-
1
-
-
81555213635
-
Pharmacological modulation of chemokine receptor function
-
1 Scholten, D.J., et al. Pharmacological modulation of chemokine receptor function. Br J Pharmacol 165 (2011), 1617–1643.
-
(2011)
Br J Pharmacol
, vol.165
, pp. 1617-1643
-
-
Scholten, D.J.1
-
2
-
-
84886819170
-
The fine balance of chemokines during disease: trafficking, inflammation, and homeostasis
-
E.A. Cardona E.E. Ubogu Humana Press Totowa, NJ
-
2 Cardona, S.M., Garcia, J.A., Cardona, A.E., The fine balance of chemokines during disease: trafficking, inflammation, and homeostasis. Cardona, E.A., Ubogu, E.E., (eds.) Chemokines: Methods and Protocols, 2013, Humana Press, Totowa, NJ, 1–16.
-
(2013)
Chemokines: Methods and Protocols
, pp. 1-16
-
-
Cardona, S.M.1
Garcia, J.A.2
Cardona, A.E.3
-
3
-
-
41149154050
-
G protein-coupled receptor sorting to endosomes and lysosomes
-
3 Marchese, A., et al. G protein-coupled receptor sorting to endosomes and lysosomes. Annu Rev Pharmacol Toxicol 48 (2008), 601–629.
-
(2008)
Annu Rev Pharmacol Toxicol
, vol.48
, pp. 601-629
-
-
Marchese, A.1
-
4
-
-
84928803976
-
Potent anti-HIV chemokine analogs direct post-endocytic sorting of CCR5
-
4 Bönsch, C., et al. Potent anti-HIV chemokine analogs direct post-endocytic sorting of CCR5. PLOS ONE, 10, 2015, e0125396.
-
(2015)
PLOS ONE
, vol.10
, pp. e0125396
-
-
Bönsch, C.1
-
5
-
-
84887512970
-
International Union of Basic and Clinical Pharmacology. LXXXIX. Update on the extended family of chemokine receptors and introducing a new nomenclature for atypical chemokine receptors
-
5 Bachelerie, F., et al. International Union of Basic and Clinical Pharmacology. LXXXIX. Update on the extended family of chemokine receptors and introducing a new nomenclature for atypical chemokine receptors. Pharmacol Rev 66 (2014), 1–79.
-
(2014)
Pharmacol Rev
, vol.66
, pp. 1-79
-
-
Bachelerie, F.1
-
6
-
-
84905658091
-
Biased and G protein-independent signaling of chemokine receptors
-
6 Steen, A., et al. Biased and G protein-independent signaling of chemokine receptors. Front Immunol, 5, 2014.
-
(2014)
Front Immunol
, vol.5
-
-
Steen, A.1
-
7
-
-
84958603422
-
CXCL12/CXCR4: a symbiotic bridge linking cancer cells and their stromal neighbors in oncogenic communication networks
-
7 Guo, F., et al. CXCL12/CXCR4: a symbiotic bridge linking cancer cells and their stromal neighbors in oncogenic communication networks. Oncogene 35 (2016), 816–826.
-
(2016)
Oncogene
, vol.35
, pp. 816-826
-
-
Guo, F.1
-
8
-
-
76249134336
-
β-Arrestin- but not G protein-mediated signaling by the “decoy” receptor CXCR7
-
8 Rajagopal, S., et al. β-Arrestin- but not G protein-mediated signaling by the “decoy” receptor CXCR7. Proc Natl Acad Sci U S A 107 (2010), 628–632.
-
(2010)
Proc Natl Acad Sci U S A
, vol.107
, pp. 628-632
-
-
Rajagopal, S.1
-
9
-
-
84924364300
-
Selective and dual targeting of CCR2 and CCR5 receptors: a current overview
-
N. Tschammer Springer International Publishing Cham
-
9 Junker, A., et al. Selective and dual targeting of CCR2 and CCR5 receptors: a current overview. Tschammer, N., (eds.) Chemokines: Chemokines and their Receptors in Drug Discovery, 2015, Springer International Publishing, Cham, 187–241.
-
(2015)
Chemokines: Chemokines and their Receptors in Drug Discovery
, pp. 187-241
-
-
Junker, A.1
-
10
-
-
84962698261
-
Tumoral immune cell exploitation in colorectal cancer metastases can be targeted effectively by anti-CCR5 therapy in cancer patients
-
10 Halama, N., et al. Tumoral immune cell exploitation in colorectal cancer metastases can be targeted effectively by anti-CCR5 therapy in cancer patients. Cancer Cell 29 (2016), 587–601.
-
(2016)
Cancer Cell
, vol.29
, pp. 587-601
-
-
Halama, N.1
-
11
-
-
84873468174
-
Targeting tumor-infiltrating macrophages decreases tumor-initiating cells, relieves immunosuppression, and improves chemotherapeutic responses
-
11 Mitchem, J.B., et al. Targeting tumor-infiltrating macrophages decreases tumor-initiating cells, relieves immunosuppression, and improves chemotherapeutic responses. Cancer Res 73 (2013), 1128–1141.
-
(2013)
Cancer Res
, vol.73
, pp. 1128-1141
-
-
Mitchem, J.B.1
-
12
-
-
84926505274
-
Modulation of cellular signaling by herpesvirus-encoded G protein-coupled receptors
-
12 de Munnik, S.M., et al. Modulation of cellular signaling by herpesvirus-encoded G protein-coupled receptors. Front Pharmacol, 6, 2015.
