Chemokine-protease interactions in cancer

New functions for the matrix metalloproteinases in cancer progression

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Involvement of chemokine receptors in breast cancer metastasis

Müller, A., Homey, B., Soto, H., Ge, N., Catron, D., Buchanan, M. E., McClanahan, T., Murphy, E., Yuan, W., Wagner, S. N., et al. (2001) · Nature · doi:10.1038/35065016 · Cited by 5,340 · see citing works

Matrix Metalloproteinases

Nagase, H., & Woessner, J. F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21491 · Cited by 3,905 · see citing works

Matrix Metalloproteinase Inhibitors and Cancer—Trials and Tribulations

Coussens, L. M., Fingleton, B., & Matrisian, L. M. (2002) · Science · doi:10.1126/science.1067100 · Cited by 2,761 · see citing works

Defects of B-cell lymphopoiesis and bone-marrow myelopoiesis in mice lacking the CXC chemokine PBSF/SDF-1

Nagasawa, T., Hirota, S., Tachibana, K., Takakura, N., Nishikawa, S.-I., Kitamura, Y., Yoshida, N., Kikutani, H., & Kishimoto, T. (1996) · Nature · doi:10.1038/382635a0 · Cited by 2,338 · see citing works

The Chemokine SDF-1 Is a Chemoattractant for Human CD34+ Hematopoietic Progenitor Cells and Provides a New Mechanism to Explain the Mobilization of CD34+ Progenitors to Peripheral Blood

Aiuti, A., Webb, I. J., Bleul, C. C., Springer, T. A., & Gutierrez‐Ramos, J. C. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.185.1.111 · Cited by 1,378 · see citing works

The Functional Role of the ELR Motif in CXC Chemokine-mediated Angiogenesis

Strieter, R. M., Polverini, P. J., Kunkel, S. L., Arenberg, D. A., Burdick, M. D., Kasper, J., Dzuiba, J., Van Damme, J., Walz, A., Marriott, D., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.27348 · Cited by 1,222 · see citing works

A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas

Basset, P., Bellocq, J., Wolf, C., Stoll, I., Hutin, P., Limacher, J. M., Podhajcer, O. L., Chenard, M., Rio, M., & Chambon, P. (1990) · Nature · doi:10.1038/348699a0 · Cited by 1,125 · see citing works

The origin and function of tumor-associated macrophages

Mantovani, A., Bottazzi, B., Colotta, F., Sozzani, S., & Ruco, L. P. (1992) · Immunology Today · doi:10.1016/0167-5699(92)90008-u · Cited by 1,088 · see citing works

Biochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9)

den Steen, P. E. V., Dubois, B., Nelissen, I., Rudd, P., Dwek, R., & Opdenakker, G. (2002) · Critical reviews in biochemistry and molecular biology · doi:10.1080/10409230290771546 · Cited by 948 · see citing works

A study of proteases and protease-inhibitor complexes in biological fluids

Granelli‐Piperno, A., & Reich, E. (1978) · The Journal of Experimental Medicine · doi:10.1084/jem.148.1.223 · Cited by 803 · see citing works

Inflammation Dampened by Gelatinase A Cleavage of Monocyte Chemoattractant Protein-3

McQuibban, G. A., Gong, J.-H., Tam, E. M., McCulloch, C. A., Clark‐Lewis, I., & Overall, C. M. (2000) · Science · doi:10.1126/science.289.5482.1202 · Cited by 772 · see citing works

Purification and characterization of a novel monocyte chemotactic and activating factor produced by a human myelomonocytic cell line.

Matsushima, K., Larsen, C. G., DuBois, G. C., & Oppenheim, J. J. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.169.4.1485 · Cited by 756 · see citing works

An Alternatively Spliced Variant of CXCR3 Mediates the Inhibition of Endothelial Cell Growth Induced by IP-10, Mig, and I-TAC, and Acts as Functional Receptor for Platelet Factor 4

Lasagni, L., Francalanci, M., Annunziato, F., Lazzeri, E., Giannini, S., Cosmi, L., Sagrinati, C., Mazzinghi, B., Orlando, C., Maggi, E., et al. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20021897 · Cited by 740 · see citing works

Solution structure and basis for functional activity of stromal cell‐derived factor‐1; dissociation of CXCR4 activation from binding and inhibition of HIV‐1

