메뉴 건너뛰기




Volumn 51, Issue 28, 2012, Pages 5642-5654

A model of GAG/MIP-2/CXCR2 interfaces and its functional effects

Author keywords

[No Author keywords available]

Indexed keywords

CHEMOKINES; G-PROTEIN COUPLED RECEPTORS; GLYCOSAMINOGLYCANS; HEPARIN BINDING; HEPARIN DISACCHARIDE; IN-VITRO; IN-VIVO; WILD TYPES;

EID: 84863965823     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3001566     Document Type: Article
Times cited : (26)

References (78)
  • 1
    • 67650730269 scopus 로고    scopus 로고
    • Chemokine signaling in embryonic cell migration: A fisheye view
    • Raz, E. and Mahabaleshwar, H. (2009) Chemokine signaling in embryonic cell migration: a fisheye view Development 136, 1223-1229
    • (2009) Development , vol.136 , pp. 1223-1229
    • Raz, E.1    Mahabaleshwar, H.2
  • 2
    • 0038608022 scopus 로고    scopus 로고
    • CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10)
    • Campanella, G. S., Lee, E. M., Sun, J., and Luster, A. D. (2003) CXCR3 and heparin binding sites of the chemokine IP-10 (CXCL10) J. Biol. Chem. 278, 17066-17074
    • (2003) J. Biol. Chem. , vol.278 , pp. 17066-17074
    • Campanella, G.S.1    Lee, E.M.2    Sun, J.3    Luster, A.D.4
  • 3
    • 34249029610 scopus 로고    scopus 로고
    • Chemokines at large: In-vivo mechanisms of their transport, presentation and clearance
    • Colditz, I. G., Schneider, M. A., Pruenster, M., and Rot, A. (2007) Chemokines at large: in-vivo mechanisms of their transport, presentation and clearance Thromb. Haemostasis 97, 688-693
    • (2007) Thromb. Haemostasis , vol.97 , pp. 688-693
    • Colditz, I.G.1    Schneider, M.A.2    Pruenster, M.3    Rot, A.4
  • 7
    • 2542428442 scopus 로고    scopus 로고
    • Chemokines in innate and adaptive host defense: Basic chemokinese grammar for immune cells
    • Rot, A. and von Andrian, U. H. (2004) Chemokines in innate and adaptive host defense: basic chemokinese grammar for immune cells Annu. Rev. Immunol. 22, 891-928
    • (2004) Annu. Rev. Immunol. , vol.22 , pp. 891-928
    • Rot, A.1    Von Andrian, U.H.2
  • 8
    • 0027533286 scopus 로고
    • Neutrophil attractant/activation protein-1 (interleukin-8) induces in vitro neutrophil migration by haptotactic mechanism
    • Rot, A. (1993) Neutrophil attractant/activation protein-1 (interleukin-8) induces in vitro neutrophil migration by haptotactic mechanism Eur. J. Immunol. 23, 303-306
    • (1993) Eur. J. Immunol. , vol.23 , pp. 303-306
    • Rot, A.1
  • 9
    • 69149105818 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans in extravasation: Assisting leukocyte guidance
    • Celie, J. W., Beelen, R. H., and van den Born, J. (2009) Heparan sulfate proteoglycans in extravasation: assisting leukocyte guidance Front Biosci. 14, 4932-4949
    • (2009) Front Biosci. , vol.14 , pp. 4932-4949
    • Celie, J.W.1    Beelen, R.H.2    Van Den Born, J.3
  • 10
    • 33745439311 scopus 로고    scopus 로고
    • The biological relevance of chemokine-proteoglycan interactions
    • Proudfoot, A. E. (2006) The biological relevance of chemokine- proteoglycan interactions Biochem. Soc. Trans. 34, 422-426
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 422-426
    • Proudfoot, A.E.1
  • 13
    • 77951245615 scopus 로고    scopus 로고
    • Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family
    • Murphy, J. W., Yuan, H., Kong, Y., Xiong, Y., and Lolis, E. J. (2010) Heterologous quaternary structure of CXCL12 and its relationship to the CC chemokine family Proteins 78, 1331-1337
    • (2010) Proteins , vol.78 , pp. 1331-1337