-
(2015)
Front Pharmacol
, vol.6
-
-
de Munnik, S.M.1
-
13
-
-
79955476625
-
Overcoming hurdles in developing successful drugs targeting chemokine receptors
-
13 Schall, T.J., Proudfoot, A.E.I., Overcoming hurdles in developing successful drugs targeting chemokine receptors. Nat Rev Immunol 11 (2011), 355–363.
-
(2011)
Nat Rev Immunol
, vol.11
, pp. 355-363
-
-
Schall, T.J.1
Proudfoot, A.E.I.2
-
14
-
-
27644510382
-
Maraviroc (UK-427,857), a potent, orally bioavailable, and selective small-molecule inhibitor of chemokine receptor CCR5 with broad-spectrum anti-human immunodeficiency virus type 1 activity
-
14 Dorr, P., et al. Maraviroc (UK-427,857), a potent, orally bioavailable, and selective small-molecule inhibitor of chemokine receptor CCR5 with broad-spectrum anti-human immunodeficiency virus type 1 activity. Antimicrob Agents Chemother 49 (2005), 4721–4732.
-
(2005)
Antimicrob Agents Chemother
, vol.49
, pp. 4721-4732
-
-
Dorr, P.1
-
15
-
-
78049255337
-
Recent advances on the use of the CXCR4 antagonist plerixafor (AMD3100, Mozobil(TM)) and potential of other CXCR4 antagonists as stem cell mobilizers
-
15 De Clercq, E., Recent advances on the use of the CXCR4 antagonist plerixafor (AMD3100, Mozobil(TM)) and potential of other CXCR4 antagonists as stem cell mobilizers. Pharmacol Ther 128 (2010), 509–518.
-
(2010)
Pharmacol Ther
, vol.128
, pp. 509-518
-
-
De Clercq, E.1
-
16
-
-
84941578575
-
Dual targeting of the chemokine receptors CXCR4 and ACKR3 with novel engineered chemokines
-
Identification of novel chemokines binding CXCR4 and ACKR3 using phage display and the scaffold of the CXCL12 chemokine. Numerous N-terminal residue substitutions in CXCL12 produced high affinity CXCR4 antagonists; however, N-terminal truncations invariably led to loss of affinity that could not be reversed by manipulating the remaining N-terminal residues. The best CXCR4 antagonist demonstrated anti-inflammatory efficacy in vivo.
-
16• Hanes, M.S., et al. Dual targeting of the chemokine receptors CXCR4 and ACKR3 with novel engineered chemokines. J Biol Chem 290 (2015), 22385–22397 Identification of novel chemokines binding CXCR4 and ACKR3 using phage display and the scaffold of the CXCL12 chemokine. Numerous N-terminal residue substitutions in CXCL12 produced high affinity CXCR4 antagonists; however, N-terminal truncations invariably led to loss of affinity that could not be reversed by manipulating the remaining N-terminal residues. The best CXCR4 antagonist demonstrated anti-inflammatory efficacy in vivo.
-
(2015)
J Biol Chem
, vol.290
, pp. 22385-22397
-
-
Hanes, M.S.1
-
17
-
-
84936818794
-
Rationally designed chemokine-based toxin targeting the viral G protein-coupled receptor US28 potently inhibits cytomegalovirus infection in vivo
-
3CR1 and towards the virally encoded US28. The resulting protein is used as a toxin carrier and shown to selectively kill infected, US28-expressing cells in vivo.
-
3CR1 and towards the virally encoded US28. The resulting protein is used as a toxin carrier and shown to selectively kill infected, US28-expressing cells in vivo.
-
(2015)
Proc Natl Acad Sci
, vol.112
, pp. 8427-8432
-
-
Spiess, K.1
-
18
-
-
84883355779
-
Neutralizing nanobodies targeting diverse chemokines effectively inhibit chemokine function
-
18 Blanchetot, C., et al. Neutralizing nanobodies targeting diverse chemokines effectively inhibit chemokine function. J Biol Chem 288 (2013), 25173–25182.
-
(2013)
J Biol Chem
, vol.288
, pp. 25173-25182
-
-
Blanchetot, C.1
-
19
-
-
84882990634
-
Development and preclinical characterization of a humanized antibody targeting CXCL12
-
19 Zhong, C., et al. Development and preclinical characterization of a humanized antibody targeting CXCL12. Clin Cancer Res 19 (2013), 4433–4445.
-
(2013)
Clin Cancer Res
, vol.19
, pp. 4433-4445
-
-
Zhong, C.1
-
20
-
-
84885594077
-
Llama-derived single variable domains (nanobodies) directed against chemokine receptor CXCR7 reduce head and neck cancer cell growth in vivo
-
20 Maussang, D., et al. Llama-derived single variable domains (nanobodies) directed against chemokine receptor CXCR7 reduce head and neck cancer cell growth in vivo. J Biol Chem 288 (2013), 29562–29572.
-
(2013)
J Biol Chem
, vol.288
, pp. 29562-29572
-
-
Maussang, D.1
-
21
-
-
78650573881
-
CXCR4 nanobodies (VHH-based single variable domains) potently inhibit chemotaxis and HIV-1 replication and mobilize stem cells
-
21 Jahnichen, S., et al. CXCR4 nanobodies (VHH-based single variable domains) potently inhibit chemotaxis and HIV-1 replication and mobilize stem cells. Proc Natl Acad Sci U S A 107 (2010), 20565–20570.