Crump, M. P., Gong, J., Loetscher, P., Rajarathnam, K., Amara, A., Arenzana‐Seisdedos, F., Virelizier, J., Baggiolini, M., Sykes, B. D., & Clark‐Lewis, I. (1997) · The EMBO Journal · doi:10.1093/emboj/16.23.6996 · Cited by 731 · see citing works

Inhibition of Angiogenesis by Recombinant Human Platelet Factor-4 and Related Peptides

Maione, T. E., Gray, G. S., Petro, J., Hunt, A. J., Donner, A. L., Bauer, S., Carson, H. F., & Sharpe, R. J. (1990) · Science · doi:10.1126/science.1688470 · Cited by 698 · see citing works

Generation of biologically active IL-1 beta by matrix metalloproteinases: a novel caspase-1-independent pathway of IL-1 beta processing.

Schönbeck, U., Mach, F., & Libby, P. (1998) · PubMed · Cited by 681 · see citing works

Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-α and leaves RANTES and MCP-2 intact

den Steen, P. E. V., Proost, P., Wuyts, A., Damme, J. V., & Opdenakker, G. (2000) · Blood · doi:10.1182/blood.v96.8.2673 · Cited by 680 · see citing works

Matrix Metalloproteinase Activity Inactivates the CXC Chemokine Stromal Cell-derived Factor-1

McQuibban, G. A., Butler, G. S., Gong, J.-H., Bendall, L. J., Power, C., Clark‐Lewis, I., & Overall, C. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107736200 · Cited by 655 · see citing works

Matrix metalloproteinase processing of monocyte chemoattractant proteins generates CC chemokine receptor antagonists with anti-inflammatory properties in vivo

McQuibban, G. A., Gong, J.-H., Wong, J., Wallace, J. L., Clark‐Lewis, I., & Overall, C. M. (2002) · Blood · doi:10.1182/blood.v100.4.1160.h81602001160_1160_1167 · Cited by 611 · see citing works

Generation of Biologically Active IL-1β by Matrix Metalloproteinases: A Novel Caspase-1-Independent Pathway of IL-1β Processing

Schönbeck, U., Mach, F., & Libby, P. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.7.3340 · Cited by 605 · see citing works

Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis.

Roldan, A. L., Cubellis, M. V., Masucci, M. T., Behrendt, N., Lund, L. R., Danø, K., Appella, E., & Blasi, F. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb08132.x · Cited by 602 · see citing works

Purification and amino acid analysis of two human glioma-derived monocyte chemoattractants.

Yoshimura, T., Robinson, E. A., Tanaka, S., Appella, E., Kuratsu, J. I., & Leonard, E. J. (1989) · The Journal of Experimental Medicine · doi:10.1084/jem.169.4.1449 · Cited by 484 · see citing works

Endothelial Interleukin-8: A Novel Inhibitor of Leukocyte-Endothelial Interactions

Gimbrone, M. A., Obin, M. S., Brock, A., Luis, E., Hass, P. E., Hébert, C. A., Yip, Y. K., Leung, D. W., Lowe, D. G., Kohr, W. J., et al. (1989) · Science · doi:10.1126/science.2688092 · Cited by 452 · see citing works

CD26, let it cut or cut it down

Meester, I. D., Korom, S., van Damme, J., & Scharpé, S. (1999) · Immunology Today · doi:10.1016/s0167-5699(99)01486-3 · Cited by 451 · see citing works

The IP-10 chemokine binds to a specific cell surface heparan sulfate site shared with platelet factor 4 and inhibits endothelial cell proliferation.

Luster, A. D., Greenberg‐Sepersky, S. M., & Leder, P. (1995) · The Journal of Experimental Medicine · doi:10.1084/jem.182.1.219 · Cited by 446 · see citing works

Identification and characterization of an inhibitor of haemopoietic stem cell proliferation

Graham, G. J., Wright, E. G., Hewick, R. M., Wolpe, S. D., Wilkie, N. M., Donaldson, D. D., Lorimore, S. A., & Pragnell, I. B. (1990) · Nature · doi:10.1038/344442a0 · Cited by 438 · see citing works

The structure and function of CD26 in the T‐cell immune response

Morimoto, C., & Schlossman, S. F. (1998) · Immunological Reviews · doi:10.1111/j.1600-065x.1998.tb01571.x · Cited by 423 · see citing works

Gelatinase B: a tuner and amplifier of immune functions

Opdenakker, G., den Steen, P. E. V., & Damme, J. V. (2001) · Trends in Immunology · doi:10.1016/s1471-4906(01)02023-3 · Cited by 398 · see citing works

Structural and functional identification of two human, tumor-derived monocyte chemotactic proteins (MCP-2 and MCP-3) belonging to the chemokine family.

