1 protein by validated antibody staining, flow cytometry, immunohistochemistry, microscopy, or proteomics. Therefore, cell-surface localization in horse should be annotated as strongly predicted from architecture and orthology, not equine experimental fact.
CXCR3 is not restricted to the cell surface after activation. A 2024 Science Signaling study showed in cultured human-receptor systems that agonist-activated CXCR3 recruits GRK2, GRK3, GRK5, and GRK6 differently at the plasma membrane and early endosomes. Maximum recruitment occurred at approximately 2 minutes at the plasma membrane versus 13 minutes at endosomes. The experiments used 100 nM CXCL9, CXCL10, or CXCL11 and generally five independent experiments. (gardner2024gpcrkinasesdifferentially pages 27-32)
GRK identity and location altered β-arrestin engagement, receptor internalization, and cytosolic versus nuclear ERK activity. Notably, CXCL11 recruited GRK2 robustly at the plasma membrane but not detectably at endosomes, illustrating that membrane recruitment does not simply predict the endosomal complex. The work was published 13 February 2024; DOI 10.1126/scisignal.add9139. (gardner2024gpcrkinasesdifferentially pages 1-3, gardner2024gpcrkinasesdifferentially pages 11-13, gardner2024gpcrkinasesdifferentially pages 9-11)
Thus, the best current localization model is plasma membrane → ligand-induced internalization → early endosome, with compartment-specific signaling and receptor regulation. Whether horse CXCR3 follows identical kinetics is untested.
Canonical CXCR3 activation engages heterotrimeric Gi/o-family signaling, demonstrated structurally by the active CXCL11–CXCR3–Gi complex. Expected proximal consequences include reduced adenylyl-cyclase/cAMP output and Gβγ-dependent pathways that produce intracellular calcium mobilization, ERK/MAPK and Akt activation, cytoskeletal polarization, integrin activation, and chemotaxis. Direct attribution of all these branches to equine A0A9L0T1D1 awaits horse-specific signaling assays. (jiao2024structuralinsightsinto pages 1-2, jiao2024structuralinsightsinto pages 2-3)
The 2024 structures reached 2.9–3.0 Å for three active complexes—CXCL11, PS372424, and VUF11222—and 3.6 Å for antagonist-bound inactive CXCR3. PS372424 partly mimics the CXCL11 N-terminal orthosteric binding mode, whereas VUF11222 penetrates more deeply and activates the receptor through a distinct arrangement involving the Trp268^6.48 microswitch. (jiao2024structuralinsightsinto pages 2-3, jiao2024structuralinsightsinto pages 7-8)
The antagonist SCH546738 occupies a noncompetitive hydrophobic pocket involving TM3, TM5, and TM6 rather than the central chemokine pocket. Mutations V261F and A265F weakened antagonism, supporting this allosteric site. These results provide a structure-based route for designing CXCR3 modulators, although horse cross-reactivity cannot be presumed without sequence and pharmacological validation. (jiao2024structuralinsightsinto pages 8-9)
CXCR3 does not generate one invariant signal. CXCL11 is more strongly biased toward receptor internalization than CXCL9 or CXCL10. In the 2024 GRK study, CXCL11 and the synthetic ligand VUF10661 were the most efficacious plasma-membrane recruiters of GRK2/3; CXCL9 produced little or no detectable GRK2/3 recruitment at physiological concentrations. Ligand-specific GRK assemblies then controlled β-arrestin, internalization, and ERK outputs. (jiao2024structuralinsightsinto pages 1-2, gardner2024gpcrkinasesdifferentially pages 3-4)
This is important for annotation: “CXCR3 signaling” is not a single linear pathway but a family of ligand-, kinase-, time-, and compartment-dependent states. Expert interpretation should therefore avoid assuming that CXCL9, CXCL10, and CXCL11 are interchangeable agonists.