-
(2010)
Proc Natl Acad Sci U S A
, vol.107
, pp. 20565-20570
-
-
Jahnichen, S.1
-
22
-
-
84926650425
-
Chemokine receptor specific antibodies in cancer immunotherapy: achievements and challenges
-
22 Vela, M., et al. Chemokine receptor specific antibodies in cancer immunotherapy: achievements and challenges. Front Immunol, 6, 2015.
-
(2015)
Front Immunol
, vol.6
-
-
Vela, M.1
-
23
-
-
77957349209
-
Phase 2a study of the CCR5 monoclonal antibody PRO 140 administered intravenously to HIV-infected adults
-
23 Jacobson, J.M., et al. Phase 2a study of the CCR5 monoclonal antibody PRO 140 administered intravenously to HIV-infected adults. Antimicrob Agents Chemother 54 (2010), 4137–4142.
-
(2010)
Antimicrob Agents Chemother
, vol.54
, pp. 4137-4142
-
-
Jacobson, J.M.1
-
24
-
-
84857603968
-
Spiegelmer NOX-E36 for renal diseases
-
J. Kurreck The Royal Society of Chemistry Cambridge, UK
-
24 Eulberg, D., et al. Spiegelmer NOX-E36 for renal diseases. Kurreck, J., (eds.) Therapeutic Oligonucleotides, 2008, The Royal Society of Chemistry, Cambridge, UK, 200–225.
-
(2008)
Therapeutic Oligonucleotides
, pp. 200-225
-
-
Eulberg, D.1
-
25
-
-
84928789604
-
Crystal structure of a mirror-image L-RNA aptamer (Spiegelmer) in complex with the natural L-protein target CCL2
-
10 helix following the N-loop of the chemokine. The crystallographically observed contacts are supported by CCL2 mutagenesis. Structure analysis explains the moderately reduced affinity of the L-aptamer to CCL8, CCL11, and CCL13.
-
10 helix following the N-loop of the chemokine. The crystallographically observed contacts are supported by CCL2 mutagenesis. Structure analysis explains the moderately reduced affinity of the L-aptamer to CCL8, CCL11, and CCL13.
-
(2015)
Nat Commun
, vol.6
-
-
Oberthur, D.1
-
26
-
-
84897880564
-
The Spiegelmer NOX-A12, a novel CXCL12 inhibitor, interferes with chronic lymphocytic leukemia cell motility and causes chemosensitization
-
26 Hoellenriegel, J., et al. The Spiegelmer NOX-A12, a novel CXCL12 inhibitor, interferes with chronic lymphocytic leukemia cell motility and causes chemosensitization. Blood 123 (2014), 1032–1039.
-
(2014)
Blood
, vol.123
, pp. 1032-1039
-
-
Hoellenriegel, J.1
-
27
-
-
84925345390
-
Phase 1/2 study of mogamulizumab, a defucosylated anti-CCR4 antibody, in previously treated patients with cutaneous T-cell lymphoma
-
27 Duvic, M., et al. Phase 1/2 study of mogamulizumab, a defucosylated anti-CCR4 antibody, in previously treated patients with cutaneous T-cell lymphoma. Blood 125 (2015), 1883–1889.
-
(2015)
Blood
, vol.125
, pp. 1883-1889
-
-
Duvic, M.1
-
28
-
-
85027927015
-
Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists
-
28 Wu, B., et al. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 330 (2010), 1066–1071.
-
(2010)
Science
, vol.330
, pp. 1066-1071
-
-
Wu, B.1
-
29
-
-
84884673669
-
Structure of the CCR5 chemokine receptor-HIV entry inhibitor Maraviroc complex
-
29 Tan, Q., et al. Structure of the CCR5 chemokine receptor-HIV entry inhibitor Maraviroc complex. Science 341 (2013), 1387–1390.
-
(2013)
Science
, vol.341
, pp. 1387-1390
-
-
Tan, Q.1
-
30
-
-
84924565531
-
Crystal structure of the chemokine receptor CXCR4 in complex with a viral chemokine
-
The report of the first X-ray structure of a receptor:chemokine complex, that of human CXC chemokine receptor 4 with a herpesvirus-encoded chemokine antagonist vMIP-II, solved to 3.1 Å resolution. The crystallization-quality complex material was obtained by model-guided disulfide trapping. The paper provides a thorough comparison of the chemokine-bound CXCR4 with CXCR4 in complexes with a small molecule and a synthetic peptide antagonist, and also draws implications for other receptor:chemokine pairs based on homology modeling and bioinformatics.
-
30•• Qin, L., et al. Crystal structure of the chemokine receptor CXCR4 in complex with a viral chemokine. Science 347 (2015), 1117–1122 The report of the first X-ray structure of a receptor:chemokine complex, that of human CXC chemokine receptor 4 with a herpesvirus-encoded chemokine antagonist vMIP-II, solved to 3.1 Å resolution. The crystallization-quality complex material was obtained by model-guided disulfide trapping. The paper provides a thorough comparison of the chemokine-bound CXCR4 with CXCR4 in complexes with a small molecule and a synthetic peptide antagonist, and also draws implications for other receptor:chemokine pairs based on homology modeling and bioinformatics.