    • Murphy, J.W.1    Yuan, H.2    Kong, Y.3    Xiong, Y.4    Lolis, E.J.5
  • 16
    • 33746901672 scopus 로고    scopus 로고
    • Probing receptor binding activity of interleukin-8 dimer using a disulfide trap
    • Rajarathnam, K., Prado, G. N., Fernando, H., Clark-Lewis, I., and Navarro, J. (2006) Probing receptor binding activity of interleukin-8 dimer using a disulfide trap Biochemistry 45, 7882-7888
    • (2006) Biochemistry , vol.45 , pp. 7882-7888
    • Rajarathnam, K.1    Prado, G.N.2    Fernando, H.3    Clark-Lewis, I.4    Navarro, J.5
  • 19
    • 79952105330 scopus 로고    scopus 로고
    • Chemokine oligomerization and interactions with receptors and glycosaminoglycans: The role of structural dynamics in function
    • Salanga, C. L. and Handel, T. M. (2011) Chemokine oligomerization and interactions with receptors and glycosaminoglycans: the role of structural dynamics in function Exp. Cell Res. 317, 590-601
    • (2011) Exp. Cell Res. , vol.317 , pp. 590-601
    • Salanga, C.L.1    Handel, T.M.2
  • 21
    • 80051492024 scopus 로고    scopus 로고
    • Oligomeric structure of the chemokine CCL5/RANTES from NMR, MS, and SAXS Data
    • Wang, X., Watson, C., Sharp, J. S., Handel, T. M., and Prestegard, J. H. (2011) Oligomeric structure of the chemokine CCL5/RANTES from NMR, MS, and SAXS Data Structure 19, 1138-1148
    • (2011) Structure , vol.19 , pp. 1138-1148
    • Wang, X.1    Watson, C.2    Sharp, J.S.3    Handel, T.M.4    Prestegard, J.H.5
  • 25
    • 22244448718 scopus 로고    scopus 로고
    • Regulation of protein function by glycosaminoglycans - As exemplified by chemokines
    • Handel, T. M., Johnson, Z., Crown, S. E., Lau, E. K., and Proudfoot, A. E. (2005) Regulation of protein function by glycosaminoglycans - as exemplified by chemokines Annu. Rev. Biochem. 74, 385-410
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 385-410
    • Handel, T.M.1    Johnson, Z.2    Crown, S.E.3    Lau, E.K.4    Proudfoot, A.E.5
  • 27
    • 72549095869 scopus 로고    scopus 로고
    • Therapy with nonglycosaminoglycan-binding mutant CCL7: A novel strategy to limit allograft inflammation
    • Ali, S., OBoyle, G., Hepplewhite, P., Tyler, J. R., Robertson, H., and Kirby, J. A. (2010) Therapy with nonglycosaminoglycan-binding mutant CCL7: a novel strategy to limit allograft inflammation Am. J. Transplant. 10, 47-58
    • (2010) Am. J. Transplant. , vol.10 , pp. 47-58
    • Ali, S.1    Oboyle, G.2    Hepplewhite, P.3    Tyler, J.R.4    Robertson, H.5    Kirby, J.A.6
  • 28
    • 1842477451 scopus 로고    scopus 로고
    • Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin
    • Peterson, F. C., Elgin, E. S., Nelson, T. J., Zhang, F., Hoeger, T. J., Linhardt, R. J., and Volkman, B. F. (2004) Identification and characterization of a glycosaminoglycan recognition element of the C chemokine lymphotactin J. Biol. Chem. 279, 12598-12604
    • (2004) J. Biol. Chem. , vol.279 , pp. 12598-12604
    • Peterson, F.C.1    Elgin, E.S.2    Nelson, T.J.3    Zhang, F.4    Hoeger, T.J.5    Linhardt, R.J.6    Volkman, B.F.7
  • 31
    • 84856413410 scopus 로고    scopus 로고
    • The monomer-dimer equilibrium and glycosaminoglycan interactions of chemokine CXCL8 regulate tissue-specific neutrophil recruitment
    • Gangavarapu, P., Rajagopalan, L., Kolli, D., Guerrero-Plata, A., Garofalo, R. P., and Rajarathnam, K. (2012) The monomer-dimer equilibrium and glycosaminoglycan interactions of chemokine CXCL8 regulate tissue-specific neutrophil recruitment J. Leukocyte Biol. 91, 259-265
    • (2012) J. Leukocyte Biol. , vol.91 , pp. 259-265