A 2024 human study showed that natural processing of CXCL10 can sharply modify CXCR3A signaling. Removing four C-terminal residues to produce CXCL10(1–73) weakened binding affinity 32.4-fold for heparin, 3.7-fold for heparan sulfate, and 15.3-fold for chondroitin sulfate A. Apparent dissociation constants changed from 1.03 to 33.42 nM for heparin, 6.73 to 25.23 nM for heparan sulfate, and 33.40 to 512.40 nM for chondroitin sulfate A. (dillemans2024naturalcarboxyterminaltruncation pages 7-8, dillemans2024naturalcarboxyterminaltruncation pages 5-7)
The truncated ligand required approximately 135–270 nM to generate calcium responses comparable to 1 nM intact CXCL10 and only weakly activated ERK1/2 and Akt at 270 nM. In primary human CD4⁺CXCR3⁺ cells, intact ligand induced significant migration from 1 nM, whereas truncated CXCL10 required 10 nM. The study was published in February 2024; DOI 10.1186/s12964-023-01453-1. (dillemans2024naturalcarboxyterminaltruncation pages 7-8, dillemans2024naturalcarboxyterminaltruncation pages 5-7)
Interestingly, truncation retained antiangiogenic effects in human microvascular endothelial assays despite weakened CXCR3A signaling. This cautions against assigning every CXCL10-associated vascular effect directly to conventional CXCR3A. (dillemans2024naturalcarboxyterminaltruncation pages 1-3, dillemans2024naturalcarboxyterminaltruncation pages 8-10)
The clearest recent receptor-specific equine evidence is a 2023 study of 12 healthy racing-bred American Quarter Horses, comprising six colts and six fillies aged 22–26 months. Blood was collected before and immediately after a 1.2-mile gallop followed by a 0.6-mile jog. An 84-gene equine immune RT-qPCR array found overall CXCR3 transcript upregulation of 2.12-fold, p = 0.001. Reported sex-stratified changes were 1.10-fold in females (p = 0.044) and 1.21-fold in males (p = 0.029). The study was published 16 January 2023; DOI 10.3390/ani13020308. (wilson2023differentialexpressionof pages 4-6, wilson2023differentialexpressionof pages 1-2, wilson2023differentialexpressionof pages 2-4)
The authors interpreted the broader expression profile as activation of chemokine, NF-κB, and Th1/Th2-related inflammatory pathways after acute exercise. CXCR3 may therefore contribute to exercise-associated immune-cell redistribution and could form part of a biomarker panel for excessive training stress. However, this was a small transcript study: it did not identify the expressing leukocyte subset, measure receptor protein, or demonstrate chemotaxis.
The apparent mismatch between the 2.12-fold overall estimate and smaller sex-stratified fold values warrants caution; it may reflect different analytical contrasts or reporting conventions in the paper and should not be reinterpreted as a direct weighted average.
Primary equine respiratory epithelial cells infected with EHV-1 increased expression of the CXCR3 ligands CXCL9 and CXCL10. Neurovirulent virus produced greater chemokine expression and bioactivity than abortigenic virus. Supernatants recruited equine T lymphocytes in Boyden-chamber assays, and deleting viral glycoprotein 2 increased recruitment of both T cells and CD172a⁺ monocytic cells. The paper was published in September/November 2019; DOI 10.1099/jgv.0.001317. (poelaert2019equineherpesvirus1 pages 3-4, poelaert2019equineherpesvirus1 pages 1-2)
This supports a biologically active equine interferon–CXCL9/CXCL10–leukocyte-homing system in the respiratory tract and suggests that EHV-1 manipulates chemokine-mediated recruitment. Nevertheless, CXCR3 was not directly measured, blocked, or disrupted. The migration response therefore cannot be assigned exclusively to CXCR3 from this experiment.
The most precise process annotation for equine CXCR3 is chemokine-guided leukocyte trafficking during type-1 inflammation. In the proposed sequence:
For horse, steps 1 and chemokine-associated migration have direct support in EHV-1 respiratory models, while exercise-dependent CXCR3 transcription supports regulated receptor availability. Steps 2–6 are principally inferred from mammalian/human mechanisms.