-
(2015)
Science
, vol.347
, pp. 1117-1122
-
-
Qin, L.1
-
31
-
-
84924561288
-
Structural basis for chemokine recognition and activation of a viral G protein-coupled receptor
-
3CL1 (fractalkine) that is known for its extremely slow dissociation kinetics. The higher resolution structure (2.9 Å) is stabilized by a nanobody. The complex architecture is consistent with that observed for the CXCR4:vMIP-II complex. US28 is found in an active-like conformation. Molecular dynamics simulations suggest an atomic-level explanation for the constitutive activity of the receptor.
-
3CL1 (fractalkine) that is known for its extremely slow dissociation kinetics. The higher resolution structure (2.9 Å) is stabilized by a nanobody. The complex architecture is consistent with that observed for the CXCR4:vMIP-II complex. US28 is found in an active-like conformation. Molecular dynamics simulations suggest an atomic-level explanation for the constitutive activity of the receptor.
-
(2015)
Science
, vol.347
, pp. 1113-1117
-
-
Burg, J.S.1
-
32
-
-
84924119193
-
Structures of human CCL18, CCL3, and CCL4 reveal molecular determinants for quaternary structures and sensitivity to insulin-degrading enzyme
-
32 Liang, W.G., et al. Structures of human CCL18, CCL3, and CCL4 reveal molecular determinants for quaternary structures and sensitivity to insulin-degrading enzyme. J Mol Biol 427:Part B (2015), 1345–1358.
-
(2015)
J Mol Biol
, vol.427
, pp. 1345-1358
-
-
Liang, W.G.1
-
33
-
-
84965115147
-
Structural basis for oligomerization and glycosaminoglycan binding of CCL5 and CCL3
-
33 Liang, W.G., et al. Structural basis for oligomerization and glycosaminoglycan binding of CCL5 and CCL3. Proc Natl Acad Sci 113 (2016), 5000–5005.
-
(2016)
Proc Natl Acad Sci
, vol.113
, pp. 5000-5005
-
-
Liang, W.G.1
-
34
-
-
0034725586
-
The crystal structure of the chemokine domain of fractalkine shows a novel quaternary arrangement
-
34 Hoover, D.M., et al. The crystal structure of the chemokine domain of fractalkine shows a novel quaternary arrangement. J Biol Chem 275 (2000), 23187–23193.
-
(2000)
J Biol Chem
, vol.275
, pp. 23187-23193
-
-
Hoover, D.M.1
-
35
-
-
84947933465
-
Engineering metamorphic chemokine lymphotactin/XCL1 into the GAG-binding, HIV-inhibitory dimer conformation
-
35 Fox, J.C., et al. Engineering metamorphic chemokine lymphotactin/XCL1 into the GAG-binding, HIV-inhibitory dimer conformation. ACS Chem Biol 10 (2015), 2580–2588.
-
(2015)
ACS Chem Biol
, vol.10
, pp. 2580-2588
-
-
Fox, J.C.1
-
36
-
-
84953289345
-
Parallel evolution of chemokine binding by structurally related herpesvirus decoy receptors
-
A crystal structure of herpesvirus-encoded chemokine inhibitor R17 in complex with mouse CCL3. The N-loop is characterized as a determinant of chemokine recognition by R17 while the 40s loop promotes formation of a kinetically stable complex. The unifying features of chemokine recognition are inferred by thorough comparison of the structure with receptor:chemokine structures as well as chemokine complexes with poxvirus vCCI, tick Evasin-1, and herpesvirus M3.
-
36•• Lubman, O.Y., Fremont, D.H., Parallel evolution of chemokine binding by structurally related herpesvirus decoy receptors. Structure 24 (2016), 57–69 A crystal structure of herpesvirus-encoded chemokine inhibitor R17 in complex with mouse CCL3. The N-loop is characterized as a determinant of chemokine recognition by R17 while the 40s loop promotes formation of a kinetically stable complex. The unifying features of chemokine recognition are inferred by thorough comparison of the structure with receptor:chemokine structures as well as chemokine complexes with poxvirus vCCI, tick Evasin-1, and herpesvirus M3.
-
(2016)
Structure
, vol.24
, pp. 57-69
-
-
Lubman, O.Y.1
Fremont, D.H.2
-
37
-
-
84936847326
-
Structures of orf virus chemokine binding protein in complex with host chemokines reveal clues to broad binding specificity
-
A crystal structure of a parapoxvirus chemokine binding protein (CBP) with in complexes with CCL2, CCL3, and CCL7. Despite the absence of sequence or structural homology with tick Evasin-1, herpesvirus M3, or herpesvirus R17, the parapoxvirus CBP engages the chemokines via the same universal interface involving the CC motif, the N-loop, and the 40s loop. The protein is also found to bind CXCL2, CXCL4 and XCL1 with low nanomoloar affinity, while no binding was observed to CXCL8, CXCL10, and CXCL12.
-
37• Couñago, R.M., et al. Structures of orf virus chemokine binding protein in complex with host chemokines reveal clues to broad binding specificity. Structure 23 (2015), 1199–1213 A crystal structure of a parapoxvirus chemokine binding protein (CBP) with in complexes with CCL2, CCL3, and CCL7. Despite the absence of sequence or structural homology with tick Evasin-1, herpesvirus M3, or herpesvirus R17, the parapoxvirus CBP engages the chemokines via the same universal interface involving the CC motif, the N-loop, and the 40s loop. The protein is also found to bind CXCL2, CXCL4 and XCL1 with low nanomoloar affinity, while no binding was observed to CXCL8, CXCL10, and CXCL12.