    • Gangavarapu, P.1    Rajagopalan, L.2    Kolli, D.3    Guerrero-Plata, A.4    Garofalo, R.P.5    Rajarathnam, K.6
  • 32
    • 0037799237 scopus 로고    scopus 로고
    • The core domain of chemokines binds CCR5 extracellular domains while their amino terminus interacts with the transmembrane helix bundle
    • Blanpain, C., Doranz, B. J., Bondue, A., Govaerts, C., De Leener, A., Vassart, G., Doms, R. W., Proudfoot, A., and Parmentier, M. (2003) The core domain of chemokines binds CCR5 extracellular domains while their amino terminus interacts with the transmembrane helix bundle J. Biol. Chem. 278, 5179-5187
    • (2003) J. Biol. Chem. , vol.278 , pp. 5179-5187
    • Blanpain, C.1    Doranz, B.J.2    Bondue, A.3    Govaerts, C.4    De Leener, A.5    Vassart, G.6    Doms, R.W.7    Proudfoot, A.8    Parmentier, M.9
  • 33
  • 35
    • 0030816246 scopus 로고    scopus 로고
    • Functional and receptor binding characterization of recombinant murine macrophage inflammatory protein 2: Sequence analysis and mutagenesis identify receptor binding epitopes
    • Jerva, L. F., Sullivan, G., and Lolis, E. (1997) Functional and receptor binding characterization of recombinant murine macrophage inflammatory protein 2: sequence analysis and mutagenesis identify receptor binding epitopes Protein Sci. 6, 1643-1652
    • (1997) Protein Sci. , vol.6 , pp. 1643-1652
    • Jerva, L.F.1    Sullivan, G.2    Lolis, E.3
  • 36
    • 0012382504 scopus 로고    scopus 로고
    • Protein Determination by UV Absorption
    • (Walker, J. M. Ed.), pp, Humana Press Inc, Totowa, NJ
    • Aitken, A. and Learmonth, M. l. (1996) Protein Determination by UV Absorption, In The Protein Protocols Handbook (Walker, J. M., Ed.), pp 3-6, Humana Press Inc, Totowa, NJ.
    • (1996) The Protein Protocols Handbook , pp. 3-6
    • Aitken, A.1    Learmonth, M.L.2
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 307-325
    • (1997) Methods Enzymol. , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 74549194551 scopus 로고    scopus 로고
    • Molecular replacement with MOLRE
    • Vagin, A. and Teplyakov, A. (2010) Molecular replacement with MOLRE Acta Crystallogr. D 66, 22-25
    • (2010) Acta Crystallogr. D , vol.66 , pp. 22-25
    • Vagin, A.1    Teplyakov, A.2
  • 40
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: model-building tools for molecular graphics Acta Crystallogr. D 60, 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 41
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D 53, 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 42
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 43
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 44
    • 0032499624 scopus 로고    scopus 로고
    • Solution structure of murine macrophage inflammatory protein-2
    • Shao, W., Jerva, L. F., West, J., Lolis, E., and Schweitzer, B. I. (1998) Solution structure of murine macrophage inflammatory protein-2 Biochemistry 37, 8303-8313
    • (1998) Biochemistry , vol.37 , pp. 8303-8313
    • Shao, W.1    Jerva, L.F.2    West, J.3    Lolis, E.4    Schweitzer, B.I.5
  • 45
    • 0033543577 scopus 로고    scopus 로고
    • Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins
    • Mulder, F. A., Schipper, D., Bott, R., and Boelens, R. (1999) Altered flexibility in the substrate-binding site of related native and engineered high-alkaline Bacillus subtilisins J. Mol. Biol. 292, 111-123
    • (1999) J. Mol. Biol. , vol.292 , pp. 111-123
    • Mulder, F.A.1    Schipper, D.2    Bott, R.3    Boelens, R.4
  • 47
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 22, 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 48