CXCR3 transcript measurement has been proposed as part of a multi-gene approach to monitor acute inflammatory responses and possible overtraining in performance horses. The 2023 cohort demonstrates analytical feasibility, but 12 animals are insufficient for a validated diagnostic threshold, and the sex- and individual-dependent variation argues against using CXCR3 alone. (wilson2023differentialexpressionof pages 4-6, wilson2023differentialexpressionof pages 1-2)
In EHV-1, CXCL9/CXCL10-associated recruitment offers a mechanistic readout for comparing neurovirulent and abortigenic strains and studying viral gp2-mediated immune evasion. Receptor-blocking experiments in primary equine lymphocytes would be required before CXCR3 could be considered a validated veterinary therapeutic target. (poelaert2019equineherpesvirus1 pages 3-4, poelaert2019equineherpesvirus1 pages 1-2)
The 2024 structural work identifies both the chemokine orthosteric cavity and a TM5/TM6 allosteric antagonist pocket, while the GRK study shows that candidate drugs should be evaluated for G-protein, arrestin, internalization, and compartment-specific ERK bias rather than only ligand binding. These are authoritative mechanistic foundations for human drug discovery but not evidence that SCH546738, AMG487, or other human CXCR3 ligands have suitable affinity, efficacy, safety, or pharmacokinetics in horses. (jiao2024structuralinsightsinto pages 8-9, gardner2024gpcrkinasesdifferentially pages 3-4, gardner2024gpcrkinasesdifferentially pages 1-3)
No retrieved horse study directly established:
Accordingly, a conservative functional annotation is:
Predicted equine C-X-C chemokine receptor type 3: a rhodopsin-like seven-transmembrane chemokine GPCR expected to bind interferon-inducible CXCL9, CXCL10, and CXCL11 and activate Gi-dependent signaling that promotes migration of activated type-1 effector lymphocytes. Functions initially at the plasma membrane and is expected to undergo ligand-dependent GRK/β-arrestin-regulated internalization and endosomal signaling. Equine evidence supports regulated CXCR3 mRNA expression and CXCL9/CXCL10-associated leukocyte migration, but receptor pharmacology and localization have not been directly demonstrated.
A0A9L0T1D1 is not symbol-ambiguous in the supplied context: its name, horse origin, and domain architecture coherently identify it as equine CXCR3. Its primary role is best understood as a chemokine-gradient sensor and signaling organizer for inflammatory lymphocyte trafficking, rather than as an enzyme, transporter, or structural protein. The receptor’s detailed molecular mechanism is strongly supported by 2024 human structural and signaling studies, but horse-specific evidence remains limited to transcript regulation and ligand-associated migration systems. The annotation should therefore explicitly distinguish direct equine evidence from high-confidence mammalian orthology inference.
References
(wilson2023differentialexpressionof pages 4-6): Judith Wilson, Marcos De Donato, Brooke Appelbaum, Carly Turner Garcia, and Sunday Peters. Differential expression of innate and adaptive immune genes during acute physical exercise in american quarter horses. Jan 2023. URL: https://doi.org/10.3390/ani13020308, doi:10.3390/ani13020308. This article has 13 citations and is from a peer-reviewed journal.
(wilson2023differentialexpressionof pages 1-2): Judith Wilson, Marcos De Donato, Brooke Appelbaum, Carly Turner Garcia, and Sunday Peters. Differential expression of innate and adaptive immune genes during acute physical exercise in american quarter horses. Jan 2023. URL: https://doi.org/10.3390/ani13020308, doi:10.3390/ani13020308. This article has 13 citations and is from a peer-reviewed journal.
(wilson2023differentialexpressionof pages 2-4): Judith Wilson, Marcos De Donato, Brooke Appelbaum, Carly Turner Garcia, and Sunday Peters. Differential expression of innate and adaptive immune genes during acute physical exercise in american quarter horses. Jan 2023. URL: https://doi.org/10.3390/ani13020308, doi:10.3390/ani13020308. This article has 13 citations and is from a peer-reviewed journal.
(poelaert2019equineherpesvirus1 pages 3-4): Katrien C. K. Poelaert, Jolien Van Cleemput, Kathlyn Laval, Jiexiong Xie, Herman W. Favoreel, and Hans J. Nauwynck. Equine herpesvirus 1 infection orchestrates the expression of chemokines in equine respiratory epithelial cells. The Journal of general virology, 100:1567-1579, Nov 2019. URL: https://doi.org/10.1099/jgv.0.001317, doi:10.1099/jgv.0.001317. This article has 13 citations.
(poelaert2019equineherpesvirus1 pages 1-2): Katrien C. K. Poelaert, Jolien Van Cleemput, Kathlyn Laval, Jiexiong Xie, Herman W. Favoreel, and Hans J. Nauwynck. Equine herpesvirus 1 infection orchestrates the expression of chemokines in equine respiratory epithelial cells. The Journal of general virology, 100:1567-1579, Nov 2019. URL: https://doi.org/10.1099/jgv.0.001317, doi:10.1099/jgv.0.001317. This article has 13 citations.
(jiao2024structuralinsightsinto pages 8-9): Haizhan Jiao, Bin Pang, Aijun Liu, Qiang Chen, Qi Pan, Xiankun Wang, Yunong Xu, Ying-Chih Chiang, Ruobing Ren, and Hongli Hu. Structural insights into the activation and inhibition of cxc chemokine receptor 3. Nature Structural & Molecular Biology, 31:610-620, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01175-5, doi:10.1038/s41594-023-01175-5. This article has 49 citations and is from a highest quality peer-reviewed journal.