-
(2015)
Structure
, vol.23
, pp. 1199-1213
-
-
Couñago, R.M.1
-
38
-
-
79960963198
-
Structural basis of chemokine sequestration by CrmD, a poxvirus-encoded tumor necrosis factor receptor
-
38 Xue, X., et al. Structural basis of chemokine sequestration by CrmD, a poxvirus-encoded tumor necrosis factor receptor. PLoS Pathog, 7, 2011, e1002162.
-
(2011)
PLoS Pathog
, vol.7
, pp. e1002162
-
-
Xue, X.1
-
39
-
-
84913593689
-
Structural analysis of a novel small molecule ligand bound to the CXCL12 chemokine
-
A crystal structure of CXCL12 in complex with a small molecule inhibitor of CXCL12-induced chemotaxis, a tetrazole derivative of a virtual screening hit from the ZINC database [42]. The molecule is bound in the N-loop/40s loop groove of the chemokine.
-
39• Smith, E.W., et al. Structural analysis of a novel small molecule ligand bound to the CXCL12 chemokine. J Med Chem 57 (2014), 9693–9699 A crystal structure of CXCL12 in complex with a small molecule inhibitor of CXCL12-induced chemotaxis, a tetrazole derivative of a virtual screening hit from the ZINC database [42]. The molecule is bound in the N-loop/40s loop groove of the chemokine.
-
(2014)
J Med Chem
, vol.57
, pp. 9693-9699
-
-
Smith, E.W.1
-
40
-
-
84978913873
-
Optimization of a scFv-based Biotherapeutic by CDR Side-chain Clash Repair
-
Protein Data Bank
-
40 Tu, C., et al. Optimization of a scFv-based Biotherapeutic by CDR Side-chain Clash Repair. 2015, Protein Data Bank.
-
(2015)
-
-
Tu, C.1
-
41
-
-
84978913887
-
Crystal Structure of CXCL13
-
Protein Data Bank
-
41 Rosenberg, E.M. Jr., et al. Crystal Structure of CXCL13. 2015, Protein Data Bank.
-
(2015)
-
-
Rosenberg, E.M.1
-
42
-
-
77952813636
-
Targeting SDF-1/CXCL12 with a ligand that prevents activation of CXCR4 through structure-based drug design
-
42 Veldkamp, C.T., et al. Targeting SDF-1/CXCL12 with a ligand that prevents activation of CXCR4 through structure-based drug design. J Am Chem Soc 132 (2010), 7242–7243.
-
(2010)
J Am Chem Soc
, vol.132
, pp. 7242-7243
-
-
Veldkamp, C.T.1
-
43
-
-
84969506287
-
Structure-based identification of novel ligands targeting multiple sites within a chemokine–G-protein-coupled-receptor interface
-
43 Smith, E.W., et al. Structure-based identification of novel ligands targeting multiple sites within a chemokine–G-protein-coupled-receptor interface. J Med Chem 59 (2016), 4342–4351.
-
(2016)
J Med Chem
, vol.59
, pp. 4342-4351
-
-
Smith, E.W.1
-
44
-
-
84870290491
-
Structure of the chemokine receptor CXCR1 in phospholipid bilayers
-
44 Park, S.H., et al. Structure of the chemokine receptor CXCR1 in phospholipid bilayers. Nature 491 (2012), 779–783.
-
(2012)
Nature
, vol.491
, pp. 779-783
-
-
Park, S.H.1
-
45
-
-
84924310089
-
Role of 3D structures in understanding, predicting, and designing molecular interactions in the chemokine receptor family
-
N. Tschammer Springer International Publishing
-
45 Kufareva, I., Abagyan, R., Handel, T.M., Role of 3D structures in understanding, predicting, and designing molecular interactions in the chemokine receptor family. Tschammer, N., (eds.) Chemokines, 2015, Springer International Publishing, 41–85.
-
(2015)
Chemokines
, pp. 41-85
-
-
Kufareva, I.1
Abagyan, R.2
Handel, T.M.3
-
46
-
-
0029010408
-
Structure–activity relationships of chemokines
-
46 Clark-Lewis, I., et al. Structure–activity relationships of chemokines. J Leuk Biol 57 (1995), 703–711.
-
(1995)
J Leuk Biol
, vol.57
, pp. 703-711
-
-
Clark-Lewis, I.1
-
47
-
-
84923141629
-
Methodological advances: the unsung heroes of the GPCR structural revolution
-
47 Ghosh, E., et al. Methodological advances: the unsung heroes of the GPCR structural revolution. Nat Rev Mol Cell Biol 16 (2015), 69–81.
-
(2015)
Nat Rev Mol Cell Biol
, vol.16
, pp. 69-81
-
-
Ghosh, E.1
-
48
-
-
84921559394
-
The importance of ligands for G protein-coupled receptor stability
-
48 Zhang, X., Stevens, R.C., Xu, F., The importance of ligands for G protein-coupled receptor stability. Trends Biochem Sci 40 (2015), 79–87.
-
(2015)
Trends Biochem Sci
, vol.40
, pp. 79-87
-
-
Zhang, X.1
Stevens, R.C.2
Xu, F.3
-
49
-
-
0033081379
-
Structure of a CXC chemokine-receptor fragment in complex with interleukin-8
-
49 Skelton, N.J., et al. Structure of a CXC chemokine-receptor fragment in complex with interleukin-8. Structure 7 (1999), 157–168.