Damme, J. V., Proost, P., Lenaerts, J., & Opdenakker, G. (1992) · The Journal of Experimental Medicine · doi:10.1084/jem.176.1.59 · Cited by 371 · see citing works

A novel, NH2-terminal sequence-characterized human monokine possessing neutrophil chemotactic, skin-reactive, and granulocytosis-promoting activity.

Damme, J. V., BEEUMEN, J. V., Opdenakker, G., & Billiau, A. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.167.4.1364 · Cited by 314 · see citing works

HIV-induced metalloproteinase processing of the chemokine stromal cell derived factor-1 causes neurodegeneration

Zhang, K., McQuibban, G. A., Silva, C., Butler, G. S., Johnston, J. B., Holden, J. K., Clark‐Lewis, I., Overall, C. M., & Power, C. (2003) · Nature Neuroscience · doi:10.1038/nn1127 · Cited by 305 · see citing works

Cell Surface Peptidase CD26/Dipeptidylpeptidase IV Regulates CXCL12/Stromal Cell-Derived Factor-1α-Mediated Chemotaxis of Human Cord Blood CD34+ Progenitor Cells

Christopherson, K. W., Hangoc, G., & Broxmeyer, H. E. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.12.7000 · Cited by 276 · see citing works

Kinetic Investigation of Chemokine Truncation by CD26/Dipeptidyl Peptidase IV Reveals a Striking Selectivity within the Chemokine Family

Lambeir, A., Proost, P., Durinx, C., Bal, G., Senten, K., Augustyns, K., Scharpé, S., Damme, J. V., & Meester, I. D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103106200 · Cited by 271 · see citing works

Amino-terminal Truncation of Chemokines by CD26/Dipeptidyl-peptidase IV

Proost, P., Meester, I. D., Schols, D., Struyf, S., Lambeir, A., Wuyts, A., Opdenakker, G., Clercq, E. D., Scharpé, S., & Damme, J. V. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7222 · Cited by 264 · see citing works

Purification and identification of 91‐kDa neutrophil gelatinase

Masure, S., Proost, P., Damme, J. V., & Opdenakker, G. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16027.x · Cited by 253 · see citing works

Amino-terminal truncation of CXCR3 agonists impairs receptor signaling and lymphocyte chemotaxis, while preserving antiangiogenic properties

Proost, P., Schutyser, E., Menten, P., Struyf, S., Wuyts, A., Opdenakker, G., Detheux, M., Parmentier, M., Durinx, C., Lambeir, A., et al. (2001) · Blood · doi:10.1182/blood.v98.13.3554 · Cited by 236 · see citing works

Leukocyte Elastase Negatively Regulates Stromal Cell-derived Factor-1 (SDF-1)/CXCR4 Binding and Functions by Amino-terminal Processing of SDF-1 and CXCR4

Valenzuela-Fernández, A., Planchenault, T., Baleux, F., Staropoli, I., Le-Barillec, K., Leduc, D., Delaunay, T., Lazarini, F., Virelizier, J., Chignard, M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111388200 · Cited by 210 · see citing works

A Role for Dipeptidyl Peptidase IV in Suppressing the Malignant Phenotype of Melanocytic Cells

Wesley, U., Albino, A., Tiwari, S., & Houghton, A. (1999) · Journal of Experimental Medicine · doi:10.1084/jem.190.3.311 · Cited by 207 · see citing works

Cell surface peptidase CD26/DPPIV mediates G-CSF mobilization of mouse progenitor cells

Christopherson, K. W., Cooper, S. H., & Broxmeyer, H. E. (2003) · Blood · doi:10.1182/blood-2002-12-3893 · Cited by 205 · see citing works

Identification of Monocyte Chemotactic Activity Produced by Malignant Cells

Graves, D. T., Jiang, Y., Williamson, M. J., & Valente, A. J. (1989) · Science · doi:10.1126/science.2781291 · Cited by 204 · see citing works

Endothelial and leukocyte forms of IL-8. Conversion by thrombin and interactions with neutrophils.