(jiao2024structuralinsightsinto pages 1-2): Haizhan Jiao, Bin Pang, Aijun Liu, Qiang Chen, Qi Pan, Xiankun Wang, Yunong Xu, Ying-Chih Chiang, Ruobing Ren, and Hongli Hu. Structural insights into the activation and inhibition of cxc chemokine receptor 3. Nature Structural & Molecular Biology, 31:610-620, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01175-5, doi:10.1038/s41594-023-01175-5. This article has 49 citations and is from a highest quality peer-reviewed journal.
(jiao2024structuralinsightsinto pages 2-3): Haizhan Jiao, Bin Pang, Aijun Liu, Qiang Chen, Qi Pan, Xiankun Wang, Yunong Xu, Ying-Chih Chiang, Ruobing Ren, and Hongli Hu. Structural insights into the activation and inhibition of cxc chemokine receptor 3. Nature Structural & Molecular Biology, 31:610-620, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01175-5, doi:10.1038/s41594-023-01175-5. This article has 49 citations and is from a highest quality peer-reviewed journal.
(jiao2024structuralinsightsinto pages 7-8): Haizhan Jiao, Bin Pang, Aijun Liu, Qiang Chen, Qi Pan, Xiankun Wang, Yunong Xu, Ying-Chih Chiang, Ruobing Ren, and Hongli Hu. Structural insights into the activation and inhibition of cxc chemokine receptor 3. Nature Structural & Molecular Biology, 31:610-620, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01175-5, doi:10.1038/s41594-023-01175-5. This article has 49 citations and is from a highest quality peer-reviewed journal.
(jiao2024structuralinsightsinto pages 3-5): Haizhan Jiao, Bin Pang, Aijun Liu, Qiang Chen, Qi Pan, Xiankun Wang, Yunong Xu, Ying-Chih Chiang, Ruobing Ren, and Hongli Hu. Structural insights into the activation and inhibition of cxc chemokine receptor 3. Nature Structural & Molecular Biology, 31:610-620, Jan 2024. URL: https://doi.org/10.1038/s41594-023-01175-5, doi:10.1038/s41594-023-01175-5. This article has 49 citations and is from a highest quality peer-reviewed journal.
(gardner2024gpcrkinasesdifferentially pages 3-4): Julia Gardner, Dylan Scott Eiger, Chloe Hicks, Issac Choi, Uyen Pham, Anand Chundi, Ojas Namjoshi, and Sudarshan Rajagopal. Gpcr kinases differentially modulate biased signaling downstream of cxcr3 depending on their subcellular localization. Science Signaling, Feb 2024. URL: https://doi.org/10.1126/scisignal.add9139, doi:10.1126/scisignal.add9139. This article has 36 citations and is from a domain leading peer-reviewed journal.
(gardner2024gpcrkinasesdifferentially pages 1-3): Julia Gardner, Dylan Scott Eiger, Chloe Hicks, Issac Choi, Uyen Pham, Anand Chundi, Ojas Namjoshi, and Sudarshan Rajagopal. Gpcr kinases differentially modulate biased signaling downstream of cxcr3 depending on their subcellular localization. Science Signaling, Feb 2024. URL: https://doi.org/10.1126/scisignal.add9139, doi:10.1126/scisignal.add9139. This article has 36 citations and is from a domain leading peer-reviewed journal.
(gardner2024gpcrkinasesdifferentially pages 32-36): Julia Gardner, Dylan Scott Eiger, Chloe Hicks, Issac Choi, Uyen Pham, Anand Chundi, Ojas Namjoshi, and Sudarshan Rajagopal. Gpcr kinases differentially modulate biased signaling downstream of cxcr3 depending on their subcellular localization. Science Signaling, Feb 2024. URL: https://doi.org/10.1126/scisignal.add9139, doi:10.1126/scisignal.add9139. This article has 36 citations and is from a domain leading peer-reviewed journal.
(gardner2024gpcrkinasesdifferentially pages 11-13): Julia Gardner, Dylan Scott Eiger, Chloe Hicks, Issac Choi, Uyen Pham, Anand Chundi, Ojas Namjoshi, and Sudarshan Rajagopal. Gpcr kinases differentially modulate biased signaling downstream of cxcr3 depending on their subcellular localization. Science Signaling, Feb 2024. URL: https://doi.org/10.1126/scisignal.add9139, doi:10.1126/scisignal.add9139. This article has 36 citations and is from a domain leading peer-reviewed journal.