-
(1999)
Structure
, vol.7
, pp. 157-168
-
-
Skelton, N.J.1
-
50
-
-
54849434087
-
Structural basis of CXCR4 sulfotyrosine recognition by the chemokine SDF-1/CXCL12
-
p. ra4
-
50 Veldkamp, C.T., et al. Structural basis of CXCR4 sulfotyrosine recognition by the chemokine SDF-1/CXCL12. Sci Signal, 1, 2008 p. ra4.
-
(2008)
Sci Signal
, vol.1
-
-
Veldkamp, C.T.1
-
51
-
-
84908548257
-
Structural basis of receptor sulfotyrosine recognition by a CC chemokine: the N-terminal region of CCR3 bound to CCL11/Eotaxin-1
-
An NMR structure of CCL11 bound to a sulfotyrosinated N-terminal fragment of CCR3. The sulfotyrosine residues binds in the N-loop/40s loop groove of the chemokine and form numerous specific interactions with residues that are conserved within the CC chemokine family. The orientation of the receptor peptide relative the chemokine is different from that observed in either CXCR1:CXCL8 NMR or in CXCR4:CXCL12 NMR, and also contradicts the geometry of crystal structures of full-length receptor:chemokine complexes.
-
51• Millard, C.J., et al. Structural basis of receptor sulfotyrosine recognition by a CC chemokine: the N-terminal region of CCR3 bound to CCL11/Eotaxin-1. Structure 22 (2014), 1571–1581 An NMR structure of CCL11 bound to a sulfotyrosinated N-terminal fragment of CCR3. The sulfotyrosine residues binds in the N-loop/40s loop groove of the chemokine and form numerous specific interactions with residues that are conserved within the CC chemokine family. The orientation of the receptor peptide relative the chemokine is different from that observed in either CXCR1:CXCL8 NMR or in CXCR4:CXCL12 NMR, and also contradicts the geometry of crystal structures of full-length receptor:chemokine complexes.
-
(2014)
Structure
, vol.22
, pp. 1571-1581
-
-
Millard, C.J.1
-
52
-
-
84938882578
-
Experiment-guided molecular modeling of protein–protein complexes involving GPCRs
-
M. Filizola Springer New York
-
52 Kufareva, I., Handel, T.M., Abagyan, R., Experiment-guided molecular modeling of protein–protein complexes involving GPCRs. Filizola, M., (eds.) G Protein-Coupled Receptors in Drug Discovery, 2015, Springer, New York, 295–311.
-
(2015)
G Protein-Coupled Receptors in Drug Discovery
, pp. 295-311
-
-
Kufareva, I.1
Handel, T.M.2
Abagyan, R.3
-
53
-
-
84959112451
-
Disulfide trapping for modeling and structure determination of receptor:chemokine complexes
-
T.M. Handel Academic Press
-
53 Kufareva, I., et al. Disulfide trapping for modeling and structure determination of receptor:chemokine complexes. Handel, T.M., (eds.) Chemokines, 2016, Academic Press, 389–420.
-
(2016)
Chemokines
, pp. 389-420
-
-
Kufareva, I.1
-
54
-
-
84919360392
-
Stoichiometry and geometry of the CXC chemokine receptor 4 complex with CXC ligand 12: molecular modeling and experimental validation
-
The first internally consistent model of the CXCR4:CXCL12 complex obtained by experiment-guided molecular modeling. Dimer dilution experiments and functional complementation experiments are conducted to probe the 2:1 versus 1:1 receptor:chemokine stoichiometry, and found to support the 1:1 stoichiometry hypothesis. Disulfide trapping helped elucidate the complex geometry. Although incompatible with the NMR structure of CXCL12 bound to the isolated N-terminus of CXCR4 [50], the predicted complex geometry is fully consistent with the two-site hypothesis and a large body of mutagenesis.
-
54• Kufareva, I., et al. Stoichiometry and geometry of the CXC chemokine receptor 4 complex with CXC ligand 12: molecular modeling and experimental validation. Proc Natl Acad Sci U S A 111 (2014), E5363–E5372 The first internally consistent model of the CXCR4:CXCL12 complex obtained by experiment-guided molecular modeling. Dimer dilution experiments and functional complementation experiments are conducted to probe the 2:1 versus 1:1 receptor:chemokine stoichiometry, and found to support the 1:1 stoichiometry hypothesis. Disulfide trapping helped elucidate the complex geometry. Although incompatible with the NMR structure of CXCL12 bound to the isolated N-terminus of CXCR4 [50], the predicted complex geometry is fully consistent with the two-site hypothesis and a large body of mutagenesis.
-
(2014)
Proc Natl Acad Sci U S A
, vol.111
, pp. E5363-E5372
-
-
Kufareva, I.1
-
55
-
-
84943650613
-
Rational design of a peptide capture agent for CXCL8 based on a model of the CXCL8:CXCR1 complex
-
A structural model CXCR1:CXCL8 is constructed using the 1999 NMR structure of CXCL8 with a peptoid derived from the N-terminus of CXCR1 [49] (which is the most accurate geometry among all receptor N-termini NMR structures) as a guide. The model is highly consistent with previously reported experimental data, as well as with the geometry suggested by later receptor:chemokine complex structures. On the basis of the model, a peptide capture agent for CXCL8 was designed and demonstrated to be a potent inhibitor of CXCL8-induced migration and CXCR1:CXCL8 association.