Hébert, C. A., Luscinskas, F. W., Kíely, J.-M., Luis, E., Darbonne, W. C., Bennett, G. L., Liu, C. C., Obin, M. S., Gimbrone, M. A., & Baker, J. B. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.145.9.3033 · Cited by 198 · see citing works

Identification of a novel granulocyte chemotactic protein (GCP-2) from human tumor cells. In vitro and in vivo comparison with natural forms of GRO, IP-10, and IL-8

Proost, P., Wolf‐Peeters, C. D., Conings, R., Opdenakker, G., Billiau, A., & Damme, J. V. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.150.3.1000 · Cited by 196 · see citing works

Processing by CD26/dipeptidyl‐peptidase IV reduces the chemotactic and anti‐HIV‐1 activity of stromal‐cell‐derived factor‐1α

Proost, P., Struyf, S., Schols, D., Durinx, C., Wuyts, A., Lenaerts, J., Clercq, E. D., Meester, I. D., & Damme, J. V. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00830-8 · Cited by 193 · see citing works

Cutting Edge: Scavenging of Inflammatory CC Chemokines by the Promiscuous Putatively Silent Chemokine Receptor D6

Fra, A., Locati, M., Otero, K., Sironi, M., Signorelli, P., Massardi, M. L., Gobbi, M., Vecchi, A., Sozzani, S., & Mantovani, A. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.170.5.2279 · Cited by 185 · see citing works

Generation of the neutrophil-activating peptide NAP-2 from platelet basic protein or connective tissue-activating peptide III through monocyte proteases.

Walz, A., & Baggiolini, M. (1990) · The Journal of Experimental Medicine · doi:10.1084/jem.171.2.449 · Cited by 167 · see citing works

Cytokines and proteases in invasive processes: Molecular similarities between inflammation and cancer

Opdenakker, G., & Damme, J. V. (1992) · Cytokine · doi:10.1016/1043-4666(92)90064-x · Cited by 158 · see citing works

In vivo properties of monocyte chemoattractant protein-1

Gu, L., RUTLEDGE, B. J., Fiorillo, J., Ernst, C. A., Grewal, I. S., Flavell, R. A., Gladue, R. P., & Rollins, B. J. (1997) · Journal of Leukocyte Biology · doi:10.1002/jlb.62.5.577 · Cited by 157 · see citing works

Cleavage by CD26/dipeptidyl peptidase IV converts the chemokine LD78β into a most efficient monocyte attractant and CCR1 agonist

Proost, P., Menten, P., Struyf, S., Schutyser, E., Meester, I. D., & Damme, J. V. (2000) · Blood · doi:10.1182/blood.v96.5.1674 · Cited by 153 · see citing works

Functional Comparison of Two Human Monocyte Chemotactic Protein-2 Isoforms, Role of the Amino-Terminal Pyroglutamic Acid and Processing by CD26/Dipeptidyl Peptidase IV

Coillie, E. V., Proost, P., Aelst, I. V., Struyf, S., Polfliet, M. M. J., Meester, I. D., Harvey, D. J., Damme, J. V., & Opdenakker, G. (1998) · Biochemistry · doi:10.1021/bi980497d · Cited by 152 · see citing works

Truncation of Macrophage-derived Chemokine by CD26/ Dipeptidyl-Peptidase IV beyond Its Predicted Cleavage Site Affects Chemotactic Activity and CC Chemokine Receptor 4 Interaction

Proost, P., Struyf, S., Schols, D., Opdenakker, G., Sozzani, S., Allavena, P., Mantovani, A., Augustyns, K., Bal, G., Haemers, A., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.7.3988 · Cited by 150 · see citing works

A potent inhibitor of endothelial cell proliferation is generated by proteolytic cleavage of the chemokine platelet factor 4.

Gupta, S. K., Hassel, T., & Singh, J. P. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7799 · Cited by 141 · see citing works

Dipeptidyl‐peptidase IV/CD26 on T cells: analysis of an alternative T‐cell activation pathway

von Bonin, A., Hühn, J., & Fleischer, B. (1998) · Immunological Reviews · doi:10.1111/j.1600-065x.1998.tb01570.x · Cited by 140 · see citing works

The chemotactic activity for granulocytes produced by virally infected fibroblasts is identical to monocyte‐derived interleukin 8

Damme, J. V., Decock, B., Conings, R., Lenaerts, J., Opdenakker, G., & Billiau, A. (1989) · European Journal of Immunology · doi:10.1002/eji.1830190706 · Cited by 137 · see citing works