(gardner2024gpcrkinasesdifferentially pages 9-11): Julia Gardner, Dylan Scott Eiger, Chloe Hicks, Issac Choi, Uyen Pham, Anand Chundi, Ojas Namjoshi, and Sudarshan Rajagopal. Gpcr kinases differentially modulate biased signaling downstream of cxcr3 depending on their subcellular localization. Science Signaling, Feb 2024. URL: https://doi.org/10.1126/scisignal.add9139, doi:10.1126/scisignal.add9139. This article has 36 citations and is from a domain leading peer-reviewed journal.
(gardner2024gpcrkinasesdifferentially pages 27-32): Julia Gardner, Dylan Scott Eiger, Chloe Hicks, Issac Choi, Uyen Pham, Anand Chundi, Ojas Namjoshi, and Sudarshan Rajagopal. Gpcr kinases differentially modulate biased signaling downstream of cxcr3 depending on their subcellular localization. Science Signaling, Feb 2024. URL: https://doi.org/10.1126/scisignal.add9139, doi:10.1126/scisignal.add9139. This article has 36 citations and is from a domain leading peer-reviewed journal.
(dillemans2024naturalcarboxyterminaltruncation pages 1-3): Luna Dillemans, Karen Yu, Alexandra De Zutter, Sam Noppen, Mieke Gouwy, Nele Berghmans, Lisa Verhallen, Mirre De Bondt, Lotte Vanbrabant, Stef Brusselmans, Erik Martens, Dominique Schols, Patrick Verschueren, Mette M. Rosenkilde, Pedro Elias Marques, Sofie Struyf, and Paul Proost. Natural carboxyterminal truncation of human cxcl10 attenuates glycosaminoglycan binding, cxcr3a signaling and lymphocyte chemotaxis, while retaining angiostatic activity. Cell Communication and Signaling : CCS, Feb 2024. URL: https://doi.org/10.1186/s12964-023-01453-1, doi:10.1186/s12964-023-01453-1. This article has 14 citations.
(dillemans2024naturalcarboxyterminaltruncation pages 7-8): Luna Dillemans, Karen Yu, Alexandra De Zutter, Sam Noppen, Mieke Gouwy, Nele Berghmans, Lisa Verhallen, Mirre De Bondt, Lotte Vanbrabant, Stef Brusselmans, Erik Martens, Dominique Schols, Patrick Verschueren, Mette M. Rosenkilde, Pedro Elias Marques, Sofie Struyf, and Paul Proost. Natural carboxyterminal truncation of human cxcl10 attenuates glycosaminoglycan binding, cxcr3a signaling and lymphocyte chemotaxis, while retaining angiostatic activity. Cell Communication and Signaling : CCS, Feb 2024. URL: https://doi.org/10.1186/s12964-023-01453-1, doi:10.1186/s12964-023-01453-1. This article has 14 citations.
(dillemans2024naturalcarboxyterminaltruncation pages 5-7): Luna Dillemans, Karen Yu, Alexandra De Zutter, Sam Noppen, Mieke Gouwy, Nele Berghmans, Lisa Verhallen, Mirre De Bondt, Lotte Vanbrabant, Stef Brusselmans, Erik Martens, Dominique Schols, Patrick Verschueren, Mette M. Rosenkilde, Pedro Elias Marques, Sofie Struyf, and Paul Proost. Natural carboxyterminal truncation of human cxcl10 attenuates glycosaminoglycan binding, cxcr3a signaling and lymphocyte chemotaxis, while retaining angiostatic activity. Cell Communication and Signaling : CCS, Feb 2024. URL: https://doi.org/10.1186/s12964-023-01453-1, doi:10.1186/s12964-023-01453-1. This article has 14 citations.
(dillemans2024naturalcarboxyterminaltruncation pages 8-10): Luna Dillemans, Karen Yu, Alexandra De Zutter, Sam Noppen, Mieke Gouwy, Nele Berghmans, Lisa Verhallen, Mirre De Bondt, Lotte Vanbrabant, Stef Brusselmans, Erik Martens, Dominique Schols, Patrick Verschueren, Mette M. Rosenkilde, Pedro Elias Marques, Sofie Struyf, and Paul Proost. Natural carboxyterminal truncation of human cxcl10 attenuates glycosaminoglycan binding, cxcr3a signaling and lymphocyte chemotaxis, while retaining angiostatic activity. Cell Communication and Signaling : CCS, Feb 2024. URL: https://doi.org/10.1186/s12964-023-01453-1, doi:10.1186/s12964-023-01453-1. This article has 14 citations.