  • 50
    • 32144444402 scopus 로고    scopus 로고
    • Methods for studying neutrophil chemotaxis
    • Dong, X. and Wu, D. (2006) Methods for studying neutrophil chemotaxis Methods Enzymol. 406, 605-613
    • (2006) Methods Enzymol. , vol.406 , pp. 605-613
    • Dong, X.1    Wu, D.2
  • 51
    • 0028965079 scopus 로고
    • The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9- resolution
    • Malkowski, M. G., Wu, J. Y., Lazar, J. B., Johnson, P. H., and Edwards, B. F. (1995) The crystal structure of recombinant human neutrophil-activating peptide-2 (M6L) at 1.9- resolution J. Biol. Chem. 270, 7077-7087
    • (1995) J. Biol. Chem. , vol.270 , pp. 7077-7087
    • Malkowski, M.G.1    Wu, J.Y.2    Lazar, J.B.3    Johnson, P.H.4    Edwards, B.F.5
  • 52
    • 0024555819 scopus 로고
    • The three-dimensional structure of bovine platelet factor 4 at 3.0- resolution
    • Charles, R., St, Walz, D. A., and Edwards, B. F. (1989) The three-dimensional structure of bovine platelet factor 4 at 3.0- resolution J. Biol. Chem. 264, 2092-2099
    • (1989) J. Biol. Chem. , vol.264 , pp. 2092-2099
    • St, C.R.1    Walz, D.A.2    Edwards, B.F.3
  • 53
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Project, C. C. (1994) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D 50, 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
    • Project, C.C.1
  • 54
    • 0031453963 scopus 로고    scopus 로고
    • OLDERADO: On-line database of ensemble representatives and domains. on Line Database of Ensemble Representatives and DOmains
    • Kelley, L. A. and Sutcliffe, M. J. (1997) OLDERADO: on-line database of ensemble representatives and domains. On Line Database of Ensemble Representatives And DOmains Protein Sci. 6, 2628-2630
    • (1997) Protein Sci. , vol.6 , pp. 2628-2630
    • Kelley, L.A.1    Sutcliffe, M.J.2
  • 55
    • 85056027974 scopus 로고    scopus 로고
    • Systematic comparison of crystal and NMR protein structures deposited in the protein data bank
    • Sikic, K., Tomic, S., and Carugo, O. (2010) Systematic comparison of crystal and NMR protein structures deposited in the protein data bank Open Biochem J 4, 83-95
    • (2010) Open Biochem J , vol.4 , pp. 83-95
    • Sikic, K.1    Tomic, S.2    Carugo, O.3
  • 57
    • 0028362141 scopus 로고
    • Monomer-dimer equilibria of interleukin-8 and neutrophil-activating peptide 2. Evidence for IL-8 binding as a dimer and oligomer to IL-8 receptor B
    • Schnitzel, W., Monschein, U., and Besemer, J. (1994) Monomer-dimer equilibria of interleukin-8 and neutrophil-activating peptide 2. Evidence for IL-8 binding as a dimer and oligomer to IL-8 receptor B J. Leukocyte Biol. 55, 763-770
    • (1994) J. Leukocyte Biol. , vol.55 , pp. 763-770
    • Schnitzel, W.1    Monschein, U.2    Besemer, J.3
  • 58
    • 34248168879 scopus 로고    scopus 로고
    • Structural and functional basis of CXCL12 (stromal cell-derived factor-1alpha) binding to heparin
    • Murphy, J. W., Cho, Y., Sachpatzidis, A., Fan, C., Hodsdon, M. E., and Lolis, E. (2007) Structural and functional basis of CXCL12 (stromal cell-derived factor-1alpha) binding to heparin J. Biol. Chem. 282, 10018-10027
    • (2007) J. Biol. Chem. , vol.282 , pp. 10018-10027
    • Murphy, J.W.1    Cho, Y.2    Sachpatzidis, A.3    Fan, C.4    Hodsdon, M.E.5    Lolis, E.6
  • 59
    • 7944221827 scopus 로고    scopus 로고
    • The X-ray structure of RANTES: Heparin-derived disaccharides allows the rational design of chemokine inhibitors