Natural Proteolytic Processing of Hemofiltrate Cc Chemokine 1 Generates a Potent Cc Chemokine Receptor (Ccr)1 and Ccr5 Agonist with Anti-HIV Properties

Detheux, M., Ständker, L., Vakili, J., Münch, J., Forssmann, U., Adermann, K., Pöhlmann, S., Vassart, G., Kirchhoff, F., Parmentier, M., et al. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.192.10.1501 · Cited by 136 · see citing works

Differential IgE recognition of recombinant Aspergillus fumigatus allergens by cystic fibrosis patients with allergic bronchopulmonary aspergillosis or Aspergillus allergy

Hemmann, S., Nikolaizik, W. H., Schöni, M. H., Blaser, K., & Crameri, R. (1998) · European Journal of Immunology · doi:10.1002/(sici)1521-4141(199804)28:04 · Cited by 130 · see citing works

Posttranslational Modifications Affect the Activity of the Human Monocyte Chemotactic Proteins MCP-1 and MCP-2: Identification of MCP-2(6–76) as a Natural Chemokine Inhibitor

Proost, P., Struyf, S., Couvreur, M., Lenaerts, J., Conings, R., Menten, P., Verhaert, P. D. E. M., Wuyts, A., & Damme, J. V. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.160.8.4034 · Cited by 128 · see citing works

Purification of melanoma growth stimulatory activity

Richmond, A., & Thomas, H. G. (1986) · Journal of Cellular Physiology · doi:10.1002/jcp.1041290316 · Cited by 128 · see citing works

Regulation of the Immune Response by the Interaction of Chemokines and Proteases

Struyf, S., Proost, P., & Damme, J. V. (2003) · Advances in immunology · doi:10.1016/s0065-2776(03)81001-5 · Cited by 122 · see citing works

Reduced Tumorigenicity and Augmented Leukocyte Infiltration After Monocyte Chemotactic Protein-3 ( MCP-3 ) Gene Transfer: Perivascular Accumulation of Dendritic Cells in Peritumoral Tissue and Neutrophil Recruitment Within the Tumor

Fioretti, F., FRADELIZI, D., Stoppacciaro, A., Ramponi, S., Ruco, L., Minty, A. J., Sozzani, S., Garlanda, C., Vecchi, A., & Mantovani, A. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.1.342 · Cited by 121 · see citing works

Cathepsin D Specifically Cleaves the Chemokines Macrophage Inflammatory Protein-1α, Macrophage Inflammatory Protein-1β, and SLC That Are Expressed in Human Breast Cancer

Wolf, M., Clark‐Lewis, I., Buri, C., Langen, H., Lis, M., & Mazzucchelli, L. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63914-4 · Cited by 97 · see citing works

Chemotactic factors, passive invasion and metastasis of cancer cells

Opdenakker, G., & Damme, J. V. (1992) · Immunology Today · doi:10.1016/0167-5699(92)90079-m · Cited by 94 · see citing works

Stimulation of extracellular matrix components in the normal brain by invading glioma cells

Knott, J. C. A., Mahesparan, R., Garcia‐Cabrera, I., Tysnes, B. B., Edvardsen, K., Ness, G. O., Mørk, S. J., Lund‐Johansen, M., & Bjerkvig, R. (1998) · International Journal of Cancer · doi:10.1002/(sici)1097-0215(19980316)75:6 · Cited by 92 · see citing works

Enhanced anti-HIV-1 activity and altered chemotactic potency of NH2-terminally processed macrophage-derived chemokine (MDC) imply an additional MDC receptor.

Struyf, S., Proost, P., Sozzani, S., Mantovani, A., Wuyts, A., Clercq, E. D., Schols, D., & Damme, J. V. (1998) · PubMed · Cited by 91 · see citing works

Identification by sequence analysis of chemotactic factors for monocytes produced by normal and transformed cells stimulated with virus, double‐stranded RNA or cytokine

Damme, J. V., Decock, B., Lenaerts, J., Conings, R., Bertini, R., Mantovani, A., & Billiau, A. (1989) · European Journal of Immunology · doi:10.1002/eji.1830191228 · Cited by 90 · see citing works

Cutting Edge: Enhanced Anti-HIV-1 Activity and Altered Chemotactic Potency of NH2-Terminally Processed Macrophage-Derived Chemokine (MDC) Imply an Additional MDC Receptor