-
55• Helmer, D., et al. Rational design of a peptide capture agent for CXCL8 based on a model of the CXCL8:CXCR1 complex. RSC Adv 5 (2015), 25657–25668 A structural model CXCR1:CXCL8 is constructed using the 1999 NMR structure of CXCL8 with a peptoid derived from the N-terminus of CXCR1 [49] (which is the most accurate geometry among all receptor N-termini NMR structures) as a guide. The model is highly consistent with previously reported experimental data, as well as with the geometry suggested by later receptor:chemokine complex structures. On the basis of the model, a peptide capture agent for CXCL8 was designed and demonstrated to be a potent inhibitor of CXCL8-induced migration and CXCR1:CXCL8 association.
-
(2015)
RSC Adv
, vol.5
, pp. 25657-25668
-
-
Helmer, D.1
-
56
-
-
34948846732
-
The human CC chemokine MIP-1β dimer is not competent to bind to the CCR5 receptor
-
56 Jin, H., et al. The human CC chemokine MIP-1β dimer is not competent to bind to the CCR5 receptor. J Biol Chem 282 (2007), 27976–27983.
-
(2007)
J Biol Chem
, vol.282
, pp. 27976-27983
-
-
Jin, H.1
-
57
-
-
0032509515
-
Monomeric monocyte chemoattractant protein-1 (MCP-1) binds and activates the MCP-1 receptor CCR2B
-
57 Paavola, C.D., et al. Monomeric monocyte chemoattractant protein-1 (MCP-1) binds and activates the MCP-1 receptor CCR2B. J Biol Chem 273 (1998), 33157–33165.
-
(1998)
J Biol Chem
, vol.273
, pp. 33157-33165
-
-
Paavola, C.D.1
-
58
-
-
84978907768
-
Signal transmission through the CXC chemokine receptor 4 (CXCR4) transmembrane helices
-
[in press] Using the technique of shotgun mutagenesis, 728 mutants covering all 352 residues of CXCR4 were generated and tested for trafficking, folding, and function. This comprehensive analysis enabled identification of five classes of residues that together form an intramolecular chain connecting the extracellular chemokine-engaging residues to the intracellular G protein coupling residues of CXCR4. A cohesive 3D model of CXCR4 activation is proposed.
-
58•• Wescott, M.P., et al. Signal transmission through the CXC chemokine receptor 4 (CXCR4) transmembrane helices. Proc Natl Acad Sci U S A, 2016 [in press] Using the technique of shotgun mutagenesis, 728 mutants covering all 352 residues of CXCR4 were generated and tested for trafficking, folding, and function. This comprehensive analysis enabled identification of five classes of residues that together form an intramolecular chain connecting the extracellular chemokine-engaging residues to the intracellular G protein coupling residues of CXCR4. A cohesive 3D model of CXCR4 activation is proposed.
-
(2016)
Proc Natl Acad Sci U S A
-
-
Wescott, M.P.1
-
59
-
-
77957055780
-
Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors
-
S.C. Sealfon Academic Press San Diego
-
59 Ballesteros, J.A., Weinstein, H., Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein-coupled receptors. Sealfon, S.C., (eds.) Methods in Neurosciences: Receptor Molecular Biology, 1995, Academic Press, San Diego, 366–428.
-
(1995)
Methods in Neurosciences: Receptor Molecular Biology
, pp. 366-428
-
-
Ballesteros, J.A.1
Weinstein, H.2
-
60
-
-
0030683638
-
Solution structure and basis for functional activity of stromal cell-derived factor-1: dissociation of CXCR4 activation from binding and inhibition of HIV-1
-
60 Crump, M.P., et al. Solution structure and basis for functional activity of stromal cell-derived factor-1: dissociation of CXCR4 activation from binding and inhibition of HIV-1. EMBO J 16 (1997), 6996–7007.
-
(1997)
EMBO J
, vol.16
, pp. 6996-7007
-
-
Crump, M.P.1
-
61
-
-
0032833999
-
Identification of residues in the monocyte chemotactic protein-1 that contact the MCP-1 receptor, CCR2
-
61 Hemmerich, S., et al. Identification of residues in the monocyte chemotactic protein-1 that contact the MCP-1 receptor, CCR2. Biochemistry 38 (1999), 13013–13025.
-
(1999)
Biochemistry
, vol.38
, pp. 13013-13025
-
-
Hemmerich, S.1
-
62
-
-
0027293058
-
Partial functional mapping of the human interleukin-8 type A receptor. Identification of a major ligand binding domain
-
62 Hébert, C.A., et al. Partial functional mapping of the human interleukin-8 type A receptor. Identification of a major ligand binding domain. J Biol Chem 268 (1993), 18549–18553.
-
(1993)
J Biol Chem
, vol.268
, pp. 18549-18553
-
-
Hébert, C.A.1
-
63
-
-
0028362650
-
Correction: partial functional mapping of the human interleukin-8 type A receptor. Identification of a major ligand binding domain
-
63 Hébert, C.A., et al. Correction: partial functional mapping of the human interleukin-8 type A receptor. Identification of a major ligand binding domain. J Biol Chem, 269, 1994, 16520.