    • Shaw, J. P., Johnson, Z., Borlat, F., Zwahlen, C., Kungl, A., Roulin, K., Harrenga, A., Wells, T. N., and Proudfoot, A. E. (2004) The X-ray structure of RANTES: heparin-derived disaccharides allows the rational design of chemokine inhibitors Structure 12, 2081-2093
    • (2004) Structure , vol.12 , pp. 2081-2093
    • Shaw, J.P.1    Johnson, Z.2    Borlat, F.3    Zwahlen, C.4    Kungl, A.5    Roulin, K.6    Harrenga, A.7    Wells, T.N.8    Proudfoot, A.E.9
  • 60
    • 0033017193 scopus 로고    scopus 로고
    • Regulation of early peritoneal neutrophil migration by macrophage inflammatory protein-2 and mast cells in experimental peritonitis
    • Mercer-Jones, M. A., Shrotri, M. S., Heinzelmann, M., Peyton, J. C., and Cheadle, W. G. (1999) Regulation of early peritoneal neutrophil migration by macrophage inflammatory protein-2 and mast cells in experimental peritonitis J. Leukocyte Biol. 65, 249-255
    • (1999) J. Leukocyte Biol. , vol.65 , pp. 249-255
    • Mercer-Jones, M.A.1    Shrotri, M.S.2    Heinzelmann, M.3    Peyton, J.C.4    Cheadle, W.G.5
  • 61
    • 23244432481 scopus 로고    scopus 로고
    • A non-glycosaminoglycan-binding variant of CC chemokine ligand 7 (monocyte chemoattractant protein-3) antagonizes chemokine-mediated inflammation
    • Ali, S., Robertson, H., Wain, J. H., Isaacs, J. D., Malik, G., and Kirby, J. A. (2005) A non-glycosaminoglycan-binding variant of CC chemokine ligand 7 (monocyte chemoattractant protein-3) antagonizes chemokine-mediated inflammation J. Immunol. 175, 1257-1266
    • (2005) J. Immunol. , vol.175 , pp. 1257-1266
    • Ali, S.1    Robertson, H.2    Wain, J.H.3    Isaacs, J.D.4    Malik, G.5    Kirby, J.A.6
  • 62
    • 24944451114 scopus 로고    scopus 로고
    • Endothelial heparan sulfate deficiency impairs l -selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses
    • Wang, L., Fuster, M., Sriramarao, P., and Esko, J. D. (2005) Endothelial heparan sulfate deficiency impairs l -selectin- and chemokine-mediated neutrophil trafficking during inflammatory responses Nat. Immunol. 6, 902-910
    • (2005) Nat. Immunol. , vol.6 , pp. 902-910
    • Wang, L.1    Fuster, M.2    Sriramarao, P.3    Esko, J.D.4
  • 63
    • 54049106148 scopus 로고    scopus 로고
    • Macrophage-specific metalloelastase (MMP-12) truncates and inactivates ELR+ CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: Potential role of the macrophage in terminating polymorphonuclear leukocyte influx
    • Dean, R. A., Cox, J. H., Bellac, C. L., Doucet, A., Starr, A. E., and Overall, C. M. (2008) Macrophage-specific metalloelastase (MMP-12) truncates and inactivates ELR+ CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: potential role of the macrophage in terminating polymorphonuclear leukocyte influx Blood 112, 3455-3464
    • (2008) Blood , vol.112 , pp. 3455-3464
    • Dean, R.A.1    Cox, J.H.2    Bellac, C.L.3    Doucet, A.4    Starr, A.E.5    Overall, C.M.6
  • 64
    • 34447508446 scopus 로고    scopus 로고
    • Eotaxin selectively binds heparin. An interaction that protects eotaxin from proteolysis and potentiates chemotactic activity in vivo
    • Ellyard, J. I., Simson, L., Bezos, A., Johnston, K., Freeman, C., and Parish, C. R. (2007) Eotaxin selectively binds heparin. An interaction that protects eotaxin from proteolysis and potentiates chemotactic activity in vivo J. Biol. Chem. 282, 15238-15247
    • (2007) J. Biol. Chem. , vol.282 , pp. 15238-15247
    • Ellyard, J.I.1    Simson, L.2    Bezos, A.3    Johnston, K.4    Freeman, C.5    Parish, C.R.6
  • 66
    • 6344284808 scopus 로고    scopus 로고
    • Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV
    • Sadir, R., Imberty, A., Baleux, F., and Lortat-Jacob, H. (2004) Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV J. Biol. Chem. 279, 43854-43860
    • (2004) J. Biol. Chem. , vol.279 , pp. 43854-43860
    • Sadir, R.1    Imberty, A.2    Baleux, F.3    Lortat-Jacob, H.4
  • 67
    • 33748751102 scopus 로고    scopus 로고
    • CCL5-CCR5-mediated apoptosis in T cells: Requirement for glycosaminoglycan binding and CCL5 aggregation
    • Murooka, T. T., Wong, M. M., Rahbar, R., Majchrzak-Kita, B., Proudfoot, A. E., and Fish, E. N. (2006) CCL5-CCR5-mediated apoptosis in T cells: Requirement for glycosaminoglycan binding and CCL5 aggregation J. Biol. Chem. 281, 25184-25194
    • (2006) J. Biol. Chem. , vol.281 , pp. 25184-25194
    • Murooka, T.T.1    Wong, M.M.2    Rahbar, R.3    Majchrzak-Kita, B.4    Proudfoot, A.E.5    Fish, E.N.6
  • 68
    • 80051521545 scopus 로고    scopus 로고
    • Status of GPCR modeling and docking as reflected by community-wide GPCR Dock 2010 assessment
    • Kufareva, I., Rueda, M., Katritch, V., Stevens, R. C., and Abagyan, R. (2011) Status of GPCR modeling and docking as reflected by community-wide GPCR Dock 2010 assessment Structure 19, 1108-1126
    • (2011) Structure , vol.19 , pp. 1108-1126
    • Kufareva, I.1    Rueda, M.2    Katritch, V.3    Stevens, R.C.4    Abagyan, R.5
  • 70
    • 23344447877 scopus 로고    scopus 로고
    • The CXCR1 and CXCR2 receptors form constitutive homo- and heterodimers selectively and with equal apparent affinities
    • Wilson, S., Wilkinson, G., and Milligan, G. (2005) The CXCR1 and CXCR2 receptors form constitutive homo- and heterodimers selectively and with equal apparent affinities J. Biol. Chem. 280, 28663-28674
    • (2005) J. Biol. Chem. , vol.280 , pp. 28663-28674
    • Wilson, S.1    Wilkinson, G.2    Milligan, G.3
  • 73
    • 0029095697 scopus 로고
    • Chemokine binding and activities mediated by the mouse IL-8 receptor
    • Lee, J., Cacalano, G., Camerato, T., Toy, K., Moore, M. W., and Wood, W. I. (1995) Chemokine binding and activities mediated by the mouse IL-8 receptor J. Immunol. 155, 2158-2164
    • (1995) J. Immunol. , vol.155 , pp. 2158-2164
    • Lee, J.1    Cacalano, G.2    Camerato, T.3    Toy, K.4    Moore, M.W.5    Wood, W.I.6
  • 75
    • 29144467674 scopus 로고    scopus 로고
    • A homolog of the human chemokine receptor CXCR1 is expressed in the mouse
    • Moepps, B., Nuesseler, E., Braun, M., and Gierschik, P. (2006) A homolog of the human chemokine receptor CXCR1 is expressed in the mouse Mol. Immunol. 43, 897-914
    • (2006) Mol. Immunol. , vol.43 , pp. 897-914
    • Moepps, B.1    Nuesseler, E.2    Braun, M.3    Gierschik, P.4
  • 77
    • 66449127755 scopus 로고    scopus 로고
    • Organ-specific heparan sulfate structural phenotypes
    • Shi, X. and Zaia, J. (2009) Organ-specific heparan sulfate structural phenotypes J. Biol. Chem. 284, 11806-11814
    • (2009) J. Biol. Chem. , vol.284 , pp. 11806-11814
    • Shi, X.1    Zaia, J.2
  • 78
    • 33846002381 scopus 로고    scopus 로고
    • The IL sequence in the LLKIL motif in CXCR2 is required for full ligand-induced activation of Erk, Akt, and chemotaxis in HL60 cells
    • Sai, J., Walker, G., Wikswo, J., and Richmond, A. (2006) The IL sequence in the LLKIL motif in CXCR2 is required for full ligand-induced activation of Erk, Akt, and chemotaxis in HL60 cells J. Biol. Chem. 281, 35931-35941
    • (2006) J. Biol. Chem. , vol.281 , pp. 35931-35941
    • Sai, J.1    Walker, G.2    Wikswo, J.3    Richmond, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.