Struyf, S., Proost, P., Sozzani, S., Mantovani, A., Wuyts, A., Clercq, E. D., Schols, D., & Damme, J. V. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.6.2672 · Cited by 79 · see citing works

Isolation of the CXC chemokines ENA‐78, GROα and GROγ from tumor cells and leukocytes reveals NH2‐terminal heterogeneity

Wuyts, A., Govaerts, C., Struyf, S., Lenaerts, J., Put, W., Conings, R., Proost, P., & Damme, J. V. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00166.x · Cited by 77 · see citing works

Human hepatoma cells produce an 85 kDa gelatinase regulated by phorbol 12-myristate 13-acetate

Masure, S., Billiau, A., Damme, J. V., & Opdenakker, G. (1990) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(90)90103-k · Cited by 72 · see citing works

Transduction of human MCP-3 by a parvoviral vector induces leukocyte infiltration and reduces growth of human cervical carcinoma cell xenografts

Wetzel, K., Menten, P., Opd�nakker, G., Damme, J. V., Gröne, H., Giese, N. A., Vecchi, A., Sozzani, S., Cornelis, J. J., Rommelaere, J., et al. (2001) · The Journal of Gene Medicine · doi:10.1002/jgm.191 · Cited by 65 · see citing works

Natural Truncation of the Chemokine MIP-1β/CCL4 Affects Receptor Specificity but Not Anti-HIV-1 Activity

Guan, E., Wang, J., Roderiquez, G., & Norcross, M. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203077200 · Cited by 63 · see citing works

Negative regulation of the anti‐human immunodeficiency virus and chemotactic activity of human stromal cell‐derived factor 1α by CD26/dipeptidyl peptidase IV

Ohtsuki, T., Hosono, O., Kobayashi, H., Munakata, Y., Souta, A., Shioda, T., & Morimoto, C. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00763-7 · Cited by 62 · see citing works

Identification of Unique Truncated KC/GROβ Chemokines with Potent Hematopoietic and Anti-Infective Activities

King, A. G., Johanson, K., Frey, C. L., DeMarsh, P. L., White, J. R., McDevitt, P. J., McNulty, D. E., Balcarek, J. M., Jonak, Z., Bhatnagar, P. K., et al. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.7.3774 · Cited by 56 · see citing works

Generation of interleukin‐8 by plasmin from AVLPR‐interleukin‐8, the human fibroblast‐derived neutrophil chemotactic factor

Nakagawa, H., Hatakeyama, S., Ikesue, A., & Miyai, H. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80526-9 · Cited by 56 · see citing works

NH2- and COOH-Terminal Truncations of Murine Granulocyte Chemotactic Protein-2 Augment the In Vitro and In Vivo Neutrophil Chemotactic Potency

Wuyts, A., D'Haese, A., Cremers, V., Menten, P., Lenaerts, J., LOOF, A. D., Heremans, H., Proost, P., & Damme, J. V. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.11.6155 · Cited by 55 · see citing works

Urokinase Plasminogen Activator and Plasmin Efficiently Convert Hemofiltrate CC Chemokine 1 into Its Active [9–74] Processed Variant

Vakili, J., Ständker, L., Detheux, M., Vassart, G., Forssmann, W., & Parmentier, M. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.6.3406 · Cited by 51 · see citing works

Chemotactic activity for mononuclear phagocytes of culture supernatants from murine and human tumor cells: Evidence for a role in the regulation of the macrophage content of neoplastic tissues

Bottazzi, B., Polentarutti, N., Balsari, A., Boraschi, D., Ghezzi, P., Salmona, M., & Mantovani, A. (1983) · International Journal of Cancer · doi:10.1002/ijc.2910310110 · Cited by 47 · see citing works

The cytokine-protease connection: Identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers

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Differential Impact of Cysteine Cathepsins on Genetic Mouse Models of De novo Carcinogenesis: Cathepsin B as Emerging Therapeutic Target

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A CD26-Controlled Cell Surface Cascade for Regulation of T Cell Motility and Chemokine Signals

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Role of CCR5 in the Pathogenesis of IL-13-Induced Inflammation and Remodeling

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Co‐inoculation of prostate cancer cells with U937 enhances tumor growth and angiogenesis in vivo

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Structure activity relationship studies of natural product chemokine receptor CCR5 antagonist anibamine toward the development of novel anti prostate cancer agents

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