-
(1994)
J Biol Chem
, vol.269
, pp. 16520
-
-
Hébert, C.A.1
-
64
-
-
0034603860
-
A novel peptide antagonist of CXCR4 derived from the N-terminus of viral chemokine vMIP-II
-
64 Zhou, N., et al. A novel peptide antagonist of CXCR4 derived from the N-terminus of viral chemokine vMIP-II. Biochemistry 39 (2000), 3782–3787.
-
(2000)
Biochemistry
, vol.39
, pp. 3782-3787
-
-
Zhou, N.1
-
66
-
-
0029919840
-
Molecular architecture of G protein-coupled receptors
-
66 van Rhee, A.M., Jacobson, K.A., Molecular architecture of G protein-coupled receptors. Drug Dev Res 37 (1996), 1–38.
-
(1996)
Drug Dev Res
, vol.37
, pp. 1-38
-
-
van Rhee, A.M.1
Jacobson, K.A.2
-
67
-
-
84872221774
-
Structure–function of the G protein-coupled receptor superfamily
-
67 Katritch, V., Cherezov, V., Stevens, R.C., Structure–function of the G protein-coupled receptor superfamily. Annu Rev Pharmacol Toxicol 53 (2013), 531–556.
-
(2013)
Annu Rev Pharmacol Toxicol
, vol.53
, pp. 531-556
-
-
Katritch, V.1
Cherezov, V.2
Stevens, R.C.3
-
68
-
-
56649122050
-
Highly potent, fully recombinant anti-HIV chemokines: reengineering a low-cost microbicide
-
68 Gaertner, H., et al. Highly potent, fully recombinant anti-HIV chemokines: reengineering a low-cost microbicide. Proc Natl Acad Sci U S A 105 (2008), 17706–17711.
-
(2008)
Proc Natl Acad Sci U S A
, vol.105
, pp. 17706-17711
-
-
Gaertner, H.1
-
69
-
-
0033534151
-
Identification of surface residues of the monocyte chemotactic protein 1 that affect signaling through the receptor CCR2b
-
69 Jarnagin, K., et al. Identification of surface residues of the monocyte chemotactic protein 1 that affect signaling through the receptor CCR2b. Biochemistry 38 (1999), 16167–16177.
-
(1999)
Biochemistry
, vol.38
, pp. 16167-16177
-
-
Jarnagin, K.1
-
70
-
-
0034724373
-
CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding
-
70 Laurence, J.S., et al. CC chemokine MIP-1 beta can function as a monomer and depends on Phe13 for receptor binding. Biochemistry 39 (2000), 3401–3409.
-
(2000)
Biochemistry
, vol.39
, pp. 3401-3409
-
-
Laurence, J.S.1
-
71
-
-
39749128458
-
Highly potent HIV inhibition: engineering a key anti-HIV structure from PSC-RANTES into MIP-1β/CCL4
-
71 Gaertner, H., et al. Highly potent HIV inhibition: engineering a key anti-HIV structure from PSC-RANTES into MIP-1β/CCL4. Protein Eng Des Select 21 (2008), 65–72.
-
(2008)
Protein Eng Des Select
, vol.21
, pp. 65-72
-
-
Gaertner, H.1
-
72
-
-
71749113474
-
Structural basis of the interaction between chemokine stromal cell-derived factor-1/CXCL12 and its G-protein-coupled receptor CXCR4
-
72 Kofuku, Y., et al. Structural basis of the interaction between chemokine stromal cell-derived factor-1/CXCL12 and its G-protein-coupled receptor CXCR4. J Biol Chem 284 (2009), 35240–35250.
-
(2009)
J Biol Chem
, vol.284
, pp. 35240-35250
-
-
Kofuku, Y.1
-
73
-
-
84928967172
-
Solution NMR characterization of WTCXCL8 monomer and dimer binding to CXCR1 N-terminal domain
-
73 Joseph, P.R.B., Rajarathnam, K., Solution NMR characterization of WTCXCL8 monomer and dimer binding to CXCR1 N-terminal domain. Protein Sci 24 (2015), 81–92.
-
(2015)
Protein Sci
, vol.24
, pp. 81-92
-
-
Joseph, P.R.B.1
Rajarathnam, K.2
-
74
-
-
0028984262
-
Mutation of Leu25 and Val27 introduces CC chemokine activity into interleukin-8
-
74 Lusti-Narasimhan, M., et al. Mutation of Leu25 and Val27 introduces CC chemokine activity into interleukin-8. J Biol Chem 270 (1995), 2716–2721.
-
(1995)
J Biol Chem
, vol.270
, pp. 2716-2721
-
-
Lusti-Narasimhan, M.1
-
75
-
-
70349263476
-
Differential activation and regulation of CXCR1 and CXCR2 by CXCL8 monomer and dimer
-
75 Nasser, M.W., et al. Differential activation and regulation of CXCR1 and CXCR2 by CXCL8 monomer and dimer. J Immunol 183 (2009), 3425–3432.
-
(2009)
J Immunol
, vol.183
, pp. 3425-3432
-
-
Nasser, M.W.1
-
76
-
-
80055081893
-
Monomeric and dimeric CXCL12 inhibit metastasis through distinct CXCR4 interactions and signaling pathways
-
76 Drury, L.J., et al. Monomeric and dimeric CXCL12 inhibit metastasis through distinct CXCR4 interactions and signaling pathways. Proc Natl Acad Sci U S A 108 (2011), 17655–17660.
-
(2011)
Proc Natl Acad Sci U S A
, vol.108
, pp. 17655-17660
-
-
Drury, L.J.